pmid	comment
PMID:10022828	establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A)
PMID:10022828	establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A)
PMID:10022921	assayed using Tf1 transposon
PMID:10022921	assayed using Tf1 transposon plasmid construct
PMID:10022921	assayed using Tf1 transposon
PMID:10022921	assayed using Tf1 transposon plasmid construct
PMID:10022921	assayed using Tf1 transposon Gag and IN
PMID:10087262	more than threefold over compared with wild-type cells (344%)
PMID:10087262	combined localization and membrane fraction
PMID:10087262	The other was observed as pairs of di- vided cells associated side-by-side (12%), the cell wall of which appeared fragile and often lysed upon division.
PMID:10087262	combined localization and membrane fraction
PMID:10087262	These results suggested that Mok1 is an stable integral membrane pro- tein, which is consistent with the presence of several trans- membrane domains (Fig. 2 a).
PMID:10087262	. mok1-664􏰌pck2 was synthetically lethal at 30􏰊C, a temperature at which either single mutant could grew (Fig. 10b)
PMID:10087262	. Synthetic lethality was not observed between mok1- 664 and 􏰌pck1, consistent with our previous result showing that pck2􏰇 plays the major role (Toda et al., 1993)
PMID:10087262	. mok1-664􏰌pck2 was synthetically lethal at 30􏰊C, a temperature at which either single mutant could grew (Fig. 10b)
PMID:10087262	pck2delta rescues ags1 ox defect
PMID:10087262	data not shown
PMID:10087262	Fig. 1 c
PMID:10087262	Fig. 1 a, 'delocalized actin'
PMID:10087262	translocation of actin from one end t the other (also fig7)
PMID:10091325	activated_by CHEBI:29108 | activated_by CHEBI:18420 | inhibited_by CHEBI:16761
PMID:10207075	In contrast to the point mutation, the rec8::ura4 strain showed no shortening of prophase in three independent time courses (data not shown). Shortening of the prophase in the point mutation strain may indicate a role of Rec8p in meiosis regulation. Alternative explanations, like shortening of prophase by an additional mutation, were not excluded.
PMID:10226032	Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6.
PMID:10226032	mcs6 requires mcs2 for CTD kinase activity but not cyclin-dependent kinase activating kinase activity. mcs2 does not cycle throughout the cell cycle.
PMID:10226032	Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins.
PMID:10364209	DNS
PMID:10364209	Fig. 1B
PMID:10364209	The same level of Myo2p co-immunoprecipitated with mutant Cdc4p as with wild-type Cdc4p (Fig. 5A).
PMID:10364209	Fig. 1B
PMID:10364209	DNS
PMID:10365961	tyrosine, possibly Y188 (but not determined experimentally)
PMID:10365961	tyrosine, possibly Y188 (but not determined experimentally)
PMID:10365961	tyrosine, possibly Y188 (but not determined experimentally)
PMID:10366596	in zygotic nucleus
PMID:10366596	in zygotic nucleus
PMID:10366596	astral
PMID:10366596	The ~14-fold increase of the disomic spores indicated that chromosome missegregation increased during meiosis I
PMID:10381387	it doesn't say old, but it is...
PMID:10381387	it doesn't say old, but it is...
PMID:10388806	cdc18delta::p[nmt*.cdc18+-LEU2]
PMID:10388806	Val: moved down from FYPO:0001429, its a fully penetrant inviable phenotype (anucleate)
PMID:10388806	cdc18delta::p[nmt*.cdc18+-LEU2]
PMID:10392445	conditions under which pat1-114 alone induces meiosis & sporulation
PMID:10398679	is response to heat a real process or should be resposne to denatured proteins or whatever?
PMID:10398680	Figure 1F & 7B (second mitosis)
PMID:10398680	These results showed that Mis12 was localized at centromeres throughout the cell cycle
PMID:10398680	(Fig. 6D): Mis12 is thus required for maintaining the inner centromere structure.
PMID:10398680	Figure 1, A and B All of these required passage through G1 (second mitosis)
PMID:10398680	Figure 2
PMID:10398680	figure 3 (before phase 3 extension)
PMID:10398680	figure 6 Hence, mis6–HA could interact with the centromere in the absence of functional Mis12.
PMID:10398680	figure 6 Conversely, the mis6-302 strain integrated with the Mis12–HA gene was used.
PMID:10398680	suggesting that sister centromeres were separated in the metaphase-arrested cells.
PMID:10398680	figure 8a
PMID:10398680	figure 8a
PMID:10398680	figure 8a
PMID:10398680	Figure 1, A and B All of these required passage through G1 (second mitosis)
PMID:10398680	figue 4
PMID:10398680	fig 1a
PMID:10398680	figure3
PMID:10398680	figure 3
PMID:10428959	figure 3
PMID:10428959	figure 3
PMID:10428959	(vw: sty1-atf1 pathway)
PMID:10428959	(vw: sty1-atf1 pathway)
PMID:10428959	Figure 5
PMID:10428959	Figure 5
PMID:10428959	Figure 6
PMID:10428959	Figure 6B
PMID:10428959	figure 7
PMID:10428959	figure 7
PMID:10428959	figure 7
PMID:10428959	Figure1/2
PMID:10428959	DNS
PMID:10428959	Figure 3 (vw severity 23.4 micron)
PMID:10428959	Figure 3 (vw: severity 20.2 micron)
PMID:10428959	table 2
PMID:10428959	figure 3b
PMID:10428959	figure 3b
PMID:10428959	table 2
PMID:10428959	Figure 1/2
PMID:10428959	figure 2C (vw: not by sty1)
PMID:10430583	same as rad51delta alone
PMID:10430583	same as rad51delta alone
PMID:10459013	present throughout mitotic cell cycle
PMID:10462529	fig3
PMID:10462529	fig1
PMID:10462529	fig1
PMID:10462529	fig2
PMID:10462529	fig2
PMID:10462529	Fig. 3
PMID:10462529	Fig. 3
PMID:10462529	4a
PMID:10462529	fig5
PMID:10462529	fig5
PMID:10462529	fig5
PMID:10462529	fig 6
PMID:10462529	fig6
PMID:10462529	fig 6
PMID:10462529	fig5
PMID:10462529	extension, of cdc25 7b
PMID:10462529	fig2
PMID:10462529	fig2
PMID:10462529	fig7
PMID:10462529	fig 7
PMID:10473641	broken
PMID:10521402	Fig3B data not shown
PMID:10521402	Fig 1A rad1 is required for meiotic DNA replication checkpoint
PMID:10521402	Fig1B cds1 is required for meiotic DNA replication checkpoint
PMID:10521402	Fig1B
PMID:10521402	Fig1B
PMID:10521402	Fig 1B double cds1delta chk1 delta has same phenotype as single cds1delta/cds1 delta
PMID:10521402	Fig 2 A,B
PMID:10521402	Fig 2 A,B
PMID:10521402	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	Fig3B data not shown
PMID:10521402	Fig3 B
PMID:10521402	Fig3 B
PMID:10521402	Fig3B
PMID:10521402	Fig 4
PMID:10521402	Fig4 present during meiotic DNA replication checkpoint arrest
PMID:10521402	Fig5A see control in Fig4A
PMID:10521402	Fig5B see Fig4B for control
PMID:10521402	Fig5A see control in Fig4A
PMID:10521402	Fig 5A see Fig4A for control
PMID:10521402	Fig 5A see Fig4A for control
PMID:10521402	Fig6C
PMID:10521402	Data not shown when rad1 is deleted checkpoint is not activated and cells attempt meiotic nuclear divisions see also Fig1, 2, 3B
PMID:10521402	Fig6A,D; meiotic cells unable to inhibit CDK1 activity in response to activation of the meiotic DNA replication checkpoint, arrest at metaphase of Meiosis I and do not undergo nuclear division
PMID:10523629	Figure 1 a
PMID:10523629	fig 2a
PMID:10523629	fig 2a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	fig 3 C
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Fig 5 G
PMID:10523629	Fig 5 C
PMID:10523629	Fig 5 J
PMID:10523629	fig 4
PMID:10523629	fig 4
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10523629	Figure 1 a
PMID:10526233	(it basically the same as cut except the nucleus is not bisected)
PMID:10526233	(it basically the same as cut except the nucleus is not bisected)
PMID:10545452	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cyto- kinesis defects at 24􏰌, a temperature at which rng2-D5 and cdc4-8 single mutants grew healthily and resembled wild-type cells in morphology (Figure 7).
PMID:10545452	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	Germinated drc1::ura4 spores were capable of po- larity establishment (shown with arrows in Figure 6C), but appeared to be incapable of polarity maintenance, causing them to become spherical and highly enlarged (Figure 6C).
PMID:10545452	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	Interestingly, unlike the drc1-191 mutant, drc1::ura4 underwent multiple nuclear division cycles causing arrested cells to accumulate up to 32 nuclei.
PMID:10545452	i.e next round of replication
PMID:10545452	The drc1-191 myo2-E1 double mutant was unable to form colonies at 24􏰌, a temperature at which both parental strains were capable of colony formation (data not shown).
PMID:10545452	The drc1-191 myo2-E1 double mutant was unable to form colonies at 24􏰌, a temperature at which both parental strains were capable of colony formation (data not shown).
PMID:10545452	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1􏰀/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mu- tant was unable to form colonies (data not shown).
PMID:10545452	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1􏰀/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mu- tant was unable to form colonies (data not shown).
PMID:10545452	i.e next round of replication
PMID:10545452	At the drc1-191 arrest point all binucleate cells were found to have Cdc7p staining localized at one SPB. Merged images of chromosomal staining with DAPI and Cdc7p staining with HA antibodies is shown in Figure 4. The drc1-191 mutant, therefore, arrests at a point in the cell cycle where the septum-promoting Cdc7p is located on one SPB.
PMID:10545452	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	Figure 1, 4 hr
PMID:10545452	Figure 1, 8 hr
PMID:10545452	Figure 1, 0 hr
PMID:10545452	Microtubule staining confirmed that the drc1-191 cells were arrested in interphase since cells blocked predominantly either with interphase arrays of microtubules or with a postana- phase array of microtubules (Figure 3A, 4 hr).
PMID:10545452	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cyto- kinesis defects at 24􏰌, a temperature at which rng2-D5 and cdc4-8 single mutants grew healthily and resembled wild-type cells in morphology (Figure 7). In both double mutant combinations (drc1-191 cdc4-8 and drc1-191 rng2- D5) highly elongated cells with multiple nuclei were seen frequently.
PMID:10547441	this should be decreased thickness at old end during veg growth
PMID:10567589	fig2d - number 7 and 8
PMID:10567589	fig2d - number 7 and 8
PMID:10567589	3c
PMID:10567589	The profile of pmt3􏰗 cells showed a decrease of the number of cells with 2C DNA content and an increase in the number of cells with a DNA content greater or less than 2C DNA content (at times 􏰔2 and 0 h in Fig. 3C)
PMID:10567589	The profile of pmt3􏰗 cells showed a decrease of the number of cells with 2C DNA content and an increase in the number of cells with a DNA content greater or less than 2C DNA content (at times 􏰔2 and 0 h in Fig. 3C)
PMID:10574765	Figure 2b Boundary of non growing cell end maintained
PMID:10574765	Figure 2a Boundary of non growing cell end maintained
PMID:10574765	Figure 2c Boundary of the non growing cell end not maintained
PMID:10574765	Figure 3 F actin is absent from non growing end
PMID:10574765	Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C
PMID:10574765	Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C
PMID:10574765	Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C
PMID:10574765	"vw: jacky suggested ""protein localisation to the lateral plasma membrane""but will keep as parent Figures 1, S1 and S2. Cor-C GFP is probably episomal but it is not clear"
PMID:10574765	Figure 3 normal at non-growing end
PMID:10574765	Figure 3 normal at non-growing end
PMID:10581266	fig6
PMID:10581266	fig9 high overexpression is lethal
PMID:10581266	fig4
PMID:10581266	fig9
PMID:10581266	fig6
PMID:10581266	fig6
PMID:10588638	inferred from Chk1 phosphorylation phenotypes
PMID:10588653	(Figure 8A). Arp2-E316K mutant protein had a reduced affinity for ATP compared with wild type Arp2p
PMID:10588653	Fig6
PMID:10588653	Fig6
PMID:10588653	Fig6
PMID:10588653	figure suggesting that the mutant protein is likely less stable than the wild-type Arp2 protein (Figure 6B), a hypothesis confirmed below (see Figure 8C).
PMID:10588653	Fig6
PMID:10588653	Fig6
PMID:10588653	figure (Figure 6)
PMID:10588653	figure (Figure 6D)
PMID:10588653	Fig 8 A After UV irradiation, we found that both wild-type Arp2p and Arp3p were labeled by 8-azido-[a-32P]ATP, indicating that these actin-related proteins bind ATP as predicted
PMID:10588653	Fig 8 A After UV irradiation, we found that both wild-type Arp2p and Arp3p were labeled by 8-azido-[a-32P]ATP, indicating that these actin-related proteins bind ATP as predicted
PMID:10588653	figure 4 In arp2-1 mutant cells grown at the restrictive temperature, the protein was not detected in patches. Rather, it appeared to be diffusely distributed throughout the cytoplasm (Figure 4C).
PMID:10588653	figure4
PMID:10588653	figure4
PMID:10588653	figure4
PMID:10588653	Fig3 synthetic rescue of cdc3
PMID:10588653	Fig3
PMID:10588653	Fig3
PMID:10588653	DNS In all tetrads, the viable colonies were Arp21 Ura2, indicating that arp21 is an essential gen
PMID:10588653	figure 1c
PMID:10588653	figure 1, after 8 hours, medial region of the cells continued to accumulate excess cell wall material
PMID:10588653	figure 1, after 5 hours
PMID:10588653	DNS after 5 hours
PMID:10588653	DNS
PMID:10588653	DNS
PMID:10588653	Figure 8 The most striking difference between wild-type Arp2p and Arp2-E316K was the failure to coimmunoprecipitate labeled Arp3p with Arp2-E316K
PMID:10588653	8B & C These results clearly establish that the mutant Arp2-E316K protein turns over more rapidly than wild-type Arp2 protein
PMID:10588653	(Figure 8A). T12A protein was also labeled by the ATP analogue, but to a much lesser degree than wild-type Arp2p
PMID:10591634	IPI and IMP evidence
PMID:10593886	only in vitro data evidence
PMID:10641037	figure 2
PMID:10641037	DNS
PMID:10641037	figure 3b
PMID:10651902	fig6
PMID:10651902	appeared thicker
PMID:10651902	normal volume?
PMID:10651902	Rho1 GTP bound form pck2 HR1 domain
PMID:10651902	fig6
PMID:10651902	Rho1 appears to have a dual role in stabilizing and localizing Pck proteins
PMID:10683155	cut if exposed to radiation during S phase, but not if exposed during G2
PMID:10683155	constant level throughout cell cycle
PMID:10698951	temperature restrictive for cdc27-P11 alone
PMID:10698951	temperature restrictive for cdc27-P11 alone
PMID:10712506	from materials and methods
PMID:10712506	from materials and methods
PMID:10712506	from materials and methods
PMID:10712506	from materials and methods
PMID:10718196	DNS
PMID:10725227	Fig7C, D The protein and mRNA levels are compared to cDNA-I which is also expressed from medium strength nmt1 promoter ON
PMID:10725227	Fig3A
PMID:10725227	Fig3B cig2 protein presence in nuc2-663 alone
PMID:10725227	Fig3B cdc13 protein presence in nuc2-663 alone
PMID:10725227	Fig4B
PMID:10725227	Fig 5A 35S Methionine pulse measured incorporation
PMID:10725227	Fig 5B 35S Methionine pulse, measured incorporation
PMID:10725227	Fig 5B 35S Methionine pulse, measured incorporation
PMID:10725227	Fig10A
PMID:10725227	Fig9
PMID:10725227	Fig8. The labelling looks wrong in this figure, not sure whether to annotate it or not
PMID:10725227	Fig8. The labelling looks wrong in this figure, not sure whether to annotate it or not
PMID:10725227	Fig6 total protein translation not affect
PMID:10725227	Fig7 B over expression of cig2+ cDNAI partially suppresses the rescue of cdc21-M68 by ded1-1D5
PMID:10725227	Fig7 B over expression of cig2+ cDNAII suppresses the rescue of cdc21-M68 by ded1-1D5
PMID:10725227	Fig7 B over expression of cig2+ cDNAIII suppresses the rescue of cdc21-M68 by ded1-1D5
PMID:10725227	Fig6 total protein translation not affected
PMID:10725227	Fig 1B there is a small G1 peak which get slightly bigger but they also cells arrested in G1 by -N, when refed and shifted to the restrictive temp cannot enter S phase but this is data not shown
PMID:10725227	Fig 1B
PMID:10725227	Fig 1B G1 arrest of ded1-1D5 is dependent on rum1+
PMID:10725227	Table 2
PMID:10725227	Table 2
PMID:10725227	Table 2
PMID:10725227	Fig2B
PMID:10725227	Fig2B
PMID:10725227	Fig2B
PMID:10725227	Fig2C ded1-78 is a cold sensitive mutant
PMID:10725227	Fig2C ded1-61 is a cold sensitive mutant
PMID:10725227	Fig2B
PMID:10725227	Fig2D the semi permissive temperature 34.5C for ded1-D5 allows it to suppress cdc19-P1 (mcm2)
PMID:10725227	Fig9
PMID:10725227	Fig10B
PMID:10725227	Fig3A
PMID:10733588	Table2
PMID:10733588	Fig. 3D and data not shown
PMID:10733588	Table2
PMID:10748059	inhibited_by(CHEBI:48828)
PMID:10749926	figure 4
PMID:10749926	figure 4 (spindle is still present, normally disaaembld by cytokinesis)
PMID:10749926	figure 1B
PMID:10749926	Fig 6
PMID:10749926	figure 1B
PMID:10749926	Fig 6
PMID:10757807	same as cds1delta alone
PMID:10757807	same as cdc27-P11 alone
PMID:10757807	same as rqh1delta alone
PMID:10766248	severity correlates positively with overexpression level, and different isolates with same construct integrated show different Cdc18 levels
PMID:10766248	severity correlates positively with overexpression level
PMID:10766248	cdc18+ low level overexpression
PMID:10769212	temperature restrictive for cdc4-8 alone
PMID:10769212	inviable at 37 degrees; some growth at 34 degrees
PMID:10769212	inviable at 37 degrees; some growth at 34 degrees
PMID:10769212	inviable at 34 or 37 degrees
PMID:10769212	temperature restrictive for cdc4-8 alone
PMID:10769212	temperature restrictive for cdc4-8 alone
PMID:10769212	temperature restrictive for cdc4-8 alone
PMID:10769212	dependent on F-actin (assayed using Latrunculin A)
PMID:10769212	early mitosis; independent of F-actin (assayed using Latrunculin A)
PMID:10770926	activated by ATP
PMID:10770926	activated by ATP
PMID:10770926	activated by ATP
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	After shift to restrictive temperature, cdc16-116 cells display two phenotypes termed type I and type II cells (Minet et al., 1979; Cerutti and Simanis, 1999). Type I cells have two nuclei and make multiple septa. Type II cells have a single nucleus and a septa. It has been proposed that the type II cells immediately septate again after division because they inherit the SPB that contains active Spg1p (Cerutti and Simanis, 1999). In support of this hypothesis, Sid1p was present at the SPB in type II cells (Figure 3A; see arrow).
PMID:10775265	fig 3c
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	Cdc7p cannot localize to the SPB(s) in cdc11 (Figure 4; Table I)
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	After shift to restrictive temperature, cdc16-116 cells display two phenotypes termed type I and type II cells (Minet et al., 1979; Cerutti and Simanis, 1999). Type I cells have two nuclei and make multiple septa. Type II cells have a single nucleus and a septa. It has been proposed that the type II cells immediately septate again after division because they inherit the SPB that contains active Spg1p (Cerutti and Simanis, 1999). In support of this hypothesis, Sid1p was present at the SPB in type II cells (Figure 3A; see arrow).
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	dns
PMID:10775265	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	GFP±Sid1p signal was not observed at SPBs in these cells although faint nuclear signal was observed (Figure 7A). This suggests that some aspect of completion of mitosis is required in order for Sid1p to localize.
PMID:10775265	Afterashifttorestrictivetemperaturefor50min to inactivate Cdc2p, cells could now be observed that were septating without undergoing anaphase (Figure 7E and F, see arrows). At this point, 96% (68/71) of cells displaying Sid1p signal at the SPB were septating without having undergone anaphase (Figure 7E and F, see arrows
PMID:10775265	Figure4;TableI;datanotshown
PMID:10775265	fig 3d
PMID:10779336	3B
PMID:10779336	fig8
PMID:10779336	1A
PMID:10779336	2B
PMID:10779336	2B
PMID:10779336	2B
PMID:10779336	1A increased size?
PMID:10779336	1B
PMID:10779336	2B
PMID:10779336	2
PMID:10779336	3A
PMID:10779336	3B
PMID:10779336	3B
PMID:10779336	3B
PMID:10779336	5.6%
PMID:10779336	3B
PMID:10779336	4C
PMID:10792724	residue=S200
PMID:10799520	combine, other binucleates should unde new term
PMID:10799520	This analysis of microtubule structures confirmed that mononucleate cells with Cdc7 local- ized to SPBs were in interphase and suggested that Byr4 was required to prevent septation during interphase.
PMID:10799520	is this the right term?
PMID:10799520	Later in anaphase, Byr4 colocalized with one SPB (Fig. 1B, 4). Byr4 colocalized with one or both SPBs in binucleate cells with septa (Fig. 1B, 5 and 6). In the vast majority of cells, Byr4 localized to SPBs that did not contain Cdc7 (Fig. 1C, 1, 4, and 5).
PMID:10799520	Spg1-HAH localized to SPBs throughout the cell cycle (Fig. 1B, second column) (8). Byr4 colocalized with Spg1-HAH during interphase (Fig. 1B, 1), but was absent from SPBs in metaphase (Fig. 1B, 2) and early anaphase
PMID:10799520	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1),
PMID:10799520	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1),, localized to both SPBs in metaphase and early anaphase cells (Fig. 1C, 2 and 3), and localized to one SPB in late mitotic cells (Fig. 1C, 4 – 6) (8).
PMID:10799520	Western analysis showed that this decrease was not due to reduced Byr4 amounts
PMID:10799520	Examination of these cells following 12 h of growth in thiamine-containing medium also showed that most cells (59%) contained Byr4 at all SPBs (Table II). In contrast to sid3–106 mutants, though, the amount of Byr4 localized to SPBs in cells depleted of Spg1 using the conditional promoter was greatly reduced (data not shown)
PMID:10799520	Western analysis showed that the reduction in Byr4 localization to SPBs in cells depleted of Spg1 was not due to reduced Byr4 protein amounts (data not shown).
PMID:10799520	Examination of these cells following 12 h of growth in thiamine-containing medium also showed that most cells (59%) contained Byr4 at all SPBs (Table II). In contrast to sid3–106 mutants, though, the amount of Byr4 localized to SPBs in cells depleted of Spg1 using the conditional promoter was greatly reduced (data not shown)
PMID:10799520	As expected, most sid3–106 mutant cells (71%) contained four or more nuclei showing that there was insufficient Spg1 function in these cells for septation.
PMID:10799520	A corresponding decrease in the fraction of cells with Spg1 localized to SPBs occurred and reached 7% at 16 h (Fig. 3)
PMID:10799520	Figure 2E. These results show that Byr4 is re- quired to prevent septation in G1 cells.
PMID:10805744	same as cdc2delta alone
PMID:10805744	not sown it is ser/thr kinase activity
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig 1c
PMID:10805785	fig2
PMID:10850973	activated_by(CHEBI:18420)| activated_by(CHEBI:29103)| inhibited_by(CHEBI:48607)| inhibited_by(CHEBI:26710)
PMID:10852821	Fig. 3B
PMID:10852821	fig9
PMID:10852821	Fig 6
PMID:10852821	fig9 maintenance
PMID:10852821	Fig. 3B
PMID:10852821	Fig 6
PMID:10852821	Fig 6
PMID:10852821	Fig. 3B
PMID:10852821	fig9
PMID:10852821	Fig 6
PMID:10852821	Fig. 3B
PMID:10852821	Fig 6
PMID:10852821	Fig 6
PMID:10852821	fig 7A
PMID:10852821	fig 7A (depends on actin)
PMID:10852821	fig8 myo2 clumped in nodes instead of ring
PMID:10852821	fig8 myo2 clumped in nodes instead of ring
PMID:10852821	fig8
PMID:10852821	fig8
PMID:10852821	fig8
PMID:10852821	fig8
PMID:10864871	2nd division
PMID:10871341	diploid; ran1 allele pat1-114 in background
PMID:10871341	diploid; ran1 allele pat1-114 in background
PMID:10871341	diploid; ran1 allele pat1-114 in background
PMID:10871341	diploid; ran1 allele pat1-114 in background
PMID:10879493	2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess
PMID:10879493	2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess
PMID:10886372	don't know veg or spore
PMID:10905343	total alpha tubulin level reduced but not known whether from nda2 or atb2 or both
PMID:10905343	total alpha tubulin level reduced but not known whether from nda3 or atb2 or both
PMID:10921876	fig1a
PMID:10921876	APC-SLP1
PMID:10921876	fig3 cdc25-22 block and release
PMID:10921876	fig3 cdc25-22 block and release
PMID:10921876	fig3 cdc25-22 block and release
PMID:10921876	APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this becase they don't whow a WT scanario.I used the ubiquitin-dependent term becasuethis is whet they were testing as we already know that this decgradation is APC/protiesome dependnet. I know its a bit of a stretch...
PMID:10921876	APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this becase they don't whow a WT scanario.I used the ubiquitin-dependent term becasuethis is whet they were testing as we already know that this decgradation is APC/protiesome dependnet. I know its a bit of a stretch...
PMID:10921876	fig 3 cdc25-22 block and release
PMID:10921876	fig 3 cdc25-22 block and release
PMID:10921876	fig3 cdc25-22 block and release
PMID:10921876	fig1 b
PMID:10921876	fig1a
PMID:10921878	during mitotic G2 arrest
PMID:10930468	DNES1-mid1p had a clear defect in nuclear export– in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	inferred from Nuclear export of mid1p was sensitive to leptomycin B (LMB), a drug that blocks the nuclear export factor crm1p (see Figure 8; Nishi et al., 1994; Kudo et al.; 1999), showing that the nuclear export of mid1p is crm1 dependent.
PMID:10930468	no NLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter (
PMID:10930468	*******during interphase**********noNLS*-mid1p was detectable in the nucleus when expressedunder the control of mid1 promoter (
PMID:10930468	localized in an identical manner to wild-type mid1p (Figure 9A) and was fully functional (Figure 7 and Table 2).
PMID:10930468	DNES1-mid1p had a clear defect in nuclear export– in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	diffuse cytoplsmic throughout the cell cycle
PMID:10930468	diffuse cytoplsmic throughout the cell cycle
PMID:10930468	Cells carrying pREP41Xmid1 exhibited a striking phenotype: they formed bulges near the cell center (Figure 1B). Medial bulges were exhibited in 40% of the cells 20 h after removal of thiamine (Figure 1C middle). Cells were longer than normal, suggestive of a cell cycle delay in interphase (Figure 1B)
PMID:10930468	and the generation time of the population was increased approximately two-fold (Figure 1C top).
PMID:10930468	No defects in nuclear positioning were apparent, as nuclei were positioned properly at the middle of the cell or in the bulge region (see Figure 2). Mid1p localization in these
PMID:10930468	DNES1-mid1p had a clear defect in nuclear export– in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	DNES1-mid1p had a clear defect in nuclear export– in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	DNES2-mid1p had a weaker, but demonstrable nuclear export defect: it retained some weak cortical staining and weak rings in addition to nuclear staining (Figure 6C), but
PMID:10930468	DNES1-mid1p had a clear defect in nuclear export– in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	DNES2-mid1p had a weaker, but demonstrable nuclear export defect: it retained some weak cortical staining and weak rings in addition to nuclear staining (Figure 6C), but
PMID:10950958	􏰇ppb1 (􏰇CN in Fig. 2) mutant. As expected, no double mutant was obtained, indicating that its3 mutation and calcineurin deletion was synthetically lethal.
PMID:10950958	In addition, its3-1 mutant had a septation index approximately twice that seen in wild-type cells at the permissive temperature.
PMID:10950958	Micro- scopic observation revealed that some mutant cells have a thick septum that was brightly stained with Calcofluor and was hardly seen in wild-type cells (Fig. 8A).
PMID:10950958	GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A).
PMID:10950958	As shown in Fig. 9B, the GFP-Its3-1 mutant protein (GFP-mIts3) was no longer localized to the plasma membrane and instead...
PMID:10950958	On the other hand, in the its3-1 mutant cells, actin patches were partially polarized at 27 °C, and the polarization was completely lost upon temperature upshift or FK506 treatment (Fig. 7A).
PMID:10950958	In wild-type cells, a shift from 27 to 33 °C caused a transient heat-induced disorganization of actin patches,
PMID:10950958	NOT PM
PMID:10950958	nterestingly, the level of PI(4)P was significantly higher than that of the wild-type cells.
PMID:10950958	NOT PLASMA MEMBRANE As shown in Fig. 5B, its3-1 mutant cells contained about 10% of the amount of PI(4,5)P2 found in wild- type cells, indicating that the mutation caused a significant decrease in PI(4)P5K activity of Its3.
PMID:10950958	Tetrad analysis of the heterozygous diploid showed two viable (Ura􏰄) and two inviable spores (Fig. 3D), indicating that the its3􏰀 gene is essential for cell growth.
PMID:10950958	􏰇ppb1 (􏰇CN in Fig. 2) mutant. As expected, no double mutant was obtained, indicating that its3 mutation and calcineurin deletion was synthetically lethal.
PMID:10950958	Purified GST fusion pro- teins were subjected to in vitro kinase reaction as described under “Experimental Procedures.” Fig. 6 shows that mutant Its3 tagged with GST had detectable but reduced PI(4)5K ac- tivity compared with the wild-type.
PMID:10950958	PI(4)5K ac- tivity kinase*********As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A).
PMID:10954610	transcription run-on assay
PMID:10954610	steady-state labeling assay; stability increases in wt but not sty1delta upon UV exposure
PMID:10954610	steady-state labeling assay; stability increases in wt but not mutant upon UV exposure
PMID:10954610	transcription run-on assay
PMID:10970777	there is another unknown gene with this activity
PMID:10970777	decreased
PMID:10978278	beta tubulin specific pathway
PMID:11007487	Fig 3B
PMID:11007487	Fig 3 H (methanol fixation)
PMID:11007487	Fig 3D
PMID:11007487	Fig 3F (methanol fixation)
PMID:11007487	Figures 4C and 4G
PMID:11007487	Fig 6 (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid
PMID:11007487	Fig 3 (methanol fixation)
PMID:11007487	Fig 3 C
PMID:11007487	Fig 1 tip1 expressed from pREP3X
PMID:11007487	Fig 1 tip1 expressed from pREP3X
PMID:11007487	Fig 1 tip1 expressed from pREP3X
PMID:11007487	Fig 1 tip1 expressed from pREP3X. I've used this term as it is the nearest to schmoozing which is the term they use in the paper. To be honest I think tapered is better as they don't know that the cells are shmooing
PMID:11007487	data not shown
PMID:11007487	"""These phenotypes establish that tip1p is required to properly position the growth zones at the antipodes of the cells."""
PMID:11007487	Fig 6 (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid
PMID:11007487	(Figure 4I)
PMID:11007487	(Figure 4I) I'm not sure if we knew it was the plus end then, but we do now ;)
PMID:11007487	( data for these cells not shown)
PMID:11007487	Fig 3 K (methanol fixation)
PMID:11007487	Fig 3 K (methanol fixation)
PMID:11007487	Fig3I
PMID:11007487	Fig 3I (Formaldehyde fixation)
PMID:11007487	Fig 4A & fig 3 G
PMID:11007487	Fig 4F However, tip1p was observed at the tips of the astral microtubules that ema- nated from the cytoplasmic face of the nuclear-located spindle pole body during anaphase and at the tips of the microtubules generated from the central region of postmitotic cells (Figures 4F).
PMID:11007487	Fig 4
PMID:11007487	figure 4H in vitro
PMID:11007487	"""We conclude that tip1p is required for the correct organization of the microtubule cytoskeleton and for the proper localization of the tea1p marker to the cell ends"""
PMID:11007487	Fig 1 B
PMID:11014802	maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.
PMID:11014802	maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.
PMID:11017199	structure
PMID:11018050	Fig 8 and Fig 5 Tea2 is not completely delocalised but is has a more extended distribution along the microtubules
PMID:11018050	Fig 2B
PMID:11018050	Fig 3
PMID:11018050	Fig 2D
PMID:11018050	Data was not shown.
PMID:11018050	Fig 4
PMID:11018050	Fig 2
PMID:11018050	forms microcolonies
PMID:11018050	Fig 2G
PMID:11018050	Fig 5
PMID:11018050	Fig 5
PMID:11018050	Fig 6 cell tip localisation increased compared to exponentially growing cells
PMID:11018050	Fig 8 (vw: I made this 'along micriotubule because we know its microtubule dept)
PMID:11018050	Fig 6
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media.
PMID:11018050	fig 8 c
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media
PMID:11018050	growth assayed on agar plates at different temperature and media.
PMID:11018050	growth assayed on agar plates at different temperature and media.
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	higher temp, restrictive for spp2-9 alone
PMID:11027257	mixed population
PMID:11027257	mixed population
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	higher temp, restrictive for spp2-9 alone
PMID:11027257	higher temp, restrictive for spp2-9 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	higher temp, restrictive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	temp semi-permissive for spp2-8 alone
PMID:11027257	higher temp, restrictive for spp2-8 alone
PMID:11027257	temp semi-permissive for spp2-9 alone
PMID:11027257	higher temp, restrictive for spp2-8 alone
PMID:11027263	same as hsk1-1312 alone
PMID:11027263	temp. restrictive for hsk1-1312 alone; fudged a bit because assayed at 32
PMID:11069657	they form parts that fail to mature
PMID:11069779	**SYNTHETIC LETHAL
PMID:11069779	toxic aa-analog
PMID:11071923	global translation, not a specific gene
PMID:11076964	dependent on F-actin (assayed using Latrunculin A)
PMID:11080156	SAC- fypo/issues/2310
PMID:11080156	with cut at second division
PMID:11080156	with cut
PMID:11080156	after passage through G1
PMID:11084332	during G1 arrest fig4 C right hand panel
PMID:11084332	total ubiquitinated
PMID:11084332	during anaphase
PMID:11084332	ubiquitinated
PMID:11084332	ubiquitinated
PMID:11084332	total protein in proteasome mutant
PMID:11084332	total protein in proteasome mutant
PMID:11084332	during G1 arrest fig4 C right hand panel
PMID:11084332	delayed during anaphase
PMID:11102508	WT 0.5%
PMID:11134033	Fig. 2
PMID:11134033	(data not shown)
PMID:11134033	figure 1 a
PMID:11134033	figure 1 b
PMID:11134033	figure 1 b
PMID:11134033	figure 1 b (I)
PMID:11134033	figure 1 b (I)
PMID:11134033	figure 1 C
PMID:11134033	indicated by decreased polysome to monosome ratio
PMID:11160827	present throughout mitotic cell cycle
PMID:11179424	residue not determined experimentally, but probably Y173
PMID:11226171	sequencing
PMID:11226171	same sensitivity as rhp54delta alone
PMID:11226171	sequencing
PMID:11226171	same sensitivity as rhp54delta alone
PMID:11231017	fig1
PMID:11231017	fig1
PMID:11231572	dependent on F-actin (assayed using Latrunculin A)
PMID:11231572	dependent on F-actin (assayed using Latrunculin A)
PMID:11238401	maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.
PMID:11238401	maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.
PMID:11250892	fig 7
PMID:11250892	figure 3
PMID:11250892	Figure 1 C
PMID:11250892	Fig 1
PMID:11252721	facs and author comment about growth
PMID:11260263	Fig 2 B
PMID:11260263	0.75 M
PMID:11260263	0.75 M
PMID:11260263	Fig 2 B
PMID:11279037	taf73 does not substitute for taf5
PMID:11290708	qualifier=predominantly
PMID:11294895	localization requires F-actin (assayed using latrunculin A)
PMID:11294895	localization requires F-actin (assayed using latrunculin A)
PMID:11294895	localization requires F-actin (assayed using latrunculin A)
PMID:11294907	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11294907	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11294907	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11294907	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11313455	chromatin fractionation assay; increased during response to DNA damage by MMS or ionizing radiation; dissociates during response to HU
PMID:11313455	chromatin fractionation assay
PMID:11313455	chromatin fractionation assay
PMID:11313465	Rad3 phosphorylates T11 in response to hydroxyurea treatment
PMID:11313465	phosphorylates Cds1
PMID:11313465	cellular response to hydroxyurea
PMID:11331883	Fig. 2c and Table 1),
PMID:11331883	Consistently, Rec8 localization was indistinguishable from wildtype from early meiosis and until metaphase I (Fig. 3). Rec8 first appeared in the centromeric regions of cells before conjugation (Fig. 3, G1 cells) and its distribution was further extended throughout chromatin during the horse-tail stage and until metaphase I. Therefore, Rec8 is properly localized and co-orientation still occurs in the absence of Bub1, indicating that the occurrence of equational segregation in Dbub1 cells may be due to a defect in functional fusion of sister kinetochores rather than to defective co-orientation of sister centromeres.
PMID:11331883	table1 Together, these results rule out the possibility that equational segregation in the absence of Bub1 is due to loss of sister-chromatid cohesion before attachment of kinetochores to microtubules.
PMID:11331883	The most straightforward interpretation is that Bub1 is required to maintain sister-chromatid cohesion at anaphase I by preventing the removal of Rec8 from centromeric regions.
PMID:11331883	table1
PMID:11331883	table1 Interestingly, sister chromatids do not segregate randomly in the absence of Rec8 but rather segregate equationally10 (Table 1), implying that cohesion must be preserved between sister centromeres to give them a mitotic-like, back-to-back orientation
PMID:11331883	In contrast, Rec8 disappeared completely in Dbub1 anaphase I cells. Rec8 was not observed in any of the >100 late-anaphase cells examined and was obviously never detected in early MII cells
PMID:11331883	In contrast, Rec8 disappeared completely in Dbub1 anaphase I cells. Rec8 was not observed in any of the >100 late-anaphase cells examined and was obviously never detected in early MII cells
PMID:11350031	all taf1 introns affected
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359920	30 degrees
PMID:11359928	Figure 4A
PMID:11359928	Figure 4A
PMID:11359928	fig 2 c
PMID:11359928	fig 8
PMID:11359928	fig 2 c
PMID:11359928	fig 3a
PMID:11369198	data not shown
PMID:11369198	fig 2B
PMID:11369198	fig 2 B
PMID:11369198	Figure 5b
PMID:11369198	movie 1A
PMID:11369198	Figure 5b
PMID:11369198	Figure 5b
PMID:11384993	a significant reduction in kinase activity (􏰑40% of Sid1)
PMID:11384993	barely above background for vector alone and Sid1C (Fig. 2B)
PMID:11387218	punctate in wild type, diffuse throughout nucleus in mutant
PMID:11405625	high penetrance = large fraction of cells
PMID:11432827	1A
PMID:11432827	3f
PMID:11432827	Fig 3B
PMID:11432827	Figure 3A, rapid loss of viability
PMID:11432827	Table 1
PMID:11432827	Figure 1 C
PMID:11432827	Figure 1 C
PMID:11432827	Figure 1 C
PMID:11432827	Figure 1 A
PMID:11432827	Figure 1 A
PMID:11432827	dependent on mitotic spindle (GO:0072686)
PMID:11432827	cut2 levels were reduced in alp14 mutant
PMID:11432827	Question could be required for, or upstream spindle checkpoint, but it could cause a problem which preceds the point where it is possible to activate the checkpoint?BUT...alp14 and mad2 in same pathway and overexpression of mad2 cannot resuce defect of double/single mutant
PMID:11432827	figure 4B
PMID:11432827	figure 4A
PMID:11432827	ind mad2 mutant loses viability
PMID:11432827	2C
PMID:11432827	2C
PMID:11432827	1A
PMID:11448769	(vw: sid2 phenotype indicates that Clp1 localization is independent of SIN)
PMID:11493649	positive regulation of meiotic cell cycle exit
PMID:11493649	negative regulation of meiotic exit
PMID:11514435	fig 6
PMID:11514435	fig 6
PMID:11514435	Figure 5
PMID:11514435	Figure 4D, lane 3
PMID:11514435	figure 1 Figure 3B and Table 2
PMID:11514435	figure 2a
PMID:11514435	from MF
PMID:11514435	figure 1 & Figure 3B and Table 2
PMID:11514435	figure 7b
PMID:11514435	figure 2a
PMID:11514435	Figure 5 E
PMID:11514435	Figure 5D
PMID:11514435	Figure 5 E to membrane
PMID:11514435	figure 1
PMID:11514435	(Figure 7b) heterologous complementation
PMID:11514435	(Figure 7D) assayed reaction products
PMID:11514435	from MF
PMID:11514435	figure 2a
PMID:11514435	figure 7b
PMID:11514435	Figure 4D, lane 3 + figure 5
PMID:11514436	figure 3biv
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	table 2, par1/2 does not supress sin phenotype
PMID:11514436	figure 3biv
PMID:11514436	figure 3a
PMID:11514436	figure 3a
PMID:11514436	figure 3a
PMID:11514436	figure 2b
PMID:11514436	(Figure 1C, lane 8
PMID:11514436	SID PHENOTYPE (Figure 2B).
PMID:11514436	(Figure 2A).
PMID:11514436	asymetric localization is normal
PMID:11514436	figure 4a
PMID:11514436	figure 4a
PMID:11514436	dns
PMID:11514436	Thefact that out of almost 200 tetrads analyzed, not a single ura spore survived confirmed that spg1 is essential for vegetative growth, and this essential function cannot be bypassed by inactivating par1 and par2 by deletion.
PMID:11532929	cdc25-22 background
PMID:11532929	cdc25-22 background
PMID:11532929	cdc25-22 background
PMID:11553781	Rad3 phosphorylates S345 in response to DNA damage caused by ionizing radiation
PMID:11553781	vw: changed from response to chemical to part of DNA damage checkpoint signalling
PMID:11554922	evidence: immunoblot using antibody that recognizes thymine dimers
PMID:11598020	fig 4a
PMID:11598020	fig 4a
PMID:11598020	fig 4a
PMID:11598020	fig 4a
PMID:11598020	fig 4a
PMID:11600706	fig 2B
PMID:11600706	(vw: in vitro purification system)
PMID:11600706	(vw: in vitro purification system)
PMID:11600706	(vw: in vitro purification system)
PMID:11600706	fig 2B
PMID:11600706	Figure 3B
PMID:11600706	figure 1C
PMID:11600706	figure 1C
PMID:11606752	level of mutant cdc18deltaCDK1-5 protein
PMID:1165770	Table 1
PMID:1165770	Table 1, Figure 2
PMID:1165770	cdc9-50 is the original name for wee1-50 allele. It was changed in subsequent publications to wee1 because of its phenotype and there is now no cdc9 gene
PMID:1165770	Table 1
PMID:1165770	Table 1
PMID:1165770	Figure 3
PMID:11676915	figure 3 b
PMID:11676915	fig 1 a
PMID:11676915	fig 1 a
PMID:11676915	fig 1 a
PMID:11676915	figure 6
PMID:11676915	figure 6
PMID:11676915	figure 6
PMID:11676915	figure 6
PMID:11676915	figure 6
PMID:11676915	figure 6
PMID:11676915	figure 6
PMID:11676915	scaffold, platform
PMID:11676915	scaffold, platform
PMID:11676915	dns
PMID:11676915	fig 5c
PMID:11676915	scaffold, platform
PMID:11676915	fig 5a
PMID:11676915	figure 3 b
PMID:11676915	figure 6
PMID:11676915	scaffold, platform
PMID:11676924	colocalizes with this region and taz1, abnormal localization in taz1-delta, and physically associates with taz1
PMID:11676924	qualifier=same_pathway
PMID:11683390	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	Fig 6 Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not degraded by defective proteasome. Rpt1 is called Mts2 in this paper
PMID:11683390	Fig 6 Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not recognised by defective APC
PMID:11683390	Fig 6 Cdc2YFP and non-degradable Cdc13YFP remain associated with spindle, SPB.Cdc13 degradation is abolished rather than delayed
PMID:11683390	Fig 6
PMID:11683390	Figure 4A. Cdc13YFP expressed from integrated pREP45. Decreased nuclear import of cdc2YFP compared to cdc13delta cig1delta mutant
PMID:11683390	Figure 4B. Cdc13YFP expressed from integrated pREP45
PMID:11683390	Data not shown. Cdc2 does not go prematurely to the SPB in a cut12 mutant (this is the stf1-1 mutant)
PMID:11683390	Figure 4A. Cdc13YFP expressed from integrated pREP45.
PMID:11683390	Figure 4A. Cdc13YFP expressed from integrated pREP45
PMID:11683390	Figure 4A
PMID:11683390	Fig 2C, pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A, Fig3 Fig5D pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A, Fig3 Fig5D pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A, Fig 3, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A, Fig 3, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 7 do not actually say it is associated with SPB just SPB region, i.e. telomere-SPB- centromere bouquet cluster
PMID:11683390	Fig2A, B pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	cdc2 is localised at the centromeres during horse tail movement. Fig 9 shows that cdc2YFP is associated with cen1GFP
PMID:11683390	Fig 8
PMID:11683390	Fig 7
PMID:11683390	Fig 7
PMID:11683390	Fig 7
PMID:11683390	Fig2A, B pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B, Fig 4C, pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	Fig2A, B pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	Fig2A, B pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11685532	mitotic, in meiosis it is only n the kinetochore during meitoic division(metaphase/anaphase) not during prophase
PMID:11694585	various abnormal shapes
PMID:11694585	30 degrees C
PMID:11694585	27 degrees C
PMID:11694585	27 degrees C
PMID:11694585	30 degrees C
PMID:11694585	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11694585	in vitro bundling, detected by microscopy; Figure 2
PMID:11694585	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11694585	assayed using purified rabbit skeletal muscle F-actin
PMID:11694585	temperature permissive for cdc4-8
PMID:11694585	temperature restrictive for cdc4-8
PMID:11694585	27 degrees C
PMID:11694585	various abnormal shapes
PMID:11696322	table1
PMID:11696322	figure 3b-g
PMID:11696322	figure 5a
PMID:11696322	table1
PMID:11696322	Figure 4, table1
PMID:11696322	Figure 3fg
PMID:11696322	figure 3
PMID:11696322	data not shown
PMID:11696322	Figure 3fg
PMID:11696322	igure 3b–g,i)
PMID:11696322	figure 3b–g,i)
PMID:11696322	figure 5e
PMID:11696322	figure 5bc
PMID:11717425	filter binding assay
PMID:11719193	magneisum activated_by(CHEBI:18420)
PMID:11737264	population is viable but sick; can't tell which individual cells are viable, but very small cells look lysed
PMID:11737264	population is viable but sick, and the elongated multiseptate cells are probably dead
PMID:11737264	population is viable, but very small cells look lysed
PMID:11737264	population is viable but sick; can't tell which individual cells are viable
PMID:11737264	population grows well, but very small cells look lysed
PMID:11737264	population is viable but sick; can't tell which individual cells are viable
PMID:11739790	Figure 2 and Table 2
PMID:11739790	Figure 4, B&D
PMID:11739790	Figure 4, B&D
PMID:11739790	arrested
PMID:11739790	arrested
PMID:11739790	arrested
PMID:11777938	NORMAL LENGTH
PMID:11777938	figure 2
PMID:11781565	Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	Fig2B
PMID:11781565	Fig2B
PMID:11781565	Fig2B
PMID:11781565	Fig3A
PMID:11781565	Fig 5 res1-S130A can rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	Fig3B
PMID:11781565	Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	FIg4E
PMID:11781565	Fig1B
PMID:11781565	Fig6
PMID:11781565	Fig2B
PMID:11781565	Fig2B
PMID:11781565	Fig2B
PMID:11781565	Fig1C 5 fold increase in HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	Fig1C no increase in presence of HU compared to no HU when all MCB elements are removed. res1 and lacZ fusion on episomal plasmids
PMID:11781565	Fig1C Shows 5 fold increase in presence of HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	Fig5 res1+ is unable to rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	Data not shown 20 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids
PMID:11781565	data not shown 8 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids
PMID:11781565	Fig1B
PMID:11781565	Fig1B
PMID:11781565	Fig1B
PMID:11781565	Fig1B
PMID:11781565	Fig1B
PMID:11781565	Fig1B
PMID:11781565	Fig1B
PMID:11781565	Fig3B
PMID:11781565	Fig4D
PMID:11781565	Fig4D
PMID:11781565	Fig4D
PMID:11792803	fig8
PMID:11792803	figure 2 b
PMID:11792803	figure 2 b chromsome detached from spindle
PMID:11792803	fig8
PMID:11792803	fig6
PMID:11792803	fig6
PMID:11792803	fig6
PMID:11792803	fig8
PMID:11792803	figure 2 b
PMID:11792803	figure 2 a ( stretched chromaitn along elongating spindle at anaphase B)
PMID:11792803	figure 2 b
PMID:11818066	Rad24 sequesters phosphorylated Mei2, preventing Mei2 binding to meiRNA (sme2)
PMID:11818066	not really sure freq is normal, because wt not shown, but text suggests it's close
PMID:11818066	does not undergo meiosis under conditions where pat1-114 single mutant does
PMID:11854402	during premeiotic DNA replication
PMID:11854402	during premeiotic DNA replication
PMID:11854402	during premeiotic DNA replication
PMID:11854402	during premeiotic DNA replication
PMID:11854402	during premeiotic DNA replication
PMID:11854409	Figure 5B
PMID:11854409	fig 1A inviable
PMID:11854409	fig 2, 3
PMID:11854409	Figure 5A
PMID:11854409	Figure 5C
PMID:11854409	UPR
PMID:11854409	UPR
PMID:11854409	UPR
PMID:11854409	fig 2, 3
PMID:11861551	fig 7
PMID:11861551	fig 1a
PMID:11861551	fig 1
PMID:11861551	fig 1a
PMID:11861551	fig 3
PMID:11861551	fig 3
PMID:11861551	4c
PMID:11861551	4
PMID:11861551	igure 7
PMID:11861551	igure 7
PMID:11861551	fig 7a
PMID:11861551	fig 7a
PMID:11861551	4
PMID:11861551	4
PMID:11861765	fig 4B
PMID:11861765	fig 8C
PMID:11861765	fig 3B
PMID:11861765	fig 3A
PMID:11861765	fig 2 B
PMID:11861765	fig 2 B
PMID:11861765	fig 2 B
PMID:11861765	fig 2 A
PMID:11861765	fig 2
PMID:11861765	fig 3C
PMID:11861765	fig 1
PMID:11861765	fig 3C
PMID:11861765	fig 3C
PMID:11861765	fig 3D
PMID:11861765	fig 4A
PMID:11861765	fig 5A
PMID:11861765	fig 5B
PMID:11861765	fig 7B
PMID:11861765	fig 7C
PMID:11861765	fig 8A
PMID:11861765	fig 8B
PMID:11861765	fig 8B
PMID:11861765	fig 3C
PMID:11861765	fig 8C
PMID:11861765	fig 3D
PMID:11861765	fig 4B,C
PMID:11861765	fig 4 D
PMID:11861765	fig 4 D
PMID:11861765	fig 4B,C
PMID:11861905	The 210-nt region resides downstream of the distal poly(A) site and it is not included in the mature rrg1+ mRNA, in contrast to other regulatory elements for post-transcriptional control. However, some recent studies on S.pombe have shown that RNA pol II transcription proceeds beyond the poly(A) site and that the downstream sequences located in the 3′ noncoding region are responsible for transcription termination and mRNA 3′-end formation, which are closely coupled to efficient gene expression
PMID:11861905	figure 1a
PMID:11861905	figure 1a
PMID:11870212	Fig. 3B
PMID:11870212	Fig. 3B
PMID:11870212	Fig. 3B
PMID:11870212	movement in anap[hase A
PMID:11870212	Fig. 3B
PMID:11870212	Fig. 3B
PMID:11870212	Fig. 3B
PMID:11882285	fig 1 (3-4um normal metaphese lenght 2-2.5 um
PMID:11882285	fig 5a ie wt like
PMID:11882285	fig 5a
PMID:11882285	S1
PMID:11882285	S1
PMID:11882285	S1
PMID:11882285	S1
PMID:11882285	figure 3
PMID:11882285	fig 2D
PMID:11882285	fig 2D
PMID:11882285	fig4
PMID:11882285	fig 1C
PMID:11882285	fig 1
PMID:11882285	fig 1
PMID:11882285	fig 1
PMID:11882285	fig 1
PMID:11884512	data not shown
PMID:11884512	same as rad17 single mutant, epistatic
PMID:11884512	Of the inhibitors we tested, only iodoacetamide (10 mM) and NEM (10 mM) inhibited Ulp1 activity
PMID:11884512	NEM, which inhibit the Pmt3-processing activity of Ulp1, and the serine protease inhibitor PMSF, have no effect on Pmt3 deconjugating activity
PMID:11884512	3B
PMID:11884512	Figure 3 C
PMID:11884512	data not shown
PMID:11884604	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	not (coincident_with(SO:0001789) | coincident_with(SO:0001795))
PMID:11884604	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	actually inferred from combination of phenotype and sequence similarity
PMID:11884604	actually inferred from combination of phenotype and sequence similarity
PMID:11884604	not much evidence of specificity for H3 vs. H4 or position
PMID:11886869	storage
PMID:11907273	2-hybrid
PMID:11907273	using chromosome III
PMID:11909965	2B
PMID:11909965	2B
PMID:11909965	Fig 2A
PMID:11909965	2B
PMID:11909965	2B
PMID:11909965	figure2C
PMID:11909965	figure2C
PMID:11909965	figure 3a cell cycle arrest in mitotic metaphase
PMID:11909965	figure 5A
PMID:11909965	figure 3a cell cycle arrest in mitotic ametaphase
PMID:11909965	figure 3a DECREASDED cell cycle arrest in mitotic anaphase
PMID:11909965	figure 5
PMID:11927555	Double mutants between ®n1D and the temperature-sensitive allele rad21-K1 (Tatebayashi et al., 1998) were synthetically lethal at all temperatures
PMID:11927555	Figure 5
PMID:11927555	Figure 5
PMID:11927555	Figure 6
PMID:11927555	fig 6 resulted in a synthetic arrest at metaphase of mitosis. This contrasts with the G1 cell cycle arrest of pim1-d1 single mutant cells (Krien et al., 1998).
PMID:11927555	fig6
PMID:11927555	Figure 6
PMID:11927555	Figure 6
PMID:11927555	suggesting the lethal synthetic interaction between ®n1D and cut11 might relate of the nuclear envelope rather than SPB anchoring during mitosis
PMID:11927555	Figure 6 which was enhanced by the presence of the pim1-d1 mutation at 36°C to include all mitotic cells (arrowed
PMID:11927555	fig6
PMID:11927555	fig6
PMID:11927555	fig6
PMID:11927555	These data show that Fin1p- mediated compaction of the chromosomes is not func- tionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	These data show that Fin1p- mediated compaction of the chromosomes is not func- tionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	These data show that Fin1p- mediated compaction of the chromosomes is not func- tionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	These data show that Fin1p- mediated compaction of the chromosomes is not func- tionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	Figure 5
PMID:11927555	(in. non mitotic cells)
PMID:11927555	The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A).
PMID:11927555	The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A).
PMID:11950879	"indicated by ""majority of the Mad2-GFP was localized to the spindle"""
PMID:11950879	"indicated by ""majority of the Mad2-GFP was localized to the spindle"""
PMID:11950879	(vw: nda3 tubulin mutant does not assemble spindle and shows Mad2 is localized to unattached kinetochores)
PMID:11950879	"indicated by ""majority of the Mad2-GFP was localized to the spindle"""
PMID:11950884	Fig6B All three mutants were able to detect and respond to pheromone by arresting in G1, as shown by FACS analysis (Fig. 6B),
PMID:11950884	Fig5 Table 4
PMID:11950884	Fig1
PMID:11950884	Fig6C
PMID:11950884	Fig8D,E pom1 has a role in the relocalisation of actin to the shmooing cell tip
PMID:11950884	Fig6C
PMID:11950884	Fig5 Table 3,4
PMID:11950884	Fig 5, Table 3,4
PMID:11950884	Fig6C
PMID:11950884	location is abolished during mating Fig4Dc and Fig4Ec
PMID:11950884	FIg 4 F location alkso exists during mating
PMID:11950884	Fig6A
PMID:11950884	Fig6A
PMID:11950884	Fig2A
PMID:11950884	Fig2A
PMID:11950884	Fig2A
PMID:11950884	Fig6A
PMID:11950884	After pheromone addition, Tea1GFP became mostly lost from the growing end and was redistributed along the cell periphery at the nongrowing larger end (Fig. 3E). After pheromone addition, Tea2GFP and Tip1YFP were also reduced at the growing end, accumulating at the non-growing end and in the cytoplasm, often as dots in a row (Fig. 3E). The same relocalisation was observed for Tea2GFP during an h90 mating. In conjugating cells, Tea2GFP was found to localise to the nongrowing ends with some dots in the..
PMID:11950884	After pheromone addition, Tea1GFP became mostly lost from the growing end and was redistributed along the cell periphery at the nongrowing larger end (Fig. 3E). After pheromone addition, Tea2GFP and Tip1YFP were also reduced at the growing end, accumulating at the non-growing end and in the cytoplasm, often as dots in a row (Fig. 3E). The same relocalisation was observed for Tea2GFP during an h90 mating. In conjugating cells, Tea2GFP was found to localise to the nongrowing ends with some dots in the..
PMID:11950884	After pheromone addition, Tea1GFP became mostly lost from the growing end and was redistributed along the cell periphery at the nongrowing larger end (Fig. 3E). After pheromone addition, Tea2GFP and Tip1YFP were also reduced at the growing end, accumulating at the non-growing end and in the cytoplasm, often as dots in a row (Fig. 3E). The same relocalisation was observed for Tea2GFP during an h90 mating. In conjugating cells, Tea2GFP was found to localise to the nongrowing ends with some dots in the..
PMID:11950884	regulation of
PMID:11950884	Fig6B
PMID:11950884	Fig6B
PMID:11950927	fig4
PMID:11950927	Pic1– 765-924, which lacks the IN box, failed to bind Ark1p,
PMID:11950927	Figure 6A)
PMID:11950927	Figure 6A)
PMID:11950927	dominent negative effect
PMID:11950927	dominent negative effect
PMID:11950927	dominent negative effect
PMID:11950927	fig 3c
PMID:11950927	fig 3c
PMID:11950927	Figure2
PMID:11950927	Figure 1C
PMID:11952833	even though cdc13 is present
PMID:11952833	even though cdc13 is present
PMID:11952833	premature SIN
PMID:11955632	tRNA
PMID:11967147	Fig 1D
PMID:11967147	fig2b
PMID:11967147	figure S1
PMID:11967147	figure S1
PMID:11967147	fig 5A
PMID:11967147	fig 5A
PMID:11967147	fig 5A
PMID:11967147	Figure 5B
PMID:11967147	Figure 5B
PMID:11967147	Figure 5B
PMID:11967147	Figure 5B
PMID:11967147	Figure 5B
PMID:11967147	Figure 5D
PMID:11967147	Figure 5D
PMID:11967147	Figure 5D
PMID:11967147	Figure 5D abolished pausing
PMID:11967147	fig2d
PMID:11967147	fig2a
PMID:11967147	fig2a
PMID:11967147	fig2b
PMID:11967147	Fig 1D
PMID:11967147	fig2d
PMID:11967147	DNS
PMID:11967147	DNs
PMID:11967147	Fig 1C
PMID:11967147	Fig 1A
PMID:11967147	Fig 1A
PMID:11967147	Fig 1A
PMID:11967147	Fig 1A
PMID:11967147	figure S1 (20% longer)
PMID:11967147	figure S1 (20% longer)
PMID:11967147	figure S1
PMID:11967147	figure S1 (20% longer)
PMID:11972332	Figure 1A
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:12000964	(vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	(vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	(vw: delayed)
PMID:12000964	(vw: DNA checkpoint dept)
PMID:12006645	tetrads only
PMID:12006658	assayed by incorporation of labeled methionine
PMID:12006658	assayed by incorporation of labeled methionine
PMID:12006658	taking authors' word that ribosome profiling phenotype is specific enough to infer role in translation initiation
PMID:12006658	"can't capture punctate cytoplasmic localization during heat or osmotic stress, because there isn't a suitable GO CC term, and they wouldn't add something as vague as ""cytoplasmic focus"""
PMID:12006658	polysome profiling
PMID:12007420	Fig4A
PMID:12007420	Fig1D
PMID:12007420	Fig1 C
PMID:12007420	Fig3B
PMID:12007420	Fig3B
PMID:12007420	Fig3B
PMID:12007420	Fig3B
PMID:12007420	Fig3B
PMID:12007420	Fig4D (jvh: tea3 does not affect polarity and the elongated cells do not branch. This is different to pom1 where cdc11-119 cells form branches)
PMID:12007420	Fig4B
PMID:12007420	Fig4C
PMID:12007420	Fig3B
PMID:12007420	Fig 3D
PMID:12007420	Fig3C
PMID:12007420	Fig2D (jvh: tea3GFP staining cell middle after nda3 block and release)
PMID:12007420	Fig2D (jvh: no tea3GFP staining cell middle in nda3 block)
PMID:12007420	Fig2A
PMID:12007420	localisation of tea3 is a late event in septation
PMID:12007420	localises at both ends, slightly enriched at non growing end
PMID:12007420	Fig1D
PMID:12007420	Fig1 C
PMID:12007420	Fig1B
PMID:12007420	Fig1
PMID:12019258	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: same as rqh1delta alone)
PMID:12023299	(mah: slighly more severe than rad50delta alone)
PMID:12023299	(mah: sensitivity depends on how highly overexpressed top3+ is; more top3+ -> lower sensitivity)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: localization to DSB sites also contributes to inference)
PMID:12023299	(mah: assayed substrate: exogenous histone H1)
PMID:12023299	(mah: residue=T215)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12023299	(mah: same as rad51delta alone)
PMID:12034771	Fig6
PMID:12034771	used endogenous tea2 gene tagged at C term with GFP. Fig1A
PMID:12034771	used endogenous tea1 gene tagged at C term with YFP and tubulin CFP for live cell imaging of tea1 on microtubules Fig1C
PMID:12034771	used endogenous tea2 gene tagged at C term with GFP. Fig1A
PMID:12034771	Figure 2A
PMID:12034771	Fig2C OUTSTANDING Q IS IT ALONG OR ON?
PMID:12034771	Fig3C
PMID:12034771	Fig3C
PMID:12034771	Fig3C
PMID:12034771	Fig6
PMID:12034771	Fig6
PMID:12034771	Fig5B
PMID:12034771	Fig5B
PMID:12034771	Fig3C
PMID:12034771	Fig3C
PMID:12034771	Fig4A
PMID:12034771	Fig4B. I know that the protein is localising to the plus end but they did not say this in this paper although they do say it is on the tips of polymerizing microtubules so it could be FYPO 0004731
PMID:12034771	Fig4B
PMID:12034771	Fig3C, Fig5A STILL TO ADD curved around cell end during mitotic interphase
PMID:12034771	Fig5A
PMID:12034771	Fig5A
PMID:12034771	Fig5B
PMID:12058079	activated_by(CHEBI:18420)
PMID:12062100	longer transcript
PMID:12062100	longer transcript
PMID:12062100	longer transcript
PMID:12065422	25 degrees figure 7
PMID:12065422	25 degrees figure 7
PMID:12065422	Introduction of either ®n1.ts1 or ®n1.D to a cut12.s11 cdc25.22 mutant background abolished the growth of cdc25.22 above 30°C that had been conferred by the cut12.s11 mutation (Figure 6C).
PMID:12065422	Figures 1C and 2C
PMID:12065422	Figure 2B and C
PMID:12065422	DNS
PMID:12065422	Table II
PMID:12065422	Table II
PMID:12065422	figure 5d
PMID:12065422	recessive, loss- of-function mutation
PMID:12065422	Figure 1C
PMID:12065422	25 degrees figure5d
PMID:12065422	DNS
PMID:12065422	Figure 1A. We concluded that the severe phenotype of a ®n1.ts1 mutant is a transitory response to loss of Fin1 function. This implied that ®n1.D haploids adapted to loss of Fin1 after the ®rst division of a germinating spore.
PMID:12065422	Figure 1C
PMID:12065422	recessive, loss- of-function mutation
PMID:12065422	Figure 2A; Table II
PMID:12065422	Figure 1B
PMID:12074602	binds to 54-bp element at 1186-1239
PMID:12093738	Fig5B
PMID:12093738	Fig1C
PMID:12093738	Fig1C
PMID:12093738	Fig1A
PMID:12093738	Fig 3A, D
PMID:12093738	Fig 4B cig2 over expression also occurs when cells blocked with HU
PMID:12093738	Fig2C the cdc2-cig2 and cdc2-cdc13 complexe have no tyrosine 15 phosphorylation
PMID:12093738	Fig2C the cdc2-cig2 and cdc2-cdc13 complexes have increased kinase activity
PMID:12093738	Fig1D
PMID:12093738	Fig1D The protein cdc2 protein assayed is in complex with cig2 as there is no cdc2-cdc13 complex present
PMID:12093738	fypo/issues/3165 Fig5C
PMID:12093738	Fig5C
PMID:12093738	fypo/issues/3165 Fig5B in the absence of cig2 there is a delay in the appearance of cut cells
PMID:12093738	Fig 4A cells block normally with 1C DNA content even when cig2 is over expressed
PMID:12093738	Fig1C
PMID:12093738	Fig5A lower panel used forward scatter to measure cell size
PMID:12093738	Fig5A lower panel
PMID:12093738	Fig5A used forward scatter to measure cell size small peak of short cells
PMID:12093738	Fig 3 data not shown cell viability is reduced at late time points
PMID:12093738	Fig5A small peak of less that 1C DNA content
PMID:12093738	Fig 3B no G1 peak is observed showing that S phase onset is not delayed
PMID:12093738	Fig 3C cig2 over expression from ~10hours after thiamine removal
PMID:12112233	actually accumulation
PMID:12112233	Figure 1
PMID:12112233	Figure 1
PMID:12181326	data not shown
PMID:12181336	fig 5
PMID:12181336	fig7
PMID:12181336	fig7
PMID:12181336	fig has 6
PMID:12181336	small amount
PMID:12181336	fig 5
PMID:12181336	fig 5
PMID:12181336	2 B
PMID:12181336	2 B
PMID:12181336	2B
PMID:12181336	Fig 3
PMID:12181336	Fig 3
PMID:12181336	Fig 3
PMID:12181336	Fig 3
PMID:12181336	Fig 3
PMID:12181336	Fig 4
PMID:12181336	Fig 4
PMID:12181336	Fig 4
PMID:12181336	fig 5 Consistent with previous immunolocalization studies (Gaits et al., 1998), wild-type Wis1-GFP showed solely cytoplasmic localization and little GFP signal was seen in the nuclear region (Figure 5A).
PMID:12185500	29 degrees C
PMID:12185500	25 degrees C
PMID:12185500	25 degrees C
PMID:12185500	25 degrees C
PMID:12185500	27 degrees C
PMID:12185500	29 degrees C
PMID:12185500	27 degrees C
PMID:12185500	restrictive temp 36
PMID:12185500	restrictive temp 32
PMID:12185840	Figure 2C
PMID:12185840	fig 2 C
PMID:12186944	localization requires microtubules (assayed using thiabendazole or carbendazim) but not F-actin (assayed using latrunculin A)
PMID:12186947	penetrance low if cells exposed to UV
PMID:12196391	same as either single mutant
PMID:12196391	same as rad3delta alone
PMID:12196391	same as rad3delta alone
PMID:12196391	same as rad3delta alone
PMID:12196391	same as rad3delta alone
PMID:12196391	same as rad26delta alone
PMID:12196391	same as either single mutant
PMID:12207036	Fig 6
PMID:12207036	Fig 6
PMID:12207036	Fig 6
PMID:12242222	fig 4
PMID:12242222	fig 4
PMID:12242222	fig 4 e
PMID:12242294	fig 8b
PMID:12242294	fig 1a
PMID:12242294	fig8d
PMID:12242294	fig8d
PMID:12242294	data not shown
PMID:12242294	data not shown
PMID:12242294	figure 9
PMID:12242294	fig 8b
PMID:12242294	fig 8a
PMID:12242294	fig 8a
PMID:12242294	fig 8a
PMID:12242294	fig 8a
PMID:12242294	data not shown
PMID:12242294	data not shown
PMID:12242294	fig 1a (maintenence of)
PMID:12390246	fig 4a b
PMID:12390246	Fig 6A
PMID:12390246	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	penetrance is mentioned in EXP accompanying fig 6A
PMID:12399381	figure 6A
PMID:12399381	fig 5A
PMID:12399381	fig 5A
PMID:12399381	fig 5A
PMID:12399381	fig5
PMID:12399381	fig5
PMID:12399381	fig5
PMID:12399381	figure2a
PMID:12399381	figure1
PMID:12399381	figure1 cdr phenotype
PMID:12399381	table4
PMID:12399381	figure 6 b during x phase?
PMID:12399381	semi wee
PMID:12399381	fig 5 CD
PMID:12399381	figure 5 CD
PMID:12399381	figure1
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure 4 cdr phenotype
PMID:12399381	figure1
PMID:12399381	figure1 cdr phenotype
PMID:12399381	figure 3
PMID:12399381	figure 2C/D
PMID:12399381	figure2a
PMID:12411492	same as plo1-ts35 alone
PMID:12411492	same as plo1-ts35 alone
PMID:12411492	same as plo1-ts35 alone
PMID:12419251	actually ectopic expression, throughout cell cycle
PMID:12419251	normal binding periodicity over cell cycle
PMID:12419251	actually ectopic expression, throughout cell cycle
PMID:12419251	normal binding periodicity over cell cycle
PMID:12419251	normal binding periodicity over cell cycle
PMID:12426374	(see rows 4±6 in Figure 1B)
PMID:12426374	Figure 1A and C
PMID:12426374	Figure 1B rows 4±6
PMID:12426374	figure 1 B
PMID:12426374	(vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	(vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	Figure 1A and C
PMID:12426374	(see rows 4±6 in Figure 1B)
PMID:12427731	assayed using myelin basic protein; doesn't rule out tyrosine phosphorylation
PMID:12427731	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:12427731	substrate myelin basic protein
PMID:12442907	small daughter at g1 Fig 1c The mutant produced daughter cells with an average length of 6 μm; whereas, the wild-type cells averaged 7.5 μm
PMID:12442907	fig 1b The estimated doubling time of the mutant was 110 min in a rich (YE) medium, while that of the wild-type cells was 150 min.
PMID:12442907	As shown in Fig. 2A, the rate of cell proliferation was immediately reduced after the amount of Rrg1 was increased.
PMID:12442907	(Figs. 3A and 3B).
PMID:12442907	(Figs. 3A and 3B). there were cells that initiated and completed the mitosis in a small portion (Table 1), which eventually led to cell proliferation until the stationary phase (Fig. 2A).
PMID:12442907	a considerable portion of the Rrg1-overproduced cells that undergo mitosis showed an abnormal accumulation of septum material (Figs. 3F, 3G, and 3H).
PMID:12442907	Fig 1c The mutant produced daughter cells with an average length of 6 μm; whereas, the wild-type cells averaged 7.5 μm
PMID:12442907	Table 1
PMID:12455694	32 degrees; mcl1-1 semi-permissive
PMID:12455694	32 degrees; mcl1-1 semi-permissive
PMID:12479804	Figure 4A
PMID:12479804	Figure 4A 10% (2/20) of anaphase cells displayed Dma1p-GFP SPB signal
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F)
PMID:12479804	Figures 3E and 3F
PMID:12479804	Figures 3E and 3F
PMID:12479804	Figure 3A, panel 3
PMID:12479804	Figure 3A, panel 3
PMID:12479804	(faintly) Figure 3A, panel 2, arrowhead
PMID:12479804	Figure 2D
PMID:12479804	Figure 2A, panels 11 and 14
PMID:12479804	Figure 2A, panels 11 and 14
PMID:12479804	fig 1B
PMID:12479804	The observation that Clp1p/Flp1p is required for sep- tation in dma1􏰋 mutants is consistent with a model where Dma1p inhibits SIN activation
PMID:12479804	fig 1A I'm modelling this as normal becasue nda3 is providing microtubule damage. Checkpoint would be expected to be o in WT in this scenario. cells failed to maintain the microtubule damage-induced checkpoint arrest and began to aberrantly form septa
PMID:12479804	fig 1A I'm modelling this as decreased because nda3 is providing microtubule damage. Checkpoint would be expected to be o in WT in this scenario. cells failed to maintain the microtubule damage-induced checkpoint arrest and began to aberrantly form septa
PMID:12479804	Figure 4B)
PMID:12479804	igure 4C, bottom
PMID:12479804	igure 4C, bottom
PMID:12479804	Fig4
PMID:12479804	Figure 5
PMID:12479804	Figure 5
PMID:12479804	fig 5
PMID:12479804	fig6
PMID:12479804	fig6
PMID:12479804	Figure 2
PMID:12479804	Table1
PMID:12479804	Table1
PMID:12479804	Table1
PMID:12479804	Table1
PMID:12479804	Table1
PMID:12482946	Fig. 2B
PMID:12482946	Fig. 2A
PMID:12482946	Fig. 2B
PMID:12482946	Fig. 1D
PMID:12482946	Fig. 2B
PMID:12482946	Fig. 2B
PMID:12526748	figure1e
PMID:12526748	figure1e
PMID:12526748	figure1e
PMID:12526748	figure1e
PMID:12526748	D.N.S?
PMID:12526748	D.N.S?
PMID:12526748	D.N.S?
PMID:12526748	Pst1p colocalizes with the otr/imr region in a cell cycle-specific manner.
PMID:12526748	fig3
PMID:12526748	fig3
PMID:12526748	fig3
PMID:12526748	fig3
PMID:12526748	fig3
PMID:12526748	fig3
PMID:12526748	fig3
PMID:12526748	fig1
PMID:12526748	fig1
PMID:12526748	fig1
PMID:12526748	fig1
PMID:12526748	fig1b
PMID:12526748	Figure S1
PMID:12526748	Figure S1
PMID:12526748	Figure S1
PMID:12526748	Figure S1
PMID:12526748	Figure 1C
PMID:12526748	fig3
PMID:12526748	figure1e
PMID:12546793	HYPERPHOSPHORYLATD FORM Together, these data demonstrate, first, that mitotic cdc2p activity is not required for hyperphosphorylation of cdc11p and, second, that activation of the SIN correlates with accu- mulation of hyperphosphorylated cdc11p.
PMID:12546793	SIN signalling complex
PMID:12546793	SIN signalling complex
PMID:12546793	(Figure 2B). Immunofluorescence showed that byr4p was also present on the SPB in the arrested cells
PMID:12546793	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36􏰁C .
PMID:12546793	In contrast, in cdc7-24, the hyperphosphorylated form of cdc11p (3) was greatly reduced, and the intensity of the hypophos- phorylated forms (1 and 2) increased (Figure 1E). A simi- lar result was observed in cdc7-A20 (data not shown). Furthermore, no mitotic hyperphosphorylation of cdc11p was seen in spg1-B8 at the nonpermissive temperature (Figure 1E), when cdc7p does not localize to the SPB [13]. Finally, when cdc7 was expressed ectopically in G2-arrested cells, cdc11p accumulated in the hyper- phosphorylated form (3) (Figure 1F).
PMID:12546793	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36􏰁C.
PMID:12546793	(DNS)
PMID:12546793	(Figure 1E) In contrast, in cdc7-24, the hyperphosphorylated form of cdc11p (3) was greatly reduced, and the intensity of the hypophos- phorylated forms (1 and 2) increased
PMID:12546793	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
PMID:12546793	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
PMID:12546793	HYPERPHOSPHORYLATION (Figure 1C) In the mutant plo1-ts4, which is defective in SIN signaling but not spindle formation [10], hyperphosphorylated cdc11p was observed during mi- tosis, even though the cells were not septating .
PMID:12546793	(Figure 1B) n G2-arrested cdc2-17 cells overexpressing spg1p, cdc11p was predominantly in the hyperphosphorylated form
PMID:12546793	(Figure 1A) In a mob1-R4 byr4::ura4􏰀 mutant, and also in cdc16-116 grown for 5 hr at 36􏰁C, cdc11p accumulated in the hyperphosphorylated (3) form. Later: in mutants such as cdc16-116 or byr4::ura4􏰀, in which cdc7p is present on both spindle pole bodies, the hyperphosphorylated form (3) of cdc11p is more abundant.
PMID:12546793	(Figure 1A) In a mob1-R4 byr4::ura4􏰀 mutant, and also in cdc16-116 grown for 5 hr at 36􏰁C, cdc11p accumulated in the hyperphosphorylated (3) form
PMID:12546793	(Figure 3B). However, at 36􏰁C, when cdc11p is no longer associated with the SPB [3, 4], most of the cdc11p was hypophosphory- lated (form 1)
PMID:12546793	Less than 10% of these cells had cdc7p on the spindle pole body, consistent with previous studies [25].
PMID:12565823	Fig 4a
PMID:12565827	Fig. 2C
PMID:12565827	Fig. 2C
PMID:12589755	same as crb2delta alone
PMID:12604790	assayed with other MCM subunits present
PMID:12606573	Figure 7A
PMID:12606573	normal rate of spindle phase I elongation. MI spindle elongation time is reduced to 40 min in rec7-146 bub1D cells (Figure 8Ad, upper panel)
PMID:12606573	decreased rate of spindle phase I elongation (70 mins. vs 40 wt)
PMID:12606573	Figure 7Ca
PMID:12606573	figure 7B
PMID:12606573	figure 7B
PMID:12606573	In zygotes undergoing meiotic divisions, WT Bub1±GFPp became associated with the centromeres after meiotic prophase and remained associated until anaphase I, con®rming previous reports using ®xed cells (Bernard et al., 2001; Figure 7B, WT, f±h).
PMID:12606573	In zygotes undergoing meiotic divisions, WT Bub1±GFPp became associated with the centromeres after meiotic prophase and remained associated until anaphase I, con®rming previous reports using ®xed cells (Bernard et al., 2001; Figure 7B, WT, f±h).
PMID:12606573	Figure 4E
PMID:12606573	figure 7A
PMID:12606573	figure 7A
PMID:12606573	figure 7A
PMID:12606573	Figure 3A during spindle checkpoint
PMID:12606573	in vitro assay for activity, phenotype for process
PMID:12646585	kinase activity increases in presence of salt
PMID:12653962	fig 6B
PMID:12653962	fig 6B
PMID:12653962	fig 6B
PMID:12653962	fig 6B
PMID:12654901	fig7a
PMID:12654901	Fig 6
PMID:12654901	Fig. 4, B and C)I
PMID:12654901	data not shown
PMID:12654901	fig2 maximum 3 septa
PMID:12654901	fig2
PMID:12654901	fig 3
PMID:12654901	not shown
PMID:12654901	fig2 maximum 3 septa
PMID:12654901	fig7b
PMID:12654901	not shown
PMID:12654901	not shown
PMID:12654901	not shown
PMID:12654901	not shown
PMID:12654901	"""exhibited well- defined, normal actin rings"""
PMID:12654901	fig7c
PMID:12654901	fig 8
PMID:12654901	fig 8
PMID:12654901	fig2
PMID:12654901	fig 7
PMID:12654901	Fig 6
PMID:12654901	Fig 6
PMID:12654901	Fig 6
PMID:12668659	unpublished obsevation
PMID:12668659	unpublished obsevation
PMID:12668659	fig1
PMID:12668659	fig1
PMID:12668659	fig1
PMID:12668659	fig5
PMID:12668659	Fig8
PMID:12668659	Fig8
PMID:12668659	Fig8
PMID:12668659	Fig8
PMID:12668659	Fig8
PMID:12668659	fig5
PMID:12668659	Fig. 7 D
PMID:12668659	fig5
PMID:12668659	fig5
PMID:12668659	fig5
PMID:12668659	fig5
PMID:12668659	fig5
PMID:12668659	fig5
PMID:12668659	fig2a colocalizes with sep3
PMID:12668659	fig5
PMID:12668659	fig5
PMID:12668659	fig4
PMID:12668659	fig4
PMID:12668659	Fig. 3 C
PMID:12668659	Fig. 3 C
PMID:12668659	Fig3
PMID:12668659	Fig3
PMID:12668659	Fig3
PMID:12668659	Fig3
PMID:12668659	Fig. 3 A, lanes 1 and 7 (control)
PMID:12668659	Fig. 3 A, lanes 1 and 7
PMID:12668659	fig2a
PMID:12676088	telomerase regulator
PMID:12697806	after 100 generations
PMID:12715160	salt stress
PMID:12715160	salt stress
PMID:12719471	at anaphase?
PMID:12719471	at anaphase?
PMID:12719471	abolished
PMID:12759375	meiosis II
PMID:12764130	Fig 5B
PMID:12764130	Fig4F Cells have a similar defect to a tea1 delta cell wall defect
PMID:12764130	Data not shown
PMID:12764130	Fig4C,D Cells shown a normal tea1 delta actin morphology
PMID:12764130	Fig 4B
PMID:12764130	Fig 4B
PMID:12764130	Fig3Biii Cells shown a normal tea1 delta morphology
PMID:12764130	Fig3B ii
PMID:12764130	Fig3A tea1 delta is a temperature dependent suppressor of loss of skb15
PMID:12764130	Fig2B. shk1 K415R mutant is expressed from a weak allele of nmt1 promoter ON but does not say whether it is expressed at wild type levels. pREP4XGST-tea1 is a multi copy plasmid promoter ON
PMID:12764130	Fig1 GST tea1 directly phosphorylated by Shk1 in vitro Fig2A GST-tea1 is phosphorylated in vivo in a Shk1 dependent manner
PMID:12764130	Fig 1B,C demonstrates in vitro kinase activity. 2A in vivo
PMID:12764130	Fig 5C,D
PMID:12764130	Fig 4E
PMID:12764130	Fig5D
PMID:12764130	Fig 6B,C
PMID:12764130	Fig6D
PMID:12764130	Fig 7A
PMID:12764130	Fig 7B,C Penetrance refers to the penetrance of the NTR old-new end growth pattern
PMID:12764130	Fig8. pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter
PMID:12764130	Data not shown. pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter
PMID:12773390	Figure 4A and B
PMID:12773390	Fig 1 a
PMID:12773390	Fig 1 a
PMID:12773390	Fig 1 a
PMID:12773390	figure 1 a
PMID:12773390	figure 1 b (is described as a pair, but is cylindrical short and wide....
PMID:12773390	figure 1 a
PMID:12773390	figure 1 a
PMID:12773390	figure 1 E
PMID:12773390	figure 1 E
PMID:12773390	figure 1 E
PMID:12773390	figure 1 E
PMID:12773390	figure 1 F
PMID:12773390	figure 1 F
PMID:12773390	Fig 2
PMID:12773390	Fig 2
PMID:12773390	fig 3 a
PMID:12773390	fig 3 a
PMID:12773390	fig 3 a
PMID:12773390	fig 3 a
PMID:12773390	fig 3 a
PMID:12773390	fig 3 a
PMID:12773390	fig 3 b (WT 11%)
PMID:12773390	fig 3 b (WT 11%)
PMID:12773390	fig 4 a
PMID:12773390	fig 4 a
PMID:12773390	Figure 4A and B
PMID:12773390	Figure 5B
PMID:12773390	Fig 6 a
PMID:12773390	Fig 6 a
PMID:12773390	Figure 7A and B
PMID:12773390	Figure 7A and B
PMID:12773390	Figure 7A and B
PMID:12773576	outer repeats
PMID:12773576	increased spatial extent of heterochromatin assembly (JUST, not at prpote4in coding gene!)
PMID:12773576	Figure 6C
PMID:12773576	Figure 6C
PMID:12773576	Figure 6C
PMID:12773576	Figure 6A, 6B
PMID:12773576	normal spatial extent of heterochromatin assembly (JUST)
PMID:12773576	increased spatial extent of heterochromatin assembly (JUST)
PMID:12773576	Figure 6C
PMID:12789340	inferred from combination of FYPO:0005798 and FYPO:0005828
PMID:12791993	Fig 1A
PMID:12791993	Fig 3E
PMID:12791993	Fig 3E, F.
PMID:12791993	Fig 3C
PMID:12791993	Fig 3C
PMID:12791993	Fig 3C
PMID:12791993	Fig 3A
PMID:12791993	Fig2 E,F
PMID:12791993	Fig 1B, C Cells arrest with a stable actinomyosin ring and fail to undergo cytokinesis
PMID:12791993	Fig 1B cell cycle arrest with post anaphase microtubule array
PMID:12791993	Fig1A
PMID:12791993	Fig 4D, E, F
PMID:12791993	Fig 4D, E, F
PMID:12791993	data not shown
PMID:12791993	Fig 4D
PMID:12791993	Fig 4C (displacemetn is supressed by inhibiting membrane trafficking
PMID:12791993	Fig2 E,F
PMID:12791993	data not shown
PMID:12791993	data not shown
PMID:12791993	data not shown
PMID:12791993	Fig 3E
PMID:12791993	Fig 3C
PMID:12796476	figure 1D but lacked both actin con- tractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	figure 1D arrested after 􏰖24 h (Fig. 1 E)
PMID:12796476	figure 1D impressive enrichment of actin filaments in ab- errant thick cables and aster-like accumulations
PMID:12796476	Thus, Cdc12(FH1FH2)p can replace the essential functions of Cdc12p in vivo when Cdc12p is nonfunctional, but is toxic when overexpressed in the pres- ence of functional Cdc12p.
PMID:12796476	abnormal (partial, broad, and misoriented) septa (Fig. 1 G)
PMID:12796476	barbed end actin capping
PMID:12796476	MF?
PMID:12796476	fission yeast Cdc12 (FH1FH2)p purified from bacteria (Fig. 1 B) stimulated ac- tin polymerization, as detailed below (see Fig. 4). This is consistent with Cdc12(FH1FH2)p and MmCPcapping the barbed (fast depolymerizing) ends of the fila- ments with high affinity (Kd 􏰃 0.1 􏰂M), allowing dissocia- tion only from the slowly depolymerizing (Pollard, 1986) pointed ends (Caldwell et al., 1989)
PMID:12796476	actin binding inhibitor pointed end
PMID:12796476	control, functional fragment
PMID:12796476	figure 1D but lacked both actin con- tractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	figure 1D impressive enrichment of actin filaments in ab- errant thick cables and aster-like accumulations
PMID:12805221	referred to in PMID:33137119
PMID:12808043	dependent on sme2 expression
PMID:12810074	Comparison of mitochondria staining with GFP–Ung1 showed no detectable co-localization of Ung1 and mitochondria (Fig. 1B, right). Thus, these cellular localization studies indicate that fission yeast Ung1 is more similar to the nuclear form of human UNG as they both localized predominantly in the nucleus
PMID:12815070	Figs.1A,4C)
PMID:12815070	Whereas cells in which the expres- sionoftheconstitutivelyactivemutantremainedre- pressed arrested cell cycle progression in interphase, 11% of those in which it had been expressed entered mitosis.This degree of suppression is very similar to the level of suppression of cdc25.22 arising from the pres- ence of the cut12.s11 mutation (Fig. 9B) and established that activation of Plo1 is sufficient to suppress the deficiency in Cdc25 function in cdc25.22 cells.
PMID:12815070	Whereas single plo1.ts2 and plo1.ts19 mutant and double cut12.s11 cdc25.22 mutant cells all entered mitosis (Fig. 9B,C), the single cdc25.22 mutant and both double cdc25.22 plo1.ts and triple cut12.s11 cdc25.22 plo1.ts mutants did not.
PMID:12815070	Whereas single plo1.ts2 and plo1.ts19 mutant and double cut12.s11 cdc25.22 mutant cells all entered mitosis (Fig. 9B,C), the single cdc25.22 mutant and both double cdc25.22 plo1.ts and triple cut12.s11 cdc25.22 plo1.ts mutants did not.
PMID:12815070	triple cut12.s11 cdc25.22 plo1.ts19 cells were unable to grow (Fig. 9A).
PMID:12815070	This established that mutating plo1 in a way that did not affect cell viability compromised the ability of cut12.s11 to suppress cdc25.22. Fig 9A. cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colo- nies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	Fig 9A. cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colo- nies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	Unlike classic “cut” mutants (Hirano et al. 1986), septation did not always follow on from the mi- toticarrest.
PMID:12815070	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	We concluded thatthePlo1-dependentkinaseactivityofbothplo1.ts2 andplo1.ts19wasgreatlyreduced.
PMID:12815070	We concluded thatthePlo1-dependentkinaseactivityofbothplo1.ts2 andplo1.ts19wasgreatlyreduced.
PMID:12815070	full-lengthproteinappearedtobelargely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	full-lengthproteinappearedtobelargely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	Western blot analysis showed that Plo1 levels in plo1.ts2cellswerenotradicallydifferentfromwildtype,
PMID:12815070	ability to form colonies o nrich medium at 36°C was indistin- guishable from that of wild-typec ells
PMID:12815070	ability to form colonies o nrich medium at 36°C was indistin- guishable from that of wild-typec ells
PMID:12815070	Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium
PMID:12815070	Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium
PMID:12815070	Kinase assays of these mitotic samples indicated that the cut12.s11 mutation promoted a 1.6 (±0.18; n = 5) in-creaseinPlo1-specificactivityduringmitosis(Fig.4D).
PMID:12815070	Plo1-associatedkinaseactivityofextractsfromarrested cdc2.33cut12.s11cellswas2.4-fold(±0.35;n=6)higher than that of the control cdc2.33 cut12+ cells (Fig. 4D). This established that cut12.s11 increased Plo1 activity ininterphase.
PMID:12815070	his suggested that the inability to promote mitotic Plo1-associated kinase activity in cut12.1 cells was not a simple consequence of an inability to assemble a bipolar spindle,or an inability to commit to mitosis.Rather,the data indicate that Cut12 function was required for full activationof Plo1-associated kinase activity during mitotic commitment. Alspp Fig. 6B
PMID:12815070	Fig. 2B
PMID:12815070	Fig. 2A;
PMID:12815070	Fig. 2A;
PMID:12815070	Fig. 2A;
PMID:12815070	Plo1.K65R,the“kinasedead”mutantprotein,onlyas- sociatedwithmitoticbutnotwithinterphaseSPBs(data not shown).
PMID:12815070	The extended and more random size of plo1.ts2cellsatdivisionsuggestedthatthismaybethe case. Despite the fact that these cells are able to enter mitosis,theyappeartobedoingsoinalessefficient,or more random manner (Fig. 8B).
PMID:12840005	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12857865	Fig 2/3
PMID:12857865	Figure 7 (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	Figure 7 (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	Figure 7
PMID:12857865	data not shown
PMID:12857865	Figure 6A
PMID:12857865	data not shown
PMID:12857865	Figure 6A
PMID:12857865	Fig4
PMID:12857865	Fig4
PMID:12857865	Fig4
PMID:12861005	same as taz1d alone
PMID:12861005	same as taz1d alone
PMID:12861005	same as taz1d alone
PMID:12861005	same as taz1d alone
PMID:12861005	same as taz1d alone
PMID:12861005	same as taz1d alone
PMID:12861005	same as taz1d alone
PMID:12861005	same as rad51d alone
PMID:12868054	n liquid YES medium at 27 ◦ C, the cells had a doubling time of ∼8 h, in contrast to 2 h 30 min for wild-type cells.
PMID:12868054	4 mM
PMID:12868054	fig 5
PMID:12868054	fig 7 prevacuolar compartment membrane
PMID:12868054	at 5 μg/ml
PMID:12868054	strong sensitiv- ity to 100 mM CaCl2 (Figure 4A)
PMID:12868054	fig 6
PMID:12868054	Fig3
PMID:12868054	2b
PMID:12868054	While both wild- type and vps33􏰗 cells grew at 26 ◦ C, vps33􏰗 cells exhibited a temperature-sensitive growth at 37 ◦C (Figure 2A).
PMID:12868054	fig 7a
PMID:12871901	homozygous diploid
PMID:12871901	homozygous diploid
PMID:12871901	permissive for cdc25-22; restrictive for cdt2-M1
PMID:12871901	Northern blot
PMID:12888492	IGI with cerevisiae
PMID:12893961	fig4
PMID:12893961	fig3
PMID:12893961	fig3
PMID:12893961	fig4
PMID:12893961	fig5
PMID:12893961	fig4
PMID:12893961	fig4
PMID:12894167	LOCALIZES OK, IS NOT RETAINED
PMID:12894167	"""These results indicate that Mal3 is required for the proper association of Tea2 with microtubules and sug- gest that Mal3 stabilizes the kinesin–microtubule interaction"""
PMID:12925774	during mitotic DNA replication initiation
PMID:12930956	assayed in pku80d haploid derived from pku80d pku+ heterozygous diploid
PMID:12951601	fig 1a thinner discontinuous spindles fypo/issues/3208
PMID:12951601	Fig 1d
PMID:12951601	Fig 1d
PMID:12951601	Fig 1e
PMID:12951601	Fig 1d
PMID:12951601	Fig. 1c, cells 1 and 3 Furthermore, multiple Mad2 dots, which have never been seen in wild type cells
PMID:12951601	Fig 1d
PMID:12966087	epistasis with Rhp51
PMID:12966087	epistasis with Rhp51
PMID:12972434	These data indicate that the decrease in ribosomal protein L25-A observed in cpc2::ura4 cells is probably due to a defect in recruitment of its mRNA to polyribosomes. The decreased amounts of both sam1 and thi2 RNAs are sufficient to account for the lowered protein abundance of each in cpc2::ura4 cells. In contrast, the decline in the level of ribosomal protein Rpl25 in cpc2::ura4 cells is not likely to be caused by an inability to accumulate its mRNA transcript.
PMID:12972434	These data indicate that the decrease in ribosomal protein L25-A observed in cpc2::ura4 cells is probably due to a defect in recruitment of its mRNA to polyribosomes. The decreased amounts of both sam1 and thi2 RNAs are sufficient to account for the lowered protein abundance of each in cpc2::ura4 cells. In contrast, the decline in the level of ribosomal protein Rpl25 in cpc2::ura4 cells is not likely to be caused by an inability to accumulate its mRNA transcript.
PMID:12972434	e pyruvate kinase, thiazole biosynthetic enzyme, and ribosomal protein L25-A
PMID:12972571	mcm4ts-td phenotype indicates that Cdc23 chromatin localization is independent of Mcm4
PMID:12972571	late anaphase
PMID:12972571	late anaphase
PMID:12972571	Promoter nmt1
PMID:1314171	inhibited by CCCP
PMID:1316996	HI used as substrate
PMID:1316996	crosses with this mutant generate a high level of diploids.
PMID:1316996	G2 arrest shown by FACS analysis.
PMID:1316996	cdc2-E8 suppresses mitotic catastrophe at high temperature
PMID:1316996	cdc2-A21 suppresses mitotic catastrophe at high temperature
PMID:1316996	cells inviable at all temperatures in presence of wee1+
PMID:1316996	Hi used as substrate
PMID:1316996	G2 arrest shown by FACS analysis.
PMID:1316996	HI used as substrate
PMID:1316996	Hi used as substrate
PMID:1316996	cdc2-E9 suppresses mitotic catastrophe at high temperature
PMID:1324908	GO:0008444 CDP-DG synthase and GO:0003882 PS synthase
PMID:1324908	regulated by inositol
PMID:1324908	regulated by inositol
PMID:1332977	phosphorylated and dephosphorylated forms both active; no PR col 17 because no evidence that dephosphorylated form is physiologically relevant (dephosphorylated in vitro)
PMID:1332977	3 sites in N-terminus (1-75) and 7 in C-terminus (1221-1485), but positions not determined
PMID:1372994	val: I used this to link to process term even though it isn't shown directly in this paper
PMID:1372994	AL added as BP since Val had added it involved_in on MF
PMID:1396704	activated_by(CHEBI:17234)
PMID:1427071	hydroxyurea absent
PMID:14519123	fig3
PMID:14519123	fig3
PMID:14519123	fig4
PMID:14519123	fig4
PMID:14519123	fig4
PMID:14528010	specific for dsDNA at ds/ssDNA junction
PMID:14528010	is not a resolvase - makes symmetric cuts on opposed strands across the junction but does not convert products to linear DNA molecules
PMID:14532136	there is good evidence for this, but not bullet proof
PMID:14585996	residue S604
PMID:14585996	in presence of hydroxyurea
PMID:14585996	in presence of hydroxyurea
PMID:14585996	phenotype indicates that mrc1/Phos:S604 has higher affinity for chromatin than Unphos:S604
PMID:14585996	residue S604
PMID:14599746	rationale: increased transversion frequency indicates that 8-oxoG persists more in mutant, but normal indel frequency suggests not NER
PMID:14599746	inferred from increased mutation rate upon UV exposure in mutant
PMID:14602073	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	before late interphase
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	independent of F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	dependent on F-actin (assayed using Latruncilin A)
PMID:14602073	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	dependent on F-actin (assayed using Latrunculin A)
PMID:14612233	activated_by(CHEBI:29108)| activated_by(CHEBI:29035)
PMID:14633985	from genetics and Sty1 consensus. Later papers say Activated Sty1 also phosphorylates Csx1
PMID:14633985	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	The H2O2-induced increase in expression of pcr1+ mRNA, which encodes a binding partner of Atf1, was similarly eliminated in csx1D cells (Figure 4A
PMID:14633985	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	This decrease correlated with a large drop in the amount of Atf1 protein (Figure 4C).
PMID:14633985	the large increase in atf1+ mRNA that is induced by H2O2 in wildtype cells was abolished in csx1D cells.
PMID:14633985	The csx1D single mutant was less sensitive to H2O2 than the spc1D mutant, whereas the csx1D spc1D double mutant was more sensitive than the spc1D strain. These ®ndings were consistent with the idea that Csx1 and Spc1 have independent functions in oxidative stress tolerance.
PMID:14633985	fig1
PMID:14633985	fig1
PMID:14633985	As shown in Figure 2C, H2O2 induced robust phosphorylation of Spc1 in csx1D cells..... Csx1 is not necessary for Spc1 activation.
PMID:14633985	fig1c
PMID:14633985	fig1c
PMID:14633985	fig1c
PMID:14633985	fig1c
PMID:14633985	fig1
PMID:14633985	fig1
PMID:14633985	Figure 4E).
PMID:14633985	Figure 6A, Csx1±GFP was detected in the cytoplasm and appeared to be excluded from the nucleus. This pattern of Csx1±GFP localization was unaffected by oxidative stress.
PMID:14633985	Figure 6A, Csx1±GFP was detected in the cytoplasm and appeared to be excluded from the nucleus. This pattern of Csx1±GFP localization was unaffected by oxidative stress.
PMID:14633985	(Figure 6B). decreased stability in response to oxidative stress
PMID:14633985	decreased stability in response to oxidative stress (Figure 6B)
PMID:14633985	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	Figure 7A
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14648198	actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler
PMID:14654689	same as rad11-D223Y alone
PMID:14654689	same as rad11-D223Y alone
PMID:14654689	same as rad50delta alone
PMID:14654689	also inferred from localization to telomere
PMID:14730319	Fig. 4a)
PMID:14730319	Fig. 4d, e)
PMID:14730319	Fig. 4c)
PMID:14730319	Fig. 4c)
PMID:14730319	Fig. 4d
PMID:14730319	Fig. 4a)
PMID:14730319	Fig. 4c)
PMID:14730319	fig 2a
PMID:14730319	fig 2a
PMID:14730319	fig 2 and 3d
PMID:14730319	Fig. 2c
PMID:14730319	Fig. 2c
PMID:14730319	Fig. 2c
PMID:14739927	interaction increases during cellular response to UV
PMID:14739927	proteins dissociate during cellular response to UV
PMID:14742702	Figure 4D
PMID:14742702	Figure 4E
PMID:14742702	Figure 4F
PMID:14742702	Figure 5A, lane 4
PMID:14742702	Figure 1D
PMID:14742702	Figure 5A, lane 4
PMID:14742702	Figure 6A
PMID:14742702	Figure 6A
PMID:14742702	Figure 6B
PMID:14742702	8C
PMID:14742702	Figure 8E
PMID:14742702	Figure 8E
PMID:14742702	Figure 8E
PMID:14742702	Figure 8E
PMID:14742702	Figure 8E
PMID:14742702	Figure 1C
PMID:14742702	Figure 1C rows 2 and 3, note chromosome missegregation in the cell of row 3, and see Supplementary Figure S1 for quantifica- tion of spindle intensity
PMID:14742702	Figure 1C
PMID:14742702	Figure 1B
PMID:14742702	Figure 1B
PMID:14742702	Figure 1A inferred from increased duration of mitosis
PMID:14742702	Figure 1A
PMID:14742702	Figure 1D
PMID:14742702	Figure 2A
PMID:14742702	On temperature shift down to 20°C, Alp7-YFP localized only to the SPB (Figure 2B). This also indicates that Alp7 does not require a microtubule cytoskeleton to localize to the SPB.
PMID:14742702	Figure 2D
PMID:14742702	Figure 1D
PMID:14742702	Figure 2A
PMID:14742702	Figure 3B
PMID:14742702	Figure 3B
PMID:14742702	Figure 4A
PMID:14742702	Figure 3B
PMID:14742702	Figure 3B
PMID:14742702	Figure 4D
PMID:1475195	other evidence = iodine staining
PMID:14766746	filter binding assay
PMID:14766746	filter binding assay
PMID:14766746	filter binding assay
PMID:14766746	filter binding assay
PMID:14972679	Figures 1B
PMID:14972679	Figures 1A and 2
PMID:14972679	Figures 1B
PMID:14972679	Figures 1A and 2
PMID:14972679	By metaphase I, 100% of cells (n 􏰆 100) contained a strong nuclear signal. Sgo1-GFP was concentrated in distinct foci in about half of these metaphase I cells (Figure 3A-2).
PMID:14972679	Furthermore, no Rec8-specific fluorescence at all could be detected in 10% of the mutant binucleates. In contrast, the distribution of Rec8- GFP fluorescence in 􏰀sgo2 mutant binucleates was in- distinguishable from wild-type.
PMID:14972679	Figures 1A and 2
PMID:14972679	Figures 1B
PMID:14972679	Figures 1A and 2
PMID:15004232	Figure 5F
PMID:15040954	qualifier=major
PMID:15047861	fig1
PMID:15047861	fig8c
PMID:15047861	When the cells were labeled with FM4-64 for 60 min, the 􏰀apm1 cells were highly frag- mented compared with wild-type cells, consistent with the findings obtained by electron microscopy (Figure 7B)
PMID:15047861	When the cells were labeled with FM4-64 for 60 min, the 􏰀apm1 cells were highly frag- mented compared with wild-type cells, consistent with the findings obtained by electron microscopy (Figure 7B)
PMID:15047861	fig6
PMID:15047861	Figure 3B, a–c accumulation of presumptive post-Golgi secretory vesicles and abnormal Golgi-like structures were also characteristic of the ypt3-i5 mutants that we reported previously (Cheng et al., 2002).
PMID:15047861	Figure 3B, a–c
PMID:15047861	fig1
PMID:15047861	fig1
PMID:15047861	fig1
PMID:15047861	DNS
PMID:15047861	fig1
PMID:15047861	fig1
PMID:15047861	fig1
PMID:15047861	fig1
PMID:15052323	Mix of IMP evidence & a proxy assay for hydrolase function
PMID:15062095	the variant caused abnormal microtubule behavior in cell-end regions, which is likely to be the cause of the previously reported shape abnormalities
PMID:15068790	Fig. 7
PMID:15068790	Fig. 7
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 1
PMID:15068790	Fig. 7
PMID:15068790	Fig. 2
PMID:15068790	Fig. 2
PMID:15068790	Fig. 6
PMID:15068790	Fig. 6
PMID:15068790	Fig. 7
PMID:15068790	Fig. 1
PMID:15068790	Fig. 2
PMID:15068790	Fig. 2
PMID:15121844	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15132994	We draw two conclu- sions from these data; first, association of Fin1 with the SPB requires activation of the SIN; second, recruitment of Fin1 to the SPB requires the SIN inhibitor Byr4, with which it interacts.
PMID:15132994	fig 1 c
PMID:15132994	fig 1 c
PMID:15132994	Fin1 binds Byr4. (A) Fin1 failed to associate with SPBs when the SIN was either inactive or hyperactive.
PMID:15132994	Fin1 binds Byr4. (A) Fin1 failed to associate withSPBs when the SIN was either inactive or hyperactive. Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1).
PMID:15132994	is this the correct term?
PMID:15132994	Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1).
PMID:15147872	fig 1 a b
PMID:15147872	fig 4 abnormally segregating nuclear membrane #2863 PENDING
PMID:15147872	fig 1 a b
PMID:15147872	fig 1 c. figure 2
PMID:15147872	table1
PMID:15147872	table1
PMID:15147872	table1
PMID:15147872	fig 2
PMID:15147872	fig 3a
PMID:15155581	Fig 5
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 1
PMID:15155581	Fig 3
PMID:15155581	Fig 1
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 4
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 2
PMID:15155581	Fig 2
PMID:15155581	Fig 2
PMID:15155581	Fig 2
PMID:15155581	Fig 2
PMID:15155581	Fig 3; same as either single mutant
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 3
PMID:15155581	Fig 4
PMID:15155581	Fig 4
PMID:15155581	Fig 4
PMID:15155581	Fig 5
PMID:15155581	Fig 5
PMID:15155581	Fig 4
PMID:15155581	Fig 5
PMID:15155581	Fig 5
PMID:15155581	Fig 5
PMID:15155581	Fig 1
PMID:15155581	basal phosphorylation on T412 & S423
PMID:15155581	Fig 1
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15173168	inferred from phenotypes of mrc1delta, rad3delta, Cds1-Rad26 fusion, other cds1 alleles, and combinations thereof
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173168	residue T11
PMID:15173383	TEV protease present; Cdc6 truncated
PMID:15173383	TEV protease present; Cdc6 truncated
PMID:15175657	dns
PMID:15177031	Fig 5E,F tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter
PMID:15177031	Fig 4A,B
PMID:15177031	Fig 4E-H Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	Fig 4C Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	Fig 1 live imaging of Tip1YFP and CFP tubulin
PMID:15177031	data not shown
PMID:15177031	Fig 4A,B
PMID:15177031	Fig 4C
PMID:15177031	Fig 4E-H
PMID:15177031	Fig 4I
PMID:15177031	data not shown
PMID:15177031	co-localises with tip1
PMID:15177031	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	colocalises with tip1
PMID:15177031	Fig6E
PMID:15177031	Fig6 E
PMID:15177031	Fig 6C,D GFPmal3 is mildly overexpressed from the repressed nmt1 promoter
PMID:15177031	Fig 6A,B GFPmal3 is mildly overexpressed from the repressed nmt1 promoter
PMID:15177031	(plus end directed)
PMID:15177031	Fig 5E,F tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter
PMID:15177031	Fig 5A,B Endogenous tea2 tagged with GFP
PMID:15177031	Fig 5C
PMID:15177031	Fig 5A,B Endogenous tea2 tagged with GFP
PMID:15177031	Fig 5A,B Endogenous tea2 tagged with GFP
PMID:15184401	Fig. 1 C
PMID:15184401	Fig 1E
PMID:15184401	Fig 1E
PMID:15184401	Fig. 1 C
PMID:15184401	Fig. 1 C/ Fig3
PMID:15184401	Fig. 4 D
PMID:15184401	Fig. 4 D
PMID:15184401	fig 4F
PMID:15184401	fig 4F
PMID:15184401	fig 4F
PMID:15184401	fig 4F
PMID:15184401	(G2) Fig. 6 B
PMID:15184401	Fig. 6 B (G2)
PMID:15184401	Fig. 6 C . (G2)
PMID:15184401	Fig. 1 C
PMID:15184401	Fig. 1 C
PMID:15184401	Fig. 1 C
PMID:15184401	fig 6F
PMID:15184401	fig 6F
PMID:15184401	fig 6F
PMID:15184402	During mitosis, tea1p persists at the cell tips, whereas for3p and bud6p leave the cell tip and accumulate more at the cell division plane.
PMID:15184402	During mitosis, tea1p persists at the cell tips, whereas for3p and bud6p leave the cell tip and accumulate more at the cell division plane.
PMID:15189983	unlike JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29), cells that elongate and die, cells of the parental strain FWP190 (git2􏰇) appear to simply arrest growth (Fig. 2)
PMID:15189983	Fig. 7 (lanes 1 and 2), we observed that both cgs1􏰀 and pka1􏰀 are transcriptionally induced by glucose starvation.
PMID:15189983	table 3
PMID:15189983	table 3
PMID:15189983	fig 6
PMID:15189983	fig 6
PMID:15189983	fig 6
PMID:15189983	fig 6
PMID:15189983	fig 6
PMID:15189983	figure1
PMID:15189983	For cgs1-1 mu- tant cells, pregrowth on YEA medium results in a nearly 100- fold loss of mating efficiency, as expected. More surprisingly, we found that pregrowth of the cgs1-1 strain on PM medium reduces the mating efficiency defect to only fourfold (Table 2).
PMID:15189983	For cgs1-1 mu- tant cells, pregrowth on YEA medium results in a nearly 100- fold loss of mating efficiency, as expected. More surprisingly, we found that pregrowth of the cgs1-1 strain on PM medium reduces the mating efficiency defect to only fourfold (Table 2).
PMID:15189983	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	figure2
PMID:15189983	figure2
PMID:15189983	figure2
PMID:15189983	git2􏰇 strains themselves were severely defective for growth on YEA medium containing 1 M KCl (Fig. 1).
PMID:15189983	fig 7
PMID:15189983	fig 7
PMID:15189983	fig 7
PMID:15189983	fig 7
PMID:15189983	Fig. 7 (lanes 1 and 2), we observed that both cgs1􏰀 and pka1􏰀 are transcriptionally induced by glucose starvation.
PMID:15189983	figure1
PMID:15189983	figure1
PMID:15189983	figure1
PMID:15194812	Cdc45 reappears quickly after shift from restrictive to permissive temperature
PMID:15194814	homozygous diploid
PMID:15194814	homozygous diploid
PMID:15219990	spectra looks the same as Adx
PMID:15226378	homozygous diploid
PMID:15226378	homozygous diploid
PMID:15226405	frequency of different stages of LE development is different though, but morphology is normal
PMID:15226405	frequency of different stages of LE development is different though, but morphology is normal
PMID:15249580	(vw fixed from GO:0052812 to GO:0016308 based on e-mail from Pgaudet) The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3.
PMID:15249580	mishapen
PMID:15249580	fig 1c
PMID:15249580	fig 1c
PMID:15249580	The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3.
PMID:15265986	in response to cytokinesis after mitosis checkpoint
PMID:15265986	in response to cytokinesis after mitosis checkpoint
PMID:15278909	during premeiotic DNA replication
PMID:15297457	would it be better/safer to annotate to parent (generic intra-S checkpoint term)?
PMID:15314153	30 degrees
PMID:15314153	25 degrees
PMID:15316017	activated_by(CHEBI:18420)| inhibited_by(CHEBI:29108)
PMID:15329725	Fig. 1h
PMID:15329725	Fig. 1f)
PMID:15329725	Fig. 1d and Fig. 1h
PMID:1533272	cdc13 expressed from own promoter on multi copy plasmid pUR18
PMID:1533272	Fig 2. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.
PMID:1533272	Fig 4 Histone H1 used as substrate. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.
PMID:1533272	Fig 5. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Phosphorylation on threonine, but position(s) not determined.
PMID:1533272	Fig 3. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.
PMID:1533272	Fig 7 Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Binds to cdc13 but this is reduced compared to binding of cdc2+ to cdc13
PMID:15367656	no hydroxyurea
PMID:15369671	fig4
PMID:15369671	fig4
PMID:15369671	fig4
PMID:15369671	fig4 (centromere)
PMID:15371542	fig 1a
PMID:15371542	fig1
PMID:15371542	fig1
PMID:15371542	fig 1a
PMID:15385632	Figure 1J Based on the lower recovery of coimmunoprecipitated proteins, this Spn1p-Spn4p complex appears to be less stable than in the presence of Spn2p or Spn3p.
PMID:15385632	Figure 2, D and E
PMID:15385632	Figure 5 C
PMID:15385632	Figure 5
PMID:15385632	Figure 5
PMID:15385632	Figure 5
PMID:15385632	Figure 5
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 5
PMID:15385632	Figure 2A,Figure 2, D and E
PMID:15385632	Figure 2A, Figure 2, D and E
PMID:15385632	Figure 2A
PMID:15385632	Figure 2A
PMID:15385632	Figure 2A Figure 2, B and C)
PMID:15385632	Figure 2A
PMID:15385632	Figure 1H and Table 1
PMID:15385632	Figure 1I
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	Figure 6, A, D, and E
PMID:15385632	fig5
PMID:15385632	fig5
PMID:15385632	erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the for- mation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expres- sion of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003). erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the for- mation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expres- sion of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003).
PMID:15385632	In this case, Spn3p-GFP was recruited to the medial region before mitosis as before (Figure 8A) and it was now assembled into highly organized ring structures that were easily visualized as split rings once septa had formed (Fig- ure 8, B and C). Virtually no diffuse disk structures were observed (Figure 8, B–D). We conclude from this experiment that Mid2p is solely responsible directly or indirectly for regulating septin ring coalesence in S. pombe.
PMID:15385632	Combining this observation with our biochemical data, we conclude that a subcomplex of Spn1p-Spn4p is sufficient for formation of ectopic structures and localizing to the medial cortex, but at least one other septin is required for assembly of a ring structure.
PMID:15385632	Combining this observation with our biochemical data, we conclude that a subcomplex of Spn1p-Spn4p is sufficient for formation of ectopic structures and localizing to the medial cortex, but at least one other septin is required for assembly of a ring structure.
PMID:15385632	fig 6
PMID:1538784	throughout_cell_cycle
PMID:15466421	homozygous diploid
PMID:15466421	homozygous diploid
PMID:15470240	fig2
PMID:15470240	fig2
PMID:15470240	fig2
PMID:15471884	low affinity
PMID:15471884	lower affinity than for Y-form DNA
PMID:15485922	same as taz1delta alone
PMID:15485922	same as taz1delta alone
PMID:15507118	inviable mononucleate aseptate vegetative cell with cell cycle arrest in mitotic G2 phase
PMID:15509783	Fig. 7B
PMID:15509783	Fig. 7B
PMID:15509783	Figure 2A
PMID:15509783	figure 1B
PMID:15509783	figure 1B
PMID:15509783	table2
PMID:15509783	table2
PMID:15509783	table2
PMID:15509783	table2
PMID:15509783	table2
PMID:15509783	Fig. 7D
PMID:15509783	checkpoint
PMID:15509783	Fig. 7D
PMID:15509865	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	data not shown , phenocopies ssm4 &dhc1
PMID:15509865	(Fig. 2A)
PMID:15509865	data not shown , phenocopies ssm4 &dhc1
PMID:15509865	(Fig. 2A)
PMID:15509865	Fig. 2B,C
PMID:15509865	DURATION Fig. 2B,C
PMID:15509865	data not shown
PMID:15509865	(Table 2).leu1 and his2 loc, reduced 12 fold
PMID:15509865	(Table 3) assayed using pairing of his2 loci
PMID:15509865	Add?
PMID:15509865	Table 3
PMID:15509865	Fig. 3C).
PMID:15509865	Table 3
PMID:15509865	Table 3
PMID:15509865	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	(Fig. 6A-C), during meiotic prophase, shmooing
PMID:15509865	meiosis
PMID:15509865	Fig. 3B
PMID:15509865	Fig. 3B
PMID:15509865	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15525536	only required when there are problems , possibly involved in repair of monoorientation
PMID:15537393	Figure 3c
PMID:15537393	figure 2d
PMID:15537393	figure 2d
PMID:15537393	figure 2e
PMID:15537393	figure 2e
PMID:15537393	figure 2e
PMID:15537393	figure 2e
PMID:15537393	figure 2e
PMID:15537393	figure 2f
PMID:15537393	figure 2f
PMID:15537393	figure 2f
PMID:15537393	Figure 3d
PMID:15537393	Figure 3d
PMID:15537393	Figure 3c
PMID:15537393	Figure 3b
PMID:15537393	Figure 3b
PMID:15537393	figure 2g
PMID:15546915	Figure 3 C shrunken cell
PMID:15546915	(Fig. 1A
PMID:15546915	Figure 3 C shrunken cell
PMID:15546915	Figure 4 GI Rho1 OEX rescues echinocandin sensitivity
PMID:15546915	figure4
PMID:15546915	Figure 5 These results indicate that Rgf3p acts as a specific Rho1p activator in S. pombe.
PMID:15546915	Fig. 6A + DAPI staining revealed that, in most multiseptate cells, each compartment contained one nucleus, indicative of a defect in cell separation after septum assembly (not shown)
PMID:15546915	(Fig. 6B)....an increase in enzymatic activity was detected in cells overexpressing rgf3+ compared with the activity observed in the wild-type strain
PMID:15546915	(1-3 beta D) As shown in Fig. 6C, there was an increase in the amount of β-glucan in cells that overexpressed rgf3+ compared with wild-type cells (16% and 10%, respectively),
PMID:15546915	As shown in Fig. 6C, there was an increase in the amount of β-glucan in cells that overexpressed rgf3+ compared with wild-type cells (16% and 10%, respectively),
PMID:15546915	replace with cytokinetic phase
PMID:15546915	(Fig. 1A
PMID:15546915	Fig. 3A
PMID:15546915	Figure 3B indicates a bypass of cytokinesis checkpoint
PMID:15548596	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15601865	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1–58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165–503) was able to tetramerize (data not shown).
PMID:15601865	Fig. 3
PMID:15601865	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1–58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165–503) was able to tetramerize (data not shown).
PMID:15601865	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1–58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165–503) was able to tetramerize (data not shown).
PMID:15601865	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1–58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165–503) was able to tetramerize (data not shown).
PMID:15615784	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15615784	assayed in vitro
PMID:15615784	assayed in vitro
PMID:15615784	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15615848	Fig. 1B
PMID:15615848	. We found that rdp1 mutants have a significantly higher percentage (􏰅20%) of cells with lagging chromosomes during late anaphase than in the wild-type strain (􏰆1%) (Fig. 3B)
PMID:15615848	Fig. 1A CenH
PMID:15615848	Fig. 1A
PMID:15615848	Fig. 1A CenH
PMID:15615848	(Fig. 3 C and D) In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telo- meres to the nuclear periphery was unaffected
PMID:15615848	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4􏰃 and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4􏰃 and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	Fig. 1B
PMID:15615848	Fig. 1B
PMID:15615848	Fig. 1B
PMID:15615848	In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telo- meres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4􏰃 and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	herefore, we conclude from these analyses that the RdRP activity of Rdp1 is essential for the generation of RITS-associated siRNAs. plus centrromeric chromatin assays
PMID:15615848	Fig. 1B
PMID:15615848	Fig. 1B
PMID:15615848	In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telo- meres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1􏰄, or dcr1􏰄 cells
PMID:15615848	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1􏰄, or dcr1􏰄 cells
PMID:15615848	hypersensitive to TBZ, indicating that chromosome segregation is not robust in these mutant cells (Fig. 3A).
PMID:15615848	(Fig. 2D). cells localization of both methylated H3–K9 and Swi6 at centromeric otr1R::ura4􏰃 was severely affected in rdp1D903A cells (Fig. 2D).
PMID:15615848	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1􏰄, or dcr1􏰄 cells
PMID:15615848	(Fig. 2D). cells localization of both methylated H3–K9 and Swi6 at centromeric otr1R::ura4􏰃 was severely affected in rdp1D903A cells (Fig. 2D).
PMID:15615848	(Fig. 2C). (otr1R::ura4􏰃) (Fig. 2B) Immunoblotting assay showed that the protein level of the Rdp1 mutant (Rdp1D903A) is comparable to that of wild-type Rdp1, suggesting that the D903A mutation does not affect the stability of the mutant protein
PMID:15615848	(Fig. 2B) Immunoblotting assay showed that the protein level of the Rdp1 mutant (Rdp1D903A) is comparable to that of wild-type Rdp1, suggesting that the D903A mutation does not affect the stability of the mutant protein
PMID:15625190	three-hybrid assay; also binds exogenous ESEs
PMID:15632064	Mutated Rpc11p subunits associate with Pol III and impair its RNA 3􏰌 cleavage activity.
PMID:15632064	fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency.
PMID:15632064	fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency.
PMID:15632064	fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency.
PMID:15632064	trna chaperone
PMID:15643072	assayed in strain with cdc10-129 to synchronize
PMID:15647375	fig4
PMID:15647375	GO:0000093 = mitotic telophase
PMID:15647375	fig 4
PMID:15647375	GO:0051329 = mitotic interpase
PMID:15647375	fig 4
PMID:15654094	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15654094	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15654094	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15654094	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15665379	fig 2
PMID:15665379	fig 3b
PMID:15665379	fig 2
PMID:15665379	fig 2
PMID:15671491	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	assayed using reporter based on S. cerevisiae MFA2
PMID:15689489	Fig. 1
PMID:15689489	Fig. 6
PMID:15689489	Fig. 6
PMID:15689489	Fig. 6
PMID:15689489	Fig. 6
PMID:15689489	Fig. 5
PMID:15689489	Fig. 2
PMID:15689489	Fig. 2
PMID:15689489	In metaphase the difference kinds of microtubules cannot be distinguished, but they can be distinguished during anaphase B
PMID:15689489	Fig. 1
PMID:15689489	Fig. 1
PMID:15689489	Fig. 1
PMID:15716270	18S rRNA positions 208, 2341
PMID:15716270	18S rRNA position 1307
PMID:15716270	25S rRNA position 1084
PMID:15716270	25S rRNA position 1723
PMID:15716270	18S rRNA position 1204
PMID:15716270	25S rRNA position 1074
PMID:15716270	25S rRNA position 3017
PMID:15716270	25S rRNA positions 2216, 2220, 2351
PMID:15716270	25S rRNA position 3069
PMID:15716270	25S rRNA positions 2298, 2401
PMID:15728720	increased centromere spindle pole body detachment during meiotic prophase fission-yeast-phenotype/2055/
PMID:15731009	dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC)
PMID:15731009	same as orb3-167 alone
PMID:15731009	dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC)
PMID:15731009	same as orb3-167 alone
PMID:15731009	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15731009	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15731009	assayed using casein; doesn't quite rule out tyrosine phosphorylation
PMID:15743909	dependent on F-actin (assayed using Latrunculin A)
PMID:15743909	dependent on F-actin (assayed using Latrunculin A)
PMID:15743909	homozygous cross
PMID:15743909	homozygous cross
PMID:15743909	homozygous cross
PMID:15772152	normal length
PMID:15797383	fig1
PMID:15797383	fig2 ln 11-12
PMID:15797383	fig2,5
PMID:15797383	fig2
PMID:15797383	fig2,3,4
PMID:15797383	fig1
PMID:15797925	punctate, similar to nuclear pore components; localization not dependent on microtubules
PMID:15797925	assayed using NLS-LacI-GFP construct
PMID:15800064	fig 5 b
PMID:15800064	fig 6 B
PMID:15800064	fig 2 a,c 2D
PMID:15800064	fig 2 a 2D
PMID:15800064	figure 3A c
PMID:15800064	Figure 3A
PMID:15800064	fig 5 a
PMID:15800064	fig 6 c
PMID:15800064	fig 5 a
PMID:15800064	figure 3A
PMID:15800064	figure 3A
PMID:15800064	Figure 3 fypo/issues/2830
PMID:15800064	fig 2 a 2D
PMID:15800064	fig 2 a,c 2D
PMID:15800064	fig 1 C
PMID:15800064	figure 3A
PMID:15800064	Figure 4
PMID:15800064	figure 3A c
PMID:15800064	Figure 3 fypo/issues/2830
PMID:15800064	Figure 3 B fypo/issues/2830
PMID:15809031	inferred from direct physical interactions between tea4,tea1 and tea4,for3, plus tea4delta phenotype
PMID:15827087	Fig1. They describe cells as swollen in their middle region
PMID:15827087	Fig2A and data not shown
PMID:15827087	data not shown Non permissive temperature is 32°C and above
PMID:15827087	data not shown, permissive temperature 25°C
PMID:15827087	Fig1 permissive temperature is 25°C
PMID:15827087	Fig1. They describe cells as swollen in their middle region
PMID:15827087	Fig1
PMID:15827087	Fig1C Table 2
PMID:15827087	Fig1 Table 2
PMID:15827087	Table 2 This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	Table 2 This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	Table 2 This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	Table 2
PMID:15827087	Fig1B This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	data not shown
PMID:15827087	Fig2A,B
PMID:15827087	Fig2A,B
PMID:15827087	Fig2D
PMID:15827087	data not shown
PMID:15827087	Fig2A and data not shown
PMID:15827087	Fig3A,B Deletion of the talin domain suppresses the premature activation of bipolar growth in a cdc10 mutant in latA
PMID:15827087	Fig4D
PMID:15827087	data for cdc25-22 block not shown but see also Fig4A
PMID:15827087	Fig 4B
PMID:15827087	data not shown, same as Fig 4C
PMID:15827087	Fig 4C
PMID:15827087	Fig4B
PMID:15827087	data not shown
PMID:15837798	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15837798	The average number of MT bundles in mto2Δ cells (n = 1.3 ± 0.7 SD; Fig. 3 E) was significantly lower than in wild-type cells (3.6 ± 0.9)
PMID:15837798	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15857958	Fig. 4
PMID:15857958	Fig. 4
PMID:15857958	Fig. 2
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 7
PMID:15857958	Fig. 6
PMID:15857958	Fig. 6
PMID:15857958	Fig. 7
PMID:15857958	Fig. 7
PMID:15857958	Fig. 7
PMID:15857958	Fig. 7
PMID:15857958	Fig. 5
PMID:15857958	Fig. 7
PMID:15857958	Fig. 5 Synthetic phenotype
PMID:15857958	Fig. 5 Synthetic phenotype
PMID:15857958	Fig. 5 Synthetic phenotype
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:15857958	Fig. 7
PMID:15857958	Fig. 3 - background: cdc25-22
PMID:15857958	Fig. 2
PMID:15857958	Fig. 2 and Fig. 3 (cdc13 signal)
PMID:15857958	Fig. 3
PMID:15857958	Fig. 2
PMID:15857958	Fig. 3 rescue of FYPO:0000324
PMID:15857958	Fig. 3 - mad2 signal. background: cdc25-22
PMID:15857958	Fig. 5
PMID:15857958	Fig. 5
PMID:1588914	the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	Table 2 the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	multicopy pwis1 does not suppress cdc25-22 ts phenotype showing that wis1 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis2 does not suppress cdc25-22 ts phenotype showing that wis2 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis3 does not suppress cdc25-22 ts phenotype showing that spo12 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis4 does not suppress cdc25-22 ts phenotype showing that wis4 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis1 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis1 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis1 does not suppress cdc2-1w phenotype
PMID:1588914	multicopy pwis1 does not suppress cdc2-3w phenotype
PMID:1588914	multicopy pwis1 does not suppress wee1-50 ts phenotype
PMID:1588914	multicopy pwis1 does not suppress cdr1-34 phenotype
PMID:1588914	multicopy pwis1 does not suppress cdr2-69 phenotype
PMID:1588914	multicopy pwis2 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis2 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis2 does not suppress cdc2-1w phenotype
PMID:1588914	multicopy pwis2 does not suppress cdc2-3w phenotype
PMID:1588914	multicopy pwis2 does not suppress wee1-50 ts phenotype
PMID:1588914	multicopy pwis2 does not suppress cdr1-34 phenotype
PMID:1588914	multicopy pwis2 does not suppress cdr2-69 phenotype
PMID:1588914	multicopy pwis3 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis3 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis3 does not suppress cdc2-1w phenotype
PMID:1588914	multicopy pwis3 does not suppress cdc2-3w phenotype
PMID:1588914	multicopy pwis3 does not suppress wee1-50 ts phenotype
PMID:1588914	multicopy pwis3 does not suppress cdr1-34 phenotype
PMID:1588914	multicopy pwis3 does not suppress cdr2-69 phenotype
PMID:1588914	multicopy pwis4 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis4 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis4 does not suppress cdc2-1w phenotype
PMID:1588914	multicopy pwis4 does not suppress cdc2-3w phenotype
PMID:1588914	multicopy pwis4 does not suppress wee1-50 ts phenotype
PMID:1588914	multicopy pwis4 does not suppress cdr1-34 phenotype
PMID:1588914	multicopy pwis4 does not suppress cdr2-69 phenotype
PMID:1588914	see Table 2
PMID:1588914	see Table 2
PMID:1588914	see Table 2
PMID:1588914	See Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13
PMID:1588914	see Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13
PMID:1588914	Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	see Table 2
PMID:1588914	see Table 2
PMID:1588914	Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	see Table 2
PMID:1588914	the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	multicopy pwis1 does not suppress cdc25-22 ts phenotype showing that wis1 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis3 does not suppress cdc25-22 ts phenotype showing that spo12 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	see Table 2
PMID:1588914	see Table 2
PMID:1588914	see Table 2
PMID:1588914	see Table 2
PMID:1588914	data not shown
PMID:1588914	Table 3 pwis4 surpresses the elongated cell phenotype of win1-1
PMID:1588914	Table 3 cells are 30-50% longer than wild type
PMID:1588914	multicopy pwis4 does not suppress cdc25-22 ts phenotype showing that wis4 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis2 does not suppress cdc25-22 ts phenotype showing that wis2 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	multicopy pwis4 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis4 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis3 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis3 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis1 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis2 does not suppress cdc13-117 ts phenotype
PMID:1588914	multicopy pwis2 does not suppress cdc2-33 ts phenotype
PMID:1588914	multicopy pwis1 does not suppress cdc13-117 ts phenotype
PMID:15908586	Figure 2
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2A However, growth of the double mutant cells was completely inhibited by TSA.
PMID:15908586	Figure 2
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2 In cultures without TSA, the hrp1D cells grew slightly faster than wt cells as reported previously (48).
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2
PMID:15908586	Figure 2
PMID:15908586	Figure 2
PMID:15908586	Figure 2 Further examination of the IF samples revealed that hrp1D single and hrp1D hrp3D double mutants cells showed elevated numbers of asymmetric segregation (large and small nuclei) in late anaphase cells
PMID:15908586	Figure 3
PMID:15908586	Figure 3
PMID:15908586	Figure 3 There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells,
PMID:15908586	Figure 3 There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells,
PMID:15908586	The mis6-302 hrp1D double mutant had a reduced growth at 30 C as compared with the mis6-302 and hrp1D single mutants (Figure 3C).
PMID:15908586	The mis6-302 hrp1D double mutant had a reduced growth at 30 C as compared with the mis6-302 and hrp1D single mutants (Figure 3C).
PMID:15908586	dhIII transcripts were detectable in hrp1D dcr1D and dcr1D cells, but not in the wild-type and hrp1D cells (Figure 4E). The dhIII transcripts were more abundant in hrp1D dcr1D cells than in dcr1D cells consistent with the reduced silencing observed at dg-dh in hrp1D (Figure 1E). If transcripts read through in hrp1D from dh-dg into the central core region, then they should be readily detectable in the intervening imrIII region. However, imrIII transcripts were not observed in hrp1D cells. From these results, we concluded that the hrp1D mutant does not cause read through of dg-dh transcripts into the central core region. Hrp1 is present at the centromere in a cell
PMID:15908586	Figure 2
PMID:15908586	Figure 1
PMID:15908586	Figure 1
PMID:15908586	Figure 1
PMID:15908586	Figure 1
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	Figure 2A In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15915339	more sensitive than either single mutant
PMID:15915339	more sensitive than either single mutant
PMID:15915339	more sensitive than either single mutant
PMID:15915339	more sensitive than either single mutant
PMID:15920625	Proxy assay for hydrolase function used and IMP evidence for catalytic activity
PMID:15925945	assayed using AlF4- to mimic GTP-bound Gpa2
PMID:15933715	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	Spores deleted for etd1 (etd1D) germinated and accumulated multiple nuclei without septation, an identical phenotype to that of etd1-1 mutant cells under restrictive conditions (Figure 1C).
PMID:15933715	Figure 1A and B).
PMID:15933715	Figure 1A and B).
PMID:15933715	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	Etd1p-GFP, demonstrating that Etd1p interacts physically with Cdc15p. Similarly, Cdc15p was detected in anti-GFP immune complexes (data not shown). Thus, Etd1p may localise to the actomyosin ring by association with Cdc15p. (the anchor is using 2022 knowledge)
PMID:15933715	We therefore analysed the localisation of Etd1p-GFP in cdc8-110 mutant cells and found that, at the restrictive temperature of 361C, Etd1p never formed a ring (Figure 3B, upper panels).
PMID:15933715	We therefore analysed the localisation of Etd1p-GFP in cdc8-110 mutant cells and found that, at the restrictive temperature of 361C, Etd1p never formed a ring (Figure 3B, upper panels).
PMID:15933715	However, in etd1-1 mutant cells, the medial ring marked with Cdc15p-GFP seems to fail constriction. To bette
PMID:15933715	Etd1p-GFP failed to localise to the medial ring at the restrictive temperature. Instead, these mutant cells accumulated Etd1-GFP in a broad band at the plasma membrane overlying the site of cytokinesis (Figure 6A, upper panel,
PMID:15933715	missing annotation, we dont have that cdc7 is on old SPB in metaphase ... Cdc7p-GFP appeared at both SPBs at the initiation of mitosis and only at one SPB as cells progressed through anaphase until the completion of cell division.
PMID:15933715	suggesting that Etd1p is somehow necessary to maintain Spg1p activity during anaphase until the completion of cytokinesis
PMID:15933715	Under derepressed conditions ( thiamine), Etd1p overproduction generated elongated and multinucleate cells in both etd1-1 mutant and wild-type backgrounds (Figure 1D and data not shown). Thus, the phenotypic defect caused by an excess of Etd1p was identical to that produced by a deficiency of this protein, suggesting that Etd1p functions in a stoichiometric protein complex.
PMID:15933715	These results indicate that Etd1p is polyubiquitinated and degraded through the ubiquitin-dependent 26S-proteasome pathway.
PMID:15933715	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	In interphase cells, Etd1p-GFP was located at the cell cortex and was more concentrated at the cell tips (Figure 2A, cell 1).
PMID:15936270	DNS
PMID:15936270	On the other hand, oxidative stress by hydrogen peroxide, which also induces Spc1 activation [34], did not significantly affect Δwsh3 cells (data not shown).
PMID:15936270	DNS
PMID:15936270	highly bent or branched morphology (Figure 2a)
PMID:15936270	(p;enetrance for m 6B) highly bent or branched morphology (Figure 2a)
PMID:15936270	(p;enetrance for m 6B) highly bent or branched morphology (Figure 2a)
PMID:15936270	We also found that, even under the optimal growth condition, the Δspc1 mutation exacerbates the morphology defects of the Δtea1 mutant; the Δtea1 Δspc1 double mutant grown at 30oC in rich YES medium contain large fractions of significantly bent and branched cells (Figure 6D).
PMID:15936270	We also found that, even under the optimal growth condition, the Δspc1 mutation exacerbates the morphology defects of the Δtea1 mutant; the Δtea1 Δspc1 double mutant grown at 30oC in rich YES medium contain large fractions of significantly bent and branched cells (Figure 6D).
PMID:15936270	Cell polarity defects with bent and branched morphology were observed after shifting the Δspc1 mutant from 25oC to 36oC (Figure 6C).
PMID:15936270	(penetrance from 6B) nWe found that high osmolarity stress by 0.6 M KCl also promotes appearance of T-shaped cells in the Δtea1 strain, to the levels comparable to the Δwsh3 mutant (Figure 6B).
PMID:15936270	Δwsh3 cells, the cell-end localization of Pom1 was lost and Pom1-GFP often accumulated in vesicle-like structures in the cytoplasm (Figure 5D)
PMID:15936270	In contrast, most of Δwsh3 cells showed highly concentrated Tea1-GFP signals at one end, while the other end contained significantly less Tea1-GFP dots (Figure 5A, right panel)
PMID:15936270	The specific localization of Wsh3-GFP was lost in the Δtea1 mutant and the Wsh3-GFP signal was diffused throughout the cytoplasm (Figure 4A)
PMID:15936270	Wsh3-GFP was abrogated by a mutation in β- tubulin, nda3-KM311 [39] even at its permissive temperature, 30oC (Figure 3B, left).
PMID:15936270	Actin patches, which are localized to the growing tips of fission yeast cells [38], were detected mostly in one tip of the Δwsh3 cell (Figure 2C).
PMID:15936270	2c Δwsh3 cells were found to grow exclusively in a monopolar fashion.
PMID:15936270	Figure 2B).
PMID:15937127	fig3
PMID:15937127	fig 5B
PMID:15937127	fig 5B
PMID:15937127	fig2
PMID:15937127	fig 4D
PMID:15937127	fig 4D
PMID:15937127	fig 4D
PMID:15937127	fig 4D
PMID:15937127	Figure 3F-3
PMID:15937127	Figure 3F-3
PMID:15937127	Figure 3F-3
PMID:15937127	Figure 3F-3
PMID:15937127	DNA at the tips, telophase delay
PMID:15937127	fig 3C
PMID:15937127	fig3 B-2 (never seen in WT)
PMID:15937127	fig3 B-2 (1.1% WT)
PMID:15937127	fig3
PMID:15937127	fig2
PMID:15937127	fig2
PMID:15937127	fig2
PMID:15937127	fig2
PMID:15941470	Tev protease present; Cdc23 truncated
PMID:15941470	Tev protease present; Cdc23 truncated; cells not synchronized
PMID:15941470	Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus
PMID:15941470	Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus
PMID:15941470	Tev protease present; Cdc23 truncated
PMID:15941470	Tev protease present; Cdc23 truncated; N starvation/recovery synchronizes cells
PMID:15957215	from the catenated plasmid experiment (and failure to separate sisters)
PMID:15992541	thiamine absent; expression level lower than with endogenous promoter but higher than when repressed
PMID:15992541	promoter repressed
PMID:16055437	figure 1a
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	assayed in intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	assayed in intergenic regions
PMID:16079916	assayed in intergenic regions
PMID:16079916	assayed in intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16079916	protein-coding genes and intergenic regions
PMID:16085489	clp1 cytoplasmic localization not maintained during cytokinetic stress. cdc7 localization to SPB not maintained during cytokinetic stress
PMID:16087707	dependent on F-actin (assayed using Latrunculin A)
PMID:16087707	specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein
PMID:16087707	also from timing of localization to patches
PMID:16087707	dependent on F-actin (assayed using Latrunculin A)
PMID:16087707	also from timing of localization to patches
PMID:16087707	also from timing of localization to patches
PMID:16087707	also from synthetic lethality with myo1, timing of localization to patches, and vrp1 mutant phenotype
PMID:16087707	specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein
PMID:16087707	dependent on F-actin (assayed using Latrunculin A)
PMID:16096637	Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1.
PMID:16096637	both SPBs in early mitosis
PMID:16111942	Fig 1A appeared at theSPB upon conjugation of haploid cells, persisted untilthe onset of meiosis I, and disappeared thereafter
PMID:16111942	S1D
PMID:16111942	Interestingly, however, azygotic asci arising from diploid hrs1D cells did not show an apparent defect in spore formation (Figure S1D
PMID:16111942	arious exp, and ectoptic mitotic exprression
PMID:16111942	arious exp, and ectoptic mitotic exprression
PMID:16120966	can incorporate NTPs or dNTPs; changed from primase activity because not tested with unprimed template
PMID:16120966	distributive; substrate preference: small gaps with a 5′-phosphate group
PMID:16138082	From these results, we conclude that the F330A mutation significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyUb chains without significantly affecting monoUb binding.
PMID:16138082	From these results, we conclude that the F330A mutation significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyUb chains without significantly affecting monoUb binding.
PMID:16141239	endocytosis restricted to cell end
PMID:16141239	endocytosis restricted to cell end
PMID:16141239	Fig. 5A,B
PMID:16141239	endocytosis restricted to cell end
PMID:16141239	Fig. 5A,B
PMID:16141239	endocytosis restricted to cell end
PMID:16141239	Fig. 5A,B
PMID:16169489	knocked out in diploid. Can't tell if it vegetative or spore?
PMID:16169489	knocked out in diploid. Can't tell if it vegetative or spore?
PMID:16169489	27% of spores produce viable colonies
PMID:1617727	splicing of artificial construct with wt or mutated splice sites assayed in mutants
PMID:16199877	DNS
PMID:16199877	fig 3B
PMID:16199877	fig 3B
PMID:16199877	fig 3A
PMID:16199877	DNS
PMID:16199877	DNS
PMID:16199877	DNS
PMID:16199877	Fig 1A
PMID:16199877	Fig 1D
PMID:16199877	Fig 1E
PMID:16199877	Fig 1B
PMID:16199877	Fig 1D
PMID:16199877	Fig. S1C
PMID:16199877	Fig. S1C
PMID:16199877	S1B
PMID:16199877	S1A
PMID:16199877	Fig 5DE
PMID:16199877	Fig. 3C).
PMID:16199877	Fig. 3C).
PMID:16199877	Figur 4B
PMID:16199877	Figur 4B
PMID:16199877	Figur 4B
PMID:16199877	Figur 4B
PMID:16199877	fig4
PMID:16199877	Fig 3C
PMID:16199877	Fig 3C
PMID:16199877	Fig. 3C).
PMID:16199877	Fig. 3C).
PMID:16199877	fig 3B
PMID:16251348	fig 2c
PMID:16251348	fig3B
PMID:16252005	same as ddb1delta alone
PMID:16252005	same as cdt2delta alone
PMID:16252005	same as ddb1delta alone
PMID:16252005	same as pcu4delta alone
PMID:16252005	same as pcu4delta alone
PMID:16252005	same as cdt2delta alone
PMID:16252005	same as csn1delta alone
PMID:16252005	(regulation ) can also infer (IC) from GO:0030674
PMID:16262791	detectable in mutants that increase bound GTP:GDP ratio, implying that protein-protein interaction is GTP-dependent
PMID:16291723	.By contrast, Rgf3p-GFP was not detected at cell ends, only at the medial region of the cell (Fig. 4D). Furthermore, Rgf3p rings constricted (Fig. 4D, inset). These differences in pattern are illustrated in Fig. 4E
PMID:16291723	rgf3+ is essential
PMID:16291723	with lysis (these are not chained cells) (Fig. 2C).....cells septum degradation appeared to initiate at a single position around the cell circumference and the entire cell wall disappeared from this area
PMID:16291723	Fig. 1A. All cells lysed while undergoing division and the daughter cells remained attached to one another.
PMID:16291723	Fig. 1A. All cells lysed while undergoing division and the daughter cells remained attached to one another.
PMID:16291723	Fig. 1A.
PMID:16291723	(50 mM)
PMID:16291723	Both proteins localized to the division site(Fig. 4B,D). Rgf1p-GFP formed rings (Fig. 4B) late in mitosis as only cells containing segregated DNA masses contained them (data not shown and Fig. 7A)
PMID:16291723	`SYNTHETIC LETHAL
PMID:16291723	asked whether Rho1p was able to localize correctly to the medial region of the cell in the lad1-1 strain that we had shown lacks medially placed Rgf3p (Fig. 5C). We found that it did (Fig. 6B).
PMID:16291723	Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B). However, Rgf3p-Myc13 was clearly detectable in the absence of Ace2p suggesting that other factors cooperate with Ace2p to regulate rgf3+ expression.
PMID:16291723	Figue 5C
PMID:16291723	Consistent with a role in vesicular trafficking, gyp10 showed a strong negative genetic interaction with cells lacking the exocyst subunit, Exo70p (Wang et al., 2002) (Fig. 3C).
PMID:16291723	Fig. 3C
PMID:16291723	Rgf1p-GFP was also detected at cell ends (Fig. 4B).
PMID:16291723	Figue 5C
PMID:16291723	To determine whether Rgf3p production was controlled by Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B
PMID:16291723	To determine whether Rgf3p production was controlled by Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B
PMID:16291723	Rgf3p appears necessary to stimulate Rho1p-mediated activation of a glucan synthase crucial after septation for proper new cell-end formation.
PMID:16291723	Figue 5C Interestingly, overexpression of gpt10+ (Fig. 5G), but not rho1+ (data not shown) restored the localization of Rgf3 in lad1-1 cells at 36°C.
PMID:16291723	Fig. 3C
PMID:16291723	Fig. 3C
PMID:16291723	(Fig. 3C).
PMID:16291723	(Fig. 3C).
PMID:16291723	rgf3+ is essential
PMID:16291723	fig 6
PMID:16291723	Fig. 3C.
PMID:16291723	(Fig. 3B). Gyp10 localized to structures reminiscent of the endoplasmic reticulum (Broughton et al., 1997) when expressed from the low strength nmt81 promoter
PMID:16317005	activated_by CHEBI:15422 | inhibited_by CHEBI:16284
PMID:16317005	activated_by CHEBI:15422 | inhibited_by CHEBI:16284
PMID:16325576	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere co- hesion also appears defective since almost all sister chroma- tids eventually separate.
PMID:16325576	figure1
PMID:16325576	Surprisingly, moa1D cells displayed slightly stronger signals of Rec8-GFP at the cluster of centromeres (Figure 6A, GFP dots in the nucleus). Subsequent ChIP assays revealed that the association of Rec8 to chromatin increased nearly 2-fold in moa1D cells, particularly at the centromeric central core region (Figure 6B).
PMID:16325576	figure1
PMID:16325576	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere co- hesion also appears defective since almost all sister chroma- tids eventually separate.
PMID:16325576	Figure 2D. Although deletion of moa1+ thus causes a centro- mere-specific defect, recombination appears to promote re- ductional segregation in moa1D cells because the defect in monopolar attachment is lessened in diploid recombination- proficient meiosis compared to haploid meiosis or diploid
PMID:16325576	S2
PMID:16325576	S1
PMID:16325576	S1
PMID:16325576	figure2a
PMID:16325576	figure2b
PMID:16325576	figure1
PMID:16325576	figure1
PMID:16325576	Figure 2C
PMID:16325576	Figure 2C/3b
PMID:16325576	figure1
PMID:16325576	Figure 2C
PMID:16325576	Figure 2C
PMID:16325576	S1
PMID:16325576	S1
PMID:16325576	S1
PMID:16325576	S1
PMID:16325576	figure2a
PMID:16325576	This hypothesis makes the key prediction that the in- crease of Rec8 at the centromeric central core would de- pend on DNA replication. To test this possibility, we blocked DNA replication by adding HU to the synchronized meiotic culture and examined by ChIP the localization pattern of Rec8 (Figure 6C). Levels of central core-associated Rec8 were the same before (+HU) or after DNA replication (-HU) in wild-type cells. Remarkably, HU treatment abolished the increase of central core Rec8 in moa1D cells, and the pattern became similar to that in moa1+ cells (Figure 6C, +HU).
PMID:16325576	(VW, I am not sure that I captured this correctly?) A ChIP assay revealed that the association of Rec8(TEV) with chromatin is partly, but not entirely, impaired only at the centromeric central core region when cen-TEV protease is coexpressed (Figure 7C), suggesting that Rec8(TEV) is cleaved in a region-specific manner. We reasoned that, even if central core Rec8 is cleaved by cen-TEV protease, newly produced or free Rec8 complexes can be reloaded, resulting in the observed association of low levels of Rec8 at the central core. Nevertheless, such ‘‘turnover’’ of cohesin complexes would eventually abolish cohesion because newly associated cohesins do not reestablish cohesion after DNA replication.
PMID:16325576	Figure 5C However, the ChIP assay demonstrated intact lo- calization of Moa1 in rec8D meiotic cells (Figure 5C). Instead, we discovered that Moa1 localization was abolished in cells lacking CENP-C (Cnp3) (Figure 5C),
PMID:16325576	Figure 5C However, the ChIP assay demonstrated intact lo- calization of Moa1 in rec8D meiotic cells (Figure 5C). Instead, we discovered that Moa1 localization was abolished in cells lacking CENP-C (Cnp3) (Figure 5C),
PMID:16325576	fig 5A
PMID:16325576	induced
PMID:16394105	fig 3
PMID:16394105	fig 4
PMID:16394105	fig 4
PMID:16394105	fig 4
PMID:16394105	fig 4
PMID:16394105	fig 4
PMID:16394105	both the growth and shrinkage rates were decreased down to 33 and 60%, respectively,
PMID:16394105	both the growth and shrinkage rates were decreased down to 33 and 60%, respectively,
PMID:16394105	Figure 9
PMID:16394105	Figure 8 D
PMID:16394105	Figure 8 D
PMID:16394105	Figure 8 D
PMID:16394105	Figure 8 C
PMID:16394105	Figure 8 AB
PMID:16394105	fig 7 a
PMID:16394105	fig 7 a
PMID:16394105	fig 7 b
PMID:16394105	Figur 6 B,C
PMID:16394105	Figur 6 B,C
PMID:16394105	table 4
PMID:16394105	table 4
PMID:16394105	table 4
PMID:16394105	table 4
PMID:16394105	table 4
PMID:16394105	fig 5 e
PMID:16394105	fig 5 d
PMID:16394105	fig 4
PMID:16394105	fig 3
PMID:16394105	morphology
PMID:16394105	Figure 1 B
PMID:16394105	Figure 1 B
PMID:16394105	supp data
PMID:16394105	Figure 1 B
PMID:16394105	Figure 1 B
PMID:16394105	Figure 1 B
PMID:16407242	higher protein level than in absence of HU, in both wild type and mutant
PMID:16407242	higher protein level than in absence of HU, in both wild type and mutant
PMID:16421249	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	Figure 4A, the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1􏰁;
PMID:16421249	positive regulation
PMID:16421249	(Figure 6B) GS activity increased during rgf1􏰃 overex- pression. This activity was fourfold higher than that ob- served in the wild-type strain
PMID:16421249	positive regulation
PMID:16421249	Figure 3A, As shown in Figure 3A, the rgf1 mutants showed a defect in actin organization in that they organized actin patches mostly at one end of the cell only
PMID:16421249	Figure 3A at cell division site
PMID:16421249	(Figure 3B) 55% of cdc10-129 cells displayed bipolar growth, whereas only 4% of cdc10-129 rgf1􏰁 cells were bipolar
PMID:16421249	rescue of multiseptate, swollen
PMID:16421249	Figure 7A,
PMID:16421249	Figure 7A, only a moderate expres- sion of bgs4􏰃 restored growth of an rgf1􏰁 mutant in the presence of the antifungal agent
PMID:16421249	Figure 7A,
PMID:16421249	Figure 4A, the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1􏰁;
PMID:16421249	Figure 4A, the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1􏰁;
PMID:16421249	Figure 4A, the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1􏰁;
PMID:16421249	increased gtp-bound gtpase (active)
PMID:16421249	DNS
PMID:16421249	Figure 7A,
PMID:16421249	Figure 4A, the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1􏰁;
PMID:16421249	Figure 4A, the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1􏰁;
PMID:16421249	(Figure 2A The resulting strain, rgf1􏰃, showed a slow growth pattern at 28°C
PMID:16421249	decreased gtp-bound gtpase (active)
PMID:16421249	Figure 4c Lack of Rga1p produces small colonies and the cells show a swollen, multiseptated or branched shape; a pheno- type similar to that seen in cells in which Rho1p is excessively activated
PMID:16421249	(Figure 2A The resulting strain, rgf1􏰃, showed a slow growth pattern at 28°C
PMID:16421249	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	Figure 8A
PMID:16421249	Figure 8A
PMID:16421249	rga1􏰁 cells were severely impaired for growth, whereas rgf1􏰁rga1􏰁 exhibited a better growth pat- tern and resembled rgf1􏰁 cells.
PMID:16421249	Figure 2A
PMID:16421249	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	Figure 8A
PMID:16421249	Figure 8A
PMID:16421249	Figure 7C,
PMID:16421249	positive regulation
PMID:16421249	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	positive regulation
PMID:16421249	this being consistent with the idea that rgf1􏰃 could act in the same pathway as rho1􏰃 (Figure 4A). Figure 5. The amount of active Rho1p increased considerably in the strain overexpressing Rgf1p compared with the wild- type strain. Moreover, only a minor amount of GTP-Rho1p was detected in the strain lacking Rgf1p.
PMID:16453724	with re-replication
PMID:16453724	ABOLISHED SEPARATION
PMID:16453724	ABOLISHED SEPARATION
PMID:16453733	suppresses cdc2-33 temperature sensitive phenotype at 32
PMID:16453733	suppresses temperature sensitive phenotype of cdc2-33 at 32
PMID:16453733	23% 2 spore asci when selfed
PMID:16453733	suppresses cdc2-M26 temperature sensitive phenotype at 32
PMID:16453733	suppresses cdc2-56 temperature sensitive phenotype at 35
PMID:16453733	suppresses cdc2-L7 temperature sensitive phenotype at 32
PMID:16453733	suppresses cdc2-M26 temperature sensitive phenotype at 32
PMID:16453733	suppresses cdc2-56 temperature sensitive phenotype at 35
PMID:16453733	suppresses cdc2-L7 temperature sensitive phenotype at 32 and weakly at 35
PMID:16453733	suppresses cdc2-M55 temperature sensitive phenotype at 32
PMID:16453733	increased expression gives increased % 2 spored asci
PMID:16453733	when selfed produces 76% 2 spore asci at 25 compared to 5% in suc1+ background
PMID:16453733	suppresses cdc2-M55 temperature sensitive phenotype at 32
PMID:1645660	inhibited_by zinc(2+) activated_by magnesium(2+)
PMID:16467379	localization dependent on F-actin (assayed using Latrunculin A)
PMID:16481403	emtoc
PMID:16481403	from both ends
PMID:16481403	Fig1 D (actually 2 bundles)
PMID:16481403	fig 1c
PMID:16481403	igure 5B
PMID:16481403	fig1
PMID:16481403	from both ends
PMID:16483313	isn't really processing, cleavage
PMID:16489217	maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.
PMID:16537923	genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed
PMID:16537923	genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed
PMID:16537923	genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed
PMID:16537923	aerobic conditions
PMID:16541024	Supplementary Fig. S2a
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 4b
PMID:16541024	Fig. 2a
PMID:16541024	fig.1
PMID:16541024	Fig. 4
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 4b
PMID:16541024	this is an inference, but almost certainly true based on the genetics
PMID:16541024	Fig. 4
PMID:16541024	Fig. 4
PMID:16541024	Notably, we detected only a single combination of PP2A subunits associated with SpSgo1, namely SpPaa1A–SpPar1B′–SpPpa2C
PMID:16541024	Fig. 2a
PMID:16541024	Fig. 2a
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 2a
PMID:16541024	Fig. 2b
PMID:16541024	fig.1
PMID:16541024	fig.1
PMID:16541024	Supplementary Fig. S2a
PMID:16541024	Supplementary Fig. S2a
PMID:16541024	Supplementary Fig. S2a
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 4b
PMID:16541024	Fig. 2b
PMID:16541024	Fig. 4b
PMID:16541024	Supplementary Fig. S2a
PMID:16541025	(Supplementary Fig. 7).
PMID:16541025	Fig. 5a
PMID:16541025	Fig. 5b however, it colocalizes with Sgo1 at centromeres during meiosis I
PMID:16541025	dns
PMID:16541025	(Fig. 5b).
PMID:16541025	We found that, like sgo1D cells, par1D cells mostly lost centromeric Rec8 localization at this stage (Fig. 5d)
PMID:16541025	(Supplementary Fig. 7)...both of these mutant cell types showed precocious centromeric dissociation after meiosis I, and random chromosome segregation following meiosis II
PMID:16541025	(Supplementary Fig. 7)
PMID:16541025	(Supplementary Fig. 7)
PMID:16541025	Fig. 5a
PMID:1655416	ADD MODIFIED FORMS
PMID:1655416	transient
PMID:1655416	is delayed but the delay is reduced compared to the single mutant
PMID:1655416	figure 10 C
PMID:1655416	figure 10 C
PMID:1655416	LENgth
PMID:1657594	fig 6
PMID:1657594	fig 6
PMID:16585273	Fig. 4 E
PMID:16611237	indicates a G2 delay
PMID:16618806	cells otherwise haploid
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	effect of mutation in substrate Cds1 molecule
PMID:16618806	effect of mutation in substrate Cds1 molecule
PMID:16618806	induced dimerization increases Cds1 autophosphorylation without prior phosphorylation on T11
PMID:16618806	abolished dimerization in kinase-dead cds1-D312E
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	has output PR:000037300
PMID:16618806	cells otherwise haploid
PMID:16618806	cells otherwise haploid
PMID:16618806	residue T11
PMID:16618806	residue T11
PMID:16618806	residue T11
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	effect of mutation in substrate Cds1 molecule
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	assayed substrate myelin basic protein
PMID:16618806	residue T11
PMID:16618806	residue T11
PMID:16618806	residue T11
PMID:16618806	assayed substrate myelin basic protein
PMID:16624923	membrane anchor
PMID:16624923	cortical location/microtubules did not show a lateral interaction with the cell corte/Ninety-two percent of microtubules in num1D cells underwent catastrophe Figure 3.—Nuclear behavior in wild-type and num1D zy- gotes. Chromosomal DNA in zygotes (JY450 or JV627) was stained with Hoechst 33342 and monitored. The numbers on the left indicate time in minutes. Microtubules were visu- alized simultaneously by GFP-tagged a-tubulin. Stained DNA is shown in red, and GFP fluorescence in green. Bar, 5 mm. within 2 min of contacting the cell cortex (n 1⁄4 59). In contrast, 80% of microtubules that interacted with the cell cortex laterally in wild-type cells remained at the cell ends for .2 min (n 1⁄4 15).
PMID:16682348	(G1 arrested cells)
PMID:16682348	G1 arrested cells
PMID:16687577	fig4
PMID:16687577	different pathway
PMID:16687577	fig7
PMID:16687577	Figure 6 asymetric during cytokinesis delay
PMID:16687577	Figure 5, D and E for maintenance of the actomyosin ring in response to cytokinesis delay upon
PMID:16687577	fig 1
PMID:16687577	Figure 5, D and E for maintenance of the actomyosin ring in response to cytokinesis delay upon
PMID:16687577	fig 5 (during ectopic SIN activation)
PMID:16687577	fig 5
PMID:16687577	fig 5
PMID:16687577	different pathway
PMID:16687577	fig 1
PMID:16687577	fig 2
PMID:16687577	fig 2
PMID:16687577	fig 3
PMID:16687577	fig 3
PMID:16687577	fig4
PMID:16687577	fig4
PMID:16687577	fig 1
PMID:16738311	homozygous diploid
PMID:16738311	32 °C
PMID:16738311	homozygous diploid
PMID:16738311	homozygous diploid
PMID:16738311	homozygous diploid
PMID:16738311	centromere outer repeat transcripts
PMID:16738311	nda3-KM311 allele also in genotype, but used as assay tool here
PMID:16738311	homozygous diploid
PMID:16738311	32 °C
PMID:16738311	32 °C; better than without cid12delta
PMID:16738311	32 °C
PMID:16738311	32 °C; same as without cid12delta
PMID:16738311	32 °C
PMID:16738311	32 °C
PMID:16738311	32 °C
PMID:16738311	26 °C
PMID:16738311	32 °C
PMID:16738311	26 °C
PMID:16738311	32 °C; very slightly worse than without cid12delta
PMID:16775007	Figure 7A
PMID:16775007	Fig2A
PMID:16775007	Figure 4C
PMID:16775007	Fig 2A
PMID:16775007	Fig 1A
PMID:16775007	Figure 5, A and B
PMID:16775007	fig 5D
PMID:16816948	pulse/chase
PMID:16822282	caspase
PMID:16822282	caspase
PMID:16822282	fig3A
PMID:16822282	fig3A
PMID:16822282	caspase
PMID:16822282	fig3A
PMID:16822282	fig3A
PMID:16822282	fig3A
PMID:16822282	fig3A
PMID:16822282	fig3A
PMID:16823445	Abstract We propose that Mei2 turns off the DSR-Mmi1 system by sequestering Mmi1 to the dot and thereby secures stable expression of meiosis-specific transcripts.
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	assayed in diploid
PMID:16823445	assayed in diploid
PMID:16823445	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05)
PMID:16823445	assayed in diploid
PMID:16824200	requires intact mitotic spindle, as shown by cold-depolymerizing microtubules and nda3 mad2 double mutant phenotype
PMID:16857197	might be abolished. Sometimes you see diploidization.
PMID:16884933	PHEROMONE TERM
PMID:16914721	microarray data shows 111 genes affected
PMID:16914721	microarray data shows 111 genes affected
PMID:16914721	microarray data shows 111 genes affected
PMID:16914721	microarray data shows 111 genes affected
PMID:16914721	assayed using ade6-M26
PMID:16920624	In contrast, the Dis16E mutant, which shows the synthetic lethality with Dmtc1, dimin- ished signals along the metaphase spindle. Thus, there is a correlation between the affinity for microtubules of the mutant versions of Dis1 and these mutants’ ability to rescue the Dmtc1 defect.
PMID:16920624	fig6
PMID:16920624	Because Dis1WT, Dis16A, and Dis16E all associated with anaphase SPBs, this as- sociation was independent of modification of the mole- cule on the Cdc2 phosphorylation sites.
PMID:16920624	UNPHOSPHORYLATED. In anaphase, Dis1WT-GFP signals abruptly increased along the spindle and at the SPBs despite being absent from the central zone.
PMID:16920624	Curiously, bent spindles were observed in late anaphase of 53 of 121 Dis16A cells in movies, whereas only 18 of 104 Dis1WT and ten of 127 Dis16E cells examined showed the bent spindle (Figure S1D).
PMID:16920624	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (ana- phase B) on each of the 30 movies of Dis1WT, Dis16A, and Dis16E strains indicated that the timing of mitosis did not seem to be affected by any mutations because mea- sured differences were within the boundaries of experi- mental error (Figure S1C)
PMID:16920624	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (ana- phase B) on each of the 30 movies of Dis1WT, Dis16A, and Dis16E strains indicated that the timing of mitosis did not seem to be affected by any mutations because mea- sured differences were within the boundaries of experi- mental error (Figure S1C)
PMID:16920624	protein localized to spindle (also a child of mislocalized protein)
PMID:16920624	Figure 2D. The double mutant mis12 Dis16A failed to produce colonies at 33
PMID:16920624	Figure 2A.
PMID:16920624	These results established that phosphorylation of Dis1 by Cdc2 is required for the high-fidelity segregation of a minichromosome. (A little bit of curator licence here)
PMID:16920624	Figure 2C. The loss rate in Dis16E was lower than Dis16A and slightly higher than that in the wild-type. (The Dis16E mutant appears to mimic at least partially the Cdc2-phosphory- lated form of Dis1)
PMID:16920624	Figure 2C. .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild- type Dis1 integrant.
PMID:16920624	Figure 2C. .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild- type Dis1 integrant.
PMID:16920624	Figure 2C. The loss rate of CN2 minichromosome in Dis16A was much higher than that of the wild-type integrant...
PMID:16920624	Figure 2B. The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type.
PMID:16920624	Figure 2B. The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type.
PMID:16920624	Figure 2B.
PMID:16920624	Figure 2B.
PMID:16920624	Figure 2B.
PMID:16920624	PHOSPHORYLATED. Fig3A The Dis1WT-GFP signals are seen as the kinetochore dots in metaphase. AND 4b
PMID:16920624	Figure 2D. However, the double mutant mis12 Dis16E could form colonies at 33􏰀C.
PMID:16920624	Figure 2D. whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
PMID:16920624	figure 1B.
PMID:16920624	figure 1B.
PMID:16920624	Figure 1C
PMID:16920624	Figure 2A.
PMID:16920624	Figure 2D. whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
PMID:16921379	sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.
PMID:16921379	in complex with Swi5
PMID:16921379	sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.
PMID:16921379	in complex with Sfr1
PMID:16963626	6b
PMID:16963626	Consistently, mutations in the php3􏰀 - and php5􏰀 -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:16963626	Consistently, mutations in the php3􏰀 - and php5􏰀 -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:16963626	using the cross-linking agent EGS, we found that the Php4 protein associates with the Php2/Php3/Php5 complex
PMID:1699136	figure2
PMID:1699136	figure 1c
PMID:1699136	figure 1c and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b)
PMID:1699136	figure 1c and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b)
PMID:17004072	table 2
PMID:17004072	figure 5 b
PMID:17004072	figure 2a
PMID:17004072	figure 2a
PMID:17005570	fig3
PMID:17005570	fig 5 A
PMID:17005570	fig 5 C
PMID:17005570	fig 1
PMID:17005570	fig 1 F
PMID:17005570	fig3
PMID:17005570	fig 1 d
PMID:17005570	fig 1 c
PMID:17005570	fig 1 b
PMID:17005570	fig 1 b
PMID:17005570	fig3
PMID:17005570	fig 1
PMID:17005570	fig 6 B, lane 3
PMID:17005570	fig 1
PMID:17005570	fig 1
PMID:17005570	fig 6 A, lane 9
PMID:17005570	fig3
PMID:17005570	fig 1 f
PMID:17005570	fig 1 f
PMID:17005570	fig3
PMID:17005570	fig3
PMID:17005570	fig 6 B, lane 9
PMID:17005570	fig 7 A
PMID:17005570	Fig 1c lane 9
PMID:17005570	fig 1
PMID:17005570	fig 1
PMID:17005570	fig 7 A
PMID:17005570	fig 1
PMID:1703321	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	cdc25 over expressed from the constitutive ADH promoter. Data not shown
PMID:1703321	data not shown
PMID:1703321	Figure 4D phospho amino acid analysis
PMID:1703321	data not shown
PMID:1703321	Figure 4D phospho amino acid analysis
PMID:1703321	I'm sure this has already been annotated. But previous annotations didn't come up, should they?
PMID:1703321	Also think this is previously annotated
PMID:1703321	Figure 4D phospho amino acid analysis
PMID:1703321	Figure 4 phospho amino acid analysis
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	These 4 proteins share homology with the S. cerevisiae DASH com- plex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	These 4 proteins share homology with the S. cerevisiae DASH com- plex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	These 4 proteins share homology with the S. cerevisiae DASH com- plex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	These 4 proteins share homology with the S. cerevisiae DASH com- plex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 tem- perature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 tem- perature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4),
PMID:17035632	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4),
PMID:17035632	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4),
PMID:17035632	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4),
PMID:17035632	Sgo1 protein signal intensity increased in two steps (52 and 20 min before the metaphase–anaphase transition of meiosis I) in a way similar to the NMS (Ndc80- Mis12-Spc7) complex proteins (Figure 7B).
PMID:17035632	Sgo1 protein signal intensity increased in two steps (52 and 20 min before the metaphase–anaphase transition of meiosis I) in a way similar to the NMS (Ndc80- Mis12-Spc7) complex proteins (Figure 7B).
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17036054	fig1b
PMID:17036054	Supplement
PMID:17036054	figure 1a
PMID:17036054	figure 1a
PMID:17036054	figure 1a
PMID:17036054	fig1b
PMID:17036054	fig1b
PMID:17036054	fig1b
PMID:17036054	fig1b
PMID:17036054	figure 1a
PMID:17036054	figure 1a
PMID:17036054	figure 1a
PMID:17036054	figure 1a
PMID:17036054	figure 1a
PMID:17038309	binds both circular and linear DNA fragments
PMID:17038309	i) xlf1 deletion is epistatic with lig4 deletion ii) IR sensitivity during spore state and inability to ligate linearised plasmids during vegetative state
PMID:17039252	especially during S and G2 phases
PMID:17039252	especially during S and G2 phases
PMID:17039252	especially during S and G2 phases
PMID:17039252	especially during S and G2 phases
PMID:17046992	cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature
PMID:17046992	TORC1 senses nutrients and pushes cells into the next cell cycle. Removing TORC1 activity, you get a buildup of rum1 and srw1 which inhibit G1/S
PMID:17046992	cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature
PMID:17085965	localization depends on microtubule cytoskeleton, as determined by treatment with carbendazim (methyl 2-benzimidazolecarbamate; MBC), and on actin cytoskeleton, as determined by treatment with latrunculin B or cytochalasin D
PMID:17112379	25 degrees
PMID:17112379	30 degrees
PMID:17112379	30 degrees
PMID:17112379	25 degrees
PMID:17112379	25 degrees
PMID:17121544	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	Figure 1B
PMID:17121544	Figure 1B
PMID:17121544	at 30 degrees// Tor1 becomes necessary for cell growth when Tor2 function is compromised.
PMID:17121544	at 30 degrees
PMID:17121544	tor1∆tor2 -19 showed only the 2C peak, and no 1C peak appeared at 36 °C
PMID:17121544	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	s expected, these double mutants behaved the same as tor1∆rhb1+o/e cells, in which growth was restored under stress conditions (the fourth row).
PMID:17121544	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	70% of ts the tor2 -13 cells committed sexual development to ts form zygotes and spores (Fig. 3B,C)
PMID:17130122	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17130122	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17130122	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17130122	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17178839	fig 4B
PMID:17178839	fig 1B
PMID:17178839	fig 1B
PMID:17178839	fig 1A
PMID:17178839	fig 1A
PMID:17178839	fig 4A
PMID:17178839	fig 4A
PMID:17178839	fig 4B
PMID:17178839	fig 4C
PMID:17178839	not sure if this is correct....
PMID:17178839	not sure if this is correct....
PMID:17178839	Fig. 4D
PMID:17178839	fig 1A
PMID:17178839	fig 1B
PMID:17178839	fig 1B
PMID:17178839	fig 1B
PMID:17178839	fig 1c/d
PMID:17178839	fig 2 a/b
PMID:17178839	fig 2 a/b
PMID:17178839	fig 2 a/b
PMID:17178839	fig 3A
PMID:17178839	fig 3B
PMID:17178839	fig 3c
PMID:17178839	fig 3C
PMID:17178839	fig 4A
PMID:17178839	fig 4A
PMID:17190600	H4K20me2 modified histone binding
PMID:17190600	H4K20me2 modified histone binding
PMID:17190600	H4K20me2 modified histone binding
PMID:17192844	The wildtype cross yielded 81 ± 7.5% viable spores, the pnu1Δ cross 82 ± 3%. As far as tested, no change of meiosis and recombination was detected in mutants abolishing the function of the Pnu1 (End1) nuclease.
PMID:17211518	proteasomal
PMID:17213188	binding by Pab2
PMID:17222800	25S rRNA positions 2304, 2497
PMID:17289569	by TGS
PMID:17289569	4B However, defect in RNAi pathway had no impact on Ccq1 localization
PMID:17289569	part of tgs
PMID:17289569	(Figure 4C), Levels of Clr3 and Mit1 were dramati- cally reduced at subtelomeres in swi6 mutant strains
PMID:17289569	In contrast to hetero- chromatic loci, SHREC recruitment to euchromatic sites was unaffected in the absence of Swi6, as shown by Clr3 and Mit1 localization at a locus encoding a noncoding RNA and an intergenic region (Figure 4D).
PMID:17289569	In contrast to hetero- chromatic loci, SHREC recruitment to euchromatic sites was unaffected in the absence of Swi6, as shown by Clr3 and Mit1 localization at a locus encoding a noncoding RNA and an intergenic region (Figure 4D).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	pericentromeric repeats, the silent mat locus, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	The role of SHREC in transcriptional silencing could be decoupled from the cis-PTGS function of the RNAi machinery since impaired SHREC had no effect on the localization of RITS Agol subunit at heterochromatin (Figure 5D).
PMID:17289569	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
PMID:17289569	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
PMID:17289569	6B
PMID:17289569	(Figure 6B)
PMID:17289569	6B
PMID:17289569	6B
PMID:17289569	by TGS
PMID:17289569	by TGS
PMID:17289569	by TGS
PMID:17289569	6D
PMID:17289569	6D
PMID:17289569	6E
PMID:17289569	part of tgs
PMID:17289569	4B clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1,
PMID:17289569	4B clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1,
PMID:17289569	4B while the levels of Ccq1 at telomeres, relative to those in wild-type cells, were unchanged in clr3D cells but decreased in taz1D
PMID:17289569	4B while the levels of Ccq1 at telomeres, relative to those in wild-type cells, were unchanged in clr3D cells but decreased in taz1D
PMID:17289569	4B
PMID:17289569	4B We found that Clr3 localization at telomere ends was completely abolished in cells defective in both Taz1 and RNAi pathways.
PMID:17304223	foci disappear in HU; without HU foci appear but with abnormal dynamics
PMID:17304223	foci disappear in HU; without HU foci appear but with abnormal dynamics
PMID:17307401	same as mus81delta alone
PMID:17307401	same as mus81delta alone
PMID:17307401	worse than either single mutant
PMID:17307401	worse than either single mutant
PMID:17307401	worse than either single mutant
PMID:17307401	worse than either single mutant
PMID:17307401	worse than either single mutant
PMID:17307401	same as mus81delta alone
PMID:17307401	same as mus81delta alone
PMID:17307401	worse than either single mutant
PMID:17307401	worse than either single mutant
PMID:17307401	worse than either single mutant
PMID:17317928	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17339332	same pathway
PMID:17352737	anaphase, elongating beyond cell end resulting in long curved spindle, requested
PMID:17363370	Fig. 4, A and B
PMID:17363370	Fig. 4, A and B
PMID:17363370	Fig. 4, A and B
PMID:17363370	Fig. 4, A and B
PMID:17363370	fig 5D
PMID:17363370	Fig. 1C
PMID:17363370	Fig 1D
PMID:17363370	Fig 1D
PMID:17363370	Fig 1D
PMID:17363370	Fig 1D
PMID:17363370	Fig 1D
PMID:17363370	HULC revealed that slower migrating band representing ubH2B was missing in cells lacking either Bre1 homologs (i.e. Rfp1 or Rfp2) or Shf1. These analyses suggest that components of HULC are required for ubiquitination of H2B.
PMID:17363370	HULC revealed that slower migrating band representing ubH2B was missing in cells lacking either Bre1 homologs (i.e. Rfp1 or Rfp2) or Shf1. These analyses suggest that components of HULC are required for ubiquitination of H2B.
PMID:17363370	figur 2b
PMID:17363370	figur 2b
PMID:17363370	figur 2b
PMID:17363370	figur 2b
PMID:17363370	figur 2b
PMID:17363370	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	Overexpression of Rhp6 abro- gates silencing of the otr1::ura4􏰁 reporter, resulting in the loss of cell viability on medium supple- mented with FOA (Fig. 3A
PMID:17363370	Interestingly, levels of trim- ethylated H3K9 (H3K9me3) were significantly reduced, although the levels of monomethylated H3K9 (H3K9me1) were increased at the dg repeat element and otr1::ura4􏰁 (Fig. 3B).
PMID:17363370	Interestingly, levels of trim- ethylated H3K9 (H3K9me3) were significantly reduced, although the levels of monomethylated H3K9 (H3K9me1) were increased at the dg repeat element and otr1::ura4􏰁 (Fig. 3B).
PMID:17363370	(supplemental Fig. 2
PMID:17363370	Fig. 4, A and B
PMID:17363370	Fig. 4, A and B
PMID:17363370	Interestingly, the H2B-K119R mutation sig- nificantly enhanced silencing of the otr1::ura4􏰁 (Fig. 5A),
PMID:17363370	Fig. 1C
PMID:17363370	Fig. 1C
PMID:17363370	fig 5D
PMID:17363370	Fig. 1C
PMID:17434129	also from localization and phenotypes
PMID:17434129	also from localization and phenotypes
PMID:17434129	data not shown
PMID:17434129	TEL2L only
PMID:17434129	data not shown
PMID:17434129	TEL2L only
PMID:17434129	TEL2L only
PMID:17440621	they only show that this is part of a complex that demethylates H3K9 so there is a chance it is not active?
PMID:17442892	inferred from the fact growth is impaired in the double mutatn spc7-23/mad2 OR spc7-23/mph1 are growth impaired, so assumption is that spindle checkpoint is active in mutant
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17450151	sense strand
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17450151	sense strand
PMID:17450151	bulk antisense transcripts
PMID:17450151	bulk antisense transcripts
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	"chromatin binding shown, and regulation of transcription shown. no evidence for dna binding BUT later paper by akayama and Toda state that "" Ams2 directly binds a consensus ""AACCCT-box"" that exists in the 5' franking regions of these histone genes."" and says that ams2 is sole responsible TF + cites this paper."
PMID:17452352	"chromatin binding shown, and regulation of transcription shown. no evidence for dna binding BUT later paper by akayama and Toda state that "" Ams2 directly binds a consensus ""AACCCT-box"" that exists in the 5' franking regions of these histone genes."" and says that ams2 is sole responsible TF + cites this paper."
PMID:17452352	fig6
PMID:17452352	fig6
PMID:17452352	fig6
PMID:17452352	fig6
PMID:17452352	5c
PMID:17452352	5c
PMID:17452352	5c
PMID:17452352	5c
PMID:17452352	5c
PMID:17452352	5c
PMID:17452352	bet this is a term Val hates :p
PMID:17452352	5a
PMID:17452352	5a
PMID:17452352	5d
PMID:17452352	5d
PMID:17452352	5d
PMID:17452352	5d
PMID:17452352	5d
PMID:17452352	5d
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452352	fig7
PMID:17452625	regulates binding by myosin; assayed in vitro using rabbit actin and unspecified myosin motor domain
PMID:17486116	assayed using bub1
PMID:17510629	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17510629	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17510629	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17531813	Fig 1C
PMID:17531813	Fig 1B
PMID:17531813	The same experiment was repeated, but HU was added at the time of release, allowing cells to progress through mitosis and stall after initiation of DNA replication. In that case, Cdc2 tyrosine 15 phosphorylation reappeared after 100 min and increased further with time. Cig2 remained present at a high level, indicating that the Cdc2-Cig2 com- plex was inhibited (Figure 5B)
PMID:17531813	2A
PMID:17531813	2A; during mitotic DNA replication checkpoint
PMID:17531813	Fig 1C
PMID:17531813	Fig 6B
PMID:17531813	Fig 6B
PMID:17531813	Fig 6 B
PMID:17531813	Fig 5B
PMID:17531813	Fig 5B
PMID:17531813	Fig5A cdc18 disappears at the end of S-phase in cig2+ strain and accumulates in the absence of cig2
PMID:17531813	Fig 4D In the absence of rad26, cdc18 is unable to stabilise rad3 on chromatin
PMID:17531813	Fig 4A
PMID:17531813	Fig 4A
PMID:17531813	Fig 4 A
PMID:17531813	Fig 4 A
PMID:17531813	Fig3 top 2 two panels (ve jacky syuggested Presence of stalled replication forks after DNA checkpoint inactivation, i just used normal initiation Figure 3. Replication Structures Are Not Lost When Cdc18 Is Depleted)
PMID:17531813	Figure 2D top of lower panel.
PMID:17531813	Figure 2C lower panel. cds1 is no longer phosphorylated because rad3 is absent in absence of cdc18
PMID:17531813	Figure 2B upper right panel. In the cytosol rad3 is present in absence of cdc18
PMID:17531813	Figure 2B lower right panel. rad3 is not present in the chromatin fraction in the absence of cdc18
PMID:17531813	Fig 1C
PMID:17531813	Fig 1C
PMID:17531813	Fig 1C (vw data not shown, but assume are elongated)
PMID:17531813	Fig 1B
PMID:17531816	ESTABLISHMENT. The reestablishmentof centromeric heterochromatin was then monitored after reintroduction of clr4+. Addition of clr4+to tas3+ cells allowed efficient establishment of heterochromatinand silencing of the cen::ura4+ transgene atdg (Figure 3A). In marked contrast, on reintroduction ofclr4+, cells expressing tas3WG failed to silence the cen::ura4+ reporter
PMID:17531816	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
PMID:17531816	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
PMID:17531816	Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin
PMID:17531816	We have previously demonstrated that Tas3 binds directly to Chp1 (Petrie et al., 2005). In addition, Tas3 binds to Ago1 and this interaction is independent of Chp1 (Figure 1A). Thus, Tas3 forms a bridge linking the Chp1 chromodomain protein to Ago1.
PMID:17531816	(dg repeat) Centromeric transcripts were only marginally elevated in tas3WG cells, in marked contrast to the 10- to 20-fold accumulation of transcripts in tas3-, dcr1-, or ago1-null cells (Figure 2B).
PMID:17531816	Consistent with these findings, tas3WG mutant cells showed no defects in chromosome segregation (Table S2).
PMID:17531816	Chromatin immunoprecipitation (ChIP) analyses showed that Ago1 was indeed localized at centromeres in the tas3WG mutant, a
PMID:17531816	the double mutant (tas3WG, F276Aago1) displayed markedly elevated levels of total centromeric transcripts (Figure 2E), similar to an ago1 null.
PMID:17531816	Further, centromeric siRNAs were similarly abundant in tas3WG and tas3+ cells (Figure 2D).
PMID:17531816	......as were Chp1 and the mutant Tas3WG protein (Figure 2C).
PMID:17531816	F276A-ago1 (Figure S3B) caused a slight defect in silencing of the dg cen::ura4+ reporter (Figure S3C).
PMID:17531816	......as were Chp1 and the mutant Tas3WG protein (Figure 2C).
PMID:17531816	Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin
PMID:17538026	fig 3a
PMID:17538026	igure 3, B and D
PMID:17538026	figure 3, B and D
PMID:17538026	fig1 a
PMID:17538026	fig 4
PMID:17538026	table 2
PMID:17538026	fig1 a
PMID:17538026	fig1 2
PMID:17538026	fig1 B
PMID:17538026	fig1 B
PMID:17538026	fig1 a
PMID:17538026	fig1a
PMID:17538026	fig1 2
PMID:17538026	fig 6 B
PMID:17538026	fig 6 B
PMID:17538026	fig 4
PMID:17538026	fig 4
PMID:17538026	table 2
PMID:17556368	add note in curator feedback to get double mutant phenotypes
PMID:17556368	add note in curator feedback to get double mutant phenotypes
PMID:17556368	add note in curator feedback to get double mutant phenotypes
PMID:17556368	add note in curator feedback to get double mutant phenotypes
PMID:17561805	tested through observing no de;ay when checkpoin is inactivated
PMID:17579515	(Figure 1).
PMID:17579515	Figure 6C (ablated Nuclear envelope)
PMID:17579515	Figure 6C
PMID:17579515	4G
PMID:17579515	Figure 3A and 3B, and Video S3)
PMID:17579515	Figure 2 C check (also nuclear envelope protrusion?
PMID:17579515	Figure S4)
PMID:17579515	Figure S4 /Figure 3A and 3B, and Video S3)
PMID:17579515	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	S1
PMID:17596513	E. coli ispA mutant used as assay system
PMID:17632059	fig1c
PMID:17632059	fig1c
PMID:17632059	fig1e twice their share of DNA and SPBs.
PMID:17632059	fig1f
PMID:17632059	fig1B
PMID:17632059	fig1B
PMID:17632059	fig1B
PMID:17632059	fig1b
PMID:17632059	fig1B
PMID:17632059	fig1B
PMID:17632059	fig1b
PMID:17632059	fig1c
PMID:17632059	fig1B
PMID:17632059	fig1B
PMID:17632059	fig1B
PMID:17632059	fig1B
PMID:17632059	Fig 1c
PMID:17632059	Fig 1c
PMID:17632059	Fig 1c
PMID:17632059	In taz1Dlig4D zygotes, SPBs move normally during the horsetail stage even though they are rarely associated with chromatin. However, as the horsetail stage ends and meiosis I begins, the Pcp1-GFP signals appear brighter than in WT cells and are markedly disorganized (Figure 2B; 75 min
PMID:17632059	fig3
PMID:17632059	fig3
PMID:17632059	fig3
PMID:17632059	fig3 V-shaped patterns indicating multiple spindles
PMID:17632059	fig3
PMID:17632059	fig3D
PMID:17632059	table S3
PMID:17632059	table S3
PMID:17632059	table S3
PMID:17632059	table S3
PMID:17632059	S3
PMID:17632059	S3
PMID:17632059	S3
PMID:17632059	S3
PMID:17632059	S3
PMID:17632059	S3
PMID:17632059	fig1b
PMID:17632059	fig s4e movie S2
PMID:17632059	Matching synonym SPB detached from nucleuss fix syn
PMID:17632059	table S3
PMID:17632059	fig3D (I)
PMID:17632059	S3
PMID:17677001	Figure 3C spreading is still within the central domain, to the flanking tRNAs
PMID:17677001	Figure 3B
PMID:17677001	Figure 3A EXP says increased, but is normal compared to WT (i.e ura4 insertion derepresses)
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure S1
PMID:17677001	Figure 2A
PMID:17677001	Figure 2A
PMID:17677001	Figure 2A
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure 2B
PMID:17677001	Figure S8
PMID:17677001	Figure 4C
PMID:17677001	Figure 4B
PMID:17690116	Fig1B At 36°C the restrictive temperature for rad3ts the checkpoint is inactive and cells expressing the mutant form of pREP4X cdc18 from the screen do not elongate and are able to form colonies
PMID:17690116	Fig 5B
PMID:17690116	Fig5C
PMID:17690116	Fig5C
PMID:17690116	Fig6A,B
PMID:17690116	Fig1B This is the mutant form of pREP4X cdc18 from the screen At 25°C rad3 checkpoint is active and cells elongate, At 36°C rad3 is inactive and cells do not elongate when cdc18+ is expressed from pREP4X promoter,
PMID:17690116	Fig 2A when cdc18TA6 is overexpressed at 36°C (non permissive temperature for rad3ts ) cells continue to grow and divide normally ( permissive temperature for cdc18TA6)
PMID:17690116	Fig 4C At 25°C rad3 is active but checkpoint cannot be activated in absence of hus1
PMID:17690116	Fig3 and previous figs shows lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	Fig3 and previous figs shows lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	Fig 6C shows Chromosome III smear is present throughout the cell cycle
PMID:17690116	Fig2 A,C cells arrested due to activation of the rad3 (permissive temperature) have normal nuclear to cell size ratio (NC ratio) compared to cdc25-22 at restrictive temp 2 hr
PMID:17690116	Fig7A, B, C after crossing out of cdc18TA6 chromosome size is stabilised and a single band is seen on PFGE which varies in size. If strains with larger Chr III are culture for <30 generations Chromosome III gradually reduces in size
PMID:17690116	Fig 8A, B
PMID:17690116	Fig9A
PMID:17690116	Fig9B, C reb1D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	Fig2D different to when pREP3X cdc18+ is over expressed in G2 block which show replicate intermediates and cells undergo re replication
PMID:17690116	Fig2 A,C cells arrested due to activation of the rad3 (permissive temperature) have normal nuclear to cell size ratio (NC ratio) compared to cdc25-22 at restrictive temp 2 hr
PMID:17690116	Fig2B cells arrested due to activation of the rad3 checkpoint gene do not rereplicate
PMID:17690116	The western in Fig 3 actually shows the TAP tagged version but they use the two strains interchangeable so don't actually show data for this strain CCL9
PMID:17690116	Fig3 This is the mutant form of pREP4X cdc18 from the screen
PMID:17690116	Fig 2A cells expressing cdc18T6A at 36°C do not elongate at the nonpermissive temperature for rad3ts due to inactivation of the mitotic DNA replication checkpoint
PMID:17690116	Fig6A,B
PMID:17690116	Fig3 cdc18 expressed from pREP3X is at a high level. They argue that higher levels cdc18 lead to rereplication and lower levels lead to a rad3 dependent block but no rereplication
PMID:17690116	Fig9B, C rad52D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	Fig1C rad3ts cells over expressing the mutated pREP4X-cdc18 construct do not rereplicate at 25°C or 36°C (the permissive and non permissive temperatures for rad3ts). This is in contrast to Control cells expressing cdc18+ from pREP3X promoter at 32°C (Fig1D , Table 2) which don't activate the mitotic DNA checkpoint and undergo DNA re-replicatiom
PMID:17690116	Fig 2A cdc18T6A expression at 25°C causes cell elongation due to activation of the mitotic DNA replication checkpoint ( permissive temperature for rad3ts)
PMID:17690116	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad26
PMID:17690116	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad1
PMID:17690116	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad17
PMID:17690116	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad9
PMID:17690116	Fig4C At the permissive temperature 25*C rad3 is active but checkpoint cannot be activated in absence of chk1
PMID:17690116	Fig1C rad3ts cells over expressing the mutated pREP4X-cdc18 construct do not rereplicate at 25°C or 36°C (the permissive and non permissive temperatures for rad3ts). This is in contrast to Control cells expressing cdc18+ from pREP3X promoter at 32°C (Fig1D , Table 2) which don't activate the mitotic DNA checkpoint and undergo DNA re-replicatiom
PMID:17690116	Fig1B At 25°C the permissive temperature rad3ts the checkpoint is active and cells expressing the mutant form of pREP4X cdc18 from the screen elongate
PMID:17690116	Fig4A
PMID:17690116	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of crb2
PMID:17690116	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of chk1 and cds1
PMID:17690116	Fig4C at 25°C rad3ts is active and the checkpoint is activated in absence of cds1
PMID:17690116	Fig4C at the permissive temperature rad3ts is active and the checkpoint is activated in absence of mrc1
PMID:17690116	Fig 5A
PMID:17804800	emsa
PMID:17868468	deleted existing genome maintence term, and annotated this instead, all things considered...
PMID:17881496	Fig. 1B
PMID:17881496	ABOLISHED Figure 3 B
PMID:17881496	Figure 3 A
PMID:17881496	Fig. 3A
PMID:17881496	Fig. 1A
PMID:17881496	Figure 3 A
PMID:17881729	the evidence isn't great
PMID:17936710	spores from mre11d/mre11d homozygous diploid
PMID:17936710	spores from mre11d/mre11d rec12d/rec12d homozygous diploid
PMID:17936710	spores from ctp1d/ctp1d homozygous diploid
PMID:17936710	same as either single mutant
PMID:17936710	actually inferred (IC) from combination of phenotype plus GO:0000014 MF
PMID:17936710	spores from ctp1d/ctp1d rec12d/rec12d homozygous diploid
PMID:17936710	spores from rec12d/rec12d homozygous diploid
PMID:17936710	assayed at ctp1 promoter
PMID:17936710	same as either single mutant
PMID:17937917	(site A)
PMID:17937917	(site B)
PMID:17937917	(site B)
PMID:18030666	spatial extent ******The assay is Ura4 expression as a reporter gene for whether heterochromatin is spreading beyond the normal boundry, which it isn't here and so the toxic analogue results in growth attenuation. But sensitivity to FOA isn't the phenotype of interest, that's just the tool
PMID:18030666	spatial extent
PMID:18030666	spatial extent
PMID:18030666	spatial extent
PMID:18030666	epigenetic variegation both 5-FOA-resistant and -sensitive colonies were found
PMID:18030666	spatial extent
PMID:18030666	spatial extent
PMID:18030666	spatial extent
PMID:18030666	spatial extent
PMID:18030666	"spatial extent ********"" These results suggested that the 5-FOA-resistant phenotype of the original mutants was indeed due to ura4 repression, presumably as a result of heterochromatin assembly occurring outside the inverted repeat region."""
PMID:18030666	"spatial extent. "" These results suggested that the 5-FOA-resistant phenotype of the original mutants was indeed due to ura4 repression, presumably as a result of heterochromatin assembly occurring outside the inverted repeat region."""
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	time course after transcription shutoff, so actually measuring degradation
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	all microarray (table 1); arz1 also northern (fig 1)
PMID:18059460	speckles in Fig. 4A
PMID:18060866	localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:18061564	minus end
PMID:18061564	figure 6F
PMID:18061564	FORMATION
PMID:18061564	figure 6F
PMID:18061564	activation
PMID:18061564	in overlap zones
PMID:18061564	bundle maintenence https://github.com/geneontology/go-ontology/issues/18215
PMID:18061564	fig6
PMID:18079700	maintenence
PMID:18079700	Supplementary Figure S2
PMID:18079700	Figure 3 A/B
PMID:18079700	Figure 3C and E
PMID:18079700	Figure 3 B
PMID:18079700	Figure 3 B
PMID:18079700	Figure 3 C/E
PMID:18079700	Figure 3 C/E
PMID:18079700	Figure 3 C/E during G1
PMID:18079700	Rad21
PMID:18079700	Figure 3 A
PMID:18079700	Figure 3 A (but not S phase)
PMID:18093330	Fig8
PMID:18093330	Fig8
PMID:18093330	fig 1
PMID:18157149	I guess this can be changed once we can do RNA mods
PMID:18157152	this is a protein modification so should be changed once we can do RNA mods
PMID:18160711	region between NdeI and XhoI sites deleted
PMID:18160711	truncated at PacI site
PMID:18160711	region between NsiI sites deleted
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18165685	comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887)
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig6, it doesn't bind dna according to later studies
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18223116	fig2
PMID:18256284	figure 1A
PMID:18256284	figure 1B (plus end)
PMID:18256284	figure 1A
PMID:18256284	figure 1B (plus end)
PMID:18256284	figure 1B (plus end)
PMID:18256284	figure 1B (plus end)
PMID:18256290	less levere than pxl1 null
PMID:18256290	less levere than pxl1 null
PMID:18256290	localization dependent on filamentous actin (GO:0031941); tested using latrunculin A
PMID:18256290	increased more than pxl1delta alone
PMID:18256290	increased more than pxl1delta alone
PMID:18256290	increased more than pxl1delta alone
PMID:18256290	increased more than pxl1delta alone
PMID:18256290	increased more than pxl1delta alone
PMID:18262494	(Fig. 1B)
PMID:18262494	after chromosome segregation
PMID:18262494	with extreme sister chromtid oscillations
PMID:18272786	data from table; nothing more specific shown
PMID:18272786	data from table; nothing more specific shown
PMID:18272786	data from table; nothing more specific shown
PMID:18272786	dependent on F-actin (assayed using Latrunculin A)
PMID:18272786	data from table; nothing more specific shown
PMID:18272786	data from table; nothing more specific shown
PMID:18276645	normal oxygen level
PMID:18276645	normal oxygen level
PMID:18328707	old end
PMID:18328707	GTP bound active form
PMID:18328707	GTP bound fig 3C
PMID:18328707	active GTP bound form
PMID:18328707	Fig1SE to cell cortex of (new) cell tip from medial cortex
PMID:18328707	Fig1SE to cell cortex of (new) cell tip from medial cortex
PMID:18328707	GTP bound
PMID:18328707	Figure 3B
PMID:18328707	Fig 1
PMID:18328707	Fig 1
PMID:18328707	GTP-bound Figure 4E
PMID:18328707	Figure 3A
PMID:18328707	Fig 2C
PMID:18328707	Fig 1
PMID:18328707	fig 1D
PMID:18328707	Fig 1D
PMID:18328707	FigS1D
PMID:18328707	Fig1SE to cell cortex of (newnon growing) cell tip from medial cortex
PMID:18328707	Fig 1D
PMID:18328707	Fig 1D (pom1 is catalytically active but not localized to cell ends)
PMID:18328707	Fig 1
PMID:18328707	Figure 4E
PMID:18328707	GTP-bound Figure 4E, polarization localization to both cell ends
PMID:18328707	*****OLD*****waiting for GO
PMID:18331722	First, we have shown that a true APC/C substrate regulates the activity of the APC/C. Cells might precisely control protein levels of each or a subset of APC/C substrate to fine-tune the APC/C itself....Mes1 transcripts and protein levels peak in late MI (Izawa et al., 2005; Mata et al., 2002) when Mes1 seques- ters the Fizzy family of proteins to inhibit APC/C, in turn slowing down cyclin B proteolysis (‘‘APC/C inhibited’’ in Figure 4G). At the same time, Mes1 is inhibited through ubiquitylation by APC/C to allow partial APC/C activation required for anaphase I onset.
PMID:18331722	in vitro assay
PMID:18337696	at time 0. they don't look at nitrogen starvation for very long, only 60 mins
PMID:18378696	same as rad51delta alone
PMID:18378696	same as either single mutant
PMID:18378696	same as either single mutant
PMID:18378696	same as either single mutant
PMID:18378696	same as nbs1delta alone
PMID:18378696	same as nbs1delta alone
PMID:18378696	same as nbs1delta alone
PMID:18378696	same as nbs1delta alone
PMID:18391219	"provides the sulfur....seems ok based on the def ""The process in which a uridine residue at position 34 in the anticodon of a tRNA is post-transcriptionally thiolated at the C2 position. **This process involves transfer of a sulfur from cysteine to position C2 by several steps"""
PMID:18399988	they show transfer to a heterologous cytochrome p450 enzyme, but pombe doesn't have any mitochondrial ones.
PMID:18411246	enclosure arrow in Figs 4Ci,ii)
PMID:18411246	(Fig. 3A)
PMID:18411246	(Fig. 3A)
PMID:18411246	Fig. 2B
PMID:18411246	Fig. 5B
PMID:18411246	Fig. 2A
PMID:18414064	penetrance at 4 hours
PMID:18414064	same with or without TBZ
PMID:18414064	penetrance at 4 hours
PMID:18414064	penetrance at 4 hours; increases upon longer time at restrictive temp
PMID:18414064	same with or without TBZ
PMID:1849107	git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	also assayed using lacZ under fbp1 promoter
PMID:1849107	glycerol = derepressing for glucose repression also assayed using lacZ under fbp1 promoter (and maltose carbon source, also derepressing)
PMID:1849107	git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence
PMID:18493607	same as sir2+ overexpression alone
PMID:18493607	slighly more severe than sir2+ overexpression alone
PMID:18493607	present throughout mitotic cell cycle
PMID:18495844	Fig3B,C
PMID:18495844	Fig 2 A-C This oscillatory movement was not perturbed by Latrunculin A treatment, but was lost in cells treated with MBC or in mto1Δ cells, and was reduced in tip1Δ cells
PMID:18495844	Fig 2B
PMID:18495844	Fig3B
PMID:18495844	Fig3B
PMID:18495844	Fig3B,C As expected, the range of SPB trajectory angles was much wider than in wild-type cells (Fig. 2C, Fig. 3B,C
PMID:18495844	Fig1B
PMID:18495844	Fig1B normal interphase MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18495844	Fig1B and 2B,C normal MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18514516	same as either single mutant
PMID:18514516	same as either single mutant
PMID:18514516	same as either single mutant
PMID:18514516	same as either single mutant
PMID:18514516	same as either single mutant
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 5A
PMID:18562692	Fig. 5A
PMID:18562692	Fig. 5B
PMID:18562692	Fig. 5B
PMID:18562692	Fig. 1
PMID:18562692	Fig. 1
PMID:18562692	Fig. 5A
PMID:18562692	Fig. 4
PMID:18562692	Fig. 3
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18562692	Fig. 6C
PMID:18615848	same as swi7-H4 alone, i.e. it's dominant
PMID:1863602	maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.
PMID:18640983	in vitro
PMID:18653539	figure 8B
PMID:18653539	figure 8B
PMID:18653539	figure 8B
PMID:18653539	figure 1B
PMID:18653539	Fig 2 F during veg phase
PMID:18653539	figure 1A, 8A
PMID:18653539	figure 2A
PMID:18653539	figure 1A
PMID:18653539	figure 2A
PMID:18653539	figure 1 C
PMID:18653539	figure 8B
PMID:18653539	figure 2A
PMID:18653539	Fig. 1D
PMID:18653539	Fig. 1D, Fig. 1F
PMID:18662319	also L-gamma-glutamyl-L-cysteine
PMID:18667531	The Nse1-Nse3 interaction is not perturbed by dele- tion of Nse1 NH-RING as tested by yeast two-hybrid assay, which is consistent with a previous report (Figure 5B and Sergeant et al., 2005).
PMID:18667531	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	The C219A mutant was not temperature sensitive (Figure 2A).
PMID:18667531	On the basis of these data, we propose that the Nse1 NH-RING contributes to the DNA repair functions of the Smc5-Smc6 holocomplex.
PMID:18667531	nulcleolus inheritance
PMID:18667531	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18667531	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18667531	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18667531	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18676809	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2–BRCT2 interaction with the peptide (Fig. 3A),
PMID:18676809	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2–BRCT2 interaction with the peptide (Fig. 3A),
PMID:18676809	fig 4 a
PMID:18676809	fig 4 a
PMID:18676809	fig 4 a
PMID:18676809	the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization
PMID:18676809	fig 4 a
PMID:18676809	fig 4 a
PMID:18676809	fig 4 a
PMID:18676809	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2–BRCT2 interaction with the peptide (Fig. 3A),
PMID:18676809	fig 4 a
PMID:18676809	the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization
PMID:18676809	fig 4 a
PMID:18676809	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	fig 4 a
PMID:18676809	fig 4 a
PMID:18676809	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2–BRCT2 interaction with the peptide (Fig. 3A),
PMID:18676809	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2–BRCT2 interaction with the peptide (Fig. 3A),
PMID:18676809	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2–BRCT2 interaction with the peptide (Fig. 3A),
PMID:18716626	(Fig. 1e, f) As predicted, the additional expression of Psc3–2CD (but not of 2CD alone) improved the localization of the cohesin complex to the peri-centromeric regions and also centromeric cohesion in swi6D cells
PMID:18716626	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	(Fig. 3f). The assay of chromosome segregation further revealed that sgo1-VE cells provoke nondisjunction in meiosis II, similarly to swi6D cells
PMID:18716626	(Fig. 3f and Supplementary Fig. 8). The Sgo1-VE protein, when fused with CDand thereby localized to the centromere, can perform its full functionin protecting Rec8
PMID:18716626	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	Fig. 1a
PMID:18716626	Fig. 1a–d
PMID:18716626	Fig. 1a–d
PMID:18716626	Fig. 1a–d
PMID:18716626	(Supplementary Fig. 2a) We confirmed that Psc3–2CD, as well as 2CD, itself localizesat discrete nuclear dots in swi6D cell
PMID:18716626	(Supplementary Fig. 2a) , but not in another heterochromatin-defect- ive strain, clr4D, which lacks H3K9me (ref. 7)
PMID:18716626	(Supplementary Fig. 3a). We confirmed that the expression of Psc3–2CD does not restore transcriptional silencing in swi6D cells
PMID:18716626	figure 1g 30% cells?
PMID:18716626	various: These results indicate that Swi6 is crucial in localizing Sgo1 and thereby promotes the protection of cohesin from separase during anaphase I.
PMID:18716626	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	(Supplementary Fig. 4). The transcriptional silencing of Swi6 is not relevant to this function, because swi6-sm1 cells have intact meiotic chromosome segregation
PMID:18716626	(Fig. 2e) Sgo1 localization is impaired in swi6D cells
PMID:18716626	(Fig. 2f) Sgo1–CD did indeed localize at the centromere regardless of swi6D
PMID:18716626	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18723894	"RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level"
PMID:18723894	no barrier activity with reversed polarity as in rtf1-S154L single mutant
PMID:18723894	no barrier activity with reversed polarity as in rtf1-S154L single mutant
PMID:18769921	during vegetative growth because non-sporulating strains used
PMID:18769921	during vegetative growth because non-sporulating strains used
PMID:18769921	during vegetative growth because non-sporulating strains used
PMID:18769921	slightly worse than sfr1delta alone
PMID:18769921	during vegetative growth because non-sporulating strains used
PMID:18769921	during vegetative growth because non-sporulating strains used
PMID:18769921	slightly more sensitive at low temperature than standard
PMID:18794373	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	binds at Ter3 site
PMID:18794373	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	arrest at Ter2 and Ter3 sites abolished
PMID:18849471	qualifier=major
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	abolished interaction between wt and mutant; interaction partially restored if both copies are mutant
PMID:18854158	abolished interaction between wt and mutant; interaction partially restored if both copies are mutant
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18951025	one or more of mutated serine residues
PMID:18951025	one or more of mutated serine residues
PMID:18957202	Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9)
PMID:18957202	As shown in Figure 5C, siRNA is barely detectable.
PMID:18957202	forward and reverse centromeric strands were detected in lid2-j and accumulated at the same level as in clr8Δ, suggesting that Lid2 is involved in the RNAi pathway.
PMID:18957202	forward and reverse centromeric strands were detected in lid2-j and accumulated at the same level as in clr8Δ, suggesting that Lid2 is involved in the RNAi pathway.
PMID:18957202	H3K4me3 staining was reduced to nearly undetectable levels in 82% of the cells overexpressing Lid2, suggesting that Lid2 can specifically demethylate H3K4 me3 (Figure 4B)
PMID:18957202	overexpressing Lid2 enhances H3K9 methylation (Figures 5G and H)
PMID:18957202	We then determined whether Lid2 is required for the recruitment of Clr4 to heterochromatin. We carried out a ChIP experiment using lid2-j or clr8Δ containing a N-terminal FLAG-tagged Clr4. The localization of Clr4 at centromeres is abrogated in both mutants (Figure 3E).
PMID:18957202	We then determined whether Lid2 is required for the recruitment of Clr4 to heterochromatin. We carried out a ChIP experiment using lid2-j or clr8Δ containing a N-terminal FLAG-tagged Clr4. The localization of Clr4 at centromeres is abrogated in both mutants (Figure 3E).
PMID:18957202	drastic reduction of Swi6 binding (Figure 3D).
PMID:18957202	In contrast, H3K4me3 methylation was increased significantly (Figure 3C)
PMID:18957202	In WT cells, Myc- Clr8 associates with centromere otr regions, but not in lid2-j suggesting that Lid2 is required for Clr8 association with heterochromatin (Figure 5E).
PMID:18957202	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	As shown in Figure 5E, while Lid2 accumulated at centromeres in the WT, the centromere localization of Lid2 in the clr8 mutant is significantly decreased.
PMID:18957202	Figure 5F, the point mutation resulted in a significant loss of silencing at the centromere otr region.
PMID:18957202	ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2)
PMID:18957202	ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2)
PMID:18957202	the point mutation had little effect on the interaction of Lid2 with its interacting partners, such as Cul4 and Set1 (Figure S3 and S8).
PMID:18957202	the point mutation had little effect on the interaction of Lid2 with its interacting partners, such as Cul4 and Set1 (Figure S3 and S8).
PMID:18957202	We also examined the GFP-Swi6 distribution in the mutants (Figure 7B). While the lid2-phd1 mutant is similar to the WT, the nuclei in the lid2-phd2 and lid2-phd3 mutants often contained excessive GFP- Swi6 dots, suggesting that euchromatin assembly is disrupted in the mutants (Figure 7B).
PMID:18957202	We next examined Swi6 localization in the lid2-j mutant using N-terminal tagged GFP-Swi6. In WT vegetative cells, 3–4 GFP-Swi6 spots are observed. This is because the three centromeres cluster on the nuclear envelope in the vicinity of the spindle pole body whereas telomeres loosely cluster on the nuclear envelope, apart from centromeres. clr4 and clr8 mutants have a diffuse Swi6 localization due to the disruption of heterochromatin. To our surprise, we did not see the same GFP-Swi6 pattern in the lid2-j mutant as in clr8Δ. Rather, we found that 78% of the cells contain more than 5 GFP-Swi6 spots, with nearly 30% having more than 10 spots (Figure 6A). The abnormal distribution of Swi6 also can be observed in meiotic horsetail stage nuclei (Figure 6A). The aberrant Swi6 localization is not caused by defects in centromere or telomere clustering since the distribution of centromeres and telomeres, as marked by Cnp1-GFP or Taz1-GFP respectively, is unaffected in the lid2-j mutant (Figure S4). We further confirmed that telomeres cluster normally by visualizing their distribution in a lid2-j strain carrying mCherry-Swi6 and the telomere marker Taz1-GFP (Figure S4). These results suggest that heterochromatin is induced in euchromatic regions in lid2-j.
PMID:18957202	RNAI dependent
PMID:18957202	About 50% (2665 out of 5241) of the genes in the genome were downregulated in mutant cells compared to WT (Figure 6C and Table S3), consistent with the formation of ectopic heterochromatin.
PMID:18957202	We further noted the striking similarity of the genome-wide transcription profiles of the lid2-j and lsd1Δ mutants (Figure 6C), suggest
PMID:18957202	In contrast to the overexpression of Lid2 alone, which leads to a dramatic decrease in H3K4me3 (Figure 4B), reduction of H3K4me3 is minimal when Set1 or Lsd1 is also overexpressed (Figure 4C).
PMID:18957202	We also examined the GFP-Swi6 distribution in the mutants (Figure 7B). While the lid2-phd1 mutant is similar to the WT, the nuclei in the lid2-phd2 and lid2-phd3 mutants often contained excessive GFP- Swi6 dots, suggesting that euchromatin assembly is disrupted in the mutants (Figure 7B).
PMID:18957202	ilencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	ilencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	As shown in Figure 3B, H3K9 methylation at the centromere was completely abolished.
PMID:18957202	mating-type region was likewise reduced (Figure 3A)
PMID:18957202	We found that deletion of the Lid2 JmjC domain resulted in the complete loss of ura4+ silencing at both the otr and imr loci (Figure 3A and Figure 7A).
PMID:18957202	We found that deletion of the Lid2 JmjC domain resulted in the complete loss of ura4+ silencing at both the otr and imr loci (Figure 3A and Figure 7A).
PMID:18957202	As shown in Figure 2E, lid2-j, like clr8Δ, is hypersensitive to TBZ
PMID:18957202	ilencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	28% of the cells contained fragmented nuclear DNA (Figure 2D), indicating that the mutant nucleus is disorganized.
PMID:18957202	WT and frequently exhibited an aberrant elongated cell shape (Figure 2C)
PMID:18957202	tetrad analysis. We deleted one copy of lid2+ by kanamycin reporter gene replacement (kan+) in a WT diploid strain (lid2+/lid2Δ::kan+) and tetrad analysis was performed after sporulation. Only two germinating spores from a tetrad were viable, confirming that lid2+ is an essential gene
PMID:18957202	Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9)
PMID:18957202	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).
PMID:18957202	Figure 2A
PMID:18957202	As shown in Figure 5D, the association of Ago1 with the centromere is significantly reduced in lid2-j, indicating that Lid2 is required for RITS to load onto centromeres.
PMID:18957202	Figure 1A
PMID:1899284	also supported by complementation of S.c. deletion
PMID:19001497	fig 2 a (this fig also has expression level for mutant alleles)
PMID:19001497	we conclude that the function of Mto2 in MT nucleation is mediated primarily, if not exclusively, via its binding to Mto1. Moreover, the failure of Mto1-334 to immunoprecipitate the γ-TuC indicates that the Mto1-Mto2 interaction is required for an efficient association of Mto1 with the γ-TuC, as detected in cytoplasmic extracts.
PMID:19001497	we conclude that the function of Mto2 in MT nucleation is mediated primarily, if not exclusively, via its binding to Mto1. Moreover, the failure of Mto1-334 to immunoprecipitate the γ-TuC indicates that the Mto1-Mto2 interaction is required for an efficient association of Mto1 with the γ-TuC, as detected in cytoplasmic extracts.
PMID:19001497	fig 1 D, 1 E
PMID:19001497	fig 1 D, 1 E
PMID:19001497	fig 1 D
PMID:19001497	fig 4 F
PMID:19001497	supplementary material Fig. S1)
PMID:19001497	fig 4 F
PMID:19001497	supplementary material Fig. S1)
PMID:19001497	Fig 1 E
PMID:19001497	Fig4D
PMID:19001497	Fig4D
PMID:19001497	Fig4c
PMID:19001497	Fig4c
PMID:19001497	Fig4a
PMID:19001497	fig3
PMID:19001497	fig3
PMID:19001497	fig3
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	Fig 2 D-F
PMID:19001497	fig 2 BC
PMID:19001497	fig 2 BC
PMID:19001497	fig 2 BC
PMID:19001497	supplementary material Movies 2-4).
PMID:19001497	supplementary material Movies 2-4).
PMID:19001497	supplementary material Movies 2-4).
PMID:19001497	supplementary material Movies 2-4).
PMID:19001497	Fig 1 E
PMID:19001497	Fig 1 E
PMID:19001497	Fig 1 E
PMID:19001497	fig 1 D, 1 E
PMID:19001497	fig 1 D, 1 E
PMID:19001497	fig 1 D, 1 E
PMID:19001497	fig 1 D
PMID:19001497	fig 1 C
PMID:19001497	fig 1 C
PMID:19001497	fig 1 C
PMID:19001497	fig 1 C
PMID:19023408	Southern blot
PMID:19023408	ChIP
PMID:19023408	forms covalent linkage upon binding (wouldn't normally use ChIP as IDA for DNA binding MF, but the phenol extraction with or without protease adds more confidence)
PMID:19023408	Southern blot
PMID:19023408	microarray
PMID:19023408	Southern blot
PMID:19023408	Southern blot
PMID:19023408	Southern blot
PMID:19026779	*****ABOLISHED*****Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19026779	Figure 4D
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	The checkpoint doesn't sense all types of dna damage eg that caused by gamma radiation or DNA adduct formation by PUVA
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19037096	Figure 4, A and B, and Supplemen- tal Movie S1
PMID:1905818	haploid, either mating type
PMID:1905818	(changed to GTPase from signal transducer)
PMID:19111658	binds centromeric transcripts
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	gave dark staining with iodine,switch to the opposite state at a low rate
PMID:19117951	gave dark staining with iodine,switch to the opposite state at a low rate
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	mat1Msmto REIIdelta mat2::ura4 gave dark staining with iodine, metastable and switch to the opposite state at a low rate
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	heterochromatin
PMID:19139265	Fig. S5
PMID:19139265	Fig. S5
PMID:19139265	fig8
PMID:19139265	fig9
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19150433	covalent binding between topoisomerase and DNA
PMID:19155267	Table S1, Supplementary Data
PMID:19155267	Table S1, Supplementary Data
PMID:19155267	Table S1, Supplementary Data
PMID:19158664	"closest we can get to ""at stalled fork"" with available terms"
PMID:19185548	qualifier=different_pathway
PMID:19185548	qualifier=different_pathway
PMID:19189958	Figure 2A
PMID:19189958	Figure 2b
PMID:19189958	Figure 2A
PMID:19189958	Figure 2A
PMID:19189958	Figure 2
PMID:19189958	Figure 2
PMID:19189958	90% viability ? We also examined cell viability of stationary phase rgf2D and rgf21 cultures incubated for 4 days at 28°; both strains were found to be .90% viable during this period.
PMID:19189958	We also examined cell viability of stationary phase rgf2D and rgf21 cultures incubated for 4 days at 28°; both strains were found to be .90% viable during this period.
PMID:19189958	Figure 1
PMID:19189958	Figure 1
PMID:19189958	Our results indicate that Rgf1p and Rgf2p share an essential role as Rho1p activators, and they suggest that in the absence of Rgf1p, Rgf2p takes over the essential functions for Rho1p during vegetative growth.
PMID:19189958	Figure 4c positive
PMID:19189958	Figure 3A
PMID:19189958	"Figure 3 ""This result indicates that Rgf2p is in- volved in b-glucan biosynthesis during sporulation."" figure4c These results clearly indicate that Rgf2p is involved in the regulation of b(1,3)-glucan biosynthesis."
PMID:19189958	10% of cells
PMID:19189958	47% of cells
PMID:19189958	Figure 1 Rgf2p, a Rho1-GEF Required for Sporulation in S. pombe 1329 6A (top) shows that rgf2 expressed from plasmids, containing the rgf21 genomic promoter (pGR13) or the strongest nmt1 promoter (pGR70), fully rescued the lysis and the Csp hypersensitivity of rgf1D cells in medium containing thiamine.
PMID:19189958	Our results indicate that Rgf1p and Rgf2p share an essential role as Rho1p activators, and they suggest that in the absence of Rgf1p, Rgf2p takes over the essential functions for Rho1p during vegetative growth.
PMID:19189958	Figue 5B How- ever, their growth was rescued in the presence of sorbitol
PMID:19189958	Figue 5B As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	Figue 5B How- ever, their growth was rescued in the presence of sorbitol
PMID:19189958	Figue 5B As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	Figure 5B viable and phenotypically in- distinguishable from the ehs2-1 mutant
PMID:19189958	None of the 11 spores predicted to be rgf1This31 rgf2Tura1 was viable, strongly supporting the idea that simultaneous disruption of rgf11 and rgf21 is lethal. To eliminate the possibility that these mutations might be affecting only sporulation or germination, we also tested for synthetic lethality during vegetative growth
PMID:19189958	GS activity was threefold higher than that observed in the wild-type strain (Figure 4C)
PMID:19189958	GS activity was threefold higher than that observed in the wild-type strain (Figure 4C)
PMID:19189958	cells were larger than wild-type cells and displayed multiple abnormal septa.
PMID:19189958	Asexpected,over- expression of the rgf2-PTTRD mutant in a pREP3X vector produced viable cells and no multiseptated phenotype was seen, even at very long times of derepresion in the absence of thiamine (Figure 4A).
PMID:19189958	the amount of active Rho1p increased considerably in the strain over- expressing Rgf2p as compared with the wild-type strain (Figure 4B
PMID:19189958	Figure 3B
PMID:19189958	Figure 2A
PMID:19189958	Figure 2A
PMID:19202278	absent beta 1,3 gal
PMID:19202289	(Fig. 3A and B)
PMID:19202289	(Fig. 2D)
PMID:19202289	(Fig. 2D)
PMID:19202289	(Fig. 2B)
PMID:19202289	(Fig. 3C)
PMID:19202289	(Fig. 3A and B)
PMID:19202289	(data not shown).
PMID:19202289	(Fig. 2B)
PMID:19202289	(Fig. 3C)
PMID:19202289	(Fig. 3B)
PMID:19202289	(Fig. 3B)
PMID:19202289	Fig. 1A
PMID:19202289	Fig. 1B
PMID:19202289	Fig. 1A
PMID:19202289	Fig. 1B
PMID:19202289	Fig. 1B
PMID:19205745	temp semi-permissive for cdc6-23 alone
PMID:19205745	temp semi-permissive for cdc6-23 alone
PMID:19205745	temp semi-permissive for cdc6-23 alone
PMID:19205745	temp semi-permissive for cdc6-23 alone
PMID:19205745	temp semi-permissive for cdc20-M10 alone
PMID:19205745	temp semi-permissive for pol1-1 alone
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19211838	spores from homozygous diploids
PMID:19214192	present throughout cell cycle but at higher level in S phase
PMID:19214192	present in late S
PMID:19214192	present at roughly constant level throughout cell cycle
PMID:19214192	DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6)
PMID:19214192	present in late S, as late as pols alpha & delta
PMID:19214192	DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6)
PMID:19214192	present in late S
PMID:19214192	present throughout cell cycle but at higher level in S phase
PMID:19214192	present in late S
PMID:19214192	present throughout cell cycle but at higher level in late S phase
PMID:19214192	present throughout cell cycle but at lower level in S phase
PMID:19214192	DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6)
PMID:19217404	abolished, fig1 d
PMID:19217404	fig S10
PMID:19217404	abolished, fig1 d
PMID:19217404	abolished, fig1 d
PMID:19217404	abolished, fig1 d
PMID:19217404	abolished, fig1 d
PMID:19217404	abolished, fig1 d
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	assayed using purified HeLa histone octamers
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19250904	same as either single mutant
PMID:19279143	Notably, Pmk1, the mitogen-activated protein kinase (MAPK), which regulates cell integrity (Toda et al., 1996; Sugiura et al., 1999; Sugiura et al., 2003), directly phosphorylates Nrd1, thereby negatively regulating the ac- tivity of Nrd1 to bind to and stabilize Cdc4 mRNA. We propose that the MAPK-dependent phosphorylation of the RNA-binding protein Nrd1 may serve as a novel mechanism for the regulation of myosin mRNA and cytokinesis in fission yeast.
PMID:19279143	fig 4F
PMID:19279143	"""Thus, Nrd1 di- rectly binds with Cdc4 mRNA in vivo and in vitro"""
PMID:19279143	fig 4F
PMID:19328067	(All at eng2 CDS)
PMID:19328067	(All at eng2 CDS)
PMID:19328067	"Mcs6 ""primes"" Rpb1 for phosphorylation by cdk9"
PMID:19328067	serine 2
PMID:19328067	serine 5/serine2
PMID:19328067	serine2
PMID:19328067	(All at eng2 CDS)
PMID:19328067	(All at eng2 CDS)
PMID:19328067	(All at eng2 CDS)
PMID:19330768	in arrested cells, indicating independent of cell cycle progression
PMID:19330768	G2 temperature shift
PMID:19330768	G1 temperature shift
PMID:1934126	same as cdc25-22 single mutant
PMID:1934126	same as cdc25-22 single mutant
PMID:1934126	same as cdc25-22 single mutant
PMID:1934126	same as cdc25-22 single mutant
PMID:19357077	Activation of Cds1 requires the recruitment by Mrc1 and subsequent phosphorylation of threonine 11 by Rad3. Phosphorylation of threonine 11 promotes homodimerization of Cds1, which facilitates the autophosphorylation of threonine 328 in the kinase domains of the dimer partners. Phosphorylation of threonine 328 directly activates Cds1. The kinase activity of Cds1 is low during a normal cell cycle. However, it increases dramatically during a perturbed S phase.
PMID:19363481	SLD1
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	Figure 5
PMID:19363481	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	Strikingly, a GST-Rad60 SLD2E380R construct did not detectably interact with Ubc9-TAP (Fig. 3a),
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19366728	fragmented
PMID:19373772	during mitotic M phase?
PMID:19373772	"happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"""
PMID:19373772	"happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"""
PMID:19373772	non fermentable carbon source
PMID:19394293	(Figure 3C).
PMID:19394293	(Figure 3C).
PMID:19394293	We found that mutant proteins coimmunoprecipitated with Chp1 and FLAG-Ago1 with similar efficiency as the wild-type protein (Figures 4A and 4B, compare lane 1 with lanes 2–5). This result demonstrates that RITS complex formation is not affected in tas3-TAM mutants and that theCterminus of Tas3 is not involved in Chp1 or Ago1 binding (also shown in Partridge et al. [2007]).
PMID:19394293	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	At the dg and dh repeats, we found a consistent 2- to 3-fold reduction in mutant Tas3 occupancy compared to wild-type (Figure 5B, compare lanes 3–6 with lane 2; and Figure 5C). Also, consistent with the otr1R::ura4+ silencing data (Figure 3B), mutant Tas3-TAM proteins associated with the ura4+ insert at otr1R less efficiently than wild-type Tas3 (Figure 5D, compare lanes 3–6 with lane 2; and Figure 5E). In
PMID:19394293	Surprisingly, we found no defect in H3K9me in tas3DTAM compared to wild-type cells at native centromeric repeats (dg1, imr1, imr2-1, or imr2-2) or the ura4+ inserts (for imr1R::ura4+,
PMID:19394293	Figure 3. tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1 (A) Schematic diagram of S. pombe centromere (cen) 1. The
PMID:19394293	Figure 3.
PMID:19394293	Figure 3. tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1 (A) Schematic diagram of S. pombe centromere (cen) 1. The
PMID:19394293	Figure 3. tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1 (A) Schematic diagram of S. pombe centromere (cen) 1. The
PMID:19394293	Figure 3. tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1 (A) Schematic diagram of S. pombe centromere (cen) 1. The
PMID:19394293	(Figure 3C).
PMID:19394293	Figure 3. To rule out that the observed silencing defects were due to instability of the mutant Tas3 proteins, we examined the levels of wild-type and mutant Tas3 protein by western blotting and found that the mutant proteins were expressed to similar levels as the wild-type protein (Figure 3C).
PMID:19416828	"RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level"
PMID:19417105	(Supplemental Table S1).
PMID:19417105	figure 1
PMID:19417105	figure 1
PMID:19417105	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	(Supplemental Table S1).
PMID:19417105	(Supplemental Table S1).
PMID:19417105	(Supplemental Table S1).
PMID:19417105	(Supplemental Table S1).
PMID:19417105	(Supplemental Table S1).
PMID:19417105	(Supplemental Table S1).
PMID:19417105	figure 5A
PMID:19417105	figure 5A
PMID:19417105	figure 5A
PMID:19417105	(Fig. 5B)
PMID:19417105	(Fig. 5B)
PMID:19417105	(Fig. 5B)
PMID:19422421	increased chromatin association in presence of HU
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	25 degrees (permissive for hsk1-89)
PMID:19422421	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	30 degrees
PMID:19422421	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:19430462	urg1, gar2, act1, adh1, pof9 and hcn1 mRNAs were shown to be direct targets by cRACE sequence analysis.
PMID:19430466	Fig. 1f ATP-dependent Supplementary Information, Movie 1)
PMID:19430466	homodimer
PMID:19430466	Fig. 2c
PMID:19430466	Fig. 2j
PMID:19430466	Fig. 2j
PMID:19430466	Fig. 2d, lane 4
PMID:19431238	ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:19431238	ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:1943699	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1944266	assayed substrate: rabbit muscle phosphorylase
PMID:19454013	Rad21
PMID:19454013	Rad21
PMID:19474789	all data These data indi- cate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	Fig. 1c and Supplementary Fig. 2a
PMID:19474789	Fig 1 a,b
PMID:19474789	Fig 1 a,b
PMID:19474789	Fig 1 a,b
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Supplementary Table 1
PMID:19474789	Fig. 2c,d,e
PMID:19474789	Fig. 2c,d,e
PMID:19474789	Fig. 2c,d,e
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Supplementary Fig. 6
PMID:19474789	Supplementary Fig. 6
PMID:19474789	Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	Supplementary Figure S8
PMID:19474789	Supplementary Figure S8
PMID:19474789	Supplementary Figure S8
PMID:19474789	Supplementary Figure S8
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	fig3
PMID:19474789	Supplementary Fig. 10
PMID:19474789	all data These data indi- cate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	Figure 4 d
PMID:19474789	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	Supplementary Table 2
PMID:19474789	all data These data indi- cate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	all data These data indi- cate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474792	table1
PMID:19474792	(Fig. 3b).
PMID:19474792	(Fig. 3b).
PMID:19474792	Supplementary Fig. 3
PMID:19474792	Supplementary Fig. 4
PMID:19474792	Fig. 2a and data not shown
PMID:19474792	Fig. 2a and data not shown
PMID:19474792	Table 1
PMID:19474792	Table 1
PMID:19474792	Table 1
PMID:19474792	Table 1
PMID:19474792	Fig. 2a and data not shown
PMID:19474792	cortex
PMID:19474792	fig 1b
PMID:19474792	fig 1b
PMID:19474792	or is this reduced with low exressivity?
PMID:19474792	table1
PMID:19474792	table1
PMID:19474792	table1
PMID:19474792	(Fig. 3b).
PMID:19474792	Table 1
PMID:19474792	Table 1
PMID:19474792	Fig. 1e in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	(Fig. 3b).
PMID:19474792	Table 1
PMID:19474792	Table 1
PMID:19474792	fig 1b
PMID:19474792	Table 1
PMID:19474792	Table 1 and Fig. 2d
PMID:19474792	Table 1 and Fig. 2d
PMID:19474792	Table 1 and Fig. 2d
PMID:19474792	(Fig. 3b).
PMID:19474792	Table 1
PMID:19474792	table1
PMID:19474792	Table 1
PMID:19474792	table1
PMID:19474792	table1
PMID:19474792	fig 1d ie not blocked in g2
PMID:19474792	Fig. 1e Fig. 1f)
PMID:19474792	Fig. 1e in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	fig 1g
PMID:19474792	Supplementary Fig. 2
PMID:19474792	Supplementary Fig. 2
PMID:19474792	Supplementary Fig. 3
PMID:19486165	(Fig. 7B)
PMID:19486165	(Fig. 7B)
PMID:19486165	Fig. 1A
PMID:19486165	Figure 4 C
PMID:19486165	Figure 4 C
PMID:19486165	(Fig. 4B)
PMID:19486165	Fig. 2B
PMID:19486165	(Fig. 7B)
PMID:19486165	Fig. 5C
PMID:19486165	(Fig. 7B)
PMID:19486165	(Fig. 7B)
PMID:19486165	(Fig. 7B)
PMID:19486165	Fig. 1C
PMID:19486165	(data not shown).
PMID:19486165	Fig. 6C
PMID:19486165	Fig. 2A
PMID:19486165	figure 7 A
PMID:19486165	Fig. 1A
PMID:19486165	Fig. 1A
PMID:19486165	Figure 4 C
PMID:19486165	Fig. 5C
PMID:19486165	Fig. 5C
PMID:19486165	Fig. 5B
PMID:19486165	Fig. 5A
PMID:19487457	insertion
PMID:19487457	Figure 1 and 2 We conclude that it is the new SPB that fails to activate and insert into the nuclear envelope in cut12.1 mutants.
PMID:19487457	Figure 1 and 2 We conclude that it is the new SPB that fails to activate and insert into the nuclear envelope in cut12.1 mutants.
PMID:19487457	gapped membrane distortions in the nuclear envelope of cut12.1 cells at 36°C (Fig. 3, A–D). 7D
PMID:19487457	(Fig. 4 C and Video 3)
PMID:19487457	our ability to identify cells in which an active SPB had apparently lost its association with the membrane completely and fallen into the middle of the nucleus (Fig. 3 E) and the proximity of the SPB to these gaps in the membrane (Fig. 3, A–C).
PMID:19487457	our ability to identify cells in which an active SPB had apparently lost its association with the membrane completely and fallen into the middle of the nucleus (Fig. 3 E) and the proximity of the SPB to these gaps in the membrane (Fig. 3, A–C).
PMID:19487457	monopolar
PMID:19487457	monopolar
PMID:19487457	Surprisingly, in 50% (n = 79) of the cut12.1 cells that successfully completed mitosis, an efflux of the NLS-GFP–-Gal marker accompanied mitotic commitment (Fig. 7, C and D).
PMID:19487461	Fig1A BrdU incorporation wee1-50 strain analysed at 32°C
PMID:19487461	Fig1G amount of tos1-GFP in nucleus is dependent on cdc10
PMID:19487461	section titled MBF-dependent gene expression...these cells undergo G1 transcription, a seemingly normal Sphase (no region specific amplifications) and can only reinitiate replication once size per genome is minimal size.
PMID:19487461	Fig5A
PMID:19487461	Fig 1B
PMID:19523829	increased dlocalization of mad2 to kinetochore
PMID:19543678	from PM (Fig. 3c
PMID:19543678	(Fig. 3)
PMID:19543678	(Fig. 3)
PMID:19546237	during recovery from stress
PMID:19570908	myo2
PMID:19570908	request and use GO:new positive regulation of (MF) microfilament motor activity instead? depends on ancestry of motor activity branch
PMID:19570908	25 degrees C, i.e. lower end of normal temp. range; penetrance higher at 29 degrees C
PMID:19570908	myo2
PMID:19571115	Fig. 5B
PMID:19571115	fig1
PMID:19571115	Fig. 5B
PMID:19571115	fig1
PMID:19571115	Fig. 5a
PMID:19571115	fig5D
PMID:19592249	fig1
PMID:19592249	figure 1a
PMID:19592249	figure 2a abolished
PMID:19592249	figure 2a abolished
PMID:19592249	figure2
PMID:19592249	figure2
PMID:19592249	figure 1E apc complex binding
PMID:19592249	figure 1E apc complex binding
PMID:19592249	fig2
PMID:19592249	figure 1a
PMID:19605557	figure 6
PMID:19605557	figure 6
PMID:19605557	However, GII activity is significantly reduced in the microsomal fraction of 􏰄GII􏰀 cells (Figure 2B), suggesting that GII􏰀 is involved in ER localization of GII􏰁
PMID:19605557	GII􏰀 Is Required for an Efficient In Vitro Glucose Trimming from G2M9 and G1M9
PMID:19605557	figure 6
PMID:19605557	figure 6
PMID:19606211	Sequence LVIAMDQLNL mentioned in the text
PMID:19606211	See Fig. 1
PMID:19624755	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA com- pared with those of Dapl4 and Daps1 cells
PMID:19624755	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA com- pared with those of Dapl4 and Daps1 cells
PMID:19624755	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA com- pared with those of Dapl4 and Daps1 cells
PMID:19624755	Fig4. suggesting that the four adaptin subunits of the AP-1 complex are all localized to the Golgi ⁄ endosomes.
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	fig5
PMID:19624755	(Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506
PMID:19624755	localized to large endosomal structures
PMID:19624755	(Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506
PMID:19624755	(Fig. 2b) whereas that of Dapl4 and Daps1 cells was partially inhibited
PMID:19624755	localized to large endosomal structures
PMID:19624755	localized to large endosomal structures
PMID:19624755	localized to large endosomal structures
PMID:19624755	n wild-type cells, most of Krp1- red fluorescent protein (RFP) colocalized with GFP- Vrg4 (Fig. 7a), indicating that Krp1 mainly localized to the Golgi apparatus
PMID:19624755	n wild-type cells, most of Krp1- red fluorescent protein (RFP) colocalized with GFP- Vrg4 (Fig. 7a), indicating that Krp1 mainly localized to the Golgi apparatus
PMID:19624755	localized to large endosomal structures
PMID:19624755	localized to large endosomal structures
PMID:19624755	localized to large endosomal structures
PMID:19624755	localized to large endosomal structures
PMID:19624755	Fig. 6a, wt, arrowheads
PMID:19624755	Fig. 6a, wt, arrowheads
PMID:19624755	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA com- pared with those of Dapl4 and Daps1 cells
PMID:19624755	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA com- pared with those of Dapl4 and Daps1 cells
PMID:19625445	Fig 1
PMID:19625445	Figure 9
PMID:19625445	Figure9
PMID:19625445	fig8
PMID:19625445	fig8
PMID:19625445	Figure 7
PMID:19625445	Figure 7
PMID:19625445	Figure 7
PMID:19625445	figure 6c,d
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	Figure 9B
PMID:19625445	fig9A
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 6a
PMID:19625445	figure 5D
PMID:19625445	figure 5D
PMID:19625445	Figure 5B
PMID:19625445	Figure 5B
PMID:19625445	Figure 5B
PMID:19625445	Figure 5B
PMID:19625445	Figure 5A
PMID:19625445	Figure 5A
PMID:19625445	Fig 2A
PMID:19625445	Fig 2A
PMID:19625445	Figure 4c
PMID:19625445	Figure 4c
PMID:19625445	Fig 1 16.5 +/- 0.78
PMID:19625445	Fig 1 IS THIS SMALL OR STUBBY? 11.6 +/- 0.45
PMID:19625445	Fig 1
PMID:19625445	Figure 4B
PMID:19625445	Figure 4B
PMID:19625445	Figure 4B
PMID:19625445	Figure 4B
PMID:19625445	Figure 4B
PMID:19625445	Figure 3D
PMID:19625445	Figure 3D
PMID:19625445	Figure 3D
PMID:19625445	Figure 3D
PMID:19625445	figure 4A IS THIS NORMAL OR EVEN HIGHER THAN WT? (this is higher than wis1DD-cpc2delet so must be increased
PMID:19625445	Fig 1
PMID:19625445	Fig 1
PMID:19625445	Figure 9B
PMID:19625445	figure 4A IS THIS NORMAL OR EVEN HIGHER THAN WT?
PMID:19625445	figure 4A
PMID:19625445	Figure 3D
PMID:19625445	Fig 2D
PMID:19625445	Fig 2D
PMID:19625445	Fig 2A
PMID:19625445	Fig 2A
PMID:19625445	Fig 1
PMID:19625445	fig 1D
PMID:19625445	Fig 2B
PMID:19625445	Fig 2B
PMID:19625445	Fig 2A
PMID:19625445	Fig 1C
PMID:19625445	Fig 1C
PMID:19625445	Fig 1 C
PMID:19625445	Fig 1C
PMID:19625445	Fig 1C
PMID:19625445	Fig 2B
PMID:19625445	Fig 2A
PMID:19625445	Fig 2B
PMID:19625445	Fig 2A
PMID:19625445	Fig 2A
PMID:19625445	Fig 2A
PMID:19625445	fig 1D
PMID:19625445	fig 1D
PMID:19625445	fig 1D
PMID:19627505	localization requires F-actin (assayed using latrunculin A) and membrane rafts (assayed using filipin)
PMID:19636559	not shown, from text
PMID:19636559	not shown, from text
PMID:19636559	not shown, from text
PMID:19643199	fig 1 d
PMID:19643199	fig 1 d
PMID:19643199	fig 1 d this term should really be trafficing
PMID:19643199	fig 1 c
PMID:19646873	S2
PMID:19646873	2f
PMID:19646873	2f
PMID:19646873	2f
PMID:19646873	2f
PMID:19680287	Fig. S2A
PMID:19680287	Fig. 2B
PMID:19680287	Fig. 2B
PMID:19680287	Fig. 3B/C moved down from congresssion to abnormal mitotic sister chromatid biorientation ?
PMID:19680287	Fig. 3B/C. SEE ABOVE
PMID:19680287	Fig. 3B/C
PMID:19680287	Fig. 3E
PMID:19680287	Fig. 3E
PMID:19680287	Fig. S2A
PMID:19680287	Fig. 3E
PMID:19680287	Fig. 1A
PMID:19680287	Fig. 1A
PMID:19680287	Fig. 3E, S9
PMID:19680287	Fig. 1A
PMID:19680287	Fig. 1A
PMID:19680287	Fig. 1A
PMID:19680287	Fig. 1B, S3
PMID:19680287	Fig. 3E, S9
PMID:19680287	Fig. 1B, S3
PMID:19680287	Fig. 1B, S3
PMID:19680287	rarely showed a delay in bi-orienting chromosomes that had been pulled towards one SPB (Fig 3B,D; supplementary Fig S4F online).
PMID:19680287	(Fig 3C), showed a similar fraction of mono-oriented chromosomes as wild-type cells
PMID:19680287	Fig. S10
PMID:19680287	Fig. S7
PMID:19680287	Fig. S6C/D
PMID:19680287	Fig. 1B, S3
PMID:19680287	Fig. 2A assayed with plo1 GFP
PMID:19680287	Fig. S6C/D
PMID:19680287	Fig. S6A/B
PMID:19680287	Fig. S2B
PMID:19680287	Fig. S2B
PMID:19680287	Fig. S2B
PMID:19680287	Fig. S2A
PMID:19686686	interphase, prophase, metaphase,anaphase A
PMID:19686686	fig 1e
PMID:19686686	Fig. 5C
PMID:19686686	interacts with unmodified Klp9 PR:000027705
PMID:19686686	fig 1e
PMID:19686686	fig 1e
PMID:19686686	Figure 3 D
PMID:19686686	Fig. 5C
PMID:19686686	Fig. 5C
PMID:19686686	Fig. 5C
PMID:19686686	Figure 3 D
PMID:19686686	fig 1e
PMID:19686686	fig 1e
PMID:19686686	mitotic anaphase B
PMID:19686686	interphase, prophase, metaphase,anaphase A
PMID:19686686	cdc2 dependent phophorylation (fig. 4B)
PMID:19686686	fig 1e
PMID:19686686	fig 1e
PMID:19686686	with monopolar spindle
PMID:19686686	interacts with unmodified Ase1 PR:000027520
PMID:19686686	interphase, prophase, metaphase,anaphase A
PMID:19686686	interphase, prophase, metaphase,anaphase A
PMID:19686686	mitotic anaphase B, mitotic telophase
PMID:19686686	mitotic anaphase B, mitotic telophase
PMID:19686686	fig 4 a
PMID:19686686	fig 4 a
PMID:19686686	Figure 3 D
PMID:19686686	Figure 3 D
PMID:19686686	Figure 3 D
PMID:19686686	cdc2 dependent phophorylation (fig. 5B)
PMID:19696784	fig 1 c
PMID:19696784	Fig 2A,B
PMID:19696784	(Fig 3B)
PMID:19696784	(Fig 3B)
PMID:19696784	(Fig 3B)
PMID:19696784	figure5
PMID:19696784	supplementary Fig S6 online
PMID:19696784	fig 1 c
PMID:19713940	temperature restrictive for cdc25-22
PMID:19713940	temperature restrictive for cdc25-22
PMID:19713940	assayed using N-terminal Rng2-Ns fragment or calponin homology domain (CHD) fragment
PMID:19713940	observed after short-duration overexpression
PMID:19713940	temperature restrictive for cdc25-22
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig 2
PMID:19723888	fig 2
PMID:19723888	figure 2B
PMID:19723888	Fig 2A III
PMID:19723888	Fig 2A III
PMID:19723888	Fig 2A III
PMID:19723888	Fig 2A III
PMID:19723888	fig1C
PMID:19723888	fig1C
PMID:19723888	fig1D
PMID:19723888	fig1D
PMID:19723888	fig1D
PMID:19723888	fig1C
PMID:19723888	fig1C
PMID:19723888	fig1C
PMID:19723888	fig1C
PMID:19723888	fig1C
PMID:19723888	fig1C,D
PMID:19723888	fig1C
PMID:19723888	fig1C
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	figure 1B
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19723888	fig1A
PMID:19736319	2% fig 6a. to dauughter
PMID:19736319	add to def, septated in interphase. one compartment is anucleate
PMID:19736319	arrested normal size (multiple rounds of cytokinesis) in interphase
PMID:19736319	Fig. S1 C, arrows
PMID:19736319	Fig. S1 B and not depicted
PMID:19736319	Fig. 4 B and not depicted
PMID:19736319	fig 4d
PMID:19736319	2% fig 6a
PMID:19736319	Fig. 4 B and not depicted
PMID:19758558	Fig. S3D
PMID:19798055	decreased overall
PMID:19804755	residues include one or more of S77, T78, T79, S87, and T89, and other(s)
PMID:19804755	ctp-Phosphorylated
PMID:19879140	MT spindown assay.
PMID:19879140	MT spindown assay
PMID:19879140	Biochemistry
PMID:19942659	major
PMID:19942659	minor
PMID:19942659	Like the gms1D mutant, neither the uge1D strain nor the uge1Dgal10D strain reacted with PNA (Fig. 2b
PMID:19942852	fig1
PMID:19942852	S2 &3
PMID:19942852	S2 &3
PMID:19942852	1D
PMID:19942852	fig3
PMID:19942852	fig1
PMID:19942852	1D
PMID:19942852	fig1
PMID:19942852	fig1
PMID:19942852	fig3
PMID:19942852	fig6a
PMID:19942852	fig3
PMID:19942852	fig6a
PMID:19942852	1D
PMID:19942852	1D
PMID:19942852	1D
PMID:19942852	1D
PMID:19942852	1D
PMID:19942852	1D
PMID:19948483	Fig. 3
PMID:19948483	Fig. 3
PMID:19948483	Fig. 3
PMID:19948483	Fig. 3
PMID:19948484	they say periphery in the text but it has TM domains
PMID:19948484	this is an adaptor
PMID:19948484	they say periphery in the text but it has TM domains
PMID:19965387	fig 3a
PMID:19965387	fig S3
PMID:19965387	4c
PMID:19965387	S3, mes1delta background
PMID:19965387	S3, mes1delta background
PMID:19965387	S3, mes1delta background
PMID:19965387	S6
PMID:19965387	fig2c, in psc3-1T background
PMID:19965387	fig2c, in psc3-1T background
PMID:19965387	fig2c, in psc3-1T background
PMID:19965387	fusion experiments fig3
PMID:19965387	fusion experiments fig3
PMID:19965387	fusion experiments fig3
PMID:19965387	fusion experiments fig3
PMID:19965387	4g
PMID:19965387	4g
PMID:19965387	4g
PMID:19965387	4g
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig S3
PMID:19965387	4c
PMID:19965387	S6
PMID:19965387	S6
PMID:19965387	S6
PMID:19965387	S6
PMID:19965387	fig2c, in psc3-1T background
PMID:19965387	fig 2e
PMID:19965387	fig 2e
PMID:19965387	fig 2e
PMID:19965387	fig 2e
PMID:19965387	fig 2f
PMID:19965387	fig 2f
PMID:19965387	fig 2f
PMID:19965387	fig 2f
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig 3a
PMID:19965387	fig S5
PMID:19965387	S3, mes1delta background
PMID:19965387	S6
PMID:19965387	S6
PMID:20062003	4
PMID:20062003	2D
PMID:20062003	3
PMID:20062003	4
PMID:20062003	4
PMID:20062003	4
PMID:20062003	4
PMID:20062003	4
PMID:20062003	S1
PMID:20062003	S1
PMID:20062003	S1
PMID:20075862	3a left panel
PMID:20089861	Indeed, the R288K and Q364R mutations in SpHCS confer diminished sensitivity to feedback inhibition by L-lysine in vitro and in vivo (Table 2 and Fig. 4)
PMID:20089861	Indeed, the R288K and Q364R mutations in SpHCS confer diminished sensitivity to feedback inhibition by L-lysine in vitro and in vivo (Table 2 and Fig. 4)
PMID:20094029	Forms gamma H2A dependent nuclear foci when over-expressed
PMID:20110347	32 degrees
PMID:20110347	32 degrees; semi-permissive for cdc8-27 alone
PMID:20110347	25 degrees
PMID:20110347	25 degrees
PMID:20110347	25 degrees
PMID:20110347	32 degrees
PMID:20110347	25 or 32 degrees; latter semi-permissive for cdc8-27 alone
PMID:20110347	32 degrees
PMID:20110347	25 degrees
PMID:20123974	also ctp1,rec12,rad22,rti1,rad51,dmc1 unequal sister chromatid recombination (USCR)
PMID:20123974	increased unequal sister chromatid recombination
PMID:20123974	increased unequal sister chromatid recombination
PMID:20123974	increased unequal sister chromatid recombination
PMID:20129053	snoRNAs with extended poly(A) tails accumulate in these foci
PMID:20129053	snoRNAs with extended poly(A) tails accumulate in these foci
PMID:20140190	full-length Rad3 or Rad3-kd-delta
PMID:20140190	same as nbs1-c60-delta alone
PMID:20140190	full-length Rad3 or Rad3-kd-delta
PMID:20140190	same as nbs1-c60-delta alone
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20164182	unstressed cells
PMID:20211136	not sure which clrc subunit it binds to?
PMID:20211136	this is the endogenous dg repeat
PMID:20211136	endogenous ade6
PMID:20211136	abolished at exogenous RNA polII transcribed gene
PMID:20226666	Figure 1 in interphase
PMID:20226666	Figure 1
PMID:20226666	Figure 1 in interphase
PMID:20226666	Figure 1
PMID:20230746	involved in negative regulation of transcription via transcription factor catabolism
PMID:20299449	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20299449	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20299449	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20299449	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20360683	assayed using GFP reporter with or without premature stop codons
PMID:20360683	assayed using GFP reporter with or without premature stop codons
PMID:20360683	assayed using ypt3 reporter with or without premature stop codons
PMID:20360683	assayed using ypt3 reporter with or without premature stop codons
PMID:2038306	pMNScdc2-DL5 is integrated. Cells observed after 12 hours over expression Figure 2. In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity . The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.
PMID:2038306	CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of kinase activity assayed. S. pombe cdc2+ is on a multi copy plasmid pMNScdc2 Figure 4A lane 1
PMID:2038306	CDC2HS complements cdc2delete phenotype Figure 4B
PMID:2038306	the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS. S. pombe cdc2+ is expressed from episomal pMNScdc2 in presence of thiamine. The cdc2 is therefore not really over expressed but I was unable to say it was 'not assayed' Figure 3C
PMID:2038306	cdc2-DL5 is over expressed from episomal pMNScdc2DL5. The endogenous cdc2+ has been replaced by the human cdc2 gene CDC2HS. Same phenotype as shown in Figure 2
PMID:2038306	the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS. S. pombe cdc2+ is on an episomal plasmid pMNScdc2 Figure 3D
PMID:2038306	pMNScdc2-DL5 fails to rescue cdc2-33 mutant at the restrictive temperature. Do not say how this was assayed
PMID:2038306	pMNScdc2-DL5 is integrated
PMID:2038306	pMNScdc2-DL5 is an episomal plasmid.
PMID:2038306	pMNScdc2-DL5 is integrated cells observed after 30 hours over expression Figure 2. In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity . The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.
PMID:2038306	Data not shown. pMNScdc2-DL5 is integrated
PMID:2038306	co ip of cdc2-DL5 and endogenous CDC2HS with anti cdc13 SP4 shows reduced kinase activity compared to CDC2HS alone Figure 7. cdc2-DL5 is on episomal pMNS cdc2DL5. The authors argue that inactive cdc2-DL5 may titrate away factors required for cdc2 kinase activity but unless I have misunderstood the experiment I think this could just as well be interpreted as SP4 iping a mixture of active and inactive cdc2 kinase activity and thus less total cdc2 kinase activity
PMID:2038306	cdc2-DL5 is expressed from episomal pMNScdc2DL5. CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity Figure 4A lane pMNSDL5-
PMID:2038306	cdc2-DL5 is over expressed from episomal pMNScdc2DL5. CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity assayed. Figure 4A lane pMNSDL5-
PMID:2038306	Data not shown. pMNScdc2-DL5 is integrated
PMID:20383139	fig3a par1, the regulatory subunit was used in the assay
PMID:20383139	fig1b
PMID:20383139	fig1b
PMID:20383139	fig1b
PMID:20383139	fig1b
PMID:20383139	Fig 1d
PMID:20383139	Fig 1e
PMID:20383139	fig1e
PMID:20383139	fig 1d
PMID:20383139	Fig. S1a
PMID:20383139	Fig. 2b
PMID:20383139	Fig. 2b
PMID:20383139	Fig. 2b
PMID:20383139	Fig. 2b
PMID:20383139	fig3a
PMID:20383139	fig3a
PMID:20383139	fig 3 c
PMID:20383139	fig 3 c
PMID:20383139	separation
PMID:20383139	fig 4 c
PMID:20383139	Fig. S5
PMID:20383139	Fig. S5
PMID:20383139	Fig. 5b
PMID:20383139	Fig. 5b
PMID:20383139	fig 5B
PMID:20383139	fig 5c
PMID:20383139	Fig. 5b
PMID:20383139	Fig. 5c
PMID:20383139	fig3a
PMID:20434336	Figures2A and 2B
PMID:20434336	Figures2A and 2B
PMID:20434336	Figures2A and 2B
PMID:20434336	Figures2A and 2B
PMID:20434336	Figures2A and 2B
PMID:20434336	Fig1
PMID:20434336	figure S1C
PMID:20434336	figure S1B
PMID:20434336	Fig 1
PMID:20434336	Fig 1
PMID:20434336	data not shown
PMID:20434336	Fig1
PMID:20434336	Fig 1
PMID:20434336	Fig 1
PMID:20434336	Fig 1
PMID:20434336	Fig 1
PMID:20434336	Fig1
PMID:20434336	Fig1
PMID:20434336	Fig 1
PMID:20434336	figure S1C
PMID:20434336	Fig 4E
PMID:20434336	Fig3 C
PMID:20434336	Fig3 C
PMID:20434336	Fig3 C protein distributed in cortex
PMID:20434336	(Figure S3A)
PMID:20434336	fig3
PMID:20434336	fig3
PMID:20434336	fig3
PMID:20434336	fig3
PMID:20434336	fig3
PMID:20434336	fig3
PMID:20434336	Fig 2D tubular/cortical
PMID:20434336	Figures2A and 2B cortical/tubular
PMID:20434336	Figures2A and 2B cortical/tubular
PMID:20434336	Figures2A and 2B
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	PCNA trimerization
PMID:20452294	PCNA trimerization
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20517925	Fig. S1
PMID:20517925	Fig. 3D
PMID:20517925	Fig. 3D
PMID:20517925	formation
PMID:20517925	Fig. 1B
PMID:20517925	Fig. 1B oreover, actin cables often significantly overgrew in these cells while the actin ring formation seemed to be unaf- fected.
PMID:20517925	Fig. 1B
PMID:20517925	Fig. 1B
PMID:20547592	Figure 5A
PMID:20547592	figure 6 a
PMID:20547592	fig 5 b
PMID:20547592	Figure 8A and B (fairly similar expression orofiles)
PMID:20547592	(Figure 7B)
PMID:20547592	fig 1
PMID:20547592	fig 1
PMID:20547592	fig 1 nuclear
PMID:20547592	fig 1 c
PMID:20547592	fig 2 e suggesting that Vgl1 might escort RNA from ER-associated polyribosomes to the cytosol under thermal stress.
PMID:20547592	fig 5 e
PMID:20547592	Figure 3A
PMID:20547592	figure 4
PMID:20547592	fig 5 a
PMID:20547592	fig 5 b
PMID:20547592	Figure 5A
PMID:20547592	fig 6 D
PMID:20547592	fig 6 c
PMID:20547592	Figure 6E)
PMID:20547592	(Figure 7A)
PMID:20605454	pol II CTD; probably S2 but can't rule out effect on S7
PMID:20605454	polII CTD; probably S5 but can't rule out effect on S7
PMID:20605454	at ste11
PMID:20605454	at ste11
PMID:20605454	at ste11
PMID:20605454	at ste11
PMID:20605454	at act1 & sam1
PMID:20605454	at act1 & sam1
PMID:20622008	at genes
PMID:20622014	temperature restrictive for mmi1-ts3
PMID:20622014	pol II localization to sme2 locus
PMID:20622014	temperature restrictive for mmi1-ts3
PMID:20622014	temperature restrictive for mmi1-ts3
PMID:20622014	temperature restrictive for mmi1-ts3
PMID:20622014	temperature restrictive for mmi1-ts3
PMID:20623139	low expressivity
PMID:20623139	high expressivity
PMID:20624975	fig 5C
PMID:20624975	Fig. S5 B–E
PMID:20624975	depolymerization (cytoplasmic?)
PMID:2065367	severity is variable, and segregates over successive generations (but not 2:2)
PMID:2065367	incomplete penetrance due to translational frameshifting
PMID:2065367	incomplete penetrance due to translational frameshifting
PMID:2065367	incomplete penetrance due to translational frameshifting
PMID:2065367	incomplete penetrance due to translational frameshifting
PMID:2065367	incomplete penetrance due to translational frameshifting
PMID:2065367	incomplete penetrance due to translational frameshifting
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase
PMID:20661445	Phosphorylated at mating type locus during S-phase in Rad3 dependent manner
PMID:20661445	Phosphorylated at mating type locus during S-phase, Rad3-dependent
PMID:20661445	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	ChIP
PMID:20661445	Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase
PMID:20661445	Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase, Rad3-dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Rad3 dependent
PMID:20661445	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20679485	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20679485	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20705466	temperature semi-permissive for cdc8-27
PMID:20705466	temperature semi-permissive for cdc8-27
PMID:20705466	temperature semi-permissive for cdc8-27
PMID:20705466	temperature semi-permissive for cdc8-27
PMID:20705471	temperature permissive for cdc8-27
PMID:20736315	Fig4
PMID:20736315	Fig1B
PMID:20736315	Fig1B
PMID:20739936	Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h)
PMID:20739936	figS6
PMID:20739936	figS6
PMID:20739936	suppressed at comparable level to Bir1–CD, These results indicate that once they are tethered at centromeres, the functionality is indistinguishable between Bir1 and Bir1-8A. Supporting this conclusion, complex formation of the CPC was intact in bir1-8A cells (Supplementary Fig. 7).
PMID:20739936	Supplementary Fig. 8a)
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	The cdc13-M7 mutant is suppressed by bir1-8D
PMID:20739936	fig2a
PMID:20739936	Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h)
PMID:20739936	fig2a,b. figS5
PMID:20739936	fig2a,b. figS5
PMID:20739936	Supplementary Fig. 8a)
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig. 1e/Fig. 1f
PMID:20739936	fig S1
PMID:20739936	fig S1. Nuclear staining of anaphase cells showed that the cdc13-M7 mutant, but not the conventional cdc13-117 mutant, often exhibited lagging chromosomes at anaphase (Fig. 1c).
PMID:20739936	fig 1b
PMID:20739936	figb
PMID:20739936	fig1
PMID:20739936	fig 1k
PMID:20739936	fig 1c
PMID:20739936	fig1d,k
PMID:20739936	fig1c
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig. 1e also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	Fig 1h
PMID:20739936	Fig 1i
PMID:20739936	fig1j
PMID:20739936	fig1j
PMID:20739936	fig1S4/ figS5
PMID:20739936	fig2a,b. figS5
PMID:20739936	fig2a
PMID:20799962	same as rid1-1 alone
PMID:20799962	same as rid2-1 alone
PMID:20805322	assayed substrate MBP
PMID:20805322	negative reg of polarization/remodelling
PMID:20805322	assayed substrate MBP
PMID:20805322	assayed substrate MBP
PMID:20805322	assayed substrate MBP
PMID:20805322	assayed substrate MBP
PMID:20805322	Fig. 1 A and Table I)
PMID:20805322	assayed substrate MBP
PMID:20805322	assayed substrate MBP
PMID:20805322	assayed substrate casein
PMID:20807799	GO:0051329= mitotic interphase
PMID:20807799	"vw: I used ""added by naa20 which is the catalytic subunit for naa25"""
PMID:20807799	PR:000037081= tropomyosin cdc8, acetylated form (fission yeast)
PMID:20807799	acetylated Cdc82 so could use PR:000037081
PMID:20826461	fig 4
PMID:20826461	fig 6
PMID:20826461	fig 5
PMID:20826461	fig 6
PMID:20826461	fig 6
PMID:20826461	fig 6
PMID:20826461	fig 5
PMID:20826461	fig 5
PMID:20826461	fig 5
PMID:20826461	fig 2C
PMID:20826461	fig 2C
PMID:20826461	fig 2C
PMID:20826461	fig 2C
PMID:20826461	fig 2B
PMID:20826461	fig 2A
PMID:20826461	fig 2A
PMID:20826461	fig 2A
PMID:20826461	(Fig. 1F
PMID:20826461	(Fig. 1F
PMID:20826461	Fig. 1
PMID:20826461	Fig. 1
PMID:20826461	(Fig. 1C
PMID:20826805	if it is there after cytokinesis + during anaphase B, then I guess it is safe to say that it is there during cytokinesis too..
PMID:20826805	seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.
PMID:20826805	seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.
PMID:20826805	seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.
PMID:20826805	if it is there after cytokinesis + during anaphase B, then I guess it is safe to say that it is there during cytokinesis too..
PMID:20829365	figure 5
PMID:20829365	figure 3
PMID:20829365	figure 1 a
PMID:20829365	figure 2 a
PMID:20829365	figure 2 a
PMID:20829365	figure 3
PMID:20829365	figure 3
PMID:20829365	figure 3
PMID:20829365	figure 1 a
PMID:20829365	figure 3
PMID:20833892	fig 3 B WT 10%
PMID:20854854	fig 1b
PMID:20854854	fig 3
PMID:20854854	fig 1c
PMID:20854854	fig 1c
PMID:20854854	fig 1c
PMID:20854854	fig 3
PMID:20854854	fig 1a
PMID:20854854	fig 1a
PMID:20854854	I don't understand the chemistry well enough to know how the HPLC shows this but I think this is enough evidence?
PMID:20854854	fig 1b
PMID:20854854	fig 1a
PMID:20885790	less sensitive than ssb3delta alone
PMID:20890290	Second, eRF1 and Dom34 increase the bind- ing of GTP to eRF3 and Hbs1, respectively, and GTP increases the binding of eRF1 and Dom34 to eRF3 and Hbs1, respectively28,32,33 (Fig. 6 and Supplementary Table 1). These interactions suggest that in both complexes the status of the nucleotide affects the interaction of the proteins and thereby modulates the function of the complex.
PMID:20890290	Second, eRF1 and Dom34 increase the bind- ing of GTP to eRF3 and Hbs1, respectively, and GTP increases the binding of eRF1 and Dom34 to eRF3 and Hbs1, respectively28,32,33 (Fig. 6 and Supplementary Table 1). These interactions suggest that in both complexes the status of the nucleotide affects the interaction of the proteins and thereby modulates the function of the complex.
PMID:20924116	regulates binding by Mrc1
PMID:20924116	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	regulates binding by Mrc1
PMID:20924116	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20929775	phosphorylated
PMID:20929775	phosphorylated
PMID:20929775	K9 methyl;ated
PMID:20929775	K9-mehtylated
PMID:20929775	phosphorylated
PMID:20929775	K9-mehtylated
PMID:20935472	during metaphase
PMID:20935472	Thus, we conclude that Cdc2 activity prevents precocious localization of Mde4 to the metaphase spindle.
PMID:20937798	in supp fig1 shows weak sensitivity at high cadmium concentrations
PMID:20944394	https://github.com/geneontology/go-ontology/issues/15345
PMID:20967237	Fig4A
PMID:20967237	Fig6D,E in presence of LatA + MBC there is no SPB separation compared to + MBC only where SPBs can separate
PMID:20967237	Fig2B in this case (high temp + MBC) cells can proceed through cell cycle and replicate their DNA
PMID:20967237	Fig5A
PMID:20967237	Fig4E
PMID:20967237	Fig4C followed the presence of clp1 in the nucleolus to monitor cen3
PMID:20967237	data not shown
PMID:20967237	Fig4B
PMID:20967237	Fig1A,B In the presence of MBC the % cut cells in wild type is almost identical to mad2 Delta at 32 and 35°c suggesting that the spindle assembly checkpoint is not active or overidden above 32°C in wild type cells in presence of MBC.
PMID:20967237	Fig1C
PMID:20967237	Fig1E
PMID:20967237	Fig1D
PMID:20967237	Fig1D
PMID:20967237	Fig1D
PMID:20967237	Fig1D; microtubules absent
PMID:20967237	Fig2 A
PMID:20967237	Fig2B in this case (high temp no MBC) the checkpoint is active at high temperature and cells are blocked in cell cycle progression at 36°C.
PMID:20967237	Fig2c
PMID:20967237	Fig2c in presence of MBC cells re-enter S phase earlier than in the absence of MBC
PMID:20967237	Fig3B just a short microtubule stub remains
PMID:20967237	Fig3C
PMID:20967237	Fig3 D
PMID:20967237	Fig 3F
PMID:20967237	Fig3E
PMID:20967237	video S3
PMID:20967237	Fig3G suggests nuclear fission is independent of spindle checkpoint
PMID:20967237	Fig4D
PMID:20980623	dma1􏰁 spg1-106 and dma1􏰁 mob1-1 cells were com- pletely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compro- mised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	Figure 4E
PMID:20980623	Figure 4E
PMID:20980623	several types of defects in FSM de- velopment in dma1􏰁 cells (Figure 6B). These defects roughly fell into three classes: (1) initially FSM formation was normal and appeared as sphere structure, but subse- quently it became smaller or collapsed (asterisks in Figure 6B); (2) crescent-shaped structures did not properly develop into cup-like structures (open arrows in Figure 6B); and (3) crescent-shaped structures broke into multiple GFP-Psy1- contaning structures which could not develop into round mature FSMs (arrows in Figure 6B).
PMID:20980623	the initiation of spore formation was delayed for 􏰃2 h com- pared with wild-type cells, and also the efficiency of spore formation was dramatically dropped with only 􏰃60% of cells containing spores (Figure 3B).
PMID:20980623	fig2
PMID:20980623	figS1
PMID:20980623	dma1􏰁 spg1-106 and dma1􏰁 mob1-1 cells were com- pletely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compro- mised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	dma1􏰁 spg1-106 and dma1􏰁 mob1-1 cells were com- pletely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compro- mised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	Fig 2 B&C At anaphase II, however, many of the Dma1-GFP signals did not accumulate at SPBs
PMID:20980623	upplemental Figure S3
PMID:20980623	figS1
PMID:20980623	Figure 3B Figure 4B the initiation of spore formation was delayed for 􏰃2 h com- pared with wild-type cells, and also the efficiency of spore formation was dramatically dropped with only 􏰃60% of cells containing spores
PMID:20980623	upplemental Figure S3
PMID:21035342	"(this is a bit of a fudge. It should probably be molecular signal transducer but that does not exist and I am prevented from using high level terms) vw: From review:Rab small GTPase emerges as a regulator of TOR complex 2""Consistently, we successfully collected genetic and biochemical data to supportthe notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7).I agree the data supports this model. Moreover, the Ryh1 I44E mutant fails to promote TORC2 signaling, implying that GTP-dependent interaction of Ryh1 with TORC2 via the effector domain drives TORC2-Gad8 signaling."
PMID:21035342	"vw: From review:Rab small GTPase emerges as a regulator of TOR complex 2 ""Consistently, we successfully collected genetic and biochemical data to support the notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7). I agree the data supports this model."
PMID:21035342	"vw: From review:Rab small GTPase emerges as a regulator of TOR complex 2 ""Consistently, we successfully collected genetic and biochemical data to support the notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7). I agree the data supports this model."
PMID:21035342	vw: bit 61 is importabt for torc2 regulation by ryh1
PMID:21095590	fig 5b
PMID:21095590	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6
PMID:21095590	fig 5b
PMID:21095590	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6
PMID:21098122	nuclease-dead allele
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098122	no expressivity extension because of decreased growth when untreated
PMID:21098141	In SGs after hyperosmotic shock (1 M KCl) but not after glucose deprivation
PMID:21099360	30 degrees; restrictive for hsk1-89 alone
PMID:21099360	25 degrees
PMID:21099360	30 degrees
PMID:21099360	30 degrees
PMID:21099360	in SQ/TQ clusters . , activated_by(CHEBI:29035)
PMID:21099360	not in SQ/TQ clusters
PMID:21099360	at ars2004 and oriChr2-1266, during early S phase
PMID:21099360	hsk1 phenotypes more informative than mrc1 itself
PMID:21099360	30 degrees
PMID:21099360	same as hsk1-89 alone
PMID:21099360	30 degrees; same as hsk1-89 alone
PMID:21099360	25 degrees, same as hsk1-89 alone
PMID:21099360	same as hsk1-89 alone
PMID:21099360	25 degrees, same as hsk1-89 alone
PMID:21099360	25 degrees, same as hsk1-89 alone
PMID:21099360	same as hsk1-89 alone
PMID:21099360	30 degrees; same as hsk1-89 alone
PMID:21099360	MBP substrate
PMID:21099360	25 degrees
PMID:21099360	25 degrees, same as hsk1-89 alone
PMID:21099360	30 degrees; same as hsk1-89 alone
PMID:21099360	30 degrees; same as hsk1-89 alone
PMID:21107719	localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:21113731	Microscopy co-localization
PMID:21118717	Deletion of both cyr1/git2 and cgs2 produces cells that are hypersensitive to both exogenous cAMP and cGMP as these can activate PKA at low micromolar concentrations. Fig. 1A, B
PMID:21118717	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21118717	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21131906	nda1- background to activate spindle checkpoint
PMID:21131906	nda1- background to activate splindle checkpoint
PMID:21131906	nda1 background to activate spindle checkpoint
PMID:21131906	un- ubiquitinated
PMID:21148300	Cdc42-GTP assayed with CRIB
PMID:21148300	Cdc42-GTP assayed with CRIB
PMID:21148300	Cdc42-GTP assayed with CRIB
PMID:21148300	Cdc42-GTP assayed with CRIB
PMID:21151114	independent of Clr4
PMID:21151114	independent of Clr4
PMID:21151114	independent of Clr4
PMID:21151114	SO:0000286 = LTR
PMID:21151114	independent of Clr4
PMID:21151114	independent of Clr4
PMID:21151114	independent of Clr4
PMID:21151114	independent of Clr4
PMID:21151114	SO:0000286 = LTR
PMID:21151114	independent of Clr4
PMID:21151114	independent of Clr4
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21217703	Consistent with the published results, deletion of taz1+ or rap1+ from yeast cells resulted in a dramatic increase in telomere length and length heterogeneity compared to wild-type cells (Fig. 6c).
PMID:21217703	Three mutants (Taz1 I379R, Taz1 L383R, and Rap1 I655R) with no detectable Taz1-SpRap1 interaction clearly exhibited altered mobility bands representing intra-chromosome fusions (Fig. 6e).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	Three point mutants (Taz1 I379R, Taz1 L383R, and Rap1 I655R) that completely abolished the Taz1-SpRap1 interaction in the ITC assay displayed a rap1Δ– and taz1Δ-like telomere length defect (Figs. 6b and 6c)
PMID:21256022	binding site L405 ndc80 loop
PMID:21256022	affecting dis1
PMID:21300781	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21300781	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21300781	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21300781	fig7
PMID:21300781	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21307936	supp fig 9A
PMID:21317872	colocalization with Pcf11
PMID:21317872	poly(A) tails longer in rrp6delta alone, but wild type not shown for meiotic cell cycle so can't annotate rrp6delta phenotype as normal or increased length
PMID:21317872	poly(A) tails longer in rrp6delta alone, but wild type not shown for meiotic cell cycle so can't annotate rrp6delta phenotype as normal or increased length
PMID:21317872	presumably in homozygous diploid
PMID:21357609	Mitochondrial dye showed diffuse staining. they think it is a loss of membrane potential so the dye is not drawn in properly
PMID:21389117	fig 1B: 4 nuclei appear later than normal.
PMID:21389117	fig 1c, no tetranucleates
PMID:21389117	fig2A
PMID:21389117	fig2A
PMID:21389117	fig2B
PMID:21389117	fig2B
PMID:21389117	fig 6C
PMID:21389117	fig 6C
PMID:21389117	fig 7A
PMID:21389117	fig 7A
PMID:21389117	fig 7A
PMID:21389117	fig 7A
PMID:21389117	also fzr3
PMID:21389117	fig2A
PMID:21389117	fig2B
PMID:21389117	also fzr2 &3
PMID:21389117	i changed this to +ve reg /AL
PMID:21389117	I'm not completely sure if the Slp1-APC degrades mes1 or only ubiquitinates it, but this is most likely correct?...
PMID:21389117	fig 1B: 4 nuclei appear later than normal.
PMID:21389117	fig 1B: 4 nuclei appear later than normal.
PMID:21429938	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21429938	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21429938	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21429938	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21437270	ch16
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21441914	no expressivity extension because of decreased growth when untreated
PMID:21444751	Collectively, these results indicate that in fission yeast, a ?-TuRC- like complex exists as a stable structure in vivo independent of the Mto1/2 complex
PMID:21449049	mei4-N136A combined with pat1-114 was efficiently blocked at the meiosis I onset with telomere clustered at SPBs (in the bouquet configuration) at 32˚C, which arrest can be released by a temperature shift down to 25˚C.
PMID:21449049	mei4-N136A combined with pat1-114 was efficiently blocked at the meiosis I onset with telomere clustered at SPBs (in the bouquet configuration) at 32˚C, which arrest can be released by a temperature shift down to 25˚C.
PMID:21450810	Rpc2-T455I was clearly more active (white) in yJI1 than in yYH1, consistent with dT(6) readthrough as expected.
PMID:21450810	C11-F32S was more active in yJI1 than in yYH1, while wild-type C11 had no effect (Sector 4).
PMID:21518960	assayed elongation from ori1-200
PMID:21518960	comment assayed at ars1 and ars2004
PMID:21518960	comment assayed at ars1 and ars2004
PMID:21518960	comment assayed at ars1 and ars2004
PMID:21518960	assayed at ars1 and ori1-200 (early-firing origins); only affects origins normally bound by Mrc1
PMID:21518960	assayed elongation from ars1 and ars2004 (early-firing origins)
PMID:21518960	assayed at ars1 and ars2004 (early-firing origins)
PMID:21518960	predominantly at early-firing origins including ars1 and ars2004, but not AT1041; Mrc1 associates with origins later than MCM complex, but slightly earlier than Cdc45
PMID:21518960	assayed at ars1 and ars2004 (early-firing origins)
PMID:21536008	"heterologous cytc as acceptor. they had to include this as etp1 wouldn't accept an electron otherwise. ""S. pombe does not express any endogenous mitochondrial cytochromes P450 that could act as terminal electron acceptors"""
PMID:21540296	figure 7c, no rescue of cnd-2
PMID:21540296	t-shift on mitotic entry fig1c
PMID:21540296	t-shift on mitotic entry fig1c
PMID:21540296	t-shift on mitotic entry fig1c
PMID:21540296	t-shift on mitotic entry fig1c
PMID:21540296	fig 4
PMID:21540296	fig 5c
PMID:21540296	fig 7a
PMID:21540296	fig 7a
PMID:21540296	fig 7a
PMID:21540296	fig 7a
PMID:21540296	figure 7e
PMID:21540296	fig 7a
PMID:21540296	fig 7a
PMID:21540296	figure 7c, no rescue of cnd-2
PMID:21540296	fig 1a
PMID:21540296	fig 1a
PMID:21540296	fig 1a
PMID:21540296	t-shift on mitotic entry fig1d
PMID:21540296	t-shift on mitotic entry fig1d
PMID:21540296	t-shift on mitotic entry fig1c
PMID:21561865	present at basal level; increased in presence of hydroxyurea
PMID:21561865	present at basal level; increased in presence of hydroxyurea
PMID:21610214	sulphate
PMID:21633354	H3-pS10 used to detect ark1 activity
PMID:21633354	centromeric
PMID:21633354	condensin, which subunit assayed?
PMID:21633354	decreased along arms
PMID:21633354	all tested chromosome loci (Fig. 2g).
PMID:21633354	all tested chromosome loci (Fig. 2g).
PMID:21652630	in fig s4b there is septal material hanging around one cell end
PMID:21652630	see S5A
PMID:21664573	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	ABOLISHED Fig 2 C
PMID:21664573	Fig 4d NORMAL SILENCING
PMID:21664573	Fig 4d NORMAL SILENCING
PMID:21664573	Figure 5B
PMID:21664573	Figure 5B
PMID:21664573	Figure 5B
PMID:21664573	Figure 5B
PMID:21664573	(Figure 4E).
PMID:21664573	(Figure 4E).
PMID:21664573	Figure 5B
PMID:21664573	Figure 5B
PMID:21664573	fig 2 b
PMID:21664573	fig 2 b c
PMID:21664573	(Supplemental Figure 2B)
PMID:21664573	(Supplemental Figure 2B)
PMID:21664573	(Supplemental Figure 2B)
PMID:21664573	(Supplemental Figure 2B)
PMID:21664573	(Supplemental Figure 2B)
PMID:21664573	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	Fig 4c NORMAL SILENCING
PMID:21664573	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	in vitro (Figure 1C & 2D)
PMID:21664573	fig 1A
PMID:21664573	fig 1A
PMID:21664573	fig 1A
PMID:21664573	fig 3A. bub3 Δklp5 double mutants arrest as inviable micro-colonies of cells
PMID:21664573	fig 3a.
PMID:21664573	fig 3 b
PMID:21664573	fig 3 b
PMID:21664573	fig 3 b
PMID:21676862	Fig 1
PMID:21693583	Fig. 8B
PMID:21693583	MF? myo1
PMID:21693583	Fig. 8A
PMID:21693583	Fig. 8B
PMID:2170029	temperature restrictive for dis2cs alone
PMID:2170029	temperature permissive for dis2cs alone
PMID:2170029	high temp is permissive
PMID:2170029	high temp is permissive
PMID:2170029	temperature restrictive for dis2cs alone
PMID:2170029	std temp is restrictive
PMID:2170029	high temp is permissive
PMID:2170029	temperature restrictive for dis2cs alone
PMID:2170029	temperature restrictive for dis2cs alone
PMID:2170029	temperature restrictive for dis2cs alone
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s
PMID:21703453	This alleles recruits Pom1 to ectopic sites at the lateral plasma membrane
PMID:21703453	not restricted to cell tips
PMID:21703453	not restricted to cell tips
PMID:21703453	in tea4-RVXF* background
PMID:21703453	required for detachment from plasma membrane
PMID:21703453	required for detachment from plasma membrane
PMID:21703453	Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s
PMID:21703453	Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:21703453	I guess some might be false positives but Sophie said it should be ok.
PMID:2172964	both partners cyr1delta
PMID:21775631	Figure S2A
PMID:21775631	Figure 1A Figure 5D
PMID:21775631	Figure S2A
PMID:21775631	Figure S2B
PMID:21775631	Figure S2B
PMID:21775631	Figure S2B
PMID:21775631	Figure S2A
PMID:21811607	basal transcription is meaningless because emm contains calcium
PMID:21813639	candidate for involved_in_or_involved_in_regulation_of qualifier
PMID:21828039	homozygous diploid
PMID:21832151	endosomal localization requires F-actin (assayed using latrunculin A)
PMID:21847092	bound by the C-terminal dsrbd domain
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Fig 1B
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Fig 1A
PMID:21849474	Fig 1A
PMID:21849474	Fig 1A
PMID:21849474	Table 1A
PMID:21849474	Fig 1A
PMID:21849474	Fig1A Fig2A
PMID:21849474	Fig 1A
PMID:21849474	Fig 1A Fig2A
PMID:21849474	Fig 1A
PMID:21849474	Fig 1A
PMID:21849474	Fig2B
PMID:21849474	Fig 2 C
PMID:21849474	Fig 2 C
PMID:21849474	Fig 3 increased cell width compared to single mutants
PMID:21849474	Fig 3 increased cell width compared to single mutants
PMID:21849474	Fig 3 cell width is wider than either of the single mutants
PMID:21849474	Fig 3 no increase in cell width compared to single mutants
PMID:21849474	Figure 4 A
PMID:21849474	Figure 4 A
PMID:21849474	Figure 4 A
PMID:21849474	Fig4B
PMID:21849474	Fig4B
PMID:21849474	Fig4B, Fig8 localisation is actin dependent
PMID:21849474	Fig4B, Fig8 localisation is actin dependent
PMID:21849474	Fig4A
PMID:21849474	Fig4C
PMID:21849474	Fig4D
PMID:21849474	Fig2B
PMID:21849474	Fig5
PMID:21849474	Fig5
PMID:21849474	Fig5
PMID:21849474	Fig 6A fusion protein driven from nmt41 promoter
PMID:21849474	Fig 6B fusion protein driven from nmt41 promoter
PMID:21849474	Fig6C
PMID:21849474	Fig6C
PMID:21849474	Fig4D
PMID:21849474	Fig 1A
PMID:21849474	Fig7A, B
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Fig 1B
PMID:21849474	Fig7A, B localisation of rga4 by blt1+ is more extensive than wild type rga4 localisation but rescues the wide cell phenotype of the rga4 deletion
PMID:21849474	Fig9 cdc42-CRIB-GFP localisation is actin dependent and sensitive to low levels (10mM) Lat A
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Table 1 wide phenotype suppressed by sorbitol
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Fig 1B
PMID:21849474	Table 1 not suppressed by sorbitol
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figure 2A
PMID:21885283	Figure 3G
PMID:21885283	Figure 3D
PMID:21885283	Figure 3C
PMID:21885283	Figures 3B
PMID:21885283	Figure 3B
PMID:21885283	Figure 3B
PMID:21885283	Figures 2L, S3P– S3R
PMID:21885283	Figures 2L, S3P– S3R
PMID:21885283	Figures 2I – 2K and S3G – S3O)
PMID:21885283	Figures 2I – 2K and S3G – S3O)
PMID:21885283	Figure 2A
PMID:21885283	Figure 2A
PMID:21885283	Figure 2A
PMID:21885283	Figure 2A
PMID:21885283	TAble II
PMID:21885283	TAble II
PMID:21885283	TAble II
PMID:21885283	Figure S1K
PMID:21885283	Figure S1K
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	Table I
PMID:21885283	Table I
PMID:21885283	Table I
PMID:21885283	Table I
PMID:21885283	Table I
PMID:21885283	Table I
PMID:21892183	microtubule sliding brake https://www.ebi.ac.uk/interpro/entry/InterPro/IPR007882/#PUB00070924
PMID:21920317	Fig 4 B
PMID:21920317	>inc merotelic kinetochore attachment
PMID:21920317	fig 4
PMID:21920317	fig 1D although sister kinetochore split, segregation ends up mostly normal
PMID:21920317	fig 1D
PMID:21920317	fig 1D
PMID:21920317	( Figure 1 A) continuous rate of spindle elongation (I)
PMID:21920317	prevents bipolar attachment
PMID:21920317	fig 1D
PMID:21920317	fig 1D
PMID:21920317	Figure 1C, 1D bipolar attachment of univalents
PMID:21920317	fig 1D although sister kinetochore split, segregation ends up mostly normal
PMID:21920317	fig 1D
PMID:21920317	( Figure S3 A)
PMID:21920317	fig 1D
PMID:21920317	( Figure 1 A) phase II (metaphase) was substantially extended
PMID:21920317	fig 1D
PMID:21920317	fig 1D although sister kinetochore sometimes split, segregation ends up mostly normal
PMID:21920317	Fig 6
PMID:21920317	( Figure 1B) We found that virtually all rec12D cells (n = 240) eventually relo- calized Ark1 to the spindle (Figure 1B), indicating that the SAC ultimately becomes satisfied in achiasmate meiosis.
PMID:21920317	( Figure 1B)
PMID:21920317	fig 4B
PMID:21920317	prevents bipolar attachment
PMID:21920317	Fig 4 A
PMID:21920317	prevents bipolar attachment (Ask Takeshi if this fits better rec role)
PMID:21931816	Ser-2 of the heptad repeat
PMID:21945095	during replication fork processing
PMID:21945095	during mitotic DNA replication initiation
PMID:21945095	delete if superseded; authors not sure if it's just a detection issue, but they don't see Rad4 moving away from origins as Mcm10 does
PMID:21945095	also inferred from interaction with Cdc23 and from timing of localization to chromatin at origins
PMID:21945095	during mitotic DNA replication initiation
PMID:21945095	during mitotic DNA replication initiation
PMID:21945095	during replication fork processing
PMID:21945095	during replication fork processing
PMID:21945095	during replication fork processing
PMID:21949882	moved down from GO:0016706 30/8/2014 . activated_by(CHEBI:29033)
PMID:21965289	dis2 is required for the retreival of unclustered kinetochores in nsk delete (additive chromosome segregation defects)
PMID:21979813	Fig 4AB
PMID:21979813	2C
PMID:21979813	4E decreased kinetochore mono orientation at meiosis I
PMID:21979813	4E decreased kinetochore mono orientation at meiosis I
PMID:21979813	2C
PMID:21979813	2C
PMID:21979813	2B abolished kinetochore mono orientation at meiosis I
PMID:21979813	2B abolished mono orientation at meiosis I
PMID:21979813	1B
PMID:21979813	4E decreased kinetochore mono orientation at meiosis I
PMID:21979813	2C
PMID:22017871	ubiquitin dependent due to need for rhp6 -AL
PMID:22017871	vw updated
PMID:22017871	fig 7c shows direct dna binding
PMID:22017871	ubiquitin dependent due to need for rhp6 -AL
PMID:22017871	ubiquitin dependent due to need for rhp6 -AL
PMID:22024164	assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown)
PMID:22024164	"30 degrees, ""high"" compared to 25 degrees"
PMID:22024164	genome-wide detection
PMID:22024164	30 degrees
PMID:22024164	30 degrees
PMID:22024164	at late-firing or dormant origins; genome-wide detection
PMID:22024164	genome-wide detection
PMID:22024164	at late-firing or dormant origins; genome-wide detection
PMID:22024164	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:22024164	assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown)
PMID:22024164	early-firing origins; HU absent
PMID:22024167	vw >50% activity
PMID:22033972	structure
PMID:2203537	30% at 120 min. (archery bow)
PMID:2203537	Figure 3 A
PMID:2203537	Figure 3 A
PMID:2203537	Figure 3 A
PMID:2203537	85% at 160 min
PMID:22042620	Fig. 7 indicated by NDB cholesterol
PMID:22042620	Fig. S2, B and C
PMID:22042620	Fig. S5 B
PMID:22042620	Fig. 3 and Fig. S3, for comparative images of an inserted pro-metaphase wild-type SPB, see Fig. S1 B
PMID:22042620	not required after insertion
PMID:22042620	Fig. S5 B
PMID:22042620	fig7
PMID:22042620	Fig. S5 B
PMID:22042620	Fig. S5 B
PMID:22042620	Fig. 1, A and B;
PMID:22042620	Fig. S5 B
PMID:22042620	fig7
PMID:22042620	fig7
PMID:22042620	Fig. S5 B
PMID:22042620	Fig. S5 B
PMID:22064476	tested using several genes, and reporter construct to test mutations at or near splice sites
PMID:22065639	GO:0000236= mitotic prometaphase
PMID:22081013	3g
PMID:22081013	In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
PMID:22081013	Real time PCR analyses of transcripts derived from the dg or dh outer repeats of the centromere (Figure 3a) demonstrated that whereas cells lacking Chp1 displayed strong accumulation of transcripts, centromeric heterochromatin was unaffected by the loss of the PIN domain in chp1ΔC strains (Figure 3b,c,d Supplementary Figure 9).
PMID:22081013	3f
PMID:22081013	3f In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
PMID:22084197	FYPO:0007229
PMID:22085934	In summary, our data show that the Edc3 and Scd6 LSm domains compete for the same Dcp2- binding motifs and that both interactions are mutually exclusive
PMID:22085934	(Supplementary Figure S8C
PMID:22085934	. We used Dcp2 constructs of increasing length (Figure 1D) and found that a Dcp2 region located between residues 255 and 266 is required for the interaction with Edc3 (Figure 1D, lane 3 versus lanes 1 and 2). B
PMID:22085934	(Figure 6A)
PMID:22093869	The phenotype is assessed by the high-throughput sequencing.
PMID:22093869	The phenotype is assessed by the high-throughput sequencing.
PMID:22093869	The phenotype is assessed by the high-throughput sequencing.
PMID:22093869	The phenotype is assessed by the high-throughput sequencing.
PMID:22119525	fig 2A
PMID:22132152	fig 6
PMID:22132152	n agreement, the corresponding fractions 15–22 iso- lated from the fission yeast strain expressing GFP-tagged Cta4p were immuno-reactive with anti-GFP antibodies
PMID:22132152	fig 8 increased calcinurin activity
PMID:22132152	fig 6
PMID:22132152	fig 6
PMID:22132152	fig 5
PMID:22132152	fig 5
PMID:22132152	fig 2, 4
PMID:22132152	fig 2
PMID:22132152	fig 1, 7
PMID:22134091	fig2AB
PMID:22134091	fig2
PMID:22134091	Fig. S3A
PMID:22134091	Fig.
PMID:22134091	ig. S1B-j
PMID:22134091	fig3
PMID:22134091	fig3
PMID:22134091	in vitro
PMID:22134091	fig7F
PMID:22134091	increased affinity
PMID:22134091	in vitro
PMID:22134091	fig7F
PMID:22134091	in vitro
PMID:22134091	in vitro
PMID:22134091	22.3%
PMID:22134091	fig 1c
PMID:22134091	fig S2
PMID:22134091	fig2B
PMID:22140232	same as ssp2delta alone
PMID:22140232	same as ssp2delta alone
PMID:22140232	same as ssp2delta alone
PMID:22140232	same as ssp2delta alone
PMID:22140232	same as ssp2delta alone
PMID:22140232	(Fig. 2A). We found that Ssp2-GFP mainly localized in the nucleus both in glucose-starved cells and in cells grown in glucose-rich medium
PMID:22140232	(Fig. 2A). We found that Ssp2-GFP mainly localized in the nucleus both in glucose-starved cells and in cells grown in glucose-rich medium
PMID:22140232	same as ssp2delta alone
PMID:22140232	same as ssp2delta alone
PMID:22140232	same as ssp2delta alone
PMID:22140232	ssp2 inferred from mutant phenotype
PMID:22140232	OK, this MF is a stretch, but based on everything we know phenotypes, export of phosphorylated (typical TF regulation, ortholog etc, I'm confident these phenotypes can be used with curator knowledge to infer this.
PMID:22144463	during vegetative growth, near genes normally expressed in meiotic cell cycle
PMID:22144463	during vegetative growth, near genes normally expressed in meiotic cell cycle
PMID:22144463	during vegetative growth, near genes normally expressed in meiotic cell cycle
PMID:22144909	(serine 2)
PMID:22172946	fig 2
PMID:22172946	fig 2
PMID:22172946	fig3
PMID:22172946	fig 1 a
PMID:22172946	fig 1 a
PMID:22173095	fig 7 sdj mutant is unstable
PMID:22173095	fig 7
PMID:22173095	fig 7 sdj mutant is unstable
PMID:22173095	abolished homodimerization Fig. 6,
PMID:22180499	floculation inhibited by galactose
PMID:22184248	figure 1a
PMID:22184248	fig 1B As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint ac- tivation. We speculate that partially degraded Mph1-KD pro- teins (Fig. S2B) might be toxic to some extent.
PMID:22184248	figure 1a
PMID:22184248	figure 1a
PMID:22184248	figure 1a
PMID:22184248	When Mad2 was turned on, the index of the chromosome condensation gradually increased from 0 to more than 50%. Binucleate cells, which passed through anaphase, however, did not increase. These results indicated that when Mad2 was turned on, the cells, which were initially at the boundary of G2/M, were arrested before anaphase (Fig. 5B).
PMID:22184248	recruitment
PMID:22184248	recruitment (is this the right way around?)
PMID:22184248	It failed to cause an arrest in a strain lacking mad2+, indicating that the arrest was due to activation of the spindle checkpoint.
PMID:22184248	As shown in Fig. 3A, ex- pression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22184248	As shown in Fig. 3A, ex- pression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22184248	fig 1B As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint ac- tivation. We speculate that partially degraded Mph1-KD pro- teins (Fig. S2B) might be toxic to some extent.
PMID:22184248	We also examined localization of Mad2. Mad2 remained on kinetochores in more than 80% of the cells, indicating that the spindle checkpoint was kept active (Fig. S1 B and C)
PMID:22184248	fig 1B As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint ac- tivation. We speculate that partially degraded Mph1-KD pro- teins (Fig. S2B) might be toxic to some extent.
PMID:22184248	fig 1a
PMID:22184248	fig 1a
PMID:22235339	also assayed using bulk histones from calf thymus
PMID:22235339	also assayed using bulk histones from calf thymus
PMID:22235339	also assayed using bulk histones from calf thymus
PMID:22268381	GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B).
PMID:22268381	localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22268381	fig 5
PMID:22268381	ocalization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22268381	Moreover, expression of the Rdp1-SV40-NLS construct appeared to suppress centromeric transcript levels below that those found in wild type
PMID:22268381	fig 5
PMID:22268381	fig 4
PMID:22268381	fig 5
PMID:22268381	fig 4
PMID:22268381	onsistent with the scenario in which Rdp1 is a cargo for Sal3, we were able to detect stable interaction between tagged Rdp1 and Sal3 by co-immunoprecipitation (Figure 2B).
PMID:22268381	Pericentric transcript levels are increased in sal3 mutants
PMID:22268381	fig 5
PMID:22268381	GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B).
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22279046	same as hsk1-89 alone
PMID:22291963	mild expressivity
PMID:22291963	in asf1-33 at higher temperature
PMID:22292001	5d
PMID:22292001	1d
PMID:22292001	5d
PMID:22292001	5d
PMID:22292001	5c
PMID:22292001	5c
PMID:22292001	5
PMID:22292001	during meiosis I
PMID:22292001	fig4
PMID:22292001	"strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation"
PMID:22292001	1d
PMID:22292001	during meiosis I
PMID:22292001	during meiosis I
PMID:22292001	1d
PMID:22292001	5
PMID:22292001	"strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation"
PMID:22292001	fig3e
PMID:22292001	5c
PMID:22292001	5c
PMID:22292001	fig2
PMID:22292001	fig2
PMID:22292001	fig2
PMID:22292001	fig3d
PMID:22292001	5
PMID:22292001	5
PMID:22292001	5
PMID:22292001	5
PMID:22292001	fig3e
PMID:22292001	1a
PMID:22328580	Fig 3A
PMID:22328580	Fig. 3B Figure 4, A and B,
PMID:22328580	Figure 2D
PMID:22328580	fig 1
PMID:22328580	Figure 4, A and B,
PMID:22328580	Figure 4, A and B,
PMID:22328580	Figure 4, A and B,
PMID:22328580	Figure 4, A and B,
PMID:22328580	fig 4 D
PMID:22328580	fig 4 D
PMID:22328580	Figure Figures 5D, 6C
PMID:22328580	Figure Figures 5D, 6C
PMID:22328580	Figure Figures 5D, 6C
PMID:22328580	fig 4 D
PMID:22328580	Figure 4, A and B,
PMID:22328580	Fig 3A
PMID:22328580	Fig. 3B Figure 4, A and B,
PMID:22344254	********nitrogen replete/with aa
PMID:22344254	fig6
PMID:22344254	fig 4a
PMID:22344254	As shown in Fig. 3, GFP–Tor2, GFP–Mip1 and Pop3–GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	As shown in Fig. 3, GFP–Tor2, GFP–Mip1 and Pop3–GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	As shown in Fig. 3, GFP–Tor2, GFP–Mip1 and Pop3–GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	We observed that Gtr2–RFP co-precipitated with Gtr1 (Fig. 2D) and that the Gtr1–Gtr2 interaction was stronger in cells growing in the presence of amino acids, indicating that the formation of the heterodimer is stimulated by amino acids.
PMID:22344254	Fig. 1B and Fig. 1C, respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344254	The observed pattern was identical, regardless of the presence or not of amino acids in the medium. To confirm the localization to the vacuole membrane, we stained the gtr1-gfp cells with the lipophilic vacuolar membrane fluorescent dye FM4-64. As shown in Fig. 2B, Gtr1–GFP colocalized with FM4-64 staining, indicating that Gtr1–GFP is concentrated at the membranes of vacuoles in S. pombe.
PMID:22344254	the Gtr1–Gtr2 heterodimer and TORC1 are located in the vacuolar membrane independently of the presence of amino acids. However, only when amino acids are present in the medium does the Gtr1–Gtr2 heterodimer interact physically with TORC1 and activate the TOR pathway to induce cell growth and repress sexual differentiation.
PMID:22344254	fig 4a
PMID:22344254	*****nitrogen replete/with aa***** vam6D mutant cells showed similar Rps6 phosphorylation levels to that of wild-type cells in the absence of amino acids. However, in contrast to wild- type cells, vam6D cells did not show an increase in Rps6 phosphorylation in the presence of amino acids.
PMID:22344254	Fig. 1A Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	We introduced Gtr1Q61L in a vam6D background and found that the double mutant was able to grow normally (Fig. 5B), indicating that constitutively active Gtr1 rescues the cell growth defect of the vam6D mutant.
PMID:22344254	Fig. 1A Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	Fig. 1A Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	Fig. 1A Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	Fig. 1A Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	The observed pattern was identical, regardless of the presence or not of amino acids in the medium. To confirm the localization to the vacuole membrane, we stained the gtr1-gfp cells with the lipophilic vacuolar membrane fluorescent dye FM4-64. As shown in Fig. 2B, Gtr1–GFP colocalized with FM4-64 staining, indicating that Gtr1–GFP is concentrated at the membranes of vacuoles in S. pombe.
PMID:22344254	The doubling time of vam6D was shorter in the presence of amino acids, indicating that these cells were still able to respond, at least partially, to the presence of amino acids (Fig. 5A) and that Vam6 has an important role in regulating cell growth in S. pombe but is not essential for responding to the availability of amino acids.
PMID:22344254	the Gtr1–Gtr2 heterodimer and TORC1 are located in the vacuolar membrane independently of the presence of amino acids. However, only when amino acids are present in the medium does the Gtr1–Gtr2 heterodimer interact physically with TORC1 and activate the TOR pathway to induce cell growth and repress sexual differentiation.
PMID:22344254	***********nitrogen replete/with aa. AND during aa starvation***********vam6D mutant cells showed similar Rps6 phosphorylation levels to that of wild-type cells in the absence of amino acids. However, in contrast to wild- type cells, vam6D cells did not show an increase in Rps6 phosphorylation in the presence of amino acids.
PMID:22344254	These results suggest that Vam6 functions upstream of Gtr1, possibly by acting as a GEF.
PMID:22344254	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	Fig. 1A Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	Fig. 1B and Fig. 1C, respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344694	not shown direct binding but want to capture the fact that it binds the oxidised form
PMID:22344694	not shown direct binding but want to capture the fact that it binds the oxidised form
PMID:22349564	(Figure 4B) A deletion mutants showed a clear growth defect on galactose medium
PMID:22349564	Similarly to the Δcbp3 and Δcbp6 mutants, Δmss51 cells were resistant to antimycin A on glucose medium, showing that they contain a functional complex V
PMID:22349564	Thus, in S. pombe, Mss51 appears to be required at a post-translational step of complex IV biogenesis
PMID:22349564	Δmss51 cells showed normal cytochrome b and c1 peaks, but cytochromes aa3 were not detectable.
PMID:22349564	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	As expected, Δppr4 cells clearly lacked Cox1
PMID:22349564	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
PMID:22349564	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
PMID:22349564	Cox2 was detectable in Δmss51 purified mitochondria, although its level was greatly reduced (Figure 5C), consistent with the reduced 35S labeling (Figure 5A)
PMID:22349564	Cox1 was clearly less stable in the Δmss51 mutant than in the wild- type, while Cox2 was poorly labeled in the mutant even before starting the chase, as noted before (Figure 5C).
PMID:22349564	5E
PMID:22349564	Figure 1C
PMID:22349564	Figure 1A
PMID:22349564	Figure 1A
PMID:22349564	Figure 1A
PMID:22349564	Figure 1A
PMID:22349564	Figure 1A
PMID:22349564	Figure 1A
PMID:22349564	Figure 1B
PMID:22349564	Figure 1B
PMID:22349564	Figure 1C
PMID:22349564	Figure 1C
PMID:22349564	Figure S4A, B, C
PMID:22349564	Figure 1C
PMID:22349564	Figure 1C
PMID:22349564	Figure 1C
PMID:22349564	Figure 2A Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant
PMID:22349564	Figure 2A Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant
PMID:22349564	Figure 2C Thus, virtually all of the Cytb protein synthesized in the Δcbp6 mutant is degraded
PMID:22349564	Figure 2D In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4)
PMID:22349564	absent respiratory complex III Figure 2D In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4)
PMID:22349564	absent respiratory complex III. Figure 2D As expected, the higher molecular weight bands of complex III were absent in the Δppr4 mutant, which lacks complex IV
PMID:22349564	The tagged Mss51 was detected only in the mitochondrial fraction and like Cox2 was strongly resistant to carbonate extraction (Figure 4A), indicating that it is a membrane protein.
PMID:22354040	fig 7 c
PMID:22354040	Fig 7 A
PMID:22354040	Fig 7
PMID:22354040	Fig 7B
PMID:22354040	Fig 7 B
PMID:22354040	figure 8 A
PMID:22375066	This result shows that Ssp2 phosphorylation by Ssp1 is required to trigger the nuclear accumulation of the former upon nitrogen or glucose starvation, and that if Ssp2 is not phosphorylated it remains in a cytoplasmic localization, regardless of the nutritional conditions of the cell.
PMID:22375066	positive
PMID:22375066	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	This finding suggested that inactive AMPK is excluded from the nucleus and, upon activation by glucose or nitrogen starvation, part of the AMPK moves into the nucleus.
PMID:22375066	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	positive
PMID:22419817	"vw deleted ""+ve regulation of"""
PMID:22426534	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22431512	localization independent of Ago1
PMID:22431512	localization independent of Ago1
PMID:22431512	SO:0001843 =ATF1/CRE; localization independent of Ago1
PMID:22431512	localization independent of Ago1
PMID:22438582	5A
PMID:22438582	Figure 1
PMID:22438582	Figure 1
PMID:22438582	S6
PMID:22438582	S6
PMID:22438582	Figure 1
PMID:22438582	Figure 1
PMID:22438582	6A
PMID:22438582	6A
PMID:22438582	Plo1 protein reorganize spindle body during meiosis: Plo1 starts to localize to spindle pole body at the onset of meiosis I, and recruits Cut12 (and Pcp1), which was absent during meiotic prophase.
PMID:22438582	6A
PMID:22438582	5A
PMID:22438582	6A
PMID:22438582	5A
PMID:22438582	5
PMID:22438582	5
PMID:22438582	5F
PMID:22438582	Figure 1
PMID:22438582	Figure 1
PMID:22438582	Figure 1
PMID:22438582	Figure 1
PMID:22438582	FIG 4B
PMID:22438582	Figure 1
PMID:2245912	Table 6
PMID:2245912	Table 4 suppressor of cdc25-disruption occasional cdc- cells observed
PMID:2245912	Table 4 stf1-1 is a suppressor of cdc25-M51
PMID:2245912	Table 4 suppressor of cdc25-22
PMID:2245912	Table 4 suppressor of cdc25-22
PMID:2245912	same phenotype as cells homozygous for stf1-1
PMID:2245912	same phenotype as cells homozygous for stf1-1
PMID:2245912	Table 4
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 5 This mutant is a revertant of cdc2-M35
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 4
PMID:2245912	stf1-1/stf1-3 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature
PMID:2245912	Table 4 suppressor of cdc25-disruption occasional cdc- cells observed
PMID:2245912	Table 4 stf1-1 is a suppressor of cdc25-M51
PMID:2245912	stf1-1/stf1-3 cells form small colonies at restrictive temperature ~20-200 cells
PMID:2245912	stf1-1/stf1-2 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature
PMID:2245912	cells homozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells
PMID:2245912	cells homozygous for stf1-1 are not as elongated as stf1-1 heterozygous cells at restrictive temperature
PMID:2245912	cells heterozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells
PMID:2245912	cells heterozygous for stf1-1 are more elongated that stf1-1 homozygous cells
PMID:2245912	the restrictive temperature for a cdc25-22 diploid is 32°C
PMID:2245912	Table 3 suppressor of cdc25-22
PMID:2245912	Table 4 suppressor of cdc25-22
PMID:2245912	Table 4 suppressor of cdc25-22
PMID:2245912	Table 5 no genetic interaction with stf1-1 cdc2-59 is a cold sensitive cdc2 mutant cdc at low (25°C) temperature and wee at high temperature (35°C)
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 5 cdc2-3w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature
PMID:2245912	Table 6 wee1-50 and stf1-1 have an additive effect to suppress cdc25-22 phenotype at the restrictive temperature
PMID:2245912	Table 8 no genetic interaction with stf1-1
PMID:2245912	Table 7 Cells are slightly shorter at high temperature when stf1-1 present
PMID:2245912	Table 7 Cells are slightly shorter at high temperature when stf1-1 present
PMID:2245912	dis2+ over expression reverses the stf1-1 suppression cdc25-22
PMID:2245912	Table 5 cdc2-1w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 5 no genetic interaction with stf1-1.
PMID:2245912	Table 5 This mutant is a revertant of cdc2-M35
PMID:2245912	Table 5 no genetic interaction with stf1-1
PMID:2245912	Table 5 cdc2-1w rescues cdc25-22 but cells are long
PMID:2245912	Table 5
PMID:2245912	Table 8 no genetic interaction with stf1-1
PMID:22484924	vw, moved down to -decreased protein targeting to vacuole, with protein secreted
PMID:22484924	fig 2c
PMID:22484924	fig 2d
PMID:22484924	Fig. 2D
PMID:22484924	(protein)
PMID:22484924	fig 5c
PMID:22484924	fig4 (I moved this down from abnormal endocytisis, is that OK?)
PMID:22484924	fig 4
PMID:22496451	"allele tyep ""unknown"" because neither nt nor aa position 324 is A"
PMID:22508988	fig 2b
PMID:22508988	fig 2c
PMID:22508988	fig 1a in vitro /in vivo
PMID:22508988	fig1 carboxy terminal region
PMID:22508988	fig 1a
PMID:22508988	fig 1e in vitro
PMID:22508988	(We also compared the activities of kinase complexes generated by translation in vitro toward Spt5. By this measurement also, Cdk9 and Cdk9􏰂C were stimulated to similar extents by Csk1 (Fig. 1F),(is this an physiological substrate?)
PMID:22508988	fig 2c
PMID:22508988	fig 2c
PMID:22508988	fig 3B
PMID:22508988	fig 2d Spt5-T1P (CTD repeat 1 residue)
PMID:22508988	fig 2d Spt5-T1P (CTD repeat 1 residue)
PMID:22508988	fig 2c
PMID:22508988	fig 2c
PMID:22508988	fig 2c MPA exacerbates growth impairment in mutants defective in transcript elongation (8, 11, 50), although the precise mechanism of this effect is un- known (34)
PMID:22508988	fig 2c
PMID:22508988	fig 2c
PMID:22508988	fig 2c
PMID:22508988	fig 1a
PMID:22508988	fig1
PMID:22508988	fig1 carboxy terminal region
PMID:22508988	fig 1a
PMID:22508988	fig 4 A/B
PMID:22508988	fig 4 A/B
PMID:22508988	carboxy terminal region
PMID:22508988	fig 3B
PMID:22558440	I specifically used that term name because I did not want to discriminate whether Cuf2 is a negative or a positive regulator of transcription, even though in the paper we have put emphasis on the fact that meiotic genes are up-regulated in the absence of Cuf2 (so that Cuf2 would be a repressor). The reason is that there are also many other genes that are down-regulated in the cuf2delta mutant compare to WT. We still don't know which effect is direct and/or indirect. Thus, we don't want to exclude that Cuf2 might act as an activator, a repressor or both, for now.
PMID:22573890	fig 5
PMID:22573890	fig 5 6 min late
PMID:22573890	fig 6
PMID:22573890	fig 2a (WT 10% @36degrees)
PMID:22573890	fig 5
PMID:22573890	fig 3 A
PMID:22573890	fig 3 A
PMID:22573890	fig 6
PMID:22573890	fig S2
PMID:22573890	fig 2a
PMID:22573890	figure 2 B/C
PMID:22573890	fig 3 A
PMID:22573890	fig 5
PMID:22582262	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/"
PMID:22582262	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/"
PMID:22645648	Figure1a
PMID:22645648	Figure6
PMID:22645648	Figure 6
PMID:22645648	Figure1a
PMID:22645648	Figure1a
PMID:22645648	Figure1a/6a . Rapamycin rescued cut1-21 and cut1-693 at 338C
PMID:22645648	Figure4d
PMID:22645648	Figure 6
PMID:22645648	Figure1a/6a . Rapamycin rescued cut1-21 and cut1-693 at 338C
PMID:22645648	Dephosphorylation of Cdc2 Tyr15 PO4 is delayed in this mutant
PMID:22645648	Figure4d
PMID:22645648	Figure4ab
PMID:22645648	Figure4e
PMID:22645648	TOR kinase activity was measured using immunoprecipitated proteins (Fig.2)
PMID:22645648	Mild sensitivity compared to tor2-S (L2048S)
PMID:22645648	"""At 37C, the cell number increase of both mutants ceased."""
PMID:22645648	"""At 37C, the cell number increase of both mutants ceased."""
PMID:22645654	Fig2e
PMID:22645654	Fig.1d, e, f
PMID:22645654	Fig1d
PMID:22645654	Fig1d
PMID:22645654	Fig1d
PMID:22645654	Fig1d
PMID:22645654	Fig1f (evidence:immunoblot using anti-thymine dimer anitbodies)
PMID:22645654	Fig1g
PMID:22645654	Fig1h
PMID:22645654	Fig2e
PMID:22645654	Fig3a-g (evidence: immunpflouresence)
PMID:22645654	Fig4
PMID:22645654	Fig5
PMID:22645654	Data from three experiments: DNA reannealing (renaturation assay) using heat-denatured DNA (ssDNA); Removal of RPA proteins associated with ssDNA, RPA-coated heat-denatured DNA (ssDNA) is renaturated; Removal of RNA associated with ssDNA, RNA/DNA hybrid is denatured by renaturation activity of condensin SMC
PMID:22645654	fig 2b,c
PMID:22645654	fig 2b,c
PMID:22645654	Fig7
PMID:22645654	Fig5
PMID:22658721	bulky
PMID:22658721	NMeed to check, its decreased duration of replication arrest?
PMID:22658721	small
PMID:22661707	more specific term required, during GO:0034599)
PMID:22665807	1d
PMID:22665807	4b
PMID:22665807	Table S1 and Figure S1
PMID:22665807	Table S1 and Figure S1
PMID:22665807	2A
PMID:22665807	2A
PMID:22665807	4b
PMID:22665807	2A
PMID:22665807	4b
PMID:22665807	2A
PMID:22665807	4b
PMID:22665807	Table S1 and Figure S1
PMID:22665807	1d
PMID:22665807	2A
PMID:22665807	2A
PMID:22665807	4b
PMID:22665807	3a
PMID:22665807	Table S1 and Figure S1
PMID:22665807	Table S1 and Figure S1
PMID:22665807	Table S1 and Figure S1
PMID:22665807	4b
PMID:22665807	2A
PMID:22665807	3b
PMID:22665807	Table S1 and Figure S1
PMID:22665807	1c
PMID:22665807	Table S1 and Figure S1
PMID:22665807	Table S1 and Figure S1
PMID:22665807	4b
PMID:22665807	Table S1 and Figure S1
PMID:22665807	Table S1 and Figure S1
PMID:22665807	4b
PMID:22665807	4b
PMID:22665807	4b
PMID:22665807	figure 2A
PMID:22682245	implies that dna2 E560A alone is inviable
PMID:22682245	implies that dna2 K961T alone is viable
PMID:22682245	cleaves unpaired nascent DNA in replication forks (vw replaced GO:0045145)
PMID:22683269	assayed using bulk RNA
PMID:22684255	fig 4d
PMID:22684255	upstream of pom1
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	fig 4d
PMID:22684255	(Figure 4b) confirming that each kinase promotes mitotic commitment.
PMID:22684255	"""mitotic commitment'"
PMID:22684255	Figure 3a. t (Table 1) indicating that inhibition of Sid2 or Fin1 delayed the timing of mitotic commitment until a new size threshold for division was me
PMID:22684255	Figure 3a. t (Table 1) indicating that inhibition of Sid2 or Fin1 delayed the timing of mitotic commitment until a new size threshold for division was me
PMID:22684255	Figure 3a
PMID:22684255	Figure 3a
PMID:22684255	Figure 2f lanes 1, 2
PMID:22684255	Figure 2f lanes 1, 2
PMID:22684255	Figure 2f lanes 1, 2
PMID:22684255	Figure 1g
PMID:22684255	Figure 1g
PMID:22684255	Figure 1b
PMID:22684255	Figure 1b
PMID:22684255	fig 1a
PMID:22696680	Figure 3, Supplemental Table S2, and Supplemental Figure S4
PMID:22696680	fig 1A
PMID:22696680	fig 1A
PMID:22696680	(growing) fig 1A
PMID:22696680	Figure 1
PMID:22696680	Figure 1
PMID:22696680	Figure 1
PMID:22696680	Figure 1
PMID:22696680	Figure 2A
PMID:22696680	Figure 2A
PMID:22696680	Figure 2B
PMID:22696680	Figure 2C
PMID:22696680	Figure 2D Figure 2F
PMID:22696680	Figure 2D Figure 2F
PMID:22696680	Supplemental Figure S1, C–E
PMID:22696680	Supplemental Figure S1, C–E
PMID:22696680	Supplemental Figure S1, C–E
PMID:22705791	not sure if it is endo, exo, or both. It is def acting on DNA. More specific terms for DNA specify endo or exo.
PMID:22705791	not sure if it is endo, exo or both? so went with more general term
PMID:22711988	implies that MIND complex is required for Sos7 to localize to the kinetochore
PMID:22711988	kinetochore localization requires MIND complex
PMID:22718908	BrdU incorporation
PMID:22718908	inferred from localization of proteins distal to origin
PMID:22718908	BrdU incorporation
PMID:22718908	inferred from localization of proteins distal to origin
PMID:22718908	BrdU incorporation
PMID:22718908	inferred from localization of proteins distal to origin
PMID:22718908	inferred from normal localization of CMG proteins at origin
PMID:22718908	BrdU incorporation
PMID:22718908	inferred from localization of proteins distal to origin
PMID:22723423	Fml1 binds to the four-way junction at a displacement (D) loop.
PMID:22723423	Fml1 catalyses the dissociation of displacement (D) loops
PMID:22727667	binds H3K9me
PMID:22727667	binds H3K9me
PMID:22727667	binds H3K9me
PMID:22737087	All the genes affect by at least 1.5 fold (61) are reported in Table S2
PMID:22737087	Fig1, Table1 affects C1 more than C2 type colonies
PMID:22737087	Fig2.
PMID:22737087	Fig S1 decreased aneuploid cell viability during vegetative growth
PMID:22737087	data not shown decreased aneuploid cell viability during vegetative growth
PMID:22737087	Fig S1, decreased aneuploid cell viability during vegetative growth
PMID:22737087	Fig S1, decreased aneuploid cell viability during vegetative growth
PMID:22737087	Fig2. decreased aneuploid cell viability during vegetative growth
PMID:22737087	Fig2.
PMID:22737087	Fig2.
PMID:22737087	Fig1, Table1 affects C1 and C2 type colonies
PMID:22737087	Fig2. decreased aneuploid cell viability during vegetative growth
PMID:22737087	Fig2. decreased aneuploid cell viability during vegetative growth
PMID:22737087	data not shown
PMID:22737087	data not shown
PMID:22737087	data not shown
PMID:22737087	data not shown
PMID:22737087	Fig2 normal population growth in presence of aneuploid cells
PMID:22737087	Fig2 normal population growth in presence of aneuploid cells
PMID:22737087	Fig2. reduced growth may not be specific to aneuploidy as it also interacts with gtb1
PMID:22737087	Fig2. reduced growth may not be specific to aneuploidy as it also interact with gtb1 though looks quite good to me
PMID:22737087	Table1 Fig1 affects C1 and C2 type colonies
PMID:22737087	Fig 3A This strain is disomic for Chromosome 3
PMID:22737087	Fig 3B This strain is disomic for Chromosome 3
PMID:22737087	Fig 3A This strain is disomic for Chromosome 3
PMID:22737087	Fig 3B This strain is disomic for Chromosome 3
PMID:22737087	Table 2 This strain is disomic for Chromosome 3
PMID:22737087	Fig 4 Type C1 colonies have highly elongated cells and are due to various types of aneuploidy. Authors suggest that not3 is required to maintain cell growth
PMID:22737087	All the genes affect by at least 1.5 fold (141) are reported in Table S2
PMID:22737087	All the genes affect by at least 1.5 fold (17) are reported in Table S2
PMID:22737087	Table 2 This strain is disomic for Chromosome 3
PMID:22737087	Fig6.
PMID:22737087	Fig6.
PMID:22737087	Fig6
PMID:22737087	Fig6
PMID:22737087	Fig6
PMID:22737087	Fig6. reduced growth may not be specific to aneuploidy as it also interacts with gtb1-93
PMID:22737087	Fig1, Table1 affects C1 and C2 type colonies
PMID:22737087	Fig1, Table1 affects C1 type colonies
PMID:22737087	Fig1, Table1 affects C1 type colonies
PMID:22737087	Table 2 This strain is disomic for Chromosome 3
PMID:22737087	Table 2 This strain is disomic for Chromosome 3
PMID:22768388	Figur 1 c
PMID:22768388	fig 1 A
PMID:22768388	Figur 1 c
PMID:22768388	figure 1c
PMID:22768388	Figur 1 c
PMID:22768388	figure 1c
PMID:22768388	figure 1c
PMID:22768388	S1 E
PMID:22768388	S1 E
PMID:22768388	S1 E
PMID:22768388	S1 E
PMID:22768388	S1 E
PMID:22768388	S1 E
PMID:22768388	fig 1 A
PMID:22768388	S1 E
PMID:22768388	S1 E
PMID:22768388	Figures 1B
PMID:22768388	Figures 1B
PMID:22768388	Figures 1B
PMID:22768388	Figures 1B
PMID:22768388	Figures S1C
PMID:22768388	Figures S1C and S1D
PMID:22768388	fig 1 A
PMID:22768388	fig 1 A
PMID:22768388	data not shown
PMID:22768388	fig 4C
PMID:22768388	data not shown
PMID:22768388	fig S4
PMID:22768388	fig 1 A
PMID:22792081	cdc25-22 background
PMID:22792081	cdc25-22 background
PMID:22792081	cdc25-22 background
PMID:22792081	cdc25-22 background
PMID:22792081	This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.
PMID:22792081	This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.
PMID:22792081	cdc25-22 background
PMID:22792081	cdc25-22 background
PMID:22792081	This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.
PMID:22809626	"happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true."
PMID:22809626	"happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true."
PMID:22809626	"happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true."
PMID:22809626	"happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true."
PMID:22825872	and the fraction of cells, in which a signal could be detected (supplementary material Fig. S1), were similar between bub3+ and bub3D cells
PMID:22825872	Fig. 4C
PMID:22825872	Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5–S10).
PMID:22825872	Fig.3A. When proper chromosome attachment was prevented by a conditional mutation in kinesin-5 (cut7-446), Mph1 localized to kinetochores, but the enrichment was abrogated by chemical genetic inhibition of Ark1 with the small molecule 1NM-PP1 (Fig. 3A).
PMID:22825872	This is S8E and F. Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5–S10).
PMID:22825872	This is S4B and C
PMID:22825872	This is S4B and C
PMID:22825872	This is S4B and C
PMID:22825872	(60% cells) Forced recruitment of wild-type Mph1 to kinetochores lead to apronounced delay in mitosis and a growth defect (Fig. 1E,F),
PMID:22825872	Mph1 localizes to unattached kinetochores in bub3D cells (Fig. 2A).
PMID:22825872	Fig. 4B Fig. S5
PMID:22825872	Fig. 4A and S1
PMID:22825872	Fig. 4A and S9
PMID:22825872	Fig. S5
PMID:22825872	Fig. S6 Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5–S10).
PMID:22825872	Fig. S7
PMID:22825872	Fig. S8
PMID:22825872	rescued by deletion of mad2, which (forced recruitment of Mph1 artificially promoted SAC signaling andthat the fusion to Mis12 did not impair kinetochore function.
PMID:22825872	35% cells (Fig. 1E,F).
PMID:22825872	and the fraction of cells, in which a signal could be detected (supplementary material Fig. S1), were similar between bub3+ and bub3D cells
PMID:22825872	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling,
PMID:22825872	In the presence of Mph1-D1-150, the SAC was still functional in bub3D cells, although the mitotic delay was shorter than in mph1-D1-150 or bub3D cells (Fig. 2C).
PMID:22825872	In the presence of Mph1-D1-302, the SAC response in bub3D cells was abrogated (Fig. 2C), demonstrating that recruitment of Mph1 to kinetochores is necessary for SAC function in bub3D cells.
PMID:22825872	Together this suggests that Ark1 is directly and continuously required to maintain Mph1 localization to kinetochores.
PMID:22825872	Fig. 3B. Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5–S10).
PMID:22825872	(Fig. S9F)
PMID:22825872	(Fig. 3C) (inhibiting Ark1 does not rescue the Mph1-kinetochore targeting, arguing that Ark1 is upstream)
PMID:22825872	(Fig. 4B).
PMID:22825872	Fig. 4A and S7
PMID:22825872	(Fig. 3C)increased mitotic index (Fig. S4A)
PMID:22825872	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling,
PMID:22825872	ditto
PMID:22825872	abolished both kinetochore localization and SAC signaling (Fig. 1C,D), suggesting that kinetochore localization is crucial for SAC activity.
PMID:22825872	Fig. 4A and S8
PMID:22825872	Fig. 4A and S8
PMID:22825872	Fig. 4A and S7
PMID:22825872	(Fig. 4C).
PMID:22891259	Explosive cell separation due to a weak primary septum. Absence of a secondary septum.
PMID:22891259	fig1 /figs1?
PMID:22891259	Localized at cell tips, actomyosin contractile ring and septum
PMID:22891259	fig1 /figs1?
PMID:22891673	assayed at 32C, which is semi-permissive for sec3-913
PMID:22891673	Weak actin cables
PMID:22891673	Assayed by FM4-64 uptake
PMID:22891673	At the end of ring constriction Filamentous projections from the unclosed ring toward the cytoplasm
PMID:22891673	decreased/delayed septum closure
PMID:22891673	normal localization in several mutants indicates that Sec3 localization is independent of exocytosis and vesicle-mediated transport along microtubules
PMID:22891673	septation index increased gradually over time
PMID:22891673	septation index constantly high
PMID:22891673	decreased septum closure
PMID:22905165	GFP-Bgs1
PMID:22905165	Cdc15-GFP
PMID:22905165	Cdc15-GFP However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22905165	(used sorbitol but multiple stresses were tested) Cdc15-GFP However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22905165	1B
PMID:22905165	1B in which the SIN signal does not turn off, Cfh3p localized to the edge of the growing septa and it remained at the septal area after the septa had been completed. Thus, Cfh3p can arrive at the cell midzone in the absence of the SIN pathway but it requires that the SIN signal must be turned off for it to be removed from the cell equator after mitosis
PMID:22905165	GFP-Cfh3 figure 1 A
PMID:22905165	S1
PMID:22905165	S1
PMID:22905165	S1
PMID:22905165	GFP-Bgs1
PMID:22905165	figure S2, A protein distributed in cortex
PMID:22905165	1B in which the SIN signal does not turn off, Cfh3p localized to the edge of the growing septa and it remained at the septal area after the septa had been completed. Thus, Cfh3p can arrive at the cell midzone in the absence of the SIN pathway but it requires that the SIN signal must be turned off for it to be removed from the cell equator after mitosis
PMID:22905165	Cdc15-GFP supplemental figure S3
PMID:22905165	GFP-Cfh3 figure 1 A
PMID:22905165	S1
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22918943	Figure 7
PMID:22918943	Figure 7
PMID:22918943	Figure 1A, 2A
PMID:22918943	Figure 1A, 2A
PMID:22918943	Figure 5, I, J, and L
PMID:22918943	Figure 5, I, J, and L
PMID:22918943	Figure 5, I, J, and L
PMID:22918943	Figure 3A
PMID:22918943	Figure 3A
PMID:22918952	unspecfied RxxS site(s)
PMID:22918952	unspecfied RxxS site(s)
PMID:22918954	fig 3B asymettrically localized septum
PMID:22918954	fig 3B
PMID:22918954	fig 3B
PMID:22918954	fig 3B
PMID:22918954	Figure 4
PMID:22918954	Figure 4
PMID:22918954	fig 3B
PMID:22918954	fig 3B
PMID:22918954	fig 3B
PMID:22918954	Figure 4
PMID:22918954	fig 3B
PMID:22918954	fig 3B
PMID:22918954	Figure 4
PMID:22918954	Figure 4
PMID:22918954	Figure 4
PMID:22918954	Figure 4
PMID:22918954	fig 3B
PMID:22959349	at Ser/Thr-Pro site
PMID:22959349	at Ser/Thr-Pro site
PMID:22959349	at Ser/Thr-Pro site
PMID:22959349	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	cdc2 phosphorylates rap1. phosphorylated rap1 binds bqt4 less efficiently. rap1-bqt4 binding is required for telomere tethering at nuclear periphery. In WT cells telomere tehtering is abolished during M phase.
PMID:22976295	In this experiment, we utilized a Psk1 mutant (Thr415Glu), a phospho-mimetic mutant of its hydrophobic motif, as the mutant exhibited higher activity than the wild-type protein. As shown in Fig. 2C, the Psk1 protein phosphorylated Rsp6 in vitro. However, the Rsp6 mutant that has two potential serine phosphorylation sites changed to alanine was not phosphorylated by Psk1.
PMID:22976295	in vitro assay using rps602 so I am inferring rps601
PMID:22976295	"I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?"
PMID:22976295	"I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?"
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	not shown
PMID:22976295	in vitro assay using rps602 so I am inferring rps601
PMID:22976295	in vitro assay using rps602 so I am inferring rps601
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	both rps proteins in extension because blot is for both of them
PMID:22976295	blotted for rps601 & rps602 simultaneously
PMID:22976295	blotted for rps601 & rps602 simultaneously
PMID:22976295	blotted for rps601 & rps602 simultaneously
PMID:22976295	blotted for rps601 & rps602 simultaneously
PMID:22976295	blotted for rps601 & rps602 simultaneously
PMID:22976295	blotted for rps601 & rps602 simultaneously
PMID:22987637	"for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable."
PMID:22987637	"for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable."
PMID:22988247	This gene has been named as otg2 in the article.
PMID:22988247	This gene has been named as otg1 in the article.
PMID:22988247	This gene has been named as otg3 in the article.
PMID:22990236	SO:0001899 = dh repeat
PMID:23028377	move down to histone chaperone (H3-?)
PMID:23032292	spacing is wrong as well as occupancy
PMID:23051734	required for wildtype rates of actin cable retrograde flow in myo52∆ cells
PMID:23051734	localization
PMID:23066505	ire1 breaks down mRNAs during ER stress, however bip1 is unusual in that ire1 cleavage stabilizes it
PMID:23066505	RIDD? - there is no RIDD term in GO, Val wants to wait with this
PMID:23071723	throughout cell cycle, with peak at M/G1
PMID:23084836	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	(NOTE IS STILL LOCALIZED TO NUCLEAR ERIPHERY) Remarkably, the association of Tf elements with centromeres was significantly compromised in pkuΔ cells (P < 0.00001, Mann-Whitney U test; Figures 3D and 3E).
PMID:23084836	1A
PMID:23084836	1A
PMID:23084836	1A
PMID:23084836	Figure S1C
PMID:23084836	(Figures S2A and S2B)
PMID:23084836	(Figures S2A and S2B). AND As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	clustering and tethering of centromeres to the nuclear periphery were not affected in pku70Δ and pku80Δ cells, although Ku does localize at centromeres (Figures 1E, 3A, and 3B)
PMID:23084836	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	clustering and tethering of centromeres to the nuclear periphery were not affected in pku70Δ and pku80Δ cells, although Ku does localize at centromeres (Figures 1E, 3A, and 3B)
PMID:23084836	(NOTE IS STILL LOCALIZED TO NUCLEAR ERIPHERY) Remarkably, the association of Tf elements with centromeres was significantly compromised in pkuΔ cells (P < 0.00001, Mann-Whitney U test; Figures 3D and 3E).
PMID:23084836	We found that Tf clustering and the association of Tf cluster with centromeres were significantly compromised in the cut14-208 condensin mutant Figures 4A and 4B),
PMID:23084836	We found that Tf clustering and the association of Tf cluster with centromeres were significantly compromised in the cut14-208 condensin mutant Figures 4A and 4B),
PMID:23084836	Figures 6A and 6B hst4Δ and clr6-1 HDAC mutations, but not other HDAC mutations, significantly compromised Tf clustering and the association of Tf cluster with centromeres; Figures 6A and 6B)
PMID:23084836	Figures 6A and 6B), see above
PMID:23084836	Figures 6A and 6B) see above
PMID:23084836	Figures 6A and 6B) see above
PMID:23084836	Moreover, only the rtt109Δ HAT mutations, but not other HAT mutations, significantly promoted the association of Tf cluster with centromeres, whereas none of the HAT mutations affected Tf clustering (Figures 6C and 6D).
PMID:23084836	Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively,
PMID:23084836	Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectivelyWe examined how H3K56 acetylation antagonizes Tf clustering at centromeres. Remarkably, binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively, suggesting that H3K56 acetylation has an inhibitory effect on Ku binding to Tf elements (Figure 6E).
PMID:23084836	Figures 6A and 6B) see above
PMID:23084836	We observed that Ku localization was diffuse after DNA damage, but this diffusion was inhibited by rtt109Δ (Figure 7D)
PMID:23084836	Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	Figure S1C
PMID:23084836	The FISH data revealed that telomere clustering was not affected by pku70Δ and pku80Δ, but telomere tethering to the nuclear periphery was significantly compromised by pkuΔ (P < 0.001, Mann-Whitney U test), suggesting that telomere clustering and tethering to the nuclear periphery are distinct processes (Figures S2A and S2B)
PMID:23087209	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23087209	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23087209	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23093942	assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	assayed in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	assayed in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093943	S1F
PMID:23093943	fiigure S1B–S1C
PMID:23093943	fig 1b fig2
PMID:23093943	fig 1b
PMID:23093943	fiigure S1B–S1C
PMID:23093943	fiigure S1B–S1C
PMID:23093943	Figure 1F–1G
PMID:23093943	S1F
PMID:23093943	S1F
PMID:23093943	T-shapes always arose in cells that the tea1D growth pattern dictated should grow at their new ends (Figure 2D–2E) but that actually grew at neither (Figure 2E and 2G)
PMID:23093943	As was observed previously [28], cytoplasmic Fic1-GFP localizes to cell tips during interphase and later to the CR during cell division (Figure 3A).
PMID:23093943	As was observed previously [28], cytoplasmic Fic1-GFP localizes to cell tips during interphase and later to the CR during cell division (Figure 3A).
PMID:23093943	fig 3c
PMID:23093943	fig 3C
PMID:23093943	fFigure 3D–3F
PMID:23093943	Figure 3G
PMID:23093943	Figure 4A–4C and Figure S3A–S3B
PMID:23093943	Mutation of PxxPs 10 and 11 in combination, or P257 of PxxP 11 alone, abolished the two-hybrid interaction (Figure S3D), and the P257A mutation eliminated co-immunoprecipitation of Fic1- FLAG3 with Cdc15 in vivo (Figure 4D).
PMID:23093943	Figure 4A–4C and Figure S3A–S3B
PMID:23093943	fig 4c
PMID:23093943	fig 4c
PMID:23093943	fig 4c
PMID:23093943	fig S3F
PMID:23093943	Cyk3-GFP localized to the CR and division site during cytokinesis, and it was retained at new ends immediately following cell division (Figure 4F).
PMID:23093943	Cyk3-GFP localized to the CR and division site during cytokinesis, and it was retained at new ends immediately following cell division (Figure 4F).
PMID:23093943	Fic1 most likely functions during late stages of cytokinesis. In line with this idea, the percentage of fic1D cells that had undergone ingression but were still joined at their division sites was more than four times that of wild-type cells (Figure 5A–5B).
PMID:23093943	Consistent with early cytokinesis events proceeding appropri- ately without Fic1, time-lapse imaging of myosin regulatory light chain Rlc1-GFP [47,48] along with spindle pole body marker Sid4-GFP revealed that the CR formed and constricted normally in fic1D cells (Figure 5C–5D). However, at the termination of CR constriction, parts of the CR persisted at the division plane (Figure 5E–5G and Figure S4D).
PMID:23093943	fig 4c/ figure 6a
PMID:23093943	Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C–6D and Figure S5A)
PMID:23093943	Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C–6D and Figure S5A)
PMID:23093943	Figure S5B
PMID:23093943	Figure S5B
PMID:23093943	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A–9B).
PMID:23093943	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A–9B).
PMID:23093943	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A–9B).
PMID:23093943	In addition to these strains, we found other cytokinesis mutants exhibiting high degrees of monopolar growth (spn1D, cdc7-24, and vps24D) to also be highly invasive and to form pseudohyphal projections into 2% agar (Figure 9A–9B and Figure S7A)
PMID:23112169	binds O6-alkylguanine, 2-aminopurine and 2,6-diaminopurine
PMID:23115244	evidence=mas spec, can I wang this into another evidence code or should we add it (or something similar?)
PMID:23133674	Y2H fig 1
PMID:23133674	bqt1 is fused to the activation domain
PMID:23133674	fig1 Y2H
PMID:23133674	fig1 only bqt1 is fused to the activation domain (that's why I am not adding this function to bqt2)
PMID:23133674	fig1 Y2H
PMID:23166349	Further supported by PMID:25057016
PMID:23166349	Coimmunoprecipitation, yeast-two-hybrid
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23188080	affects intermolecular, but not intramolecular, end joining
PMID:23200991	Observed with probe for active Cdc42 (CRIB)
PMID:23200991	Observed with probe for active Cdc42 (CRIB)
PMID:23200991	inferred from localization plus GTPase activity
PMID:2320127	Fig1c threonine is the minor phosphoamino acid
PMID:2320127	Fig1c Serine is the major phosphoamino acid
PMID:2320127	Fig4a. Cells blocked in mitosis
PMID:2320127	Fig4a. Cells blocked in G2
PMID:23209828	MBC sensitivity phenotype and ubiquitylation and degradation phenotype
PMID:23209828	MBC resistance phenotype and pap1 ubiquitylation phenotype
PMID:23209828	Pap1 is ubiquitylated by Rhp6 and Ubr1
PMID:23209828	Pap1 is ubiquitylated by Rhp6 and Ubr1
PMID:23209828	MBC sensitivity phenotype and ubiquitylation and degradation phenotype
PMID:23209828	MBC resistance phenotype and pap1 ubiquitylation phenotype
PMID:23211746	same as exo1delta alone
PMID:23211746	same as chk1delta alone
PMID:23211746	same as chk1delta alone
PMID:23211746	gel electrophoresis + southern blot
PMID:23211746	same as rad2delta alone
PMID:23211746	same as rad2delta alone
PMID:23211746	same as exo1delta alone
PMID:23223230	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	However, the larger band preferentially accumulated under zinc-replete conditions in wild-type cells and constitutively accumulated in SPCC13B11.02c cells. Thus, changes in adh1AS levels influence the levels of Adh1 protein, suggesting that this mechanism may exist to conserve zinc.
PMID:23223230	When adh1AS and adh1 transcript levels were examined in SPCC13B11.02c cells, the adh1AS transcript was not detected, and adh1 mRNAs were detected in both zinc-limited and zinc-replete cells (Fig. 1C).
PMID:23223230	When adh1AS and adh1 transcript levels were examined in SPCC13B11.02c cells, the adh1AS transcript was not detected, and adh1 mRNAs were detected in both zinc-limited and zinc-replete cells (Fig. 1C).
PMID:23223230	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	Taken together, the Northern and array analyses indicate that adh1AS transcripts preferentially accumulate in zinc-limited cells, whereas adh1 mRNAs accumulate in zinc-replete cells.
PMID:23231582	represses Pho7-mediated transcription activationin phosphate-replete conditions; does not regulate Pho7 DNA binding
PMID:23231582	at pho1+ and SPBC1271.09
PMID:23231582	also inferred from chromatin localization and reporter gene expression
PMID:23236291	Figure 6A (PMID:23236291)
PMID:23236291	Figure 8E (PMID:23236291)
PMID:23236291	Figure 8E (PMID:23236291)
PMID:23236291	Figure 8B (PMID:23236291)
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Figure 8B (PMID:23236291)
PMID:23236291	Figure 8A (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 8B (PMID: 23236291)
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Requested new term from Sequence Ontology: CArG-box
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Figure 8D (PMID: 23236291)
PMID:23236291	Figure 3 (PMID: 23236291)
PMID:23236291	Figure 1A and 1B (PMID: 23236291)
PMID:23236291	Figure 1A (PMID: 23236291)
PMID:23236291	Figure 1B (PMID: 23236291)
PMID:23236291	Figure 7A (PMID:23236291)
PMID:23236291	Figure 7A (PMID:23236291)
PMID:23236291	Figure 6A and 6C (PMID:23236291)
PMID:23245849	Mag2 binds stronger to the abasic oligonucleotide than to non-damaged DNA (Figure 2), with a dissociation rate constant more than 15 times higher for non-damaged DNA (kd 26 × 10−3 s −1) as compared to DNA containing the AP site analogue tetrahydrofuran (THF) (kd 1.6 × 10−3 s−1). Mag2 injected on sensor chips coated with oligonucleotides containing a single ethenoadenine or 8-oxoguanine lesion showed the same resonance levels as non-damaged DNA (data not shown), demonstrating that Mag2 preferentially binds to AP sites in DNA.
PMID:23245849	Figure 1C
PMID:23245849	supp S1 Also the MMS sensitivity of the nth1 − mutant was suppressed by the deletion of mag1 but not mag2 (Figure S1), which contrasts previous results (Kanamitsu et al., 2007). We do not know the reason for this discrepancy, but it could be because of different strain backgrounds, as the strains used by Kanamisu and co-workers tolerate much higher MMS doses (0.03% versus 0.007% in our experiments)
PMID:23245849	fig 1D
PMID:23245849	fig 1D
PMID:23245849	fig 1D
PMID:23245849	A. Unexpectedly, Mag2 showed no DNA glycosylase activity for alkylated bases, even at very high enzyme concentration and under different assay conditions (titration of NaCl, Mg2+, ATP; data not shown). Further, heterologous expression of Mag2 did neither rescue the extreme alkylation sensitive phenotype of an E. coli mutant lacking the two 3mA DNA glycosylases AlkA and Tag, nor the corresponding Saccharomyces cerevisiae mag1 deletion mutant (data not shown). Mag2 was assayed for activity towards a variety of different base lesions which are known substrates for other DNA glycosylases including alkylated, oxidized and deaminated bases, base mismatches and AP sites; however no enzymatic activity was observed for any of the lesions tested (Table S1) Crystal Structure of Mag2 in Complex With DNA Reveals Novel Non-Enzymatic AP Site Recognition and DNA Sculpting
PMID:23245849	multiple experiments
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	Fig 3. galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosyla- tion of cell-surface proteins
PMID:23254763	Fig 3. galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosyla- tion of cell-surface proteins
PMID:23254763	fig 5a There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	fig 5a There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	fig 5a There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	complemented by S. cerevisiae GAL2
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2.
PMID:23254763	FIgure 2. +25 μg/ml Hyg.B
PMID:23260662	same as lsd1-E918 single mutant
PMID:23260662	same as lsd1-E918 single mutant
PMID:23260662	same as lsd1-E918 single mutant
PMID:23260662	same as lsd1-E918 single mutant
PMID:23260662	inferred indirectness from author description and different effect of swi1delta
PMID:23260662	inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2)
PMID:23260662	inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2)
PMID:23273506	Figures 4B and 4C: Asp56Ser mutation endows Mag2 with the ability to excise εA at levels similar to Mag1.
PMID:23297348	S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T123 and S334 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S267 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S321 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T297 and S364 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S303 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S57 and S206 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S57 and S206 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S183 and S372 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S183 and S372 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S674 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S502 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	Sal3 is required for the nuclear import of Clp1 as shown by microscopy.
PMID:23297348	S196 and S252 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S196 and S252 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S372 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T554 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S411 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	Localization of Clp1 to nucleoplasm requires the presence of the nuclear localization sequence (NLS), which was identified to locate right at the end of the C-terminal.
PMID:23297348	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	Phosphorylation site S265 was identified by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S345 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T297 and S364 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T123 and S334 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T123 and S334 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S74 and S95 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S74 and S95 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S370 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	serine residues, presumably some or all of those mutated
PMID:23297348	serine residues, presumably some or all of those mutated
PMID:23297348	serine residues, presumably some or all of those mutated
PMID:23297348	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S301 and S499 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S301 and S499 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S216 and S298 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S216 and S298 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S65 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S148 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	T106 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S220 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S436 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	S558 was identified as phosphorylation sites by mass spectrometry.
PMID:23311928	non-flocculating cells
PMID:23314747	Southern Blot of teb1-1 cells grown at permissive and restrictive temperatures shows no change in telomere length, compared to wild type cells
PMID:23314747	AACCCT box, subtelomere
PMID:23314747	AACCCT box, subtelomere
PMID:23314747	AACCCT box, subtelomere
PMID:23314747	Cnp1 localisation to centromere reduced in teb1-1 cells grown at 36C (based on immunofluorescence)
PMID:23333317	Fig2I single mutant cut12. T75A binds dis2
PMID:23333317	Fig1 D & E
PMID:23333317	Fig1D
PMID:23333317	Fig1D
PMID:23333317	Fig1C increased interaction in 2 hybrid
PMID:23333317	Fig1 E
PMID:23333317	Fig1E
PMID:23333317	Fig1E
PMID:23333317	Fig1E
PMID:23333317	Fig1 E
PMID:23333317	"Fig1A, 2A. vw""Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)"""
PMID:23333317	Fig2A
PMID:23333317	Fig 2A,C Cut12.PD swap can no longer suppress cdc25-22 at 36°C because dis2.NGBP can bind to cut12.PDswap. When dis2 is deleted cdc25-22 suppression is restored
PMID:23333317	Fig2G
PMID:23333317	Fig2H
PMID:23333317	Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	Fig 2E unphosphorylatable cut12 mutants are unable to rescue cdc25 mutant (vw changed from decreased to abolished?)
PMID:23333317	Fig2E single mutant T78D does not rescue cdc25-22 as well as double T75DT78D. (vw changed from increased to decreased as we are comparing to WT , bottom row)
PMID:23333317	Fig2E single mutant T75D does not rescue cdc25-22 as well as double T75DT78D or singleT78D mutants. (vw: changed to decreased)
PMID:23333317	Fig2I single mutant cut12.T78A binds Dis2
PMID:23333317	Fig2I single mutant cut12. T75D reduces dis2 binding
PMID:23333317	Fig2I single mutant cut12. T78D reduces dis2 binding
PMID:23333317	Fig2I Fig3C double mutant cut12.T75A T78A binds dis2
PMID:23333317	Fig4A HU arrest Fig4E synchronous culture
PMID:23333317	Fig4A fin1 activation is dependent on sid1
PMID:23333317	Fig4A an antibody that recognized Cut12 when phosphorylated on T75 [Figure S2C] alone established that MPF phosphorylates T75 in vitro [Figure 4D]).
PMID:23333317	Fig4E in absence of fin1 activity dis2 remains bound to cut 12
PMID:23333317	Fig4F dis2 remains bound to cut12
PMID:23333317	Fig4F T75 T78 no longer phosphorylated and dis2 remains bound to cut12
PMID:23333317	Fig5A No increase in recruitment of plo1 to SPB when fin1 is active if T75 T78 mutated to A
PMID:23333317	vw: could this one be abolished? Fig5A No change in recruitment of plo1 to SPB when fin1 is inactivated T75 T78 mutated to D
PMID:23333317	Fig5A plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	Fig5A plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B. premature recruitment of protein to the mitotic SPB
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 decreased specific activity
PMID:23333317	Fig5B Dis2NGBP binds to cut12GFP and suppresses the cut12PDswap phenotype
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 decreased specific activity
PMID:23333317	Fig5B DELAYED
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 decreased specific activity
PMID:23333317	Fig5B DELAYED
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 decreased specific activity
PMID:23333317	Fig5B DELAYED
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig5B plo1 increased specific activity
PMID:23333317	Fig5B
PMID:23333317	Fig5B
PMID:23333317	Fig1H cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (vw changed form increased to normal, compared to WT)
PMID:23333317	Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue). [ie The cut12.s11 (G71V) mutation enables cdc25+ null cells (cdc25.D) to form microcolonies of 1 to 20 cells [14]. ]
PMID:23333317	Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	Fig2E
PMID:23333317	T75T78
PMID:23333317	T75
PMID:23333317	Fig 1b, F and G. (T75T78 UNPHOSPHORYLATED FORM)
PMID:23333317	Fig 1b, F and G. (T75T78 PHOSPHORYLATED FORM)
PMID:23333317	Fig1 C 2 hybrid
PMID:23333317	Fig1c 2-hybrid
PMID:23333317	Fig1 C 2 hybrid
PMID:23333317	Fig1C 2 hybrid
PMID:23333317	Fig1C 2 hybrid
PMID:23333317	Fig2H
PMID:23333317	Fig2H (VWI added this and man=de the original 'abnormal cell size' small (variable size at division, mixed sized see #3800)
PMID:23333317	Fig1H cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (vw changed form increased to normal, compared to WT)
PMID:23333317	Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	Fig1c 2-hybrid
PMID:23333317	Fig1D
PMID:23348717	assayed using cell growth with AspRec8c–FGFP–Mei2SATA construct (degradation frees Mei2SATA to arrest cell cycle)
PMID:23348717	assayed using ArgDHFRts–HA–Mcm4ts construct or AspRec8c–FGFP construct
PMID:23348717	also assayed using AspRec8c–FGFP construct, which persists longer than unmodified full-length Rec8
PMID:23348717	assayed using ArgDHFRts–HA–Mcm4ts construct or AspRec8c–FGFP construct
PMID:23348717	assayed using AspRec8c–FGFP construct
PMID:23348717	assayed using AspRec8c–FGFP construct
PMID:23349636	more specifically, response to mitotic DNA replication checkpoint signaling
PMID:23349808	during cytokinesis
PMID:23349808	during G2 phase of mitotic cell cycle
PMID:23349808	during G2 phase of mitotic cell cycle
PMID:23349808	during G2 phase of mitotic cell cycle
PMID:23349808	during G2 phase of mitotic cell cycle
PMID:23394829	also present in early anaphase; disappears by late anaphase
PMID:23394829	also present in early anaphase; disappears by late anaphase
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	rec25-204::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	rec27-205::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	rec25-204::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23427262	vw after attachment
PMID:23427262	vw after attachment
PMID:23442800	required for ubiquitination of Slp1
PMID:23462181	Fig. 2A and B
PMID:23462181	Fig. 2A and B
PMID:23462181	Fig. 2A and B
PMID:23462181	Fig. 2A and B
PMID:23462181	Fig. 2A and B
PMID:23496905	fig 4 (40% act remaining)
PMID:23496905	fig 4 (60%)
PMID:23496905	Figure 2
PMID:23496905	Figure 1
PMID:23496905	fig 2
PMID:23496905	fig 2
PMID:23496905	Figure 1
PMID:23496905	Figure 3
PMID:23496905	Figure 1
PMID:23496905	fig 2
PMID:23496905	Figure 3
PMID:23496905	Figure 3
PMID:23496905	Figure 1
PMID:23496905	fig 2
PMID:23496905	Figure 1
PMID:23496905	fig 2
PMID:23496905	Figure 3
PMID:23503588	in vitro
PMID:23551936	cellular response to rapamycin = GO:0072752 cellular response to caffeine =GO:0071313
PMID:23551936	cellular response to rapamycin = GO:0072752 cellular response to caffeine =GO:0071313
PMID:23555033	to CSL_response_element
PMID:23555033	overexpression
PMID:23555033	occurs_at CSL_response_element in vivo
PMID:23555033	occurs_at CSL_response_element, overexpression, in vitro
PMID:23555033	to CSL_response_element
PMID:23555033	major region affecting localization between aa 395–465
PMID:23576550	anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension
PMID:23576550	anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension
PMID:23609449	figure 10 (check specificty)
PMID:23609449	figure 10 (check specificty). Taken together, the results demonstrate that substitution of Trp-409 in the context of the full-length GIIβ has a moderate to high (60% inhibitory) effect on GII activity.
PMID:23609449	binds the non trimmed part of the N-glycan
PMID:23615450	complements deletion Figure 6A
PMID:23615450	(Figure 3).
PMID:23615450	(Figure 3).
PMID:23615450	(Figure 3).
PMID:23615450	Supple- mental Figure S9C)
PMID:23615450	in interphase
PMID:23615450	complements deletion Figure 6A
PMID:23615450	complements deletion Figure 6A
PMID:23615450	complements deletion Figure 6A
PMID:23615450	complements deletion Figure 6A
PMID:23615450	Figure 4C
PMID:23615450	Figure 4C
PMID:23615450	Figure 4F
PMID:23615450	Figure 4F inferred penetrance because growth not m,uch affected
PMID:23615450	Figure 4F
PMID:23615450	complements deletion
PMID:23615450	fig 5
PMID:23615450	complements deletion
PMID:23615450	Kd ≈ 20 μM Supplemental Figure S5B
PMID:23615450	complements deletion
PMID:23615450	complements deletion
PMID:23615450	complements deletion
PMID:23615450	complements deletion
PMID:23615450	complements deletion
PMID:23615450	complements deletion
PMID:23615450	Figure 1D
PMID:23615450	Figure 1C and Supplemental Figure S1C
PMID:23615450	Figure 1E and Supplemental Figure S1C
PMID:23615450	Figure 1E and Supplemental Figure S1C
PMID:23615450	Figure 1E and Supplemental Figure S1C
PMID:23628763	fig2
PMID:23628763	fig3c
PMID:23628763	fig3c
PMID:23628763	boosts expression of the APC activator Fzr1/Mfr1
PMID:23628763	binds chromatin at promoter, and phenotypes suggest this
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	same as cpc2delta alone
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	vw edited
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	same as gcn2delta alone
PMID:23671279	worse than cpc2delta alone
PMID:23671279	same as cpc2delta alone
PMID:23671279	same as either single mutant
PMID:23671279	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23677513	same as rad9delta alone
PMID:23677513	same as hus1delta alone
PMID:23677513	same as rad9delta alone
PMID:23677513	same as hus1delta alone
PMID:23677513	same as rad9delta alone
PMID:23677513	same as rad9delta alone
PMID:23677513	same as hus1delta alone
PMID:23677513	same as hus1delta alone
PMID:23687372	occurs_during(G1 to G0 transition)
PMID:23687372	occurs_during(G1 to G0 transition)
PMID:23687372	occurs_during(G1 to G0 transition)
PMID:23687372	homothallic h90
PMID:23687372	homothallic h90
PMID:23687372	move down to G1, nitrogen induced
PMID:23687372	occurs_during(G1 to Go transition)
PMID:23695302	they don't say whether the OEP populations continue to grow like normal (viable/inviable). Also data not shown.
PMID:23754748	fig s1, can't tell after germination or before
PMID:23770677	We incubated cell ghosts in the presence of ATP and the myosin-II ATPase inhibitor blebbistatin (0.1 mM; ref. 17). Whereas rings underwent rapid contraction in the absence of blebbistatin, ring contraction was abolished in the presence of blebbistatin (Fig. 3a, nD8).
PMID:23770679	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	meiosis I
PMID:23770679	fig 7c
PMID:23770679	Fig 7
PMID:23770679	Figure 6 b/d (d used chromosome tethered polo mutants, I did not curate these phenotypes)
PMID:23770679	Fig 6a
PMID:23770679	fig 4c
PMID:23770679	Is this phase correct
PMID:23770679	Is this phase correct
PMID:23770679	fig 3d
PMID:23770679	Fig 2 b-d nvolved in kinetochore retrieval during meiotic prophase
PMID:23770679	figure 2a
PMID:23770679	fig 5b
PMID:23770679	Fig 5. d,e (unattached)
PMID:23770679	fig 2g
PMID:23770679	Fig 2 b-d involved in kinetochore retrieval during meiotic prophase
PMID:23770679	fig 5b
PMID:23770679	figure 4
PMID:23770679	Supp Fig S6
PMID:23770679	figure 4c
PMID:23770679	fig 4d
PMID:23770679	fig 3d
PMID:23770679	Fig 3b
PMID:23770679	fig 2G
PMID:23770679	fig 4d
PMID:23770679	Fig 6c or abolished?
PMID:23770679	fig 4c
PMID:23770679	Is this phase correct
PMID:23770679	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	polo consensus fig 6b
PMID:23770679	Supp Fig S6
PMID:23770679	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
PMID:23770679	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
PMID:23851719	results in retaining specifically modified histone H3 at the genes in question
PMID:23874237	The SO ID's correspond to tRNA lys/gln/glu
PMID:23874237	The SO ID's correspond to tRNA lys/gln/glu
PMID:23874237	The SO ID's correspond to tRNA lys/gln/glu
PMID:23885124	throughout cell cycle; present in approximately equal stoichiometry with Alp4/GCP2 (immunoblotting and quantification of GFP-Mzt1 and GFP-Alp4 signals at the SPB)
PMID:23885124	throughout cell cycle; present in approximately equal stoichiometry with Alp4/GCP2 (immunoblotting and quantification of GFP-Mzt1 and GFP-Alp4 signals at the SPB)
PMID:23907979	The mating rate was not affected in mtl2Dh+ 9 mtl2Dh
 or wsc1Dh+ 9 wsc1Dh
 homozygous crosses,
PMID:23907979	wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B)
PMID:23907979	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cul- tures.
PMID:23907979	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23907979	In tea4D cells, Wsc1p-GFP localized mainly to the growing tip that was stained with Cfw (Fig. 3C).
PMID:23907979	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concen- trated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	Repres- sion of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	Repres- sion of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	The mating rate was not affected in mtl2Dh+ 9 mtl2Dh
 or wsc1Dh+ 9 wsc1Dh
 homozygous crosses,
PMID:23907979	mtl2D cells were unable to grow on plates sup- plemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	Figure 4B, the activation of Rho1p, through the expres- sion of a constitutively active form of Rho1p or overex- pression of the wild-type Rho1p or Rgf1p, efficiently restored the growth of a strain (P81nmt-mtl2 wsc1D) unable to grow in the presence of thiamine (promoter off).
PMID:23907979	GTP bound modified form . Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	GTP bound modified form. Interest- ingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	. Interest- ingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	. Interest- ingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	Mtl2p-GFP showed an even membrane distribution with little intra- cellular signals.
PMID:23907979	wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B)
PMID:23907979	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	. Interest- ingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	The wsc1Drgf2D double mutant was viable, but we failed to find any double- mutant spore wsc1Drgf1D. T
PMID:23907979	described as rounded , but more 'stubby'
PMID:23907979	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cul- tures.
PMID:23907979	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cul- tures.
PMID:23907979	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concen- trated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	Moreover, when we looked at the cell wall composition of mtl2D mutants we found a decrease in the total amount of glucose incorpo- rated in the cell wall as compared with wild-type cells (30% in wild-type cells and 25% in mtl2D). The differ- ence was mainly due to a decrease in the b–glucan content (17% in the wild type and 13% in the mtl2D) (Fig. 1E).
PMID:23907979	We found that GS activity was slightly reduced in mtl2D null cells (Fig. 1D)
PMID:23907979	wsc1D cell growth was inhibited above 2 lg/mL of Csp (Fig. 1C)
PMID:23907979	mtl2D cells were unable to grow on plates sup- plemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23907979	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	mtl2D cells were unable to grow on plates sup- plemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23936074	increased staining of all chromatin
PMID:23936074	assayed using minichromosomes and internal telomeric repeat arrays
PMID:23956092	was branched, elongated, multiseptate cell
PMID:23962284	recombinant hal3 not a strong inhibitor in vitro
PMID:23962284	we don't know if they germinate or not
PMID:23966468	FYPO_EXT:0000001=high penetracne
PMID:23966468	This is inferred from a combination of genetic interactions, localizations and phenocopy experiments, it has not been directly assayed but it feels 'safe' (VW)
PMID:23977061	I changed this to exocytosis. This is required for cell wall organization, as it is causally upstream (val)
PMID:23977061	effect on secretion is specific for cell wall enzymes; secretion of acid phosphatase is normal (but assayed acid phosphatase activity in medium, so can't tell which gene(s))
PMID:23986474	(Fig. 2B). The M167F mutation in either the orb5.as1 or orb5.as2 backbone generated the orb5.as8 and orb5.as9 alleles, which were more sensitive to analogue inhibition than the respective parental allele
PMID:23986474	The static FACS profiles established that replication was indeed inhibited in analogue-released cdc10.v50 wee1.as8 cdc25.22 cells after analogue addition (Fig. 7B, right panel).
PMID:23986474	as arrested at 36 ̊C for 4.25 hours and released into synchronous mitosis by Wee1 inhibition using 30 mM 3BrB-PP1. The figure shows tubulin immunofluorescence and DAPI signals of cells 3 hours after release to reveal the characteristic ‘crows foot’ configuration of microtubules of cut7 mutants as the two halves of the mitotic spindle fail to interdigitate.
PMID:23986474	Analogue-released wee1.as8 cdc25.22 cut9.665 cells transiently accumulated much higher levels of metaphase spindles than wild-type cells before they ‘leaked’ through this mitotic arrest to execute telophase and cytokinesis with the classic ‘cut’ phenotype that originally led to the identification of the cut9.665 mutation (Fig. 6A,B)
PMID:23986474	dns
PMID:23986474	fig 4c.
PMID:23986474	fig 3c. We therefore compared the ability of wee1.as1 and wee1.as8 to suppress cdc25.22 lethality at 36 ̊C. Inhibition of Wee1.as8 but not Wee1.as1 activity with analogue addition suppressed cdc25.22 lethality at 36 ̊C (Fig. 3B). A comparison of four ATP analogues revealed that the suppression (and therefore Wee1 inhibition) was most effective with 3BrB-PP1 (Fig. 3C).
PMID:23986474	fig 1. Chronic exposure to analogue through growth on solid medium reiterated the acute impact of analogue inhibition in liquid culture (Fig. 1A) and established that plo1.as8 is most effectively inhibited by 3BrB- PP1 (Fig. 1B).
PMID:23986474	Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	Fig 1. Chronic exposure to analogue through growth on solid medium reiterated the acute impact of analogue inhibition in liquid culture (Fig. 1A) and established that plo1.as8 is most effectively inhibited by 3BrB- PP1 (Fig. 1B).
PMID:23986474	Fig 1.
PMID:23986474	Fig 1.
PMID:23986474	Fig 1
PMID:23986474	DNS
PMID:23986474	Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	(Fig. 2B). The M167F mutation in either the orb5.as1 or orb5.as2 backbone generated the orb5.as8 and orb5.as9 alleles, which were more sensitive to analogue inhibition than the respective parental allele
PMID:23986474	rb5.as8 inhibition did not produce the ‘orb’ phenotype observed in the original orb5.ts mutants at the restrictive temperature (data not shown)
PMID:23986474	(Table 1; Fig. 3A)
PMID:23986474	(Table 1; Fig. 3A)
PMID:23986474	fig 3c
PMID:23986474	fig 3c. We therefore compared the ability of wee1.as1 and wee1.as8 to suppress cdc25.22 lethality at 36 ̊C. Inhibition of Wee1.as8 but not Wee1.as1 activity with analogue addition suppressed cdc25.22 lethality at 36 ̊C (Fig. 3B). A comparison of four ATP analogues revealed that the suppression (and therefore Wee1 inhibition) was most effective with 3BrB-PP1 (Fig. 3C).
PMID:24003116	Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS.
PMID:24003116	Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS.
PMID:24003116	Via EMSA binds directly to adh4 promoter.
PMID:24003116	Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS.
PMID:24003116	Visualized via Florescence using an integrated LOZ1::GFP construct grown in EMM +/- ZnSo4
PMID:24003116	directly regulates adh4
PMID:24006256	wee1-50 epistatic to dnt1delta; shows that cell cycle regulation by Dnt1 depends on Wee1
PMID:24006256	Dnt1 down-regulates Wee1 kinase. Had to remove extensions: independent_of(PomBase:Cdc25)| independent_of(PomBase:Rad3)| independent_of(PomBase:Chk1)| independent_of(PomBase:Cds1)| independent_of(PomBase:Clp1)| independent_of(PomBase:Pom1)| independent_of(PomBase:Cut12)| dependent_on(PomBase:Wee1) | acts_upstream_of(wee1) (mah 2015-11-06)
PMID:24006488	fig4
PMID:24006488	fig4
PMID:24006488	fig4
PMID:24006488	fig4
PMID:24006488	fig4
PMID:24006488	Serine 114 and Threonine 115 are phosphorylated by Cds1 upon activation of the DNA replication checkpoint. Yox1 phosphorylation by Cds1 releases Yox1 from MBF and activates MBF-dependent transcription.
PMID:24006488	localizes the MBF complex
PMID:24006488	Serine 720 and Serine 732 are phosphorylated by Chk1 Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.
PMID:24006488	fig4
PMID:24006488	Serine 720 and Serine 732 are phosphorylated by Chk1 Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.
PMID:24013504	dependent_on(GO:0006312)| not_dependent_on(GO:0007004)
PMID:24021628	heterologous complemetation of S. c HMO1
PMID:24039245	in vitro assay with purified proteins
PMID:24047646	Fig3, Table 1
PMID:24047646	Fig1 In early G2 nif1 localisation is monopolar and in late G2 it is bipolar
PMID:24047646	Fig1
PMID:24047646	Fig1
PMID:24047646	Fig1
PMID:24047646	Fig1
PMID:24047646	Fig3, Table 1
PMID:24047646	Fig3, Table 1
PMID:24047646	Fig 6, shows pom1delta cells still have G2-M size control
PMID:24047646	Fig 6, shows nif1delta cells still have G2-M size control
PMID:24047646	Fig 6, shows wee1-50 cells at restrictive temperature have lost G2-M size control
PMID:24055157	assayed with human CK1, process from phenotypes (dma1 dependent pathway)
PMID:24055157	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	In cells growing asynchronously, both Hhp1-GFP and Hhp2-GFP localized to the nucleus, SPBs, and the cell division site, although Hhp2-GFP was more prominent at the division site compared to Hhp1-GFP (Figure 3B).
PMID:24055157	assayed with human CK1
PMID:24055157	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	In dma1Δ cells, a single slower migrating form of Sid4 was detected, which was collapsed by phosphatase treatment, indicating that Sid4 is phosphorylated in vivo (Figure 1A, lanes 3 and 4). In vivo radiolabeling experiments validated Sid4 as a phospho-protein and revealed that Sid4 is phosphorylated on serines and threonines (Figure S1A–C).
PMID:24055157	Although mutating S278 to alanine abolished Sid4 ubiquitination (Figure 1D)
PMID:24055157	mutating S278 to a glutamate did not affect Sid4 ubiquitination (Figure 1D).
PMID:24055157	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F),
PMID:24055157	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F),
PMID:24055157	Thus, phosphorylation on both T275 and S278 is necessary and sufficient to support binding of the Dma1 FHA domain to Sid4 and Sid4 ubiquitination.
PMID:24055157	cells bypassed the arrest after 5 hrs (Figure 2C). ......These data indicate that mutating T275 eliminates Dma1-dependent checkpoint signaling.
PMID:24055157	cells bypassed the arrest after 5 hrs (Figure 2C).
PMID:24055157	In corroboration of these findings, sid4(T275A) mutants were refractory to dma1 overexpression lethality (Figure 2D).
PMID:24055157	In cells growing asynchronously, both Hhp1-GFP and Hhp2-GFP localized to the nucleus, SPBs, and the cell division site, although Hhp2-GFP was more prominent at the division site compared to Hhp1-GFP (Figure 3B).
PMID:24055157	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F),
PMID:2406029	same as cdc2-ww single mutant
PMID:24074952	residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215
PMID:24074952	residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215
PMID:24074952	residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215
PMID:24081329	evidence for all FYPO:0001908 = northern blot
PMID:24095277	siRNA
PMID:24095277	has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+
PMID:24095277	does it produce 5' monoesters?
PMID:24095277	has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+
PMID:24115772	inhibits
PMID:24115772	dependent on septation initiation signaling (GO:0031028)
PMID:24115772	during(GO:0051329)
PMID:24118096	Trx1's involvement in tis process is to recycle mxr1 for met-O conversion to met
PMID:24127216	fig1b
PMID:24127216	fig1a
PMID:24127216	fig1b
PMID:24127216	fig3e
PMID:24127216	fig3e
PMID:24127216	Depends on Cdc15 to localize to the contractile ring during Anaphase A. Viewed by fluorescent fusion protein. AL - exists during anaphase A and anaphase B
PMID:24127216	Depends on Cdc15 to localize to the contractile ring during Anaphase A. Viewed by fluorescent fusion protein. AL - exists during anaphase A and anaphase B
PMID:24127216	Truncation of Cdc12 at N-terminus leads to a requirement of For3 actin assembly for contractile ring assembly.
PMID:24127216	Truncation of Cdc12 at N-terminus leads to a requirement of For3 actin assembly for contractile ring assembly. AL -also see fig 2fgh
PMID:24127216	figs2a
PMID:24127216	fig2a
PMID:24127216	fig2a
PMID:24127216	figS1a
PMID:24127216	fig 1h
PMID:24127216	fig 1d-g
PMID:24127216	fig 1d-g
PMID:24127216	fig 1D-G
PMID:24146635	prolonged heat exposure (more than ~45 min)
PMID:24146635	prolonged heat exposure (more than ~45 min)
PMID:24146635	prolonged heat exposure (more than ~45 min)
PMID:24146635	prolonged heat exposure (more than ~45 min)
PMID:24146635	Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.
PMID:24146635	"""Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells"""
PMID:24146635	"""Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells"""
PMID:24146635	shorter duration of heat exposure (up to ~45 min)
PMID:24146635	shorter duration of heat exposure (up to ~45 min)
PMID:24146635	shorter duration of heat exposure (up to ~45 min)
PMID:24146635	prolonged heat exposure (more than ~45 min)
PMID:24146635	prolonged heat exposure (more than ~45 min)
PMID:24146635	Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.
PMID:24146635	36 degrees (not brief heat shock)
PMID:24146635	punctate; shorter duration of heat exposure (up to ~45 min)
PMID:24147005	6A
PMID:24147005	7c
PMID:24155978	5S
PMID:24155978	all independent of Sty1 (effects of H2O2 & NAC unchanged in sty1delta)
PMID:24155978	5X
PMID:24161933	fig1
PMID:24161933	abundances of 40% or lower, cells lacked checkpoint activity.
PMID:24161933	(Fig. 2d)
PMID:24161933	In cells with 30% Mad1, the checkpoint was markedly impaired in minimal medium, although largely functional in rich medium
PMID:24161933	Even reduction to about 10% of the original Mad1 level, which is hardly visible by fluorescence microscopy (Fig. 2e), did not fully abolish the SAC
PMID:24161933	5a.
PMID:24167631	FYPO:0001178 + PECO:0000240 captures info for requested new term (Term name: loss of viability upon long-term nutrient starvation Definition: A cell population phenotype in which a smaller than normal proportion of the population remains viable when cells in a culture in stationary phase are deprived of nitrogen. Use this term to annotate experiments in which a culture is cultivated in stationary phase under nitrogen-depleted conditions for a long time (more than 1 week), and then the number of cells viable enough to form a colony upon return to conditions supporting vegetative growth is measured and compared to wild type.) -mah
PMID:24186976	supp fig7
PMID:24186976	supp fig7
PMID:24224056	in response to carbon source change from glucose to maltose regulates agl1
PMID:24224056	in response to carbon source change from glucose to maltose regulates agl1
PMID:24224056	The decrease in cell growth on maltose medium is suppressed by neighboring wild-type cells but not by agl1 delta cells, which are defective in maltase secretion.
PMID:24239120	Fig. 3
PMID:24239120	Fig. S1 (This is a partial rescue of FYPO:0004307)
PMID:24239120	Fig. 4
PMID:24239120	Fig. S1
PMID:24239120	Fig. S1
PMID:24239120	Fig. 1
PMID:24239120	Fig. 1
PMID:24239120	Fig. 1
PMID:24239120	Fig. 3
PMID:24239120	Fig. 1
PMID:24239120	Fig. S1 The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker, it really is anaphase onset that is measured.
PMID:24239120	Fig. 1
PMID:24239120	Fig. 3
PMID:24239120	Fig. 1
PMID:24239120	Fig. S1 The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker, it really is anaphase onset that is measured.
PMID:24239120	Fig. S1 The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker, it really is anaphase onset that is measured.
PMID:24239120	Fig. S1 The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker, it really is anaphase onset that is measured.
PMID:24239120	Fig. S1 (This is a rescue of FYPO:0000324)
PMID:24239120	Fig. 3
PMID:24239120	Fig. 1
PMID:24239120	Fig. 1
PMID:24239120	Fig. 2 (This is a rescue of FYPO:0004395)
PMID:24239120	Fig. 1
PMID:24239120	Fig. S1 (This is a rescue of FYPO:0000324)
PMID:24239120	Fig. 1
PMID:24239120	Fig. 4
PMID:24239120	Fig. 1
PMID:24239120	Fig. 3
PMID:24239120	Fig. 2 (This is a rescue of FYPO:0004395)
PMID:24239120	Fig. 2 (This is a rescue of FYPO:0000324)
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24240238	Rap1-GBD + low-level swi6+ overexpression allows assays using a reporter gene away from the telomere, to distinguish effects of taz1 and pot1 mutations.
PMID:24240238	Rap1-GBD + low-level swi6+ overexpression allows assays using a reporter gene away from the telomere, to distinguish effects of taz1 and pot1 mutations.
PMID:24240238	Rap1-GBD + low-level swi6+ overexpression allows assays using a reporter gene away from the telomere, to distinguish effects of taz1 and pot1 mutations.
PMID:24240238	experiment introduced otr::ura4+ in either a silenced state (from wild-type cells) or a desilenced state (from clr4delta cells) into poz1delta dcr1delta cells by genetic crosses
PMID:24240238	silencing normal as long as heterochromatin assembly can take place normally
PMID:24240238	Southern blot to detect telomeric sequence
PMID:24244528	However, the lower molecular weight form of -E1 failed to accumulate over time following protease addition (Figure 4C), suggesting an altered conformation more sensitive to proteolysis.
PMID:24244528	decreased. (atpase activity assay) However, -E1 motors exhibited relatively low activity under either condition (Figure S1). These experiments performed in the absence of actin suggest that defects in -E1 motors are not specific to actin displacement and motility, and probably reflect a general defect in conformation and function.
PMID:24244528	Our data indicates thatRng3p is required to establish active Myo2p motors.The control experiments (where cells were shifted to 37uC at 22hours post-induction) indicated that Rng3p was not essential formaintaining Myo2p motility once an active population of motorshad been synthesized, as previously reported [24]...........Collectively our findings suggest that Rng3p is required to generate an active and stable population of Myo2p motors.
PMID:24244528	However, most filaments (99%) bound by -E1 were non-motile, while most filaments bound by wild-type Myo2p were motile (Movie S2).
PMID:24247430	I think this is real i.e. downregulation of growth to allow differentiation
PMID:24268782	vw: fixed extensions to link F-P and to delete GO:0051091
PMID:24268782	vw: fixed extensions to link F-P and to delete GO:0051091 vw: move up to from thioredoxin-disulfide reductase activity
PMID:24291789	Fig. 1a
PMID:24291789	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	Fig. 1c,d part_of extension is 'positive regulation of mitotic cohesin loading'
PMID:24291789	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 1c,d (part_of extension is 'positive regulation of mitotic cohesin loading'
PMID:24291789	Fig. 1a
PMID:24291789	fig 4 b part_of extension is 'positive regulation of mitotic cohesin loading'
PMID:24291789	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	(Fig. 2e) Fig. 2f) Fig. 3a,b). contributes to, mis4 is sufficient?
PMID:24291789	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	(Fig. 2e) Fig. 2f) Fig. 3a,b).
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	Fig. 2a,b and Extended Data Fig. 2a
PMID:24297439	Two hybrid interaction using Gpa2K270E activated protein with Sck1.
PMID:24297439	Effect of sck1 deletion to increase cell length in git3 delete cells depends on Gpa2 activity. Otherwise, Sck1 acts in parallel with Pka1 to increase cell length.
PMID:24297439	Two hybrid interaction using Gpa2K270E activated protein with Sck1.
PMID:24297439	it's a bit indirect, but they show this via consensus site mutations....I think it is borderline ok
PMID:24313451	assayed using cell extract, overexpressed protien and synthetic UB conjugate
PMID:24314397	inhibited by α-(hydroxymethyl)serine (CHEBI:28187)
PMID:24316795	high overexpression
PMID:24316795	same as cdr2-S755A-758A alone
PMID:24316795	same as cdr2-S755A-758A alone
PMID:24316795	Pom1-as1 protein may preferentially localize to non-growing end.
PMID:24316795	Phosphorylates cdr2 at S755 in vitro
PMID:24316795	Cdr2 phosphorylated by Pom1 at the CTD negatively regulates its activity
PMID:24316795	Negatively regulated by Pom1 via phosphorylation of C-ter
PMID:24316795	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	high concentration (1 uM) 3MB-PP1
PMID:24316795	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	high concentration (1 uM) 3MB-PP1
PMID:24316795	high concentration (1 uM) 3MB-PP1
PMID:24316795	high concentration (1 uM) 3MB-PP1
PMID:24316795	high overexpression
PMID:24316795	moderate overexpression
PMID:24327658	accelerates degradation of active Sre1 transcription factor
PMID:24327658	Binds specifically to active Sre1 transcription factor and not full-length precursor
PMID:24327658	in vitro kinase assay using recombinant Sre1 aa 1-440
PMID:24327658	in vitro kinase assay using recombinant Sre1 aa 1-440
PMID:24327658	in vitro kinase assay using recombinant Sre1 aa 1-440
PMID:24327658	Ok as a single mutant despite sre1-N mutant?
PMID:24327658	hhp2 deletion increases steady-state ergosterol
PMID:24344203	same as isp7+ overexpression alone
PMID:24344203	isp7+ overexpression decreases Gad8's kinase activity towards substrate Fkh2
PMID:24344203	same as isp7+ overexpression alone
PMID:24475199	Expression level up 22 times
PMID:24475199	Expression level up 31 times
PMID:24475199	Expression level up 43 times
PMID:24475199	Expression level up 38 times
PMID:24475199	Expression level up 23 times
PMID:24475199	Expression level up 25 times
PMID:24475199	Expression level up 2 times
PMID:24475199	Expression level up 2 times
PMID:24475199	Expression level up 2 times
PMID:24475199	Expression level up 3 times
PMID:24475199	Expression level up 2 times
PMID:24475199	Expression level up 2.5 times
PMID:24475199	Expression level up 35 times
PMID:24475199	Expression level up 8 times.
PMID:24477934	Fig S2C,D,E
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	Fig S4a
PMID:24477934	(Fig 1F
PMID:24477934	fig1F
PMID:24477934	Fig1F
PMID:24477934	Fig1F
PMID:24477934	Fig 1A, C–E
PMID:24477934	Fig 1A, C–E
PMID:24477934	Fig S4A
PMID:24477934	Fig S4A
PMID:24477934	Fig1C/D
PMID:24477934	Fig 1I–L
PMID:24477934	Fig 1I–L
PMID:24477934	Fig 1I–L
PMID:24477934	Fig3 B/C
PMID:24477934	Fig3 B/C
PMID:24477934	Fig 3 D
PMID:24477934	Fig 3D
PMID:24477934	Fig S1B
PMID:24477934	Fig S1B
PMID:24477934	Fig S1I
PMID:24477934	Fig S1I
PMID:24477934	Fig S1I
PMID:24477934	Fig S2F
PMID:24477934	Fig S2F
PMID:24477934	Fig S2C,D,E
PMID:24477934	Fig S2C,D,E
PMID:24477934	Fig S2C,D,E
PMID:24477934	Fig S2F
PMID:24477934	Fig S2F
PMID:24477934	Fig S1A and D
PMID:24477934	Fig 1A, C–E
PMID:24477934	Fig 1A, C–D
PMID:24477934	1H
PMID:24477934	Fig 1H
PMID:24477934	Fig 1H
PMID:24477934	Fig 2B
PMID:24477934	(Fig (Fig 2D and E). mad1 localized did not rescue,
PMID:24477934	Fif 3F
PMID:24477934	. A complex between the checkpoint proteins Mad1 and Mad2 provides a platform for Mad2:Mad2 dimerization at unattached kinetochores, which enables Mad2 to delay anaphase. Here, we show that mutations in Bub1 and within the Mad1 C-terminal domain impair the kinetochore localization of Mad1:Mad2 and abrogate checkpoint activity. Artificial kinetochore recruitment of Mad1 in these mutants co-recruits Mad2; however, the checkpoint remains non-functional. We identify specific mutations within the C-terminal head of Mad1 that impair checkpoint activity without affecting the kinetochore localization of Bub1, Mad1 or Mad2. Hence, Mad1 potentially in conjunction with Bub1 has a crucial role in checkpoint signalling in addition to presenting Mad2.
PMID:24478458	phosphorylates rgf1 during HU response, part of maintenance of protien lcoation in nucleus
PMID:24493644	fig5
PMID:24514900	Required for phosphatydil serine reorganization at the inner leaflet of plasma membrande during cell fusion
PMID:24514900	high penetrance
PMID:24514900	low expressivity
PMID:24521463	mild phenotype
PMID:24521463	decreased cell pop is not a child of this term
PMID:24521463	high expressivity (strong phenotype)
PMID:24521463	low expressivity
PMID:24521463	mild expressivity
PMID:24554432	necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2
PMID:24554432	more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape
PMID:24554432	sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2
PMID:24554432	more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape
PMID:24554432	more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape; similar pom1 deletion phenotype indicates that Tea4 is at least partly independent of Pom1 for Rga4 localization
PMID:24554432	more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape
PMID:24554432	sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2; tea1/pom1 double mutant phenotype shows that Tea4 role is independent of Pom1
PMID:24554432	necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2
PMID:24554432	sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2
PMID:24569997	changed from transcription because mrna measured (fig 1)
PMID:24569997	changed from transcription because mrna measured (fig 1)
PMID:24569997	Observed at this location during spore maturation by indirect immunofluorescence
PMID:24569997	changed from transcription because mrna measured (fig 1)
PMID:24569997	*******during copper excess****** changed from transcription because mrna measured fig2
PMID:24569997	changed from transcription because mrna measured fig2 (copper excess)
PMID:24569997	figure 5B
PMID:24569997	figur 5B
PMID:24569997	changed from transcription because mrna measured fig2
PMID:24583014	Fig. 2A, , complex seen here in anaphase although it normally forms in prometaphase and disassembles before anaphase
PMID:24583014	Fig. 1A
PMID:24583014	Fig. 1B,
PMID:24583014	Fig. 1A indicating that CDK1 activity remained high
PMID:24583014	Fig. 1A
PMID:24583014	Fig. 1A
PMID:24583014	Fig. S1B,C
PMID:24583014	Fig. 2B,C
PMID:24583014	Fig. 2B,C
PMID:24583014	figure S1B
PMID:24583014	Fig. 3A,B,E, securin abnormally stabilized during anaphase
PMID:24583014	Fig. 1D,E
PMID:24586893	the extension means that the phenotype has low expressivity (i.e. weak sensitivity)
PMID:24637836	Our strains expressing GFP-tagged nucleoporins were all viable, but four of them (spNup45-GFP, spNup184-GFP, GFP-spRae1, and spNup189n-GFP) showed growth deficiencies
PMID:24637836	Fluorescence microscopy of Sec13 tagged with GFP at either its N-terminal or C-terminal end.
PMID:24637836	sensitivity is weak.
PMID:24637836	sensitivity is weak.
PMID:24637836	weak sensitivity
PMID:24637836	sensitivity is weak
PMID:24637836	sensitivity is weak.
PMID:24652833	it affects suc22 binding to cdc22. There is no evidence thta it is involved in catabolism and I dont think I can make a MF from it.
PMID:24652833	no MF possible
PMID:24662054	binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system
PMID:24662054	binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system
PMID:24663817	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	(phosphorylated rad9)
PMID:24663817	affected by rad4
PMID:24663817	3a/b
PMID:24663817	3a/b. cds1-T11
PMID:24663817	3a/b
PMID:24663817	Fig. 5A and B
PMID:24663817	Consistent with the previous report [58], the interaction between Rad9 and Rad4 was dependent on Rad9 phosphorylation because the phosphorylation site mutant Rad9-T412A could not pull-down Rad4 (Fig. 5A, first lane on the left) and the interaction between Rad9 and Rad4 was sensitive to l-phosphatase treatment (Fig. S5A).
PMID:24663817	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B).
PMID:24663817	E368K mutation abolished the binding to Rad9 as previously reported [47] (Fig. 5A and B)
PMID:24663817	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B).
PMID:24663817	The C13Y and K56R mutations abolished the scaffolding function of Rad4 required for the activation of Chk1 but not Rad3
PMID:24663817	f3
PMID:24663817	f3
PMID:24663817	3D
PMID:24663817	3D
PMID:24663817	Interestingly, the DC mutant with the deletion of the whole C-terminus between amino acid 498 and 648 was resistant to HU and MMS almost like the wild type cells (Fig. 1D and 2B). The only difference we could readily find for the DC mutant was that the protein level was higher than in the wild type cells (Fig. 2C), suggesting that the C-terminus may not contain a robust AAD (see below).
PMID:24663817	1D, Fig. 2B
PMID:24663817	1D,Fig. 2B
PMID:24663817	3D
PMID:24663817	3D
PMID:24663817	1D
PMID:24663817	We found that combinations of the previously reported E368K mutation [47] with K56R or F303S were lethal suggesting a defect in DNA replication.
PMID:24663817	We found that combinations of the previously reported E368K mutation [47] with K56R or F303S were lethal suggesting a defect in DNA replication.
PMID:24663817	1D, Fig. 2B
PMID:24663817	1D, Fig. 2B
PMID:24663817	1D,Fig. 2B
PMID:24663817	1D,Fig. 2B
PMID:24663817	1D
PMID:24663817	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	1D
PMID:24663817	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)The slight decrease in Cds1 phosphorylation may be caused indirectly by a minor defect in DNA replication
PMID:24696293	supp fig
PMID:24710126	central core
PMID:24710126	convert to double mutant (cnp1 overexpression)
PMID:24710126	central core
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	"[Term] id: FYPO_EXT:0000003 name: low def: ""small fraction of cells (penetrance) or weak phenotype (expressivity)"" [PomBase:curators]"
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	Observed in cells undergoing vegetative growth.
PMID:24713849	Observed in cells undergoing vegetative growth.
PMID:24713849	Observed in cells undergoing vegetative growth.
PMID:24713849	Observed in cells undergoing vegetative growth.
PMID:24713849	Observed in cells undergoing vegetative growth.
PMID:24713849	Observed in cells undergoing vegetative growth.
PMID:24741065	tor2 phosphorylates mei2. Phosphorylated mei2 is ubiquitylated which targets it for degradation via the proteasome.
PMID:24741065	phosphorylation of mei2 targets it for degradation via the proteasome
PMID:24755092	SPAC12G12.09-mCherry localizes to stress granules
PMID:24755092	Exo2-GFP localizes to stress granules
PMID:24758716	qualifier=major
PMID:24758716	qualifier=minor Hsp3106 (synonym: spDJ-1) has a lower in vitro glyoxalase III activity than Hsp3101 and Hsp3102
PMID:24758716	qualifier=major
PMID:24768994	Figure 3
PMID:24768994	Figure 2B
PMID:24768994	Figure 5
PMID:24768994	Figure 5
PMID:24768994	Figure 2B
PMID:24768994	Figure 2C
PMID:24768994	Figure 2A
PMID:24768994	Figure 5
PMID:24768994	Figure 3
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	add other complex members
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24774534	fig6
PMID:24787148	ubiquitin monmomer inhibits sst2
PMID:24790093	Yeast two hybrid
PMID:24790095	exists_during( metaphase? anaphase A????)
PMID:24790095	exists_during( metaphase? anaphase A????)
PMID:24790095	mitotic interphase
PMID:24798735	"this annotation extension means ""small fraction of cells"""
PMID:24798735	"this annotation extension means ""small fraction of cells"""
PMID:24798735	"this annotation extension means ""small fraction of cells"""
PMID:24798735	"this annotation extension means ""small fraction of cells"""
PMID:24806815	This localisation requires phosphorylated histone H2A.
PMID:24806815	Mdb1 binds to Hta1 phosphorylated on Ser-129. PR:000027566 = H2A phosphorylated on S129
PMID:24815688	"transferres from term suggestion to allow approval decreased growth under low-glucose conditions Definition: ""decreased growth under low-glucose conditions"" is an ""decreased cell population growth"" that occurs specifically on media supplied with a lower concentration of glucose than regular media. ditto all the others"
PMID:24818994	figure 1D
PMID:24818994	figure 1 A
PMID:24818994	Figure 1 A
PMID:24818994	Figure 1 A
PMID:24818994	Figure 1 A
PMID:24818994	Figures 3 and 6
PMID:24818994	Figures 3 and 6
PMID:24818994	Figures 3 and 6
PMID:24818994	Figures 3 and 6
PMID:24818994	Figure 5A, +
PMID:24818994	minor
PMID:24818994	figure 1D
PMID:24818994	figure 1D
PMID:24831008	fig4
PMID:24831008	Fig 2
PMID:24831008	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	Fig 2
PMID:24831008	fig 4g
PMID:24831008	fig2
PMID:24831008	Fig 2
PMID:24831008	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	Fig 2
PMID:24831008	fig1
PMID:24831008	fig1
PMID:24831008	fig4
PMID:24831008	Figure 7 - the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains and an upstream accessory domain
PMID:24831008	Figure 7 - the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains and an upstream accessory domain
PMID:24831008	Figure 7 - the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains
PMID:24847916	The phenotype is assessed by the high-throughput sequencing.
PMID:24876389	internalization abolished
PMID:24876389	have guessed at deleted residues
PMID:24876389	SPBC18H10.20c protein appears to have a function as arrestin-related trafficking adaptor, which is involved in ubiquitination of membrane transporters and subcellular localization of them. val, I changed the 'with' field to pub1, but I want to also add *****
PMID:24876389	abolished internalization
PMID:24876389	ubiquitinated probably at K263.
PMID:24876389	abolished internalization
PMID:24876389	abolished internalization
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	abnormal RNA localization to chromatin
PMID:24920274	fig3
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	fig3
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920274	fig3
PMID:24920274	fig3
PMID:24920274	"the def includes ""maintenance of lcoalization WITHIN nucleus"" so it fits the def, but maybe the term looks weird"
PMID:24920274	"the def includes ""maintenance of lcoalization WITHIN nucleus"" so it fits the def, but maybe the term looks weird"
PMID:24920274	at sme2 locus (one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	at sme2 locus (one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	figS1
PMID:24920274	figS1
PMID:24920823	results from collapse of actomyosin contractile ring
PMID:24920823	S326, T429, S499: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	S326, T429, S499: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	anaphase B
PMID:24920823	medium penetrance
PMID:24920823	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	Term name: supports establishment of SIN asymmetry Definition: characterized by asymmetric localization of the SIN initiator kinase Cdc7 in anaphase
PMID:24920823	affecting Cdc7
PMID:24920823	targets Byr4 at S248A, S326A, T412A, T429A, S499A, T502A, S533A, results in Byr4 removal from metaphase spindle pole bodies
PMID:24920823	Cdk1-dependent, Cdk1 non-phosphorylatable Byr4 localizes to one or both SPBs in >90% of metaphase cells
PMID:24920823	low penetrance
PMID:24925530	starts with longer telomeres than wild type, which then shorten
PMID:24928430	Fig. 3
PMID:24928430	Fig. 3
PMID:24928430	Fig. 3 - minor rescue
PMID:24928430	Fig. 3 - minor rescue
PMID:24928430	Fig. 3 - minor rescue
PMID:24928430	Fig. 1
PMID:24928430	Fig. 1
PMID:24928430	Fig. 2
PMID:24928430	Fig. 4 - minor rescue
PMID:24928430	Fig. 3 - minor rescue
PMID:24928430	Fig. 4 - minor rescue
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	Phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	Protein phosphorylation assayed in vitro
PMID:24928510	Protein phosphorylation assayed in vitro
PMID:24928510	Phosphorylation assayed in vitro
PMID:24928510	Phosphorylation assayed in vitro
PMID:24928510	Phosphorylation assayed in vitro
PMID:24928510	Phosphorylation assayed in vitro
PMID:24928510	Phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24928510	protein phosphorylation assayed in vitro
PMID:24936793	also inferrable (IC) from GO:0051787
PMID:24937146	affecting Pcp1 and Alp4
PMID:24937146	affecting Pcp1 and Alp4
PMID:24937146	affecting Alp7
PMID:24945319	I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex).
PMID:24945319	I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex).
PMID:24945319	I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex).
PMID:24947517	Data not shown
PMID:24947517	Fig. 3F
PMID:24947517	Fig. 3F
PMID:24947517	Fig 1 F
PMID:24947517	fig 1 F
PMID:24947517	Fig 1 E
PMID:24947517	Fig 1 E
PMID:24947517	Fig 1 D
PMID:24947517	Fig 1 D (decreased rate of cell separation)
PMID:24947517	Fig. 1C
PMID:24947517	Data not shown
PMID:24947517	Data not shown
PMID:24947517	Fig 4 A
PMID:24947517	Fig 4 A
PMID:24947517	Fig 4 A
PMID:24947517	Fig 4 A
PMID:24947517	Fig. 4A
PMID:24947517	Fig 6 B.
PMID:24947517	Fig 6 B.
PMID:24947517	Fig 6 B.
PMID:24947517	Fig 6 B.
PMID:24947517	Fig 6 B.
PMID:24947517	Fig. 6A
PMID:24947517	Fig 6 B.
PMID:24947517	Fig. 6A
PMID:24947517	Fig 5 B
PMID:24947517	Fig 5 A
PMID:24947517	Fig 6 C.
PMID:24947517	Fig. 5A
PMID:24947517	Fig 6 C, D
PMID:24947517	Fig 6 D.
PMID:24947517	(Fig. 6D)
PMID:24947517	Fig 4 C,D,E
PMID:24947517	Fig. 1B
PMID:24947517	Fig. 3A
PMID:24947517	Fig. 5A
PMID:24947517	Fig. 1B
PMID:24947517	Fig. 1B
PMID:24947517	Fig. 4A
PMID:24947517	Fig 1 F
PMID:24947517	fig 1 F
PMID:24947517	Figure 3 C
PMID:24947517	Figure 3 C
PMID:24947517	Data not shown
PMID:24947517	Fig. 3F
PMID:24954052	PR:000037081= ID for acetylated form of cdc8
PMID:24954052	GO:0051286 = cell tip PR:000037082 = ID for unacetylated form of cdc8
PMID:24954111	bipolar spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	bipolar/spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	fig1
PMID:24954111	fig1
PMID:24954111	Fig 6 A,B even in the presence of the bipolar spindle
PMID:24954111	never observed 37/37
PMID:24954111	never observed 54/54
PMID:24954111	spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	fig1 In wild-type cells, monopolar or nonpolar spindles were not observed (Fig. 4C).
PMID:24957674	xap5 genetically interacts with pht1 to repress antisense transcripts. In the ∆xap5∆pht1 double mutants the level of antisense transcription is exacerbated as observed using RNA-seq. Selected loci also showed antisense RNA production in histone deacetylase (HDACs) gene mutants.
PMID:24957674	SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element
PMID:24957674	SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element
PMID:24957674	SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element
PMID:24963130	(GO:0000279) = mitotic M-phase
PMID:24963130	2 sub populations spindle elongation delayed during anaphase A spindle elongation delayed during anaphase B
PMID:24963130	GO:0000087 mitotic M-phase
PMID:24963130	should this move down to lobate? http://www.pombase.org/spombe/related/FYPO:0002005
PMID:24963130	GO:0000236 mitotic prometaphase
PMID:24997422	). Interestingly, growth of transformants over- expressing truncated Fxn1 with a disrupted mitochondrial localization sequence (Fxn1Δ2–11) is similar to pREP3X at all concentrations of thi- amine (Fig. 1A). These observations demonstrate that the growth inhi- bition resulting from Fxn1 overexpression is related to mitochondrial levels or improper processing of Fxn1.
PMID:25002536	occurs at LTR and ncRNA
PMID:25002536	LTR and ncRNA
PMID:25002536	occurs at LTR and ncRNA
PMID:25002536	LTR and ncRNA
PMID:25002536	occurs at LTR and ncRNA
PMID:25002536	occurs at LTR and ncRNA
PMID:25009287	Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane.
PMID:25009287	Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane.
PMID:25015293	same as spt20delta alone
PMID:25015293	punctate
PMID:25015293	multinucleate inferred from DNA content
PMID:25015293	multinucleate inferred from DNA content
PMID:25015293	multinucleate inferred from DNA content
PMID:25015293	multinucleate inferred from DNA content
PMID:25015293	multinucleate inferred from DNA content
PMID:25015293	same as spt20delta alone
PMID:25015293	same as spt20delta alone
PMID:25040903	Figure S1E
PMID:25040903	Figure S1C
PMID:25040903	Figure S1C
PMID:25040903	Figure S1E
PMID:25057016	Fig. 4
PMID:25057016	Fig. 6
PMID:25057016	Fig. 6
PMID:25057016	Fig. 6
PMID:25057016	Fig. S5D
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4 (BiFC)
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4 (BiFC)
PMID:25057016	Fig. 4
PMID:25057016	Fig. 4
PMID:25057016	Fig. 3
PMID:25057016	Fig. 3
PMID:25057016	Fig. 3
PMID:25057016	Fig. S1D
PMID:25057016	Fig. 2
PMID:25057016	Fig. 2
PMID:25057016	Fig. 1
PMID:25057016	Fig. 1
PMID:25057016	Fig. 1
PMID:25057016	Fig. 1
PMID:25057016	Thorough experiments throughout using both full deletions as well as phospho mutants. Direct physical interaction is confirmed by Y2H
PMID:25057016	Good evidence for this is the colocalisation with cnp3 in Fig. 3A in the csi1D background, where alp7 does not go to the spindle, or nda3 mutant where the spindle does not form, but alp7 still goes to the kinetochore, as seen by cnp3
PMID:25066056	The heterozygous deletion h+/ h+ strains with exchanged one copy of SPBC2A9.06c ORFs for kanMX4 cassette (Genome-wide Deletion Mutant Library (Bioneer) was able to produce viable spores only when transformed with plasmid expressing Giardia lamblia cis-prenyltransferase but not carrying empty vector.
PMID:25066056	rer2 was shown to be indispensable subunit of dehydrodolichyl diphosphate synthase. It is not active cis-prenyltransferase by itself but it forms active enzyme with nus1
PMID:25066056	nus1 was shown to be indispensable subunit of dehydrodolichyl diphosphate synthase. It is not active cis-prenyltransferase by itself but it forms active enzyme with rer2 (SPAC4D7.04c)
PMID:25081204	cmk1 seems to phosphorylate prz1 which makes prz1 cytoplasmic. During response to calcium, calcineurin dephosphorylates prz1 and it goes to the nucleus.
PMID:25081204	prz1 is the pombe equivalent to NFAT (functional equivalent rather than orholog)
PMID:25081204	prz1 is the pombe equivalent to NFAT (functional equivalent rather than orholog)
PMID:25081204	the pop grows more slowly but I guess they are viable en large
PMID:25103238	Failure of NE fenestration during mitosis in the double tts1del cut1-6 mutant
PMID:25103238	large fraction of cells = annotation_extension=has_penetrance(FYPO_EXT:0000001)
PMID:25106870	RER should probably be a child of this
PMID:25106870	fig 1
PMID:25106870	fig5
PMID:25106870	Tolerance of the 8oxoguanine lesion during DNA gap-filling inserting the ribonucleotide ATP. This acitivity can be coupled to the non-homologous end joining (NHEJ) of double strand breaks (DSBs). changed from dna repair to translesion synthesis. /AL
PMID:25106870	Incision of ribonucleotides paired to 8oxoguanine in the DNA
PMID:25109267	Ricinoleic acid, RA moieties from phospholipids
PMID:25122751	At stress response genes
PMID:25195688	transmembrane import into Golgi lumen
PMID:25195688	transmembrane import into Golgi lumen
PMID:25203555	regulator of structure-specific DNA nuclease
PMID:25203555	not sure
PMID:25204792	defect in sexual development in response to zinc or iron limitation
PMID:25204792	defect in sexual development in response to zinc or iron limitation
PMID:25245948	cDNA; no introns
PMID:25245948	cDNA; no introns
PMID:25245948	cDNA; no introns
PMID:25245948	cDNA; no introns
PMID:25245948	cDNA; no introns
PMID:25245948	cDNA; no introns
PMID:25254656	figure 3C
PMID:25254656	Figure 4E
PMID:25254656	Figure 4E
PMID:25254656	in vitro Figure S1A, right pane
PMID:25254656	in vitro Figure S1A, right pane
PMID:25254656	figure 3C
PMID:25254656	Figure 4A)
PMID:25254656	figure 3C the N erminal domain has a dominent -ve effect in in vitro assay (not expression should ne n/a)
PMID:25254656	Figure 3A
PMID:25254656	Figure S15
PMID:25254656	Figure S2A
PMID:25254656	igure 3B Figure 3C
PMID:25313826	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25313826	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25313826	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25318672	restrictive temperature for bbl1-9
PMID:25318672	Determined by thin layer chromatography (TLC)
PMID:25318672	Determined by thin layer chromatography (TLC)
PMID:25318672	Determined by thin layer chromatography (TLC)
PMID:25318672	Mutant cells grow normally in liquid minimal medium supplemented with ethanolamine.
PMID:25318672	Mutant cells grow normally in liquid minimal medium supplemented with choline.
PMID:25318672	Determined by thin layer chromatography (TLC)
PMID:25318672	The endoplasmic reticulum is wrapped around the abnormally large lipid droplets
PMID:25318672	restrictive temperature for bbl1-9
PMID:25318672	restrictive temperature for bbl1-9
PMID:25318672	Mutant cells grow normally in liquid rich medium
PMID:25318672	Slow population growth rate can be rescued by supplementing the minimal medium with choline or ethanolamine, the precursors required for phospholipid biosynthesis through the de novo Kennedy pathway
PMID:25318672	At the restrictive temperature of 36C, cells accumulate very large lipid droplets surrounded by the endoplasmic reticulum. These lipid droplets arise from persistent growth rather than fusion.
PMID:25318672	At high temperature (36C), the mutant protein appeared to bind PA nearly as well as the wild-type enzyme but exhibited a strongly decreased rate of catalysis.
PMID:25318672	permissive temperature for bbl1-9
PMID:25330395	Tpz1-L439R,L445R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments.
PMID:25330395	Tpz1-L449R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments. In combination with poz1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase cannot be recruited to telomeres since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is eliminated by tpz1-L449R.
PMID:25330395	Tpz1-[1-485] disrupts interaction with Poz1 but retain interactions with Pot1 and Ccq1 based on co-IP experiments. In combination with ccq1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase recruitment to telomeres is increased since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is increased in tpz1-[1-485] cells.
PMID:25330395	Tpz1-W498R,I501R disrupts interaction with Poz1 but retain interactions with Pot1 and Ccq1 based on co-IP experiments. In combination with ccq1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase recruitment to telomeres is increased since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is increased in tpz1-W498R,I501R cells.
PMID:25375240	figure 5E
PMID:25375240	Figure 7D
PMID:25375240	indicated by increased mad2 on unattached kinetochores
PMID:25375240	Tracking of the inter-SPB distance indicated that the kinetics of spindle elongation in the kis1-1 mad2D double mutant was ameliorated compared with the kis1-1 single mutant (Figure S9).
PMID:25375240	Figure 4G
PMID:25375240	Figure 7D
PMID:25378562	mutants defective in vacuolar sorting do not deliver SpCPY to the 185 vacuole but rather to the outside of the cells.
PMID:25378562	Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane.
PMID:25378562	mutants defective in vacuolar sorting do not deliver SpCPY to the 185 vacuole but rather to the outside of the cells.
PMID:25378562	Sensitive to 3 mM ZnCl2
PMID:25378562	Sensitive to 3 mM ZnCl2. Suppressed by overexpression of budding yeast VAM7.
PMID:25378562	Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane.
PMID:25392932	SO:0001272 = tRNA gene
PMID:25392932	SO:0001272 = tRNA gene
PMID:25392932	Our data only demonstrate that this true for RNA Polymerase III // MOVED UP TO 'REGULATION' FROM NEG REG BASED ON NEW PUBLICATION
PMID:25402480	"They couldn't make the knockout in haploid, and diploid inviable, hence inferring inviable vegetative rather than more general ""inviable cell pop"" (or inviable spore pop)"
PMID:25402480	"SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced.."
PMID:25402480	"SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced.."
PMID:25402480	"SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced.."
PMID:25402480	"SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced.."
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	strain lacked Gm34 in its tRNAPhe, and had Cm levels comparable to those of wild type (0.86 versus 0.91 moles/mole) (Table 3; Fig. 4A).
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	yW formation was impaired in the Sp trm734△ mutant (44% of wild-type levels) and to a lesser extent in the Sp trm732△ mutant (73%) (Fig. 4F), consistent with the increased m1G levels (Table 3; Fig. 4A)
PMID:25404562	specific term requested
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	diploid lacked detectable Cm in its tRNAPhe and had normal levels of Gm compared with that from wild type (0.88 versus 0.90 moles/mole) (Table 3; Fig. 4A)
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	Table 2
PMID:25404562	specific term requested
PMID:25404562	Table 2
PMID:25404562	specific term requested
PMID:25404562	yW formation was impaired in the Sp trm734△ mutant (44% of wild-type levels) and to a lesser extent in the Sp trm732△ mutant (73%) (Fig. 4F), consistent with the increased m1G levels (Table 3; Fig. 4A)
PMID:25404562	strain lacked Gm34 in its tRNAPhe, and had Cm levels comparable to those of wild type (0.86 versus 0.91 moles/mole) (Table 3; Fig. 4A).
PMID:25404562	diploid lacked detectable Cm in its tRNAPhe and had normal levels of Gm compared with that from wild type (0.88 versus 0.90 moles/mole) (Table 3; Fig. 4A)
PMID:25404562	Fig. 2A (11 days for visible colonies)
PMID:25404562	Fig. 3A
PMID:25404562	Table 2
PMID:25410910	yes it looks like pol II?! (val: changed to DNA binding term)
PMID:25411334	changed from bud neck to medial cortex ring but the def will be updated so it does not refer to double ring https://sourceforge.net/p/geneontology/ontology-requests/11819/ || depends on septins to localize to the division site.
PMID:25411334	check supp S2A
PMID:25411334	A GEF of Rho4
PMID:25411334	check supp S2A
PMID:25411334	check supp S2A is this increased septation index?
PMID:25411334	check supp S2A
PMID:25411338	during cellular response to glucose starvation
PMID:25411338	during cellular response to glucose starvation
PMID:25411338	during cellular response to glucose starvation
PMID:25411338	during cellular response to glucose starvation
PMID:25411338	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	The ght5 gene, the transcription of which is repressed in the WT cells, is transcribed at a high level in the presence of 111 mM glucose in the scr1 delta cells.
PMID:25411338	strong phenotype = has_severity(FYPO_EXT:0000001)
PMID:25411338	the level of ght5 transcription, which increases in the WT during glucose limitation, fails to increase in this mutant cells in low-glucose medium.
PMID:25411338	the level of ght5 transcription, which increases in the WT during glucose limitation, fails to increase in this mutant cells in low-glucose medium.
PMID:25411338	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	strong phenotype = has_severity(FYPO_EXT:0000001)
PMID:25414342	21.46% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	38.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25414342	(Table S2)
PMID:25414342	117% of wild-type recombination assayed at various loci (Fig. 1, Table S2)
PMID:25414342	78.4% of wild-type spore viability (Table S2)
PMID:25414342	28.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25414342	39.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25414342	85.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 4C, Table S5)
PMID:25414342	61.1% of wild-type spore viability (Fig. 4D, Table S5)
PMID:25414342	61.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4)
PMID:25414342	42.4% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4)
PMID:25414342	82.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 4C, Table S5)
PMID:25414342	95.2% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4)
PMID:25414342	27.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4)
PMID:25414342	82.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 3C, Table S4)
PMID:25414342	108.5% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	49.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4)
PMID:25414342	49.2% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4)
PMID:25414342	90.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 3C, Table S4)
PMID:25414342	133.5% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	16.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25414342	9.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25414342	87.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 4C, Table S5)
PMID:25414342	77.7% of wild-type spore viability (Fig. 4D, Table S5)
PMID:25414342	31.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S6)
PMID:25414342	8.0% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 6, Table S6)
PMID:25414342	(Fig. 5, Table S6)
PMID:25414342	43.6% of wild-type spore viability (Table S6)
PMID:25414342	0.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	12.3% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	1.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3)
PMID:25414342	47% of wild-type spore viability (Fig. 2A, Table S3), 18.3-fold higher spore viability than mus81 single mutant
PMID:25414342	19.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	2.2% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	10.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3)
PMID:25414342	42.9% of wild-type spore viability, 16.7-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3)
PMID:25414342	26.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	30.1% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	9.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3)
PMID:25414342	21.2% of wild-type spore viability, 8.3-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3)
PMID:25414342	6.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	57.9% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	7.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3)
PMID:25414342	28.9% of wild-type spore viability, 11.3-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3)
PMID:25414342	58.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	36.3% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	6.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3)
PMID:25414342	44.7% of wild-type spore viability, 17.4-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3)
PMID:25414342	48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig.3B, Table S4)
PMID:25414342	32.3% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 3A, Table S4)
PMID:25414342	85.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 3C, Table S4)
PMID:25414342	117.1% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	55.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 3B, Table S4)
PMID:25414342	44.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 3A, Table S4)
PMID:25414342	78.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 3C, Table S4)
PMID:25414342	104.8% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5)
PMID:25414342	0.42% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5)
PMID:25414342	3.7% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	4.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5)
PMID:25414342	2.5% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5)
PMID:25414342	18.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. 4C, Table S5)
PMID:25414342	13.0% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	33.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5)
PMID:25414342	14.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5)
PMID:25414342	84.1% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 4C, Table S5)
PMID:25414342	93.8% of wild-type spore viability, epistatic relationship (Fig. 4D, Table S5)
PMID:25414342	26.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5)
PMID:25414342	25.7% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5)
PMID:25414342	91.4% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 4C, Table S5)
PMID:25414342	76.9% of wild-type spore viability, epistatic relationship (Fig. 4D, Table S5)
PMID:25414342	0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5)
PMID:25414342	2.1% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5)
PMID:25414342	106.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 4C, Table S5)
PMID:25414342	9.9% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	65.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5)
PMID:25414342	21.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5)
PMID:25414342	76.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship; skewed recombinant classes (Figs. 4C & 7A, Table S5)
PMID:25414342	55.5% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	54.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S5)
PMID:25414342	31.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Table S5)
PMID:25414342	75.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. S2, Table S5)
PMID:25414342	50.7% of wild-type spore viability, synergistic relationship (Table S5)
PMID:25414342	15.4% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	76.1% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S6)
PMID:25414342	7.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship - similar to rqh1delta (Fig. 6, Table S6)
PMID:25414342	124.3% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship - similar to fml1delta (Fig. 5, Table S6)
PMID:25414342	60.64% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	7.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6A, Table S6)
PMID:25414342	24.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	115.17% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 5A, Table S6)
PMID:25414342	25.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	2.55% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig.6A, Table S6)
PMID:25414342	115.12% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. 5A, Table S6)
PMID:25414342	54.78% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	28.85% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	3.55% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig.6A, Table S6)
PMID:25414342	119.91% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 5A, Table S6)
PMID:25414342	55.62% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, partial rescue from rad55Δ levels (Table S6)
PMID:25414342	35.42% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6)
PMID:25414342	111.64% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 5B, Table S6)
PMID:25414342	53.76% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	15.19% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	8.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6)
PMID:25414342	127.22% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. 5B, Table S6)
PMID:25414342	3.68% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	15.53% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	12.19% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6)
PMID:25414342	136.75% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. 5B, Table S6)
PMID:25414342	4.11% of wild-type spore viability (Table S6)
PMID:25414342	69.41% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	36.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6)
PMID:25414342	101.33% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; higher than rlp1Δ-7, lower than fml1Δ, skewed recombinant categories (Figs. 5C & 7A, Table S6)
PMID:25414342	46.52% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	52.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Table S6)
PMID:25414342	102.17% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, higher than rdl1Δ-25, lower than fml1Δ, skewed recombinant categories (Fig. S3, Table S6)
PMID:25414342	73.46% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	32.13% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	8.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6)
PMID:25414342	116.19% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. 5C, Table S6)
PMID:25414342	37.75% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	59.57% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	7.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6)
PMID:25414342	130.25% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship (Fig. 5C, Table S6)
PMID:25414342	21.45% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	49.8% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	27.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6D, Table S6)
PMID:25414342	122.65% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship (Fig. 5D, Table S6)
PMID:25414342	91.68% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	38.89% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	10.34% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6D, Table S6)
PMID:25414342	101.4% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories (Fig. 5D, Table S6)
PMID:25414342	45.45% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	15.59% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig.6D, Table S6)
PMID:25414342	114.54% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories (Fig. 5D, Table S6)
PMID:25414342	20.24% of wild-type spore viability (Table S6)
PMID:25414342	55.49% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	37.89% of wild-type recombination assayed between ade6-3083 and ade6-469, similar to dmc1Δ-12 and rlp1Δ single mutants, but higher than dmc1Δ-12 rlp1Δ double mutant (Fig.6E, Table S6)
PMID:25414342	79.92% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories (Figs. 5E & 7A, Table S6)
PMID:25414342	7.8% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	30.92% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	9.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6E, Table S6)
PMID:25414342	101.76% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories (Figs. 5E & 7A, Table S6)
PMID:25414342	31.18% of wild-type spore viability (Table S6)
PMID:25414342	20.15% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S6)
PMID:25414342	6.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6E, Table S6)
PMID:25414342	111.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant classes (Figs. 5E & 7A, Table S6)
PMID:25414342	13.87% of wild-type spore viability (Table S6)
PMID:25414342	(Table S2)
PMID:25414342	83.9% of wild-type spore viability (Fig. 4D, Table S5)
PMID:25414342	(Fig. 4C, Table S5)
PMID:25414342	33.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25417108	affecting: highly transcribed genes antisense transcription of tDNA and rDNA
PMID:25417108	occurs at rDNA, tRNA gene, protein coding gene
PMID:25417108	affecting: highly transcribed genes antisense transcription of tDNA and rDNA
PMID:25417108	affecting antisense transcription at tDNA
PMID:25417108	occurs at rDNA, tRNA gene, protein coding gene
PMID:25417108	Affecting Rad52 enrichment at rDNA
PMID:25417108	occurs at tDNA
PMID:25417108	affecting: highly transcribed genes antisense transcription of tDNA and rDNA
PMID:25417108	Affecting Dcr1-terminated genes
PMID:25417108	occurs at rDNA, tRNA gene, protein coding gene
PMID:25417108	Affecting Rad52 enrichment at rDNA
PMID:25417108	affecting antisense transcription at rDNA
PMID:25428589	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	In contrast, nc-tgp1, nc-pho1 and sme2þ RNA levels were clearly elevated in cells lacking Mmi1-mediated exosome degradation (mmi1D and rrp6D). Th
PMID:25428589	Our ChIP analyses confirmed that Pho7–green fluorescent protein (Pho7–GFP) accumulates on the pho1 þ promoter in phosphate- depleted cells (Supplementary Fig. 8). In addition, Pho7–GFP levels accumulate over the region upstream of tgp1þ when activated (Fig. 6a
PMID:25428589	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	Cells lacking SPNCRNA.1343 (ncRNA.1343 for short) displayed a phenotype: hypersensitivity to TBZ, HU and caffeine but not to temperature extremities, ultraviolet- irradiation or oxidative stress (Supplementary Fig. 1c and Supplementary Fig. 2).
PMID:25428589	(repressed condition; Fig. 1c)
PMID:25428589	We identified a consensus DSR motif for Mmi1 binding at position þ820 nt within the nc-tgp1 transcript and RNA IP (RIP) experiments confirmed a direct interaction between Mmi1 and the nc-tgp1 RNA (Supplementary Fig. 5).
PMID:25428589	prevented nc-tgp1 transcription, induced tgp1þ expression to levels observed in 1343D levels and increased sensitivity of these cells to TBZ, HU and caffeine (Fig. 3b,c). These analyses demonstrate that it is nc-tgp1, not nc-1343, that is critical for repressing tgp1þ in the presence of phosphate.
PMID:25428589	Trun- cations of nc-1343 (that is, AD and BD) that retain its 50 end did not result in the drug-sensitivity phenotype presented by 1343D cells (Fig. 3b) and, similarly, did not induce tgp1þ expression (Fig. 3c)
PMID:25428589	To determine whether the drug sensitivity of 1343D cells is a direct result of increased tgp1þ expression, the tgp1þ gene was deleted from 1343D cells (tgp1D1343D). This manipulation restored TBZ, HU and caffeine tolerance to levels comparable with wild-type cells (Fig. 1d). We conclude that increased tgp1þ expression is directly responsible for the drug-sensitivity phenotype of cells lacking ncRNA.1343.
PMID:25428589	Trun- cations of nc-1343 (that is, AD and BD) that retain its 50 end did not result in the drug-sensitivity phenotype presented by 1343D cells (Fig. 3b) and, similarly, did not induce tgp1þ expression (Fig. 3c)
PMID:25428589	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	In agreement with this, significantly less RNAPII associates with the nc-tgp1 transcription unit in both phosphate- starved wild-type cells and phosphate-replete 1343D cells, which do not transcribe nc-tgp1 (Fig. 4c).
PMID:25428589	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428987	mitotic interphase
PMID:25451933	Surprisingly, contractile rings began to constrict earlier in 􏰀aip1 cells than wild type cells (Fig. 7, A and B, and Table 3), foreshortening the maturation period before constriction
PMID:25451933	SpAip1 dramatically stimulated severing by 100 nM cofilin, with a maximum rate at 1.5 􏰋M SpAip1 and lower rates at higher concentrations (Fig. 3C).At all SpAip1 concentrations tested 􏰅80% of new barbed ends created by severing events depolymerized (Fig. 3D) at rates that decreased insignificantly with SpAip1 concentration (Fig. 3E). These depolymerization rates were higher than published values (2), likely because severing near barbed ends was difficult to distin- guish from filament depolymerization.
PMID:25451933	The fission yeast lacking Aip1 have normal appearing actin patches, cables, and contractile rings (Fig. 5B).
PMID:25451933	As a result, ring constriction in 􏰀aip1 cells takes 􏰅 5 min less than in wild type cells (Table 3). Overall, cytokinesis was 􏰅16 min (24%) faster in 􏰀aip1 cells than wild type cells, because the maturation period was shorter and the rings constricted faster.
PMID:25451933	competatively with cofilin
PMID:25451933	igs. 6B and C and Table 3
PMID:25471935	assayed Cdc20 recruitment
PMID:25472718	Overall, our data suggest that Klp5–Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	Fig. 2C,D
PMID:25472718	fig 2A
PMID:25472718	fig 3 d
PMID:25472718	Fig. 4C,D)
PMID:25472718	Fig. 4A,B
PMID:25472718	Fig. 4E reduced by >70%
PMID:25472718	Fig. 4A,B
PMID:25472718	fig 1A
PMID:25472718	Fig 1A
PMID:25472718	(Fig. 1C–E; Type I
PMID:25472718	(Fig. 1C–E; Type I
PMID:25472718	(Fig. 1C–E; Type I
PMID:25472718	Fig 1A
PMID:25472718	(supplementary material Fig. S1A
PMID:25472718	fig 2 A
PMID:25472718	fig 3A
PMID:25472718	fig 3A
PMID:25472718	fig 3A
PMID:25472718	fig 3A
PMID:25472718	In any case, the results shown here imply that Klp5–Klp6 localises to the kinetochores through interaction with the Alp7–Alp14 complex.
PMID:25472718	Overall, our data suggest that Klp5–Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	In any case, the results shown here imply that Klp5–Klp6 localises to the kinetochores through interaction with the Alp7–Alp14 complex.
PMID:25472718	Fig. 5D
PMID:25472718	Fig. 5D
PMID:25472718	fig 2 A
PMID:25472718	Fig. 5A
PMID:25472718	fig S2B
PMID:25472718	fig S2B
PMID:25472718	Fig. 5A
PMID:25472718	Fig. 5A
PMID:25472718	Fig. 4E reduced by >70%
PMID:25472718	Fig. 1C; Fig. 3D
PMID:25472718	Fig. 1C; Fig. 3D
PMID:25472718	fig 3C
PMID:25473118	the ring seems to start off forming normally but maturation is delayed, this leads to delayed constriction.
PMID:25473118	independent of actin
PMID:25473118	fig6
PMID:25473118	fig6
PMID:25487150	unphosphorylated form
PMID:25500221	secretion of acid phosphatase
PMID:25500221	secretion of acid phosphatase
PMID:25501814	fig1c
PMID:25501814	(Fig. 3C).
PMID:25501814	Cdc7p–GFP never disappeared from the old SPB (Sohrmann et al., 1998) and the type 1 nodes did not reform (Fig. 3B; supplementary material Movie 3)
PMID:25501814	fig 2g
PMID:25501814	fig1
PMID:25501814	fig1
PMID:25501814	fig1
PMID:25501814	fig1
PMID:25501814	fig1
PMID:25501814	fig1
PMID:25519804	high suppression of phenotype
PMID:25519804	efficient suppression of ade6-M26; very poor suppression of ade6-M375
PMID:25519804	high suppression of phenotype
PMID:25519804	suppresses ade6-M26 efficiently; suppresses ade6-M375 weakly
PMID:25519804	low suppression of phenotype
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	full-length Cut14 present; not sure how to interpret this, check
PMID:25520186	I only captured the OEX Experiment
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	I only captured the OEX experiment
PMID:25520186	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	of condensin complex
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	of condensin complex
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	full-length Cut14 present; not sure how to interpret this, check
PMID:25520186	full-length Cut14 present; not sure how to interpret this, check
PMID:25520186	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25533340	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180
PMID:25533340	This looks like direct regulation because it phosphorylates xlf1
PMID:25533340	leu1
PMID:25533340	increased end-joining activity in vegetative cells
PMID:25533340	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192
PMID:25533340	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180
PMID:25533340	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533348	WT 3%
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533348	greater range of legths
PMID:25533348	greater range of legths
PMID:25533348	greater range of legths
PMID:25533348	fig 3 A
PMID:25533348	WT 3%
PMID:25533348	WT 3%
PMID:25533348	WT 3%
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533348	fig 3 A
PMID:25533956	RECRUITS
PMID:25533956	fig5 e
PMID:25533956	fig5 e
PMID:25543137	Diffuse cytoplasmic localisation at 37°C, no stress granules
PMID:25543137	Dcr1 is not released from cytoplasmic inclusions at 37°C in hsp104Δ
PMID:25543137	A prionogenic reporter (S. cerevisiae Sup35 prion domain) aggregates in cytoplasmic inclusions in dcr1Δ
PMID:25543137	Dcr1 represses hsp104 levels
PMID:25543137	hsp104 refolds dicer and is required for robust centromeric silencing at 37°C
PMID:25543137	Cytoplasmic localisation in electron-dense inclusions at 37°C
PMID:25543137	Nuclear localization at 30°C
PMID:25543137	Dcr1 localizes in electron-dense cytoplasmic inclusions at 37°C together with hsp104. Hsp104 is required for dissolution of these inclusions.
PMID:25543137	Nuclear localization at 30°C
PMID:25590601	ii) in the presence of glucose
PMID:25590601	ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546
PMID:25590601	ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546
PMID:25590601	iii) decreased during glucose starvation
PMID:25590601	ii) removed during nitrogen starvation iv) T415
PMID:25590601	strong phenotype = has_severity(FYPO_EXT:0000001)
PMID:25590601	ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546
PMID:25619765	pNBg was used
PMID:25619765	cen2-lacO
PMID:25619998	(S2)
PMID:25619998	(S2)
PMID:25619998	(S2)
PMID:25619998	(S2)
PMID:25639242	figure 2a
PMID:25639242	2D & 4B
PMID:25639242	figure S2B
PMID:25639242	S3A
PMID:25639242	Fig 3G
PMID:25639242	However, no difference in CaMKKSsp1 protein levels or phos- ppk34 phorylation status was observed in CaMKK .D mutants compared with wild-type cells (Figures S4A and S4B
PMID:25639242	figure 5a
PMID:25639242	fig 3B
PMID:25639242	An increase in AMPKaSsp2 Thr189 phosphorylation was also observed in the cbs2 .D AMPKg .D double mutant (Figure S2F).
PMID:25639242	figure S2g
PMID:25639242	causally upstream of ssp2
PMID:25639242	However, no difference in CaMKKSsp1 protein levels or phos- ppk34 phorylation status was observed in CaMKK .D mutants compared with wild-type cells (Figures S4A and S4B
PMID:25639242	fig s4c&d
PMID:25639242	Fig 6G
PMID:25639242	causally upstream of ssp2
PMID:25639242	figure 2b 9% longer
PMID:25639242	figure 2a
PMID:25639242	figure 6E
PMID:25639242	figure 6E
PMID:25639242	fig 6A
PMID:25639242	FIG 3F
PMID:25639242	Fig 4C
PMID:25639242	Figure 4C
PMID:25639242	figure 4D
PMID:25639242	fig 3d
PMID:25639242	Fig 3C
PMID:25639242	FIG 3F DECOUPLED CELL GROWTH ASND DIVISION
PMID:25639242	figure 4D
PMID:25639242	figure 4E
PMID:25688133	residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM
PMID:25688133	mCherry-cdc15,Rlc-GFP
PMID:25688133	mCherry-cdc15,Rlc-GFP
PMID:25688133	LifeAct-mCherry Sid4-GFP
PMID:25688133	Cdc12-mNeonGreen, Ain1-GFP, GFP-Adf1
PMID:25688133	LifeAct-mCherry Sid4-GFP
PMID:25688133	LifeAct-mCherry Sid4-GFP
PMID:25688133	Live-cell imaging of Rlc1-GFP Sid4-GFP 23% slower
PMID:25688133	Live-cell imaging of Rlc1-GFP Sid4-GFP 26% slower
PMID:25688133	smears as does not self associate, but localizes to medial cortex
PMID:25688133	Cdc12-mNeonGreen, GFP-Adf1, Ain1-GFP
PMID:25688133	LifeAct-mCherry Sid4-GFP
PMID:25688133	mCherry-cdc15,Rlc-GFP
PMID:25688133	residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM
PMID:25688133	mCherry-cdc15,Rlc-GFP
PMID:25724335	Gene name : aco2
PMID:25724335	Gene name : aco2
PMID:25724335	Gene name : aco2
PMID:25724335	Gene name : aco2
PMID:25724335	Gene name : aco2
PMID:25724335	Gene name : aco2
PMID:25736293	S4A
PMID:25736293	fig 4 A
PMID:25736293	fig 3 B , supp S 3 B) abolished microtubule cortical anchoring
PMID:25736293	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	fig 3 B , supp S 3 B)
PMID:25736293	accumulates on shrinking microtubules Fig. 2B,
PMID:25736293	accumulates on shrinking microtubules Fig. 2B,
PMID:25736293	accumulates on shrinking microtubules Fig. 2B,
PMID:25736293	Figure S2C
PMID:25736293	Figure S2C
PMID:25736293	figure S2
PMID:25736293	figure S2
PMID:25736293	(Fig. 1C; supplementary material Fig. S1C),
PMID:25736293	(Fig. 1C; supplementary material Fig. S1C),
PMID:25736293	(Fig. 1C; supplementary material Fig. S1C),
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	3B?
PMID:25736293	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	Fig. 7F; supplementary material Table S1
PMID:25736293	Fig. 7F; supplementary material Table S1
PMID:25736293	Fig. 7F; supplementary material Table S1
PMID:25736293	Fig. 7F; supplementary material Table S1
PMID:25736293	Fig. 7F; supplementary material Table S1
PMID:25736293	fig 7A
PMID:25736293	fig 7a
PMID:25736293	fig 7a
PMID:25736293	figS1B
PMID:25736293	figS1B
PMID:25736293	abnormal movement of dynein
PMID:25736293	abnormal movement of dynein
PMID:25736293	fig 6a
PMID:25736293	fig 6a
PMID:25736293	fig 5 c
PMID:25736293	fig 5 c
PMID:25736293	S4B
PMID:25736293	S4B
PMID:25736293	(Fig. 5C
PMID:25736293	(Fig. 5C
PMID:25736293	S4B
PMID:25736293	S4B
PMID:25736293	S4A
PMID:25736293	S4A
PMID:25736293	S4A
PMID:25771684	"Affecting Sre1 is ""abolished protein processing"" that is specific for defects in Sre1 protein processing."
PMID:25771684	"The term ""Decreased protein binding to Sre1"" is ""decreased protein binding"" that is specific for decreased binding to the protein Sre1."
PMID:25778919	Fig 3
PMID:25778919	Fig 2 CD decreased telomere dispersion
PMID:25778919	Fig 2 D
PMID:25778919	fig 4
PMID:25778919	fig 4 decreased telomere dispersion
PMID:25778919	Fig. S4 A
PMID:25778919	Fig. 4 decreased telomere dispersion
PMID:25778919	Fig 3
PMID:25778919	Fig 3D
PMID:25778919	Fig. 5 A
PMID:25778919	Together, these experiments suggest that Aurora-dependent re- moval of Swi6/HP1 and consequently cohesin Rad21 from telo- meres in early mitosis contributes to telomere dispersion.
PMID:25778919	Together, these experiments suggest that Aurora-dependent re- moval of Swi6/HP1 and consequently cohesin Rad21 from telo- meres in early mitosis contributes to telomere dispersion.
PMID:25778919	fig 6
PMID:25778919	fig6
PMID:25778919	fig7
PMID:25778919	Fig 2 CD
PMID:25778919	Fig. S2 A, right
PMID:25778919	telomere disjunction
PMID:25778919	(Fig. 2 A, 0–3 min, arrows)
PMID:25778919	(requested negative regulation of) synonym mitotic telomere dispersion during metaphase
PMID:25793410	Sensitivity was rescued by 0.6 M KCl 4 mM lithium for 4 h followed by recovery on YES
PMID:25793410	10 ug/ml phleomycin for 4 h followed by recovery on YES
PMID:25793410	Sensitivity was rescued by 0.6 M KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES
PMID:25793410	Sensitivity was rescued by 0.6 M KCl but not 60 mM KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES
PMID:25793410	100 ug/ml G418 for 4 h followed by recovery on YES
PMID:25793410	Rad3-dependent phosphorylation of Chk1 is observed in the presence of phleomycin, but this is suppressed by KCl concentrations above 0.3 M
PMID:25793410	Sensitivity was rescued by 0.6 M KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES
PMID:25793410	Sensitivity was rescued by 150 mM, but not 70 mM KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES
PMID:25793410	Sensitivity was rescued by 0.6 M, but not 60 mM KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES
PMID:25793410	10 ug/ml G418 for 4 h followed by recovery on YES
PMID:25793410	Sensitivity was rescued less efficiently than for the wt by 150 - 600 mM KCl
PMID:25795664	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses csn1delta sensitivity to DNA damage agents
PMID:25795664	more than in csn1delta alone
PMID:25795664	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	same as brc1delta alone
PMID:25795664	same as brc1delta alone
PMID:25795664	same as brc1delta alone
PMID:25795664	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses csn1delta sensitivity to DNA damage agents
PMID:25795664	same as in csn1delta alone
PMID:25795664	A spd1 deletion partially suppresses the synthetic growth defect in a brc1 csn1 double mutant background
PMID:25795664	spd1 deletion suppresses csn1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	A spd1 deletion partially suppresses the synthetic growth defect in a brc1 ddb1 double mutant background
PMID:25795664	spd1 deletion suppresses csn1delta sensitivity to DNA damage agents
PMID:25798942	ATPase domain mutant phenotype fig 5 and S6
PMID:25803873	no peptidase activity acting on azocoll substrate in isp6 null
PMID:25837586	Not affected by short-term actin cytoskeleton depolymerization by Latrunculin A
PMID:25837586	more severe in presence of LatA
PMID:25837586	Increased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	Internally tagged functional allele, allowing live-imaging of Cdc42
PMID:25837586	Normal levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	Increased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	Normal levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	Decreased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	Decreased levels of Cdc42 and Cdc42-GTP
PMID:25847133	Cut14 accumulates at the mitotically-upregulated gene regions in mitosis. Cut14 enrichment requires a forkhead transcription factor Sep1.
PMID:25847133	Abnormally streaked chromosomes in anaphase
PMID:25847133	GO:0000087 = mitosis
PMID:25847133	This mutant protein decreased chromatin binding at heat-shock genes, ssa1+ and hsp90+
PMID:25847133	Cut14 accumulates at the mitotically-upregulated gene regions in mitosis. Cut14 enrichment requires a forkhead transcription factor Sep1.
PMID:25869666	Fig. 4
PMID:25869666	Fig. 4
PMID:25869666	Fig. 1
PMID:25869666	Fig. 1
PMID:25869666	Fig. 4
PMID:25869666	Fig. 1
PMID:25869666	Single deletion slows down nuclear congression (minus-end diretcted), double deletion with klp2 inhibits it.
PMID:25869666	Single deletion slows down nuclear congression (minus-end diretcted), double deletion with dhc1 inhibits it.
PMID:25869666	Fig. S3A
PMID:25869666	Fig. 1
PMID:25869666	Phenocopies dhc1
PMID:25869666	Fig. 1
PMID:25869666	Delayed nuclear congresion in klp2D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1))
PMID:25869666	Fig. 1
PMID:25869666	Delayed nuclear congresion in dhc1D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1))
PMID:25869666	Localization of GFP-tagged protein
PMID:25869666	Localization of GFP-tagged protein
PMID:25869666	Fig. 1
PMID:25869666	Fig. S1
PMID:25891897	zygotic / >80% of asci have 4 spores
PMID:25891897	zygotic/ random spore analysis
PMID:25891897	This phenotype is not seen when cells undergo azygotic meiosis
PMID:25891897	presence of more than 2 SPBs dots after meiotic nuclear divisions 19.6% zygotes exhibit abnormal meiotic division during zygotic meiosis
PMID:25891897	azygotic/ slight advance in the timing of MI and MII
PMID:25891897	zygotic meiosis random spore analysis,
PMID:25891897	zygotic meiosis random spore analysis
PMID:25891897	zygotic
PMID:25891897	zygotic
PMID:25891897	zygotic meiosis random spore analysis
PMID:25891897	zygotic random spore analysis
PMID:25891897	azygotic// presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication
PMID:25891897	zygotic meiosis random spore analysis,
PMID:25891897	azygotic
PMID:25891897	zygotic meiosis
PMID:25891897	azygotic/ slight advance in the timing of MI and MII
PMID:25891897	zygotic
PMID:25891897	azygotic meiotic cell cycle/timing of pre-meiotic DNA replication is normal
PMID:25891897	zygotic
PMID:25891897	zygotic
PMID:25891897	zygotic
PMID:25891897	zygotic
PMID:25891897	zygotic
PMID:25891897	azygotic meiotic cell cyle
PMID:25891897	zygotic
PMID:25891897	zygotic
PMID:25891897	zygotic meiosis random spore analysis
PMID:25891897	zygotic
PMID:25891897	zygotic//presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication
PMID:25891897	azygotic meiosis, rem1 and crs1 do not have a major role in azygotic meiosis
PMID:25891897	zygotic meiosis/ Random spore analysis
PMID:25959226	However, contractile ring assembly was significantly faster in mid13A than in mid1+ cells (Figure S6, C–F),
PMID:25959226	In contrast, monomerization only slightly reduced the affinity to PS.
PMID:25959226	which interacts with the N-terminus of Mid1 and stabilizes Mid1 at the division plane (Ye et al., 2012; Zhu et al., 2013). As expected, mid13A gef2Δ double mutants had strong synthetic defects in division-plane placement and septum formation at 36°C (Figure 6, F–H).
PMID:25959226	which interacts with the N-terminus of Mid1 and stabilizes Mid1 at the division plane (Ye et al., 2012; Zhu et al., 2013). As expected, mid13A gef2Δ double mutants had strong synthetic defects in division-plane placement and septum formation at 36°C (Figure 6, F–H).
PMID:25959226	Mutations of the hydrophobic C2-C2 interface shifted Mid1 into monomeric state (Figure 6A),
PMID:25959226	which showed > 10-fold lower affinity to PI(4,5)P2 (Figure 3D).
PMID:25959226	Indeed, the morphology and positioning of the contractile ring marked with myosin regulatory light chain Rlc1 were normal in mid13A cells (Figure S6, C-D)
PMID:25959226	Interestingly, it binds to PI(4,5)P2 strongly, with a Kd up to 0.12 μM (Figure 3C and 3D).
PMID:25959226	In contrast, the monomeric Mid13A remained concentrated in the nucleus and its signals on the plasma membrane were more widespread, even reached the cell poles (Figure 6E
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as either single mutant
PMID:25965521	same as either single mutant
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as mus81delta alone; mus81 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25965521	same as brc1delta alone; brc1 epistatic
PMID:25977474	abnormal cleavage furrow disc formation fig 3
PMID:25977474	abnormal cleavage furrow disc formation fig 3
PMID:25977474	abnormal cleavage furrow disc formation fig 3
PMID:25977474	abnormal cleavage furrow disc formation fig 3
PMID:25977474	abnormal cleavage furrow disc formation fig 3
PMID:25987607	I want to represent the microtubule based-transporter function and cargo
PMID:25987607	non additive
PMID:25987607	I think the pkl rigor is spb tethered here?
PMID:25987607	during mitotic M phase
PMID:25987607	during mitotic M phase
PMID:25987607	Fig. 5 B and Videos 1–4
PMID:25987607	during mitotic M phase
PMID:25987607	Fig. 5 B and Videos 1–4
PMID:25987607	Fig. 5 B and Videos 1–4
PMID:25987607	Fig. 5 B and Videos 1–4
PMID:25987607	I want to represent the microtubule based-transporter function and cargo
PMID:25993311	table2
PMID:25993311	table 1
PMID:25993311	table 1
PMID:25993311	table 1
PMID:25993311	table 1
PMID:25993311	table 2
PMID:25993311	table 2
PMID:25993311	table2
PMID:25993311	table2
PMID:25993311	table2
PMID:25993311	table2
PMID:25993311	table2
PMID:25993311	table2
PMID:25993311	table 1
PMID:25993311	table 1
PMID:25993311	table 2
PMID:25993311	Table S3
PMID:25993311	Table S3
PMID:25993311	Table S3
PMID:25993311	Table S3
PMID:25993311	fig 2 a
PMID:25993311	fig2
PMID:25993311	fig2
PMID:25993311	fig 2 a
PMID:25993311	fig 2 a
PMID:25993311	table 3
PMID:25993311	table 3
PMID:25993311	table 3
PMID:25993311	fig 3
PMID:25993311	fig 3
PMID:25993311	fig 3
PMID:25993311	fig 3
PMID:26007660	https://github.com/geneontology/go-ontology/issues/12379 I submitted an EC NTR
PMID:26031557	Fig. 3
PMID:26031557	Fig. 1. I guess reporter gene assay is the right category, since they do this with the minichrosome bearing the ade6 gene from cerevisiae to rescue ade6-M210
PMID:26031557	Fig. 2. I guess reporter gene assay is the right category, since they do this with the minichrosome bearing the ade6 gene from cerevisiae to rescue ade6-M210
PMID:26031557	Fig. 2
PMID:26031557	Fig. S2 Pkl1md-GFP localized primarily to the spindle poles
PMID:26031557	Fig. S2 In contrast, in pkl1D msd1D cells, Pkl1md-GFP localized primarily to the spindle and only partially rescued the protrusion phenotype
PMID:26031557	Fig. S2 Pkl1md-GFP localized primarily to the spindle poles and almost completely rescued the protrusion phenotype
PMID:26031557	Fig. 3 MT buckling during prolonged contact with the cell tip cortex—its associated chromosome mass to the medial cell division site (Fig. 3c). Subsequent cytokinesis appeared to cut through the chromosome mass, resulting in aneuploidy in 12% of mitotic cells.
PMID:26031557	Fig. 4
PMID:26031557	Fig. S4
PMID:26031557	Fig. 3 This is important as it indicates that the delay in pkl1D is likely not due to a delay in chromosome capture, but rather spindle formation in prophase.
PMID:26031557	Fig. 2. It's only a bit worse (+3% chromosome loss). Not sure if worth including
PMID:26088418	increased length hererogeneity*****************. Indeed, yeast cells expressing the L431R and L445R mutants exhibited significant loss of function in telomere length regulation and showed long and highly heterogenous telomeres that were as severe as that in taz1Δ cells (Figure 1K)
PMID:26088418	Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown).
PMID:26088418	Both mutant proteins were expressed at near wild-type levels, suggesting that these acidic residues are not required for protein stability (data not shown).
PMID:26088418	Both mutant proteins were expressed at near wild-type levels, suggesting that these acidic residues are not required for protein stability (data not shown).
PMID:26088418	increased length hererogeneity
PMID:26088418	increased length hererogeneity. taz1-4A cells still exhibited extremely heterogeneous telomeres similar to taz1Δ and taz1-4R cells (Figure 1E).
PMID:26088418	increased length hererogeneity
PMID:26088418	While wild-type Taz1 bound to DNA with an equilibrium dissociation constant (Kd) of ~600 nM (Figure 1I), the L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is required for its efficient association with the telomeric DNA in vitro.
PMID:26088418	he L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is
PMID:26088418	Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown).
PMID:26088418	increased length hererogeneity*****************. Indeed, yeast cells expressing the L431R and L445R mutants exhibited significant loss of function in telomere length regulation and showed long and highly heterogenous telomeres that were as severe as that in taz1Δ cells (Figure 1K)
PMID:26092938	decreased local concentration of the myosin-II
PMID:26092938	increased local concentration of the myosin-II
PMID:26092938	localization of the myosin-II is abolished
PMID:26092938	large portion of the mutant forms cytoplasmic dots
PMID:26092938	decreased local concentration of the myosin-II
PMID:26098872	figure 8a
PMID:26098872	figure 8a
PMID:26098872	figure 8a
PMID:26098872	figure 8c
PMID:26098872	figure 8 b
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26108447	Figure 6
PMID:26122634	polysomal profiling
PMID:26122634	polysomal profiling
PMID:26124291	Fig 7 E/F
PMID:26124291	Fig 7 E
PMID:26124291	Fig Fig. S5 E
PMID:26124291	FFig. S5 E
PMID:26124291	Fig 7 CD abnormal Q-MT bundle elongation upon G1 re-entry/interphase bundle reassembly
PMID:26124291	Fig S5A C
PMID:26124291	Fig 6 C
PMID:26124291	Fig 6 C
PMID:26124291	(Fig. 4 C)
PMID:26124291	(Fig. 4 C)
PMID:26124291	(Fig. 4 C)
PMID:26124291	(Fig. 4 C)
PMID:26124291	(Fig. 4 C)
PMID:26124291	(Fig. 4 C)
PMID:26131711	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone
PMID:26131711	modified forms of Cdc2 present differ from wild type
PMID:26131711	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone
PMID:26131711	modified forms of Cdc2 differ from both wild type and cdc2-1w alone
PMID:26131711	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26132084	figure 1c
PMID:26132084	Fig 2D and 2E
PMID:26132084	figure 4B
PMID:26132084	figure 1 A,B
PMID:26132084	fig 3C&D vw: changed to incomplete septum
PMID:26132084	fig 5 SH3 domain of Cdc15 is required for the proper concentration of Pxl1 at the CAR
PMID:26132084	fig6
PMID:26132084	fig6 Coupling of the Actomyosin ring contraction and septation onsetRing sliding even after the onset of septum synthesis, causing a longitudinal deposition along the plasma membrane of linear β-glucan as detected by CW staining until septum ingression started
PMID:26132084	figure 1
PMID:26132084	Fig 2A and B fragmented with RLC strands
PMID:26132084	P.P. Bgs4 and Ags1 abnormal localization in the septum membrane
PMID:26132084	P.P. Bgs4 and Ags1 abnormal localization in the septum membrane
PMID:26132084	figure 3
PMID:26132084	fig 3C
PMID:26132084	fig 4C
PMID:26137436	table 1
PMID:26137436	we failed to detect a band corresponding to the full-length Nup189 fused with GFP (Nup98–Nup96–GFP), indicating that autocleavage occurs with no remains of the joint molecule. The same bands corresponding to Nup98 and Nup96-GFP were also detected in the splicing-defective mutant, as expected (Fig. 2B and C,
PMID:26150232	of cell tip
PMID:26152587	Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation
PMID:26152587	Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation
PMID:26152587	1h in proline medium
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	1h in proline medium, a mild phenotype
PMID:26152587	1h in proline medium, a mild phenotype
PMID:26152587	1h in proline medium, a mild phenotype
PMID:26152587	a mild phenotype
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	fig1a
PMID:26152587	Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation
PMID:26152587	a mild phenotype
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	assayed by nuclear localization of Gaf1-GFP
PMID:26160178	affecting binding to histone H2A (hta1)
PMID:26160178	affecting binding to Mdb1
PMID:26221037	modification(s) not identified
PMID:26221037	higher than without nup132d
PMID:26221037	higher than without nup132d
PMID:26221037	modification(s) not identified
PMID:26258632	fig1a
PMID:26258632	fig1a
PMID:26258632	fig1e
PMID:26258632	fig 3 b
PMID:26258632	fig2d
PMID:26258632	Fig. 2b (mad1 locaizes to unattached kinetochores) and fig 3a
PMID:26258632	fig 5 c
PMID:26258632	fig2a (diminished relocation from kinetochore)
PMID:26258632	kinetochore localization of Cut7 is unaffected
PMID:26258632	fig1b
PMID:26258632	fig1b
PMID:26258632	fig1b
PMID:26258632	fig1b
PMID:26258632	fig1a
PMID:26258632	fig1a
PMID:26258632	fig1a
PMID:26258632	fig1a
PMID:26258632	fig1e
PMID:26258632	"fig 5c ""gliding"" new GO term requested"
PMID:26258632	ABOLISHED tetermerization fig4f monomer
PMID:26258632	ABOLISHED tetermerization
PMID:26258632	fig 3c
PMID:26258632	fig 3 a/b
PMID:26258632	fig 3 a/b
PMID:26258632	fig2a
PMID:26258632	fig2a
PMID:26258632	figure 2a (GO:0000090= mitotic anaphase)
PMID:26258632	figure 2a GO:0000236=mitotic prometaphase
PMID:26258632	fig2d GO:0000089= mitotic metaphase unattached kinetohore nda3-KM311 arrested cell
PMID:26258632	fig 3 a/b
PMID:26275423	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	Chromatin immunoprecipitation of this protein is highly enriched in centromeric DNA
PMID:26275423	Chromatin immunoprecipitation of this protein is highly enriched in centromeric DNA
PMID:26275423	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26365378	Indirect evidence, could be upstream
PMID:26365378	Indirect evidence, could be upstream
PMID:26365378	Indirect evidence, could be upstream
PMID:26365378	4h
PMID:26365378	macroautophagy? - selective autophagy is a child of macroautophagy
PMID:26365378	s3
PMID:26365378	s3
PMID:26365378	"microscopy shows ""protein localization to vacuole with protein mislocalized to cytosol"" but with additional vacuolar processing phenotypes I think we can make the BP phenotypes /AL"
PMID:26366556	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	low penetrance
PMID:26366556	low penetrance
PMID:26366556	large fractions of both abnormally long and abnormally short cells are present in the population
PMID:26366556	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	determined by EMSA. Substrate: dsDNA oligonucleotide derived from promoters of cut6 and ptl1 genes (contain the CSL_response_element)
PMID:26366556	ChIP-seq and microarray data indicate that Cbf11 regulates lipid metabolism genes.
PMID:26366556	low penetrance
PMID:26368543	Chk1
PMID:26368543	Chk1
PMID:26401015	abolishes preference for K4-trimethylated H3
PMID:26401015	acetyltransferase normally processive in presence of K4-trimethylated H3 (bound by Sgf29)
PMID:26401015	abolishes preference for K4-trimethylated H3
PMID:26401015	acetyltransferase normally processive in presence of K4-trimethylated H3 (bound by Sgf29)
PMID:26412298	Inferred from in vitro biochemical assay using K63-linked di-ubiquitin
PMID:26412298	Inferred from in vitro biochemical assay using K48-linked di-ubiquitin
PMID:26412298	Inferred from in vitro biochemical assay using K48-linked di-ubiquitin
PMID:26412298	Inferred from in vitro biochemical assay using K63-linked di-ubiquitinase (vw JAnel made this annotation , I transferred from process to MF)
PMID:26412298	Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate
PMID:26412298	Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate
PMID:26412298	Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate
PMID:26412298	Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate
PMID:26412298	Inferred from in vitro biochemical assay using K63-linked di-ubiquitin
PMID:26412298	Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate
PMID:26422458	Biochemical and mutagenic studies demonstrated that the [2Fe-2S]2+ cluster substantially inhibits the phosphatase activity of Asp1, thereby increasing its net kinase activity.
PMID:26424849	waiting for go-ontology/issues/12536
PMID:26424849	in response to queuosine incorporation into tRNA-Asp
PMID:26436826	alkaline DNA preparation
PMID:26436826	alkaline DNA preparation
PMID:26438724	fig6
PMID:26438724	changed from: heterochromatin organization involved in chromatin silencing
PMID:26438724	supp 1b
PMID:26438724	supp 1b
PMID:26438724	supp 1b
PMID:26438724	supp 1b
PMID:26438724	EV3
PMID:26438724	EV3
PMID:26438724	EV3
PMID:26438724	4a
PMID:26438724	4a
PMID:26438724	4a
PMID:26438724	EV3
PMID:26438724	EV3
PMID:26438724	fig5
PMID:26438724	fig5
PMID:26438724	fig5
PMID:26438724	fig5
PMID:26438724	fig5
PMID:26438724	fig5
PMID:26438724	fig6
PMID:26438724	EV3
PMID:26438724	EV3
PMID:26438724	changed from: heterochromatin organization involved in chromatin silencing
PMID:26443059	actually inferred from protein binding phenotypes
PMID:26443059	actually inferred from protein binding phenotypes
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Pom1 relocalization to cell sides
PMID:26443240	Pom1 relocalizes to cell sides
PMID:26443240	Pom1 relocalizes to cell sides
PMID:26443240	Pom1 relocalizes to cell sides
PMID:26443240	Pom1 relocalizes to cell sides
PMID:26443240	absent when glucose limited
PMID:26443240	Pom1 does not relocalize to cell sides
PMID:26443240	Tea4 does not relocalize to cell sides
PMID:26443240	through negative regulation of Cls1
PMID:26443240	Pom1 relocalizes to cell sides
PMID:26483559	Fig. 3, A and B; Fig. S5
PMID:26483559	Fig 2
PMID:26483559	(Fig. 6) increased or premature
PMID:26483559	fig1b (vw moved down form) abnormal meiotic chromosome segregation
PMID:26483559	(Fig. 6) increased or premature
PMID:26483559	(Fig. 8, B and C), increased or premature
PMID:26483559	(Fig. 1 B)
PMID:26483559	fig 9a, there other evidence elsewhere but we don't have this annotation on mad2 at present...
PMID:26483559	fig 9A
PMID:26483559	fig 9A
PMID:26483559	fig 9A
PMID:26483559	fig 9A
PMID:26483559	fig 9A
PMID:26483559	fig 9A
PMID:26483559	fig 9A
PMID:26483559	(Fig. 7 C)
PMID:26483559	(Fig. 7, B and C)
PMID:26483559	Fig S1. Assayed by assaying depletion of securin from spindle
PMID:26483559	(Fig. 1 D)
PMID:26483559	(Fig. 1 D)
PMID:26483559	Fig. S2
PMID:26483559	(Fig. 1 B)
PMID:26483559	(Fig. 4, C and D)
PMID:26499799	cerevisiae substrate
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 4)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5) (VW: fixed from normal to decreased -compared to WT)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	ev4,ef
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	(Figure 7)
PMID:26518661	ev4
PMID:26518661	ev4
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 5)
PMID:26518661	(Figure 1)
PMID:26518661	(Figure 1)
PMID:26518661	(Figure 1)
PMID:26518661	(Figure 1)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26518661	(Figure 2)
PMID:26527280	Fig. 1J
PMID:26527280	Fig. 3A/B
PMID:26527280	Fig. 3E/F
PMID:26527280	Fig. 5C
PMID:26527280	Fig. 4D,E
PMID:26527280	Fig. 6G, S7F,G, TUBE pull-down
PMID:26527280	Fig. 7D,E (tetrad dissection)
PMID:26527280	(tetrad disection) Fig. 7D,E
PMID:26527280	(tetrad dioscection) Fig. 7C,E
PMID:26527280	Fig. S2B
PMID:26527280	Fig. S3A,B (control for increased proteasome in nucleus)
PMID:26527280	Fig. S3A,C
PMID:26527280	Fig. S3D
PMID:26527280	Fig. S3G,H
PMID:26527280	Fig. S3I,J
PMID:26527280	Fig. S6D
PMID:26527280	Fig. S6L,M
PMID:26527280	Fig. 4G,H
PMID:26527280	(Figure S2F export of CDK1 from the nucleus, which depends on cyclin B degradation ,, was delayed
PMID:26527280	(Figures 3B and 3D). sister chromatid separation (which depends on securin degradation, not on cyclin B degradation) was delayed as well
PMID:26527280	chromosomes failed to split, but Plo1 was removed from SPBs with timing similar to that in wild-type cells (Figures 2A and 2C).
PMID:26527280	chromosomes failed to split, but Plo1 was removed from SPBs with timing similar to that in wild-type cells (Figures 2A and 2C).
PMID:26527280	In contrast, there was only a very slight delay in sister chromatid separation (Figures 2A and 2B).
PMID:26527280	Figure 2A Plo1 to SPBs persisted for more than 20 min
PMID:26527280	Fig. 1I
PMID:26536126	inability to take up 14-C uracil in fur4 deletion mutant
PMID:26536126	grown in EMM or YES medium
PMID:26536126	nitrogen rich condition
PMID:26536126	nitrogen rich condition
PMID:26536126	uracil uptake enhancement in pub1 deletion
PMID:26536126	cell lysis on uracil depleted medium
PMID:26536126	auxotrophic for cytosine, uridine and UMP
PMID:26536126	assayed_using(PomBase:fur4)
PMID:26545917	2c
PMID:26545917	they don't actually use pombe isu1 because they couldn't purify it, but they try both C. thermophilum and S. cerevisiae Isu1 and get similar results & sequence conservation is good to pombe.
PMID:26545917	they don't actually use pombe isu1 because they couldn't purify it, but they try both C. thermophilum and S. cerevisiae Isu1 and get similar results & sequence conservation is good to pombe.
PMID:26582768	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26582768	Increased MMS sensitivity
PMID:26582768	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26582768	Increased MMS sensitivity
PMID:26582768	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26582768	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26652183	2 or 5 J/m2 UV; Fig. 3F, Fig. S6
PMID:26652183	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	5 J/m2 UV; Fig. 3C
PMID:26652183	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	5 J/m2 UV; Fig. 1B, Fig. 3E
PMID:26652183	5 J/m2 UV; Fig. 1B
PMID:26652183	5 J/m2 UV; Fig 1A, Fig. S2
PMID:26652183	5 J/m2 UV; figure 1B, figure 3D, figure S6
PMID:26652183	5 J/m2 UV; duration is similar to eso1-D147N alone (see Fig. 3H)
PMID:26652183	5 J/m2 UV; duration is similar to rad8delta or rhp18delta single mutants (see Fig. 3G)
PMID:26652183	5 J/m2 UV; Delay is greater than rad51delta alone (see Fig. S7)
PMID:26652183	25 J/m2 UV; delay is greater than rad51delta alone (Fig. 5A)
PMID:26652183	5 or 10 J/m2 UV; similar sensitivity to rev1delta and rev3delta single mutants (Fig. 3I, Fig. 4A, Fig. S6)
PMID:26652183	5 J/m2 UV; similar sensitivity to eso1-D147N single mutant (Fig. 3H)
PMID:26652183	5 J/m2 UV; Fig. S3
PMID:26652183	5 J/m2 UV; sensitivity similar to rad8delta and rhp18delta single mutants (Fig. 3G)
PMID:26652183	5 J/m2 UV; Sensitivity is greater than rad51delta or eso1-D147N single mutants (see Fig. S7)
PMID:26652183	2 or 5 J/m2 UV; Fig. 3F, Fig. S6
PMID:26652183	5 J/m2 UV; Fig. 3C
PMID:26652183	5 J/m2 UV; Fig. 3B
PMID:26652183	5 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	5 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	5 J/m2 UV; Fig. 3E
PMID:26652183	5 J/m2 UV; Fig. 3D
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	increase > 5-fold
PMID:26670050	fig S5e
PMID:26670050	Fig. S4B
PMID:26670050	gene affected: rps2202
PMID:26670050	gene locus affected: dbp2
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 40-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	SPBC1289.13c
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold; Mmi1 binds the 5' extended region of the overlapping regulatory lncRNA prt
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	SPCC1235.04c
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 5-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 10-fold
PMID:26670050	increase > 50-fold
PMID:26670050	gene locus affected: rps2202
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	gene locus: rps2202
PMID:26670050	affects unspliced pre-mRNA
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26670050	enrichment in CRAC > 10-fold
PMID:26687354	(Figure 6C) acetylated form acts as a DNA sensor
PMID:26687354	(Figure 6B) acetylated form acts as a DNA sensor
PMID:26687354	(Figure 6A)
PMID:26687354	(Figure 6A)
PMID:26687354	(Figure S4C)
PMID:26687354	exit gate opening https://github.com/geneontology/go-ontology/issues/12608 (checked) (Figures 4B and S4A) current extension is part of mitotic cohesin unloading
PMID:26687354	figure 3B
PMID:26687354	(checked) figure 3B
PMID:26687354	(Figure 2B)
PMID:26687354	(Figure 6C)
PMID:26687354	(Checked) (Figure 2B) (dependent on pds5)
PMID:26687354	(fig 2)
PMID:26687354	(fig 2)
PMID:26687354	(checked) Figure 1C
PMID:26687354	(checked) Figure 1C
PMID:26687354	figure 3B
PMID:26687354	figure 3B
PMID:26687354	(checked) figure 3B
PMID:26697368	link to GEO dataset- GSE71820
PMID:26697368	link to GEO dataset- GSE71820
PMID:26702831	2c in cos7
PMID:26730850	Figure 1C transient
PMID:26730850	Figure 1D and 2D - examined via RT-PCR Figure 2A examined via RNA-Seq
PMID:26730850	Fig 4
PMID:26730850	Fig3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 4
PMID:26730850	Fig 4
PMID:26730850	Fig 4
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Fig 5
PMID:26730850	Figure 1D
PMID:26730850	(S1 Fig)
PMID:26730850	regulation of efficiency at weak donor
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 3
PMID:26730850	Fig 4
PMID:26730850	Fig 4
PMID:26730850	Fig 4
PMID:26730850	Fig 4
PMID:26730850	Figure 1D
PMID:26730850	Figure 4 efficiency of introns displaying weak splice sites
PMID:26730850	Figure 3+5 efficiency/ of introns displaying weak splice sites
PMID:26730850	Figure 1A-1C transient growth arrest
PMID:26730850	Figure 1D efficiency/ of introns displaying weak splice sites
PMID:26730850	Figure 1D efficiency/ of introns displaying weak splice sites
PMID:26744419	Fig 4 b & c
PMID:26744419	fig 5c
PMID:26744419	fig 1c
PMID:26744419	5
PMID:26744419	5
PMID:26744419	4e
PMID:26744419	4e
PMID:26744419	4e
PMID:26744419	fig 4
PMID:26744419	fig 4
PMID:26744419	fig 3d
PMID:26744419	fig 3c
PMID:26744419	fig 3c
PMID:26744419	3b
PMID:26744419	3b
PMID:26744419	3b
PMID:26744419	3b
PMID:26744419	s5a
PMID:26744419	fig 3
PMID:26744419	fig 3
PMID:26744419	fig 3
PMID:26744419	fig 3
PMID:26744419	fig 3
PMID:26744419	fig 3
PMID:26744419	fig 3
PMID:26744419	s2
PMID:26744419	s2
PMID:26744419	s2
PMID:26744419	fig 1c
PMID:26744419	fig S2
PMID:26744419	fig S2
PMID:26744419	fig S2
PMID:26744419	S4
PMID:26744419	1d
PMID:26744419	fig 1b
PMID:26744419	1d
PMID:26744419	1d
PMID:26744419	1d
PMID:26744419	fig S2
PMID:26744419	fig S2
PMID:26744419	fig 1c
PMID:26744419	Fig 5b
PMID:26744419	Fig 5b
PMID:26744419	Fig 5b
PMID:26744419	Fig 5b
PMID:26744419	fig 5c
PMID:26744419	Fig 7b
PMID:26744419	fig 1b
PMID:26744419	fig S1c
PMID:26744419	Fig 7b
PMID:26744419	fig 6a (in combination with csi1∆; phenocopies lem2∆ csi1∆)
PMID:26744419	fig 3c
PMID:26744419	fig 6e
PMID:26744419	fig 6e
PMID:26744419	fig 6d
PMID:26744419	fig 6d
PMID:26744419	fig 6d
PMID:26744419	fig 6e
PMID:26744419	fig 6c
PMID:26744419	fig 6c
PMID:26744419	fig 6e
PMID:26744419	fig 6d
PMID:26744419	fig 1c
PMID:26744419	fig 1c
PMID:26744419	Fig 1c SHOULD BRE ORGANIZATION
PMID:26744419	pericentric Fig 1c, In conclusion, while other tethering mechanisms in S. pombe could be functionally coupled to heterochroma- tin, the LEM-mediated centromere recruitment and the MSC-dependent silencing are independent mechanisms, although they are mediated by the same protein.
PMID:26744419	Fig 1c,Fig 4e
PMID:26744419	Fig 5c
PMID:26744419	Fig 5c. parent GO:0003682?
PMID:26744419	Fig 5c. parent GO:0003682?
PMID:26744419	fig 1c
PMID:26744419	s10
PMID:26744419	fig 1c
PMID:26744419	s10
PMID:26744419	s10
PMID:26744419	7
PMID:26744419	fig 7
PMID:26744419	7
PMID:26744419	7
PMID:26744419	7
PMID:26744419	fig 7
PMID:26744419	fig 7
PMID:26744419	fig 7
PMID:26744419	fig 7
PMID:26744419	Fig 7b
PMID:26744419	Fig 7b
PMID:26744419	Fig 7b
PMID:26744419	Fig 7b
PMID:26746798	fig 2 C
PMID:26746798	fig 2 C
PMID:26746798	fig 2 B
PMID:26746798	fig 2 B
PMID:26746798	fig 1 A
PMID:26746798	fig 2 A
PMID:26746798	fig 2 A
PMID:26746798	fig 2 A
PMID:26746798	fig 2 B
PMID:26746798	fig 3C
PMID:26746798	fig 3C
PMID:26746798	fig 3C
PMID:26746798	Fig 7B
PMID:26746798	Fig 7A
PMID:26746798	fig 6
PMID:26746798	fig 6
PMID:26746798	fig 6
PMID:26746798	fig 6
PMID:26746798	fig 3B
PMID:26746798	fig 1 A
PMID:26746798	fig 1 A
PMID:26746798	fig 1 A
PMID:26746798	fig 1 A
PMID:26746798	Fig 7B
PMID:26746798	fig 3B
PMID:26746798	fig 3B
PMID:26746798	fig 3A
PMID:26746798	fig 3A
PMID:26746798	fig 3A
PMID:26746798	fig 2 C
PMID:26746798	fig 1 A Defect in Checkpoint Signaling.
PMID:26746798	fig 2 C
PMID:26746798	fig 3C
PMID:26746798	fig 1 A
PMID:26746798	fig 1 A
PMID:26746798	fig 1 A
PMID:26746798	fig 2 C
PMID:26749213	(Supporting Information Fig. S4A)
PMID:26749213	(Fig. 6D); evidence: filipin staining
PMID:26749213	moved down from abnormal protein localization to cell tip (new term)
PMID:26749213	(Fig. 3B–D) (Fig. 4A and movies 3 and 4) slow dynamics of actin patch components: Sla1, wsc1, arc5, Crn1
PMID:26749213	moved down to new term from :protein mislocalized to cytoplasm during vegetative growth
PMID:26749213	moved down to new term from :protein mislocalized to cytoplasm during vegetative growth
PMID:26749213	figure 1a
PMID:26749213	figure 1a
PMID:26749213	figure 1a
PMID:26749213	fig 1B
PMID:26749213	fig 1B
PMID:26749213	fig 1B
PMID:26749213	fig 1B
PMID:26749213	fig 1B
PMID:26749213	fig 1B
PMID:26749213	fig. S2 A&B
PMID:26749213	Fig. S2C
PMID:26749213	fig 1c
PMID:26749213	fig 7b
PMID:26749213	fig 2 d
PMID:26749213	fig 2 D
PMID:26749213	moved down drom endocytosis. Delayed FM4-64 uptake when in combination with a clathrin mutationSlow dynamics of endocytic patch markers
PMID:26749213	FM4-64 uptake (I made Henars original annotation into a double mutant so the attribution has changed)
PMID:26776736	important when growing on poor nitrogen sources
PMID:26776736	MOVE EXTENSION DOWN TO NITROGEN This can be inferred from all of the proposed EXP and is part of the proposed model, we can delete if we can make in a better way
PMID:26776736	again confirms other systems Endosulfines are small phosphoproteins, highly conserved from yeasts to humans, that specifically bind to and inhibit the PP2A$B55 protein phosphatase subcomplex [8, 9]. PP2A$B55 has been shown to be cell-cycle-regulated in Xenopus, following the opposite pattern of activity to Cdk1$Cyclin B (high in inter- phase and low in mitosis) [15]. To determine whether Ser64-phosphorylated Igo1 inhibits the PP2A$B55 (PP2A$Pab1 in fission yeast) phosphatase activity, we purified PP2A$Pab1 phosphatase from cells expressing GST- Pab1 using glutathione sepharose beads and assayed them for phosphatase activity. Wild-type Igo1 thiophosphorylated in vitro at Ser64 by Xenopus Greatwall, but not Igo1-S64A, in- hibited more than 90% the phosphatase activity of PP2A$Pab1 (B55) (Figures S4B and S4C). This result indicates that Ser64- phosphorylated Igo1 inhibits the activity of PP2A$B55, analogous to the situation in budding yeast [27, 28, 35] and animal cells [8, 9].
PMID:26776736	we need to give this a signal treansduction parentage positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation
PMID:26776736	vw, changed to directly activates and added part_of Phosphorylation of Igo1 was severely impaired in cells deleted for ppk18 or expressing a kinase-dead version of ppk18 (ppk18- K595A or ppk18-KD) but was still present in cek1-deleted cells (Figure 4B), consistent with the idea that Ppk18 is the main greatwall kinase that phosphorylates Igo1 in medium with low nitrogen. They are deomstrating that the system is conserved...In Xenopus and mammalian cells, phosphorylation of ENSA by greatwall at serine 67 promotes its binding to and inhibition of PP2A$B55 phosphatase [8, 9]. enough evidence for function by IMP ALSO Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as sub- strates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in or- der to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as sub- strates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in or- der to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as sub- strates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in or- der to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A (Figure S4A), indicating that fission yeast Ppk18 can act as a greatwall kinase.
PMID:26804021	fig 3 B
PMID:26804021	fig 1a. AND fig 4 (knob)
PMID:26804021	fig 4c
PMID:26804021	fig 5
PMID:26804021	fig 5
PMID:26804021	Fig. 7b increased occurance
PMID:26804021	Fig. 7a
PMID:26804021	fig 5
PMID:26804021	fig 5
PMID:26804021	fig 5
PMID:26804021	fig 5
PMID:26804021	fig 5A
PMID:26804021	fig 5A
PMID:26804021	fig 5 C
PMID:26804021	fig 5A
PMID:26804021	fig 4c
PMID:26804021	fig 4
PMID:26804021	fig 3 B
PMID:26804021	fig 3 B
PMID:26804021	fig S6 check allele????
PMID:26804021	fig 3 D
PMID:26804021	fig 1a
PMID:26804917	Serine 481 is phosphorylated by Cig2/Cdc2 during meiosis I. Phosphorylation decreases Fkh2 DNA binding affinity
PMID:26804917	EMSA fig4
PMID:26804917	EMSA fig4
PMID:2682257	Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Data not shown assayed by colony growth on plates
PMID:2682257	Fig6a B. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Fig6bB. Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Fig6aC. Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Figs 1, 2, 3, 4,5 cells blocked in late G2 and in mid mitosis . I have used the term MOD00048 as I'm told that tyrosine phosphorylation is always 04' but in the paper they just show that the Y15 residue is phosphorylated
PMID:2682257	Fig 6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	Figs 1, 2, 3, 4,5 cells blocked in late G2 and in mid mitosis . I have used the term MOD00048 as I'm told that tyrosine phosphorylation is always 04' but in the paper they just show that the Y15 residue is phosphorylated
PMID:26869222	This is in presence of 30µM Cutin-1 for 6 hours. Wild type cells show 36.3% abnormal chromosome segregation in same conditions
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	Cells grown at 29°C
PMID:26869222	cells grown at 29°C
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	Cells show partial resistance to 30µM Cutin-1 for 6 hours.
PMID:26869222	growth in presence of 10-100µM Cutin-1 for 15 hours at 100µM Cutin-1 reduced to 70% compared to ~10% in wild type; assayed in presence of 30µM Cutin-1 for 6 hours shows no chromosome defects or cell length defects
PMID:26869222	+10µM Cutin-1
PMID:26869222	assayed in presence of 30µM Cutin-1 for 6 hours shows no chromosome defects or cell length defects growth in presence of 10-100µM Cutin-1 for 15 hours at 100µM Cutin-1 reduced to 70% compared to ~10% in wild type
PMID:26869222	Growth was assayed in presence of 10µM Cutin-1.
PMID:26869222	This is in presence of 30µM Cutin-1 for 6 hours. Wild type cells show 36.3% abnormal chromosome segregation in same conditions
PMID:26869222	The size of the nucleus is not actually abnormal, it is the right size for the cell size but is variable because of the variable cell size at division
PMID:26869222	the resistance to Cutin-1 is dependent on nuclear size. Longer cells have a larger nucleus and are more resistant compared to smaller cells with a smaller nucleus
PMID:26869222	Cells show increased mitotic chromosome segregation defects in presence of Cutin-1
PMID:26869222	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26877082	Figure Figure S4C
PMID:26877082	Figures 1A, S1A, S1B, 1D, S1E medial ring assembly
PMID:26877082	Figures 1A, S1A, S1B, 1D, S1E
PMID:26877082	Figures 2
PMID:26877082	Figures 2C
PMID:26877082	Figure 2D (single clump!) condensation
PMID:26877082	Figure 2D abnormal cable clusering
PMID:26877082	Figure 4A
PMID:26877082	Figure 2D (single clump!) condensation
PMID:26882497	1d
PMID:26882497	4a
PMID:26882497	2bc,5
PMID:26882497	4a
PMID:26882497	5a
PMID:26882497	5a
PMID:26882497	5a
PMID:26882497	5a
PMID:26882497	Fig S4A and 2C
PMID:26882497	it looks like it is involved in MAINTAINING the checkpoint, fig S4A and 2C
PMID:26882497	text to fig2
PMID:26882497	text to fig2
PMID:26882497	2b
PMID:26882497	2b
PMID:26882497	2bc
PMID:26882497	2bc,5
PMID:26882497	2bc
PMID:26882497	3 E2s mixed in the same assay so can't specify a substrate
PMID:26882497	2bc,5
PMID:26882497	in text relevant to fig1
PMID:26882497	in text relevant to fig1
PMID:26882497	in text relevant to fig1
PMID:26882497	in text relevant to fig1
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	1b
PMID:26882497	Fig6 they incubate with 3 different E2s so can't specify a substrate
PMID:26882497	2bc,5
PMID:26882497	5a
PMID:26882497	5a
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	1b
PMID:26882497	1a - they don't really show that the modification is phosphorylation, but considering the rest of the data this annotation seems ok.
PMID:26882497	Fig S4A and 2C
PMID:26882497	1d
PMID:26882497	1d
PMID:26882497	2a 20 mins after synchronized released into mitosis. I wouldn't want to guess exactly what stage of mitosis this is
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	S3
PMID:26882497	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	S3
PMID:26882497	S3
PMID:26882497	S3
PMID:26890608	cellular response to HU = GO:0072711
PMID:26891792	Fig. 5
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 1
PMID:26891792	Fig. 3
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 4
PMID:26891792	Fig. 5
PMID:26891792	Fig. 5
PMID:26891792	Fig. 4
PMID:26891792	Fig. 5
PMID:26891792	Fig. 5
PMID:26900649	"chromatin recruiter Together, we concluded that the primary defects observed in the ndc80-AK01 mutant can be attributed to impaired Mph1 recruitment to kinetochores, which leads to failure in recruitment of the other SAC components and abortive mitotic arrest. COUld also get 'upstream of/affects SAC"""
PMID:26912660	exists during veg growth & glucose starv & HU stress
PMID:26912660	exists during veg growth & glucose starv & HU stress
PMID:26912660	exists during veg growth & glucose starv & HU stress
PMID:26941334	localization dependent on actin cytoskeleton
PMID:26942678	some up some down
PMID:26942678	some up some down
PMID:26942678	Erh1 localizes with Mmi1 both during mitotic cell cycle and meiosis
PMID:26942678	author statement
PMID:26960792	can't assess viability
PMID:26960792	can't assess viability
PMID:26960792	growing tips were longer and thinner than those of wild-type cells. This morphology is similar to the one caused by overexpression of Rga4.
PMID:26960792	RhoGAP, GTPase activating protein for Cdc42 and Rho2
PMID:26960792	hard to be more specific when cell shape is also abnormal (Rga6 normally goes to lateral cortex & non-growing tip)
PMID:26960792	can't assess viability
PMID:26960792	can't assess viability
PMID:26960792	can't assess viability
PMID:26960792	can't assess viability
PMID:26960792	can't assess viability
PMID:26990381	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	There were a negligible number of BODIPY 493/503-stained droplets throughout those elongated double knockout cells compared to positive controls (Figure 1F,G).
PMID:26990381	Thus, plh1Δdga1Δ double knockouts appear to have hampered droplet biogenesis events and it is probable that TAG plays a crucial role in the ER escape hatch mechanism with minimal amounts needed even for SE lipid droplet formation [40].
PMID:26990381	Thus, plh1Δdga1Δ double knockouts appear to have hampered droplet biogenesis events and it is probable that TAG plays a crucial role in the ER escape hatch mechanism with minimal amounts needed even for SE lipid droplet formation [40].
PMID:26990381	As expected, these cells contained negligible amounts of TAG after lysis and TLC analysis (Figure 3K).
PMID:26990381	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	The same cells were not viable when grown in YPO (Figure S2B,C).
PMID:26990381	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	Yeast cells lacking both genes (plh1Δdga1Δ) had no droplets but instead showed vesicle-shaped BODIPY 493/503-stained structures when grown in YE5S (Figure 3J).
PMID:26990381	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:27023709	fig. 2i
PMID:27023709	fig. 2i
PMID:27023709	fig. 2i
PMID:27023709	fig 2 H, cell free system
PMID:27023709	fig 2 H, cell free system
PMID:27023709	fig 2 H, cell free system
PMID:27023709	fig 2 H, cell free system
PMID:27023709	fig 2 H, cell free system
PMID:27069798	Bundling activity inferred from pull-down experiments as well as from fluorescence microscopy
PMID:27075176	6C
PMID:27075176	(Figure 3A and Supplemental Video 3).
PMID:27075176	mixed orientations
PMID:27075176	6C
PMID:27075176	6C
PMID:27075176	(Figure 1, C and D).
PMID:27075176	6C
PMID:27075176	6C
PMID:27075176	6C
PMID:27082518	Fig S4F and S4G
PMID:27082518	fig 6 AB
PMID:27082518	Fig S4E
PMID:27082518	Fig 7E
PMID:27082518	fig 1 C-E
PMID:27082518	fig 7C/D
PMID:27082518	fig 7C/D
PMID:27082518	fig 6c
PMID:27082518	fig 6 AB
PMID:27082518	fig 6 AB
PMID:27082518	fig 5a
PMID:27082518	Fig S 3 B
PMID:27082518	Fig 3B
PMID:27082518	fig 1 C-E
PMID:27082518	Fig 7E
PMID:27082518	Fig 7E
PMID:27082518	fig 7A
PMID:27082518	Fig 3B
PMID:27082518	Fig 6E
PMID:27082518	Fiig 6 AB
PMID:27082518	Figure S4D
PMID:27082518	Fig 6E
PMID:27082518	fig 7D
PMID:27082518	Fig S6A
PMID:27082518	Fig S6A
PMID:27082518	Fig S6 B probably due to delayed fusion of TRAPP containing vesicles with PM
PMID:27082518	Fig S6 C probably due to delayed fusion of TRAPP containing vesicles with PM
PMID:27082518	Fig 6E
PMID:27082518	fig 2H, 7A
PMID:27082518	fig 1 B
PMID:27098497	same as without csn5delta
PMID:27098497	same as rhp6delta alone
PMID:27098497	same as without exo1delta
PMID:27098497	worse than without rqh1delta
PMID:27098497	same as rhp6delta alone
PMID:27098497	same as without exo1delta
PMID:27098497	same as without exo1+ overexpression
PMID:27098497	same as without htb1-K119R
PMID:27098497	distal to break point
PMID:27098497	same as without csn1delta
PMID:27101289	binds with high affinity to diverged S. pombe telomeric repeats
PMID:27101289	binds with high affinity to mammalian-type 5'-TTAGGG-3' telomeric repeats, and with very low affinity to diverged S. pombe telomeric repeats // I moved this to sequence specific DNA binding, appears to be author intent AL
PMID:27146110	Figure 3
PMID:27146110	Figure 2
PMID:27146110	Figure 8 (anaphase B)
PMID:27146110	Figure 8
PMID:27146110	Figure 8
PMID:27146110	Figure 7
PMID:27146110	DELAYED Figure 7
PMID:27146110	***DELAYED Figure 7
PMID:27146110	Figure 7
PMID:27146110	Figure 7
PMID:27146110	Figure 7
PMID:27146110	Figure 7 &1
PMID:27146110	Figure 6
PMID:27146110	Figure 6
PMID:27146110	Figure 6
PMID:27146110	Figure 6
PMID:27146110	Figure 5
PMID:27146110	Figure 5
PMID:27146110	Figure 5
PMID:27146110	Figure 5
PMID:27146110	Figure 4
PMID:27146110	Figure 4
PMID:27146110	Figure 3
PMID:27146110	Figure 2
PMID:27146110	Figure 2
PMID:27146110	Figure 2
PMID:27146110	*****The definition of this term is not right Figure 2
PMID:27146110	*****The definition of this term is not right Figure 2
PMID:27146110	Figure 2
PMID:27146110	Figure 2
PMID:27146110	Figure 2
PMID:27146110	Figure 1, 2
PMID:27146110	Figure 1, 2
PMID:27146110	Figure 1, 2
PMID:27146110	Figure 1, 2
PMID:27146110	Figure 1, 2
PMID:27146110	********Sensitive to cold shock Table 1
PMID:27146110	********Sensitive to cold shock Table 1
PMID:27146110	********Sensitive to cold shock Table 1
PMID:27146110	********Sensitive to cold shock Table 1
PMID:27151298	K63-ubiquitin chain from 3 to 8 ubiquitin molecules
PMID:27151298	K63-diubiquitin chain
PMID:27151298	Delete K63-ubiquitin chains from 3 to 8 ubiquitins
PMID:27151298	Ubp2 is inhibited by hydrogen peroxide
PMID:27151298	K63-ubiquitin chain from 3 to 8 ubiquitin molecules
PMID:27151298	K63-diubiquitin chain
PMID:27168121	Fig 1 C
PMID:27168121	Figure 3B
PMID:27168121	Figure 3C
PMID:27168121	fig 1b
PMID:27168121	Figure 3D
PMID:27168121	Figure 3C
PMID:27168121	Figure 3E
PMID:27168121	fig 1 b
PMID:27168121	Figure 3B
PMID:27183912	comma separated extension as can't distinguish transcipts (identical seq)
PMID:27183912	can't distinguish tlh1 and tlh2 as identical sequences hence comma separated; assayed_using(PomBase:tlh1),assayed_using(PomBase:tlh2)
PMID:27188733	says increased proportion, which is a synonym
PMID:27191590	Fig 1C, Fig 4
PMID:27191590	Fig 7C
PMID:27191590	Fig 6D
PMID:27191590	Fig 4E
PMID:27191590	Fig 6E-G
PMID:27191590	Fig 1B
PMID:27191590	Fig 1C, Fig 6C, Fig 7C, Fig S5
PMID:27191590	Fig 7C
PMID:27191590	Fig 6B
PMID:27191590	Fig 6C
PMID:27191590	happens during cellular resposne to BFA Fig 3A, Fig 4A-B, Fig 5B, Fig S3
PMID:27191590	Fig 6B
PMID:27191590	Fig 6C
PMID:27191590	Fig 6C
PMID:27191590	Fig 4D
PMID:27191590	Fig 5A
PMID:27191590	Fig 1C, Fig 4
PMID:27191590	Fig 6C
PMID:27194449	of human pyruvyltransferase activity for the LacNAc-pNP
PMID:27194449	of human pyruvyltransferase activity for the LacNAc-pNP
PMID:27325741	temperature permissive for ts cdc17-K42
PMID:27325741	temperature permissive for ts cdc17-K42
PMID:27325741	temperature permissive for ts cdc17-K42
PMID:27327046	Figures 2 and 3A, B
PMID:27327046	I changed the evidence from IDA to IMP /AL
PMID:27327046	Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.
PMID:27327046	Deletion of both homologues fex1 and fex2 make cells highly sensitive to fluoride. Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.
PMID:27327046	I changed the evidence from IDA to IMP /AL
PMID:27327046	fig S2 & 3
PMID:27327046	fig S2 & 3
PMID:27327046	fig S2 & 3
PMID:27327046	fig S2 & 3
PMID:27334362	Fig. 2D
PMID:27334362	Fig3 D, added assayed genes, vw
PMID:27334362	fig3 c
PMID:27334362	fig 3 c
PMID:27334362	fig 7 B
PMID:27334362	fig 6b
PMID:27334362	fig 3 c
PMID:27334362	fig 3 c split into decreased at outer, abolished at inner (val)
PMID:27334362	fig 3 c
PMID:27334362	fig 3 c
PMID:27334362	fig 9 D
PMID:27334362	fig 9 D
PMID:27334362	fig 9D
PMID:27334362	fig 9A
PMID:27334362	Fig 8B/tableB
PMID:27334362	Fig 8B/tableB
PMID:27334362	Fig 8B/tableB
PMID:27334362	fig 9 D
PMID:27334362	fig 7 B
PMID:27334362	fig 3 c split into decreased at outer, abolished at inner (val)
PMID:27334362	Fig3 D, added assayed genes, vw
PMID:27334362	Fig. 3C (made this specific for inner and added decreased at outer)
PMID:27334362	Fig. 3A,B changed from CENP-A containing nucleosome (val)
PMID:27334362	fig 1a
PMID:27334362	fig 1A
PMID:27334362	Fig. 2C)
PMID:27334362	Fig. 2B
PMID:27334362	fig 2a
PMID:27334362	fig 2D
PMID:27334362	(Fig. 2D) additive
PMID:27334362	Fig. 2D
PMID:27334362	Fig3 D, added assayed genes, vw
PMID:27350684	conditional synthetic lethal with rna14-11
PMID:27350684	splicing of rad21, nda3 and mad2 is also affected
PMID:27350684	splicing of rad21, nda3 and mad2 is also affected
PMID:27350684	splicing of rad21, nda3 and mad2 is also affected
PMID:27350684	splicing of rad21, nda3 and mad2 is also affected
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27385337	figure 5 d/ figure 6
PMID:27385337	fig 3 C
PMID:27385337	Figure 3 F
PMID:27385337	figure 3 F
PMID:27385337	figure 3 F
PMID:27385337	figure 3 F
PMID:27385337	figure 3 F
PMID:27385337	figure 3 F
PMID:27385337	figure 3 F
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27385337	figure 5 d/ figure 6
PMID:27385337	table 1, fig 3 C
PMID:27385337	Supplemental Figure S4F and Table 2
PMID:27385337	Supplemental Figure S4B
PMID:27385337	figure 4 G (localizes as a dot rather than a disk)
PMID:27385337	fig 3 C
PMID:27385337	fig 3 C
PMID:27385337	Figure 1F
PMID:27385337	figure 4 G
PMID:27385337	fig5a
PMID:27385337	Figure 4 F
PMID:27385337	fig 5 a
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27385337	table 1
PMID:27388936	fig 8a
PMID:27388936	fig 8a
PMID:27388936	fig 5 b
PMID:27388936	fig 5 a
PMID:27388936	fig 5 a
PMID:27388936	fig 8c
PMID:27388936	fig 8c
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees C
PMID:27398807	30 degrees C
PMID:27398807	30 degrees C
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees C
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27398807	30 degrees; semi-permissive for slx8-29
PMID:27401558	ChIP at rps2 gene
PMID:27401558	ChIP at rps2 gene
PMID:27401558	ChIP at rps2 gene
PMID:27401558	ChIP at rps2 gene
PMID:27401558	ChIP at rps2 gene
PMID:27401558	ChIP at rps2 gene
PMID:27444384	through conserved cysteines
PMID:27451393	Fig. 2, F and G
PMID:27451393	Fig. 5, C and D
PMID:27451393	Fig. 5, C and D
PMID:27451393	fig 5A
PMID:27451393	fig 5A
PMID:27451393	DNS
PMID:27451393	DNS
PMID:27451393	Fig. 4, A and B
PMID:27451393	Fig. 3E
PMID:27451393	Fig. 3E
PMID:27451393	Fig. 3, A–D
PMID:27451393	Fig. 3, A–D
PMID:27451393	Fig. 2, B and C Fig. 2, D and E
PMID:27451393	Fig. 1A
PMID:27451393	Fig. 1A
PMID:27451393	Fig. 1B, D, E
PMID:27451393	Fig. 1B, D, E
PMID:27451393	Fig. G
PMID:27451393	Fig. G
PMID:27548313	VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by ace2 deletion)
PMID:27548313	VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by 343.20 deletion)
PMID:27548313	VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by eng1 deletion)
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting gst2
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting gst2
PMID:27558664	affecting sua1 affecting cys11 affecting met14
PMID:27558664	affecting gst2
PMID:27587357	deleted in error, added back
PMID:27587357	deleted in error, added back
PMID:27587357	deleted in error, added back
PMID:27587357	deleted in error, added back
PMID:27587357	deleted in error, added back
PMID:27587357	deleted in error, added back
PMID:27587357	deleted in error, added back
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	fig1d
PMID:27587357	see ttps://github.com/pombase/fypo/issues/3152#issuecomment-340506554 A reduced UDP-glucose transport is a decreased transporter activity that produces an abnormal lower level of UDP-glucose in the endoplasmic reticulum lumen
PMID:27587357	fig1d
PMID:27587357	fig1
PMID:27587357	endoplasmic reticulum quality control of glycoprotein folding The quality control of glycoprotein folding is a process that facilitates glycoprotein folding and retains in the endoplasmic reticulum folding intermediates.
PMID:27587357	(vw: inferred from cell wall galactomannan defects)
PMID:27587357	(vw: inferred from cell wall galactomannan defects)
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27587357	Fig 3
PMID:27611590	assayed Cdc20 recruitment
PMID:27611590	assayed Cdc20 recruitment
PMID:27611590	assayed Cdc20 recruitment
PMID:27611590	assayed Cdc20 recruitment
PMID:27613427	AA medium (Rose et al 1990 Methods in Yeast Genetics: A Laboratory Course Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.)
PMID:27613427	AA medium (Rose et al 1990 Methods in Yeast Genetics: A Laboratory Course Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.)
PMID:27618268	fig 1A
PMID:27618268	fig 1A
PMID:27618268	fig 1A
PMID:27618268	(Figures 4C and S4B). non kinetochore bound
PMID:27618268	fig 1B
PMID:27618268	fig 1B
PMID:27618268	fig 1A
PMID:27618268	fig 1A
PMID:27618268	fig 1A
PMID:27618268	Figures 4B and S4A
PMID:27618268	Figures 4B and S4A
PMID:27618268	fig 1B
PMID:27618268	(Figures 4C and S4B). non kinetochore bound
PMID:27618268	((Figure S4C)). non kinetochore bound
PMID:27618268	Figure S3E
PMID:27618268	Figure S3E
PMID:27618268	Figure S3E
PMID:27618268	fig 3C
PMID:27618268	fig 3C
PMID:27618268	fig 3C
PMID:27618268	Figure 2D
PMID:27618268	Figure 2E (how is this abnormal? i got confused here)
PMID:27618268	fig 2E
PMID:27618268	fig 2D
PMID:27618268	(Figure 2B)
PMID:27618268	(Figure 2A)
PMID:27618268	(Figure 2A)
PMID:27618268	fig 1D
PMID:27618268	Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1.
PMID:27618268	Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1.
PMID:27618268	fig 1D
PMID:27618268	fig 1B
PMID:27618268	fig 1B
PMID:27618268	fig 1B
PMID:27627185	(unphosphorylated form of tif211)
PMID:27627185	(unphosphorylated form of tif211) inhibited by stress-inducedphosphorylation of Ser51 in the a subunit of eIF2(tif211)
PMID:27630265	Figure 4, 5, Supplemental Figure S4
PMID:27630265	initiation of forespore membrane delayed (Figure 3, Table 2)
PMID:27630265	Figure 8, Supplemental Figure S9
PMID:27630265	(Supplemental Figure S11)
PMID:27630265	Supplemental Figure S11
PMID:27630265	Supplemental Figure S11
PMID:27630265	Figure 6, Supplemental Figure S6
PMID:27630265	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6)
PMID:27630265	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S3)
PMID:27630265	during meiosis (Figure 5, Supplemental Figure S4)
PMID:27630265	in sporulating cells (Figure 9, Supplemental Figure S9) (Supplemental Figure S10)
PMID:27630265	in vegetative cells (Supplemental Figure S10);
PMID:27630265	Figure 1, Supplemental Figure S1
PMID:27630265	Figure 1
PMID:27630265	Figure 2
PMID:27630265	from metaphase II to postmeiosis (Figure 2)
PMID:27630265	Figure 1 and Supplemental Figure S1
PMID:27630265	Spo13 interacted with both GTP- and GDP-bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	Figure 1
PMID:27630265	Figure 4, 5
PMID:27630265	upplemental Figure S5A
PMID:27630265	Figure 5C, Supplemental Figure S4B
PMID:27630265	Figure 1
PMID:27630265	Supplemental Figure S12
PMID:27630265	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6)
PMID:27630265	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6)
PMID:27630265	(Supplemental Figure S11B)
PMID:27630265	(Supplemental Figure S11B)
PMID:27630265	(Supplemental Figure S10A)
PMID:27630265	(Supplemental Figure S10A)
PMID:27630265	(Supplemental Figure S10A)
PMID:27630265	(Figure 8A)
PMID:27630265	(Figure 8A)
PMID:27630265	(Figure 8A)
PMID:27630265	Sec2 interacted with specifically with GTP- bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	upplemental Figure S5A
PMID:27630265	Figure 6A and Supplemental Figure S3)
PMID:27630265	upplemental Figure S5A
PMID:27630265	Figure 6A and Supplemental Figure S3)
PMID:27648579	not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone
PMID:27648579	not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone
PMID:27648579	substrate: recombinant mono-nucleosomes
PMID:27648579	substrate: bulk histone octamers
PMID:27655872	Figure 3 D
PMID:27655872	Fig 1E
PMID:27655872	"Fig 2B, lanes ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	Fig 2C
PMID:27655872	Fig 2C
PMID:27655872	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	Fig 8C 8D Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	Fig 8C 8D Western blot analysis show decreased Sre1 cleavage activation under low oxygen
PMID:27655872	Fig 2A
PMID:27655872	Fig 2A
PMID:27655872	Fig 2A
PMID:27655872	"Fig 2B, lanes ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	Fig 2B, lanes 5–13
PMID:27655872	Fig 2D, lane 3
PMID:27655872	Fig 2G, lanes 10– 12
PMID:27655872	Fig 2G, lanes 6–8
PMID:27655872	Fig 3A, lane 4 both cleavage products
PMID:27655872	Fig 3A, lane 3
PMID:27655872	Fig 3A, lane 3
PMID:27655872	Fig 3D, compare lanes 3 and 4
PMID:27655872	Fig 3D,
PMID:27655872	Fig 3D,
PMID:27655872	Fig 3D,
PMID:27655872	Fig 3D, compare lanes 3 and 4
PMID:27655872	PRECURSOR Figure 3 E
PMID:27655872	Fig 3E and Figure 3 D
PMID:27655872	Fig 3E and Figure 3 D
PMID:27655872	PRECURSOR Fig 5D and F (4.5 fold)
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	PRECURSOR Fig 5E and F
PMID:27655872	Fig 5E and F
PMID:27655872	fig 6 B
PMID:27655872	fig 6 B
PMID:27655872	fig 6 B
PMID:27655872	fig 6 B
PMID:27655872	Fig 7A, lanes 4–6
PMID:27655872	Fig 7A, lanes 4–6
PMID:27655872	Fig 8A
PMID:27655872	Fig 8
PMID:27655872	Fig 8A
PMID:27655872	Fig 8
PMID:27655872	Fig 9A
PMID:27655872	Fig 9A
PMID:27655872	Fig 9A
PMID:27655872	Fig 9A
PMID:27655872	Fig 3A, lane 4 both cleavage products
PMID:27664110	text
PMID:27664110	text
PMID:27664110	text
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	1b severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive tempera- ture
PMID:27664110	1c
PMID:27664110	2
PMID:27664110	2
PMID:27664110	3
PMID:27664110	3
PMID:27664110	3
PMID:27664222	Supplementary Figure S1B
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	subcategory of oxidative stress known as GSH or disulfide stress (4). Indeed, a lower GSH/GSSG ratio was found after treatment with diamide or Cd (Supplementary Figure S4) in WT and in the SPBC29A10.12Δ strain
PMID:27664222	detoxification of thiol disulphide (in response to disulphide stress)
PMID:27664222	detoxification of thiol disulphide (in response to disulphide stress)
PMID:27664222	Figure 5A
PMID:27664222	Figure 5A
PMID:27664222	Figure 5A
PMID:27664222	diamide-induced promoters
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Figure 2A
PMID:27664222	Figure 2A
PMID:27664222	Supplemen- tary Figure S3A
PMID:27664222	Supplemen- tary Figure S3A NaCl or KCl)
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Fig- ure 3A
PMID:27664222	Supplementary Figure S1B
PMID:27664222	detoxification of thiol disulphide (in response to disulphide stress)
PMID:27666591	Figure S1G
PMID:27666591	not sure if this is quite right
PMID:27666591	Figures 2B and 2C
PMID:27666591	Figure 1B Figure S1F
PMID:27666591	Figure 1B Figure S1F
PMID:27666591	Figure S1F
PMID:27666591	VW: added exists_during..
PMID:27666591	7F
PMID:27666591	7e
PMID:27666591	Figure 7B
PMID:27666591	Figure 5C
PMID:27666591	Figure 5C
PMID:27666591	Figure 5A
PMID:27666591	Figure 5C
PMID:27666591	Figure 5B
PMID:27666591	Figure 5A
PMID:27666591	Figure 4D
PMID:27666591	Figure S5B)
PMID:27666591	Figure 4C
PMID:27666591	Figure 3A
PMID:27666591	Figures 2D and S3B
PMID:27666591	Figure 2D
PMID:27666591	Figures 1F and S2B
PMID:27666591	Figures S2A and S2B
PMID:27666591	Figures S1A and S1B
PMID:27666591	Figure 1A. Figures S1C–S1E
PMID:27666591	Fig- ure 7D
PMID:27666591	Figure 7C)
PMID:27666591	Figure 2A
PMID:27687771	target genes: cut6, vht1, bio2
PMID:27687771	at cut6 gene promoter
PMID:27687771	target genes: cut6, vht1, bio2
PMID:27687771	target genes: cut6, vht1, bio2
PMID:27687771	target genes: cut6, vht1, bio2
PMID:27687866	acetaldehyde absent
PMID:27687866	acetaldehyde absent
PMID:27687866	acetaldehyde absent
PMID:27697865	6E
PMID:27697865	fig 5c
PMID:27697865	vw: changed to increased activation, and D333A allele (as compared to WT)
PMID:27697865	fig 1A
PMID:27697865	fig4
PMID:27697865	fig4E
PMID:27697865	fig 5c
PMID:27697865	fig6 fig 7
PMID:27697865	fig6A
PMID:27697865	fig 6E
PMID:27697865	Fig. S4
PMID:27697865	Fig.
PMID:27697865	Fig.
PMID:27697865	(anaphase)
PMID:27697865	fig 6E
PMID:27697865	fig5
PMID:27729451	replced GO:1990601 (which acts on ss DNA)
PMID:27736299	Fig1. 11.63% longer than control mean
PMID:27736299	Fig3. Cdc2 level reduced to about 48% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 14.43% longer than control mean
PMID:27736299	Fig3. cdc25 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 15.55% longer than control mean
PMID:27736299	Fig3. Nup186 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 15.82% longer than control mean
PMID:27736299	Fig3. cdc13 level reduced to ~44% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 16.78% longer than control mean
PMID:27736299	Fig3. Sal3 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig3. Nup189 level reduced to ~50% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 16.50% shorter than control mean
PMID:27736299	Fig3 Wee1 level reduced to ~32% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 11.15% shorter than control mean
PMID:27736299	Fig3. Pom1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 10.86% shorter than control mean
PMID:27736299	Fig3. Suc1 level reduced to ~60% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 10.81% longer than control mean
PMID:27736299	Fig3. Ppa2 reduced to~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig3. Cdr1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 9.10% shorter than control mean
PMID:27736299	Fig1. 8.74% longer than control mean
PMID:27736299	Fig3. Cpc2 level reduced to about 55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 8.78% longer than control mean
PMID:27736299	Fig3. nup45 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig3 Nup97 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 18.92% longer than control mean
PMID:27736299	Fig3. Nsp1 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 19.29% longer than control mean
PMID:27736299	Fig3. Nup184 level reduced to 30% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	Fig1. 23.46% longer than control mean
PMID:27736299	Fig3. Dea2 level reduced to 50%
PMID:27736299	Fig1. 31.94% longer than control mean
PMID:27736299	Fig1. 8.80% longer than control mean
PMID:27737912	fig 6
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	2 day G0 ChIP
PMID:27738016	2 day G0 ChIP
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	S13; Tetrad dissection
PMID:27738016	S13; Tetrad dissection
PMID:27738016	S13; Tetrad dissection
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	Decreased RNA polymerase I at rDNA during vegetative growth; nuc1-FLAG
PMID:27738016	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	Increased RNA polymerase II at rDNA during vegetative growth
PMID:27738016	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	G0-exit
PMID:27738016	Rad22-YFP, G0-exit
PMID:27738016	small-RNA-seq
PMID:27738016	small-RNA-seq
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	mutant defective in maintenance of quiescence
PMID:27738016	24h G0 cell microscopy
PMID:27738016	Fig S6; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	Fig S6; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	Fig S6; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	Fig S6; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	mutant defective in maintenance of quiescence
PMID:27738016	mutant defective in maintenance of quiescence
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	15 ug/ml thiabendazole
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	G0 viability assay
PMID:27738016	24h G0 cell microscopy
PMID:27746023	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	during nitrogen starvation. Although many mutants in the SAPK pathway have defects in mating and meiosis, this result may help to explain why sty1D and wis1D mutants in particular continue to elongate upon N starvation, unlike other mutants in the pathway
PMID:27746023	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	Figures 2A and S1A; Movie S1
PMID:27746023	Figure S1B
PMID:27746023	unlike WT cell elongation continued after actin depolymerization, (Figures 2A and 2B; Movie S1) conclusions. 1. the SAPK pathway is required for CRIB dispersal after LatA treatment. 2 the actin cytoskeleton per se is not required for stability of the Cdc42 polarity module at cell tips. 3. cell elongation can occur in the complete absence of the actin cytoskeleton.
PMID:27746023	unlike WT cell elongation continued after actin depolymerization, (Figures 2A and 2B; Movie S1) conclusions. 1. the SAPK pathway is required for CRIB dispersal after LatA treatment. 2 the actin cytoskeleton per se is not required for stability of the Cdc42 polarity module at cell tips. 3. cell elongation can occur in the complete absence of the actin cytoskeleton.
PMID:27746023	Figure 2C
PMID:27746023	Figure 2C
PMID:27746023	Figure 2D
PMID:27746023	Figures S1C and S1D
PMID:27746023	Figures S1C and S1D
PMID:27746023	arrested
PMID:27811944	mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage
PMID:27811944	mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage
PMID:27811944	deletion of Sre1 aa 877-900 also destabilized Sre1 and prevented proteolytic activation
PMID:27851962	Figure 1
PMID:27851962	Figure 1
PMID:27851962	Figure 1
PMID:27851962	Figure 1
PMID:27851962	Figure 1
PMID:27851962	Figure 1
PMID:27851962	Figure 1
PMID:27852900	fig 7
PMID:27852900	fig 7
PMID:27852900	Figure 3, A and E
PMID:27852900	Figure 3, A and E
PMID:27852900	fig 4 GFP-LactC2 probe expressed from pREP3X
PMID:27852900	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	fig4 GFP-LactC2 probe expressed from pREP3X
PMID:27852900	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	fig 4B. GFP-LactC2 probe expressed from pREP3X
PMID:27852900	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	Figure 5D
PMID:27852900	Figure 8e
PMID:27852900	fig8d
PMID:27852900	fig 8d
PMID:27852900	fig 8a
PMID:27852900	fig 8 a
PMID:27852900	fig 8 a
PMID:27871365	3H
PMID:27871365	3H
PMID:27871365	from later paper: We speculate that SPRTN is able to degrade DPCs to peptide adducts that are sufficiently small for efficient TLS. https://www.sciencedirect.com/science/article/pii/S1097276518309948
PMID:27872152	Fig. 7D)
PMID:27872152	Fig. 7D)
PMID:27872152	(Fig. 7B,C)
PMID:27872152	adaptor for dis1-microtubule
PMID:27872152	Fig. 7D)
PMID:27872152	(Fig. 2A) (Fig. 2B; Fig. S2B).
PMID:27872152	(2.0% versus <0.1%) (Fig. 7F)
PMID:27872152	Fig. 7E issues/2984
PMID:27886462	figure 3C
PMID:27886462	Table 2
PMID:27886462	Table 2
PMID:27886462	Table 2
PMID:27886462	Table 2
PMID:27886462	Table 2
PMID:27886462	Table 4
PMID:27886462	Table 2
PMID:27886462	Table 2
PMID:27886462	Figure 1C
PMID:27886462	figure 2A
PMID:27886462	figure 2A
PMID:27886462	figure 2A
PMID:27886462	figure 2A
PMID:27886462	figure 3A
PMID:27886462	figure 3A
PMID:27886462	Table 2
PMID:27886462	Table 2
PMID:27886462	Figure 4, Table 3
PMID:27886462	Figure 4, Table 3
PMID:27886462	Figure 4, Table 3
PMID:27886462	Figure 4, Table 3
PMID:27886462	figure 3A
PMID:27886462	figure 3A
PMID:27886462	figure 3C
PMID:27886462	Figure 4, Table 3
PMID:27886462	figure 3C
PMID:27886462	Figure 4, Table 3
PMID:27886462	Figure 4, Table 3
PMID:27886462	Figure 4
PMID:27886462	Table 3
PMID:27886462	Table 3
PMID:27886462	Table 3
PMID:27886462	Table 3
PMID:27886462	Table 3
PMID:27886462	Figure 1C
PMID:27886462	Figure 1C
PMID:27886462	Figure 1C
PMID:27886462	Figure 1C
PMID:27886462	Figure 1C
PMID:27886462	Figure 1C
PMID:27886462	Figure 1B
PMID:27886462	Figure 1B
PMID:27886462	Figure 1B
PMID:27886462	Figure 1B
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1A
PMID:27886462	Figure 1C
PMID:27886462	Table 3
PMID:27886462	Table 3
PMID:27886462	Table 3
PMID:27886462	Table 4
PMID:27886462	Table 4
PMID:27886462	Table 4
PMID:27886462	Table 4
PMID:27886462	figure 3C
PMID:27889481	Figure 1
PMID:27889481	Figure 1B
PMID:27889481	Figure 1B
PMID:27889481	Figure 1C In contrast, in the absence of the bouquet, the duplicated SPBs often fail to separate. Indeed, 75.5% of bqt1Δ cells with defective meiosis show problems in SPB separation at MI
PMID:27889481	Figure 1C In contrast, in the absence of the bouquet, the duplicated SPBs often fail to separate . Indeed, 75.5% of bqt1Δ cells with defective meiosis show problems in SPB separation at MI
PMID:27889481	Figure 1D
PMID:27889481	Figure 1D
PMID:27889481	Figure 1 E In contrast, Alp4 localization is defective (ie one or both SPB signals lack any detectable Alp4 colocalization at MI onset) in 59% of bqt1Δ meiocytes (n= 100, p<0.01) from the onset of MI onwards,
PMID:27889481	Figure 1 E and all (n=50, p<0.01) those SPBs failing to recruit Alp4 show SPB separation problems and failed spindle nucleation (Figure 1E).
PMID:27889481	Figure In 100% of the bqt1Δ cells that show monopolar spindles (n=11), those spindles are nucleated specifically from the old SPB (Figure S1I). Hence, failed spindle nucleation in the absence of the bouquet is specific to the new SPB.
PMID:27889481	Figure 1C, I Figure 1F and 1G. We previously observed a tendency for the SPB to dissociate from the NE just prior to meiotic spindle formation in the bqt1Δ setting (Fennell et al., 2015; Tomita and Cooper, 2007); indeed, SPBs showing problems in separation typically appear to dislodge into the cytoplasm (Figure 1C, yellow arrowheads
PMID:27889481	Figure I
PMID:27889481	Figure 1
PMID:27889481	fig2c
PMID:27889481	fig2c
PMID:27889481	fig2c
PMID:27889481	fig2c
PMID:27889481	Figure 3A. Sad1.2-GFP remains stably associated with the SPB throughout interphase, in contrast to Sad1.1-GFP, which is destabilized at 36°C
PMID:27889481	Figure 3A. Sad1.2-GFP remains stably associated with the SPB throughout interphase, in contrast to Sad1.1-GFP, which is destabilized at 36°C
PMID:27889481	Figures 3B–C, S4A
PMID:27889481	Figures 3B–C, S4A
PMID:27889481	Figure S4B
PMID:27889481	Figure S4B
PMID:27889481	fig 3DE sad1.2 cells often show extra Mis6-GFP foci unassociated with the SPB, even at permissive temperature
PMID:27889481	(Figure 3DE) At restrictive temperature, a population of sad1.2 cells emerges in which all three centromeres are clearly dissociated from the SPB
PMID:27889481	fig 3DE
PMID:27889481	(Figure 3DE)
PMID:27889481	(Figure 4B)
PMID:27889481	(Figures 4D–E, S5B, S5D) sad1.2 cells exhibiting total centromere dissociation not only fail to insert but also appear to separate from the NE, dislodging into the cytoplasm
PMID:27889481	fig 5.C
PMID:27889481	Figure 5B. centromeres are also released from LINC in bouquet-defective cells
PMID:27889481	Figure 5C. spindle formation occurs normally at both MI and MII in sad1.2 meiosis
PMID:27889481	abolished
PMID:27889481	fig6
PMID:27889481	fig6
PMID:27898700	Fig S3B
PMID:27898700	Fig S4D S4E
PMID:27898700	Fig 4
PMID:27898700	Fig 2 A (3x WT)
PMID:27898700	Fig 2 A (2x WT)
PMID:27898700	Fig 2 A
PMID:27898700	Fig 2 A
PMID:27898700	Fig 2 A
PMID:27898700	fig 1FG slides along axis from midpoint
PMID:27898700	fig 1FG
PMID:27898700	Fig 4
PMID:27898700	Fig 4
PMID:27898700	Fig 4
PMID:27898700	Fig 4
PMID:27898700	Fig 4
PMID:27898700	Fig 4
PMID:27898700	fig 1A
PMID:27898700	fig 1A during cytokinesis
PMID:27898700	fig 1B swollen multiseptate elongated
PMID:27898700	fig 1C
PMID:27898700	fig 1C
PMID:27898700	fig 1C
PMID:27898700	fig 1FG
PMID:27898700	fig 1FG
PMID:27898700	Fig S3B
PMID:27901072	1d
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	fig6
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27901072	asynchronous fig 3a
PMID:27902423	Promoter analysis
PMID:27902423	Promoter analysis
PMID:27902423	Promoter analysis
PMID:27966061	indicates Hsf1 activation
PMID:27974503	Cpy1 missorting in null mutant
PMID:27974503	Aberrant Golgi stacks
PMID:27974503	Cpy missorting in null mutant
PMID:27974503	Suquence homology, localization, co-immunoprecipitation
PMID:27974503	Slow growth. Reduced colony size
PMID:27974503	Cpy1 missorting in null mutant
PMID:27974503	Sequence similarityto ChAPs, protein localization, Co-immunoprecipitation
PMID:27974503	Abnormal GFP-Syb1 localization
PMID:27974503	Abnormal GFP-Syb1 distribution
PMID:27974503	Cpy1 missorting in null mutant
PMID:27984744	Fig. 2E-F
PMID:27984744	Fig. 2E-F
PMID:27984744	Fig. 2E-F
PMID:27984744	Fig. 2A-B
PMID:27984744	ChIP-seq; Fig. 1C-D
PMID:27984744	Fig. S2
PMID:27984744	Fig. 1B
PMID:27984744	Fig. 1A
PMID:27984744	Fig. 1B
PMID:27984744	Fig. 1A
PMID:27984744	Fig. 1A
PMID:27984744	Fig. 1B
PMID:27984744	Fig. 1A
PMID:27984744	Fig. 1B
PMID:27984744	Fig. 1A
PMID:27984744	Fig. 1B
PMID:27984744	Fig. 1A
PMID:27984744	Fig. 1B
PMID:28011631	Fig. 1F and Fig. 2C
PMID:28011631	Fig. 4A,C)
PMID:28011631	(Fig. 4B)
PMID:28011631	(Fig. 4B)
PMID:28011631	Fig. 3B (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	Fig. 4A
PMID:28011631	Fig. 3B (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	Fig. 3B normal lipid droplet localization to FSM leading edge
PMID:28011631	2C (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	2C (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	2C (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	2C
PMID:28011631	Figure S3 LP clustering at nucleus
PMID:28011631	figure S2
PMID:28011631	figure S2
PMID:28011631	Fig. 4F Assembly of Isp3-GFP onto the spore surface was defective in the dga1Δplh1Δ mutant.
PMID:28011631	Fig. 3B
PMID:28011631	Fig. 1H and Fig. 3B
PMID:28011631	Fig. 4F Isp3-GFP was improperly assembled in the dga1Δplh1Δ mutant.
PMID:28011631	Fig. 4B The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28011631	Fig. 4A, 4C, and 4D Using spore colony formation assay and microscopic observation, most of the dga1Δplh1Δ mutant spores failed to form colonies showed no sign of germination.
PMID:28011631	Fig. 4B The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28017606	136 amino acids of Mad1 containing a coiled-coil region (CC) were removed, preventing Mad1-Mad2 interaction with Mlps and the nuclear envelope and also removing the Cut7 interaction site. These mad1-DCC cells were also able to arrest efficiently when TetR-Spc7-9TE and TetR-D(1-302)Mph1 were co-expressed (Figure 3E). We conclude that the Mad and Bub proteins do not need to be enriched at kinetochores, spindle poles, or the nuclear periphery for a robust checkpoint arrest to be generated in fission yeast. Most likely a diffuse, soluble pool of Spc7
PMID:28017606	Strains co-expressing Spc7 and Mph1 do not accumulate Mad2-GFP at spindle poles in strains containing the mad1-KAKA mutation that disrupts the Mad1-Cut7 kinesin motor interaction.
PMID:28017606	Figures 1D and 1E / ectopic. show a very striking result: co-expression of TetR-Spc7-9TE with TetR-D(1-302)Mph1 was sufficient to arrest cells in mitosis.
PMID:28017606	Spc7-wt arrested significantly faster than Spc7-9TE, with $60% mitotic arrest after 12 hr compared to 16 hr for Spc7-9TE.
PMID:28017606	advance (by 
4 hr) in the timing of arrest in bub3D cells arresting due to Spc7-9TE cells (although there is no effect with Spc7-wt, see Figure S4C).
PMID:28017606	This demonstrates that the ‘‘activated’’ Spc7-9TE binding platform is sufficient to recruit these three checkpoint proteins constitutively, and that this works ectopically and thus does not require additional kinetochore factors. and Figure 1C. thus, we believe that this Spc7-Bub-Mad3 complex likely acts as an independent signaling module
PMID:28031482	figure 1 E
PMID:28031482	figure 1 E
PMID:28031482	figure 1 E
PMID:28031482	figure 1 D
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28031482	Figure 6 c
PMID:28031482	Figure 6 c
PMID:28031482	Figure 6 A
PMID:28031482	Fig. 5G, left panel
PMID:28031482	Fig. 5G, left panel
PMID:28031482	Fig. 5G, left panel
PMID:28031482	Fig. 5D
PMID:28031482	Fig. 5B
PMID:28031482	Fig. 5C
PMID:28031482	Fig. 5A
PMID:28031482	Fig. 4H, right panel
PMID:28031482	Fig. 4D
PMID:28031482	Fig. 4B Fig. 4D
PMID:28031482	Fig. 1D
PMID:28031482	pdc2 is required for mRNA decapping. Fig. 2A 2B
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28031482	Fig. 2B
PMID:28031482	figure 2D
PMID:28031482	figure 2D
PMID:28031482	figure 2B
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	Fig 6 C
PMID:28031482	figure 7A
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28031482	Fig 6 D
PMID:28103117	fig 2a INCREASED
PMID:28103117	fig 2a INCREASED
PMID:28103117	fig 2a
PMID:28103117	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	fig 2a INCREASED
PMID:28103117	fig 2a INCREASED
PMID:28103117	fig 2a INCREASED
PMID:28103117	The cell cycle was 20 min longer in clp1D cells compared with wild type cells.
PMID:28103117	changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2)
PMID:28103117	changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2)
PMID:28103117	fig3a Cdk1 consensus sites
PMID:28160081	fig2B
PMID:28160081	fig 2A
PMID:28160081	fig2B
PMID:28160081	fig 2A
PMID:28160081	fig2B
PMID:28160081	fig2A
PMID:28160081	fig 2A
PMID:28160081	fig2B
PMID:28160081	fig 5
PMID:28160081	fig 4c
PMID:28160081	fig2B
PMID:28178520	requires motor activity
PMID:28178520	Fig 1 requires Clp1 activity
PMID:28178520	vw: moved down to nucleoplasm
PMID:28178520	Fig 5
PMID:28178520	Fig 5
PMID:28178520	Fig 4 D
PMID:28178520	Fig 4 D
PMID:28178520	Fig 4 D
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	(Figure 5B)
PMID:28178520	(Figure 5B)
PMID:28178520	Fig 5
PMID:28178520	Fig 5
PMID:28178520	Figure 4E
PMID:28178520	Fig 4 D
PMID:28178520	Figure 4E
PMID:28178520	Fig 4 D
PMID:28178520	Fig 4 D
PMID:28178520	Fig 4 D
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Fig 4 A
PMID:28178520	Figure 4A
PMID:28178520	(Figure S4C)
PMID:28178520	(Figure S4C)
PMID:28178520	(Figure S4C)
PMID:28178520	(Figure S4C)
PMID:28178520	Figure S3C/D
PMID:28178520	Figure 2B
PMID:28178520	Figure 2B
PMID:28178520	Figure S3B
PMID:28178520	Figure S3B
PMID:28178520	Figure 2A; Figure S3A
PMID:28178520	Figure 2A; Figure S3A
PMID:28178520	figure 2A
PMID:28178520	(Figures S2B)
PMID:28178520	(Figures S2B)
PMID:28178520	(Figures S2A)
PMID:28178520	(Figures S2A)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	(Figures 1J)
PMID:28178520	Figure 1I
PMID:28178520	Figure 1I
PMID:28178520	(Figures 1H)
PMID:28178520	(Figures 1H)
PMID:28178520	Figure 1H
PMID:28178520	(Figures 1G and 1I; Figure S1F)
PMID:28178520	(Figures 1G and 1I; Figure S1F)
PMID:28178520	Figure 1E
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	(Figure 1D)
PMID:28178520	(Figure 1D)
PMID:28178520	(Figures S1D and S1E)
PMID:28178520	Figure 1C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	Figure 1B and S1B,C
PMID:28178520	fig1
PMID:28178520	FIg 3
PMID:28178520	Fig 1 requires Klp9, Clp1 activity
PMID:28191457	SDS-PAGE followed by western blotting and proteinase K treatment. Dot plots with extracts for pellet, soluble and total cell fractions with and without pre-treatment with 2% SDS. SDD-AGE gels of samples treated at room temperature and at 95°C, both with and without curing with GdnHCl.
PMID:28191457	Phenotype is inherited in non-Mendelian manner, via protein aggregates (prion-like).
PMID:28193844	9
PMID:28193844	8b
PMID:28193844	fig4
PMID:28193844	6a
PMID:28193844	fig4
PMID:28193844	6
PMID:28193844	they show it is GPI anchored, the specified residue is predicted
PMID:28202541	Scp1-13xMyc used for Scp1, pulled on Myc
PMID:28202541	Anp1-GFP mislocalized from Golgi puncta to ER and vacuole
PMID:28202541	Ost1-mCherry increased signal in ER
PMID:28202541	Anp1-GFP degradation as assayed by appearance of free GFP
PMID:28202541	Ost1-mCherry, mCherry antibody
PMID:28202541	improved relative to WT Sre1
PMID:28202541	pulled on Dsc2
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq; same severity as spt16-1 alone
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28218250	ChIP-seq
PMID:28242692	severe leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation, figure 4 B
PMID:28242692	Remarkably, double-mutant cells displayed WT-like nuclei, although a few examples of probable nuclear fenestrations were observed in lem2Δ single-mutant cells (Fig. 5G).
PMID:28242692	Remarkably, double-mutant cells displayed WT-like nuclei, although a few examples of probable nuclear fenestrations were observed in lem2Δ single-mutant cells (Fig. 5G).
PMID:28242692	and the NPCs that were present were localized to re- gions that were largely free of karmellae and tubulo-vesicular structures (Fig. 4D).
PMID:28242692	Fig. 4B, asterisk
PMID:28242692	cells with abnormal NE morphology at the beginning of the exper- iment, by contrast, lost nuclear GFP completely over the time course (Fig. S3B). Thus, cytoplasmic GFP resulted from loss of nuclear integrity rather than from defects in nuclear import.
PMID:28242692	partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation
PMID:28242692	partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation
PMID:28242692	partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation
PMID:28242692	4B, arrowheads, and Fig. 5B
PMID:28242692	Fig S1C
PMID:28242692	Fig S1C
PMID:28242692	Fig. 1 D–F
PMID:28242692	rescue
PMID:28242692	Fig S1AB
PMID:28242692	Fig 1C
PMID:28242692	Fig 1C
PMID:28242692	Fig 1C
PMID:28242692	Fig. 1C
PMID:28242692	Fig. 1B, supp table S1
PMID:28242692	Fig. 1B, supp table S1
PMID:28242692	Fig 1A
PMID:28242692	Fig. 2B)
PMID:28264193	fig5 fusion mutant not currently capturable
PMID:28264193	Supp
PMID:28264193	Supp2
PMID:28264193	Supp2
PMID:28264193	Supp2
PMID:28264193	Supp2
PMID:28264193	Supp2
PMID:2827111	table 1
PMID:2827111	table1
PMID:2827111	table1
PMID:2827111	fig 7 B
PMID:2827111	table 1
PMID:28281664	Figure 1
PMID:28281664	figure 1a
PMID:28281664	Figure 1B
PMID:28281664	Figure 2
PMID:28281664	Figure 2
PMID:28281664	figure 1d
PMID:28281664	figure 1c & d
PMID:28281664	figure 1D
PMID:28281664	Figure 2
PMID:28281664	Figure 2.
PMID:28281664	Figure 2
PMID:28281664	Figure 3.
PMID:28281664	Figure 3.
PMID:28281664	Figure 3.
PMID:28281664	Figure 3.
PMID:28281664	Figure 1D
PMID:28281664	Figure 2
PMID:28281664	Figure 2
PMID:28281664	Figure 2
PMID:28281664	Figure 2
PMID:28281664	Figure 3.
PMID:28281664	Figure 3.
PMID:28281664	Figure 3.
PMID:28281664	Figure 3.
PMID:28281664	figure 1b divides longer than WT in the same conditions
PMID:28292899	Fig. 7
PMID:28292899	Fig. 6
PMID:28292899	Fig. 5B
PMID:28292899	Fig. 5B
PMID:28292899	Fig. 5B A(ALSO FOR THE myo-1TH3 domain deletion(need genotype description)
PMID:28292899	Fig. 5B
PMID:28292899	Fig. 4 D–F
PMID:28292899	Fig 2 & Fig. 3C
PMID:28292899	Fig. 1A, Inset and Movie S1/ number of Mcp5 molecules per cluster 10 ± 2 ( Fig. 1D)
PMID:28292899	Fig. 7
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	normal NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	normal NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	normal NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	normal NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	normal NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28292918	decreased NHEJ repair of hairpin-capped chromosome breaks
PMID:28334955	Supplementary Figure S3B (abolished by galactose addition)
PMID:28334955	S3
PMID:28334955	S3
PMID:28334955	Figure 2B (barely detectable level )
PMID:28334955	Figure 2B
PMID:28334955	Figure 2B
PMID:28334955	Figure 2B, 8B,8C
PMID:28334955	Figure 2C
PMID:28334955	figure 6 c
PMID:28334955	figure 6 c
PMID:28334955	figure 6 a
PMID:28334955	figure 6 a
PMID:28334955	Fig 7 A
PMID:28334955	Fig 7 A
PMID:28334955	fig 7 B
PMID:28334955	Fig 7 c
PMID:28334955	Supplementary Figure S7
PMID:28334955	fig 1B inferred from
PMID:28334955	Supplementary Figure S3B
PMID:28334955	S3
PMID:28334955	figure 8 A
PMID:28334955	Figure 8B,8C (barely detectable level )
PMID:28334955	Figure 8B,8C
PMID:28334955	Figure 8B,8C
PMID:28334955	figure 8 D
PMID:28334955	figure 8 D
PMID:28334955	figure 8 D
PMID:28334955	figure 8 D
PMID:28334955	figure 8 D
PMID:28334955	figure 8 D
PMID:28334955	figure 9A
PMID:28334955	fig 9C
PMID:28334955	figure Supp S8
PMID:28334955	figure 9 d
PMID:28334955	Based on what we know about lon in other species, i think the rescue of mpa1 phenotype is enough to predict a catabolic role
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	figure 9 F
PMID:28334955	We named this gene mpa1
PMID:28334955	Fig 1 A
PMID:28334955	Fig 1 A
PMID:28334955	Fig 1 A
PMID:28334955	fig 1B
PMID:28334955	fig 1B
PMID:28334955	fig 1B
PMID:28334955	fig 1B inferred from
PMID:28334955	Fig 1 C
PMID:28334955	Fig 1 C
PMID:28334955	Fig 1 E/F
PMID:28338873	assayed in vitro
PMID:28338873	assayed in vitro
PMID:28343969	Fig 1B
PMID:28343969	Fig 2C, 2D, 2G
PMID:28343969	18degC Fig 2C, 2D, 2G This phenotype is largely suppressed by tethering Hrk1 to centromeres. (bw, I made an annotation to represent this suppression below)
PMID:28343969	Fig 4H (cut9-665 move to background for this one)
PMID:28343969	Fig 4F, 4H (cut9-665 move to background for this one)
PMID:28343969	Fig S2A, S2C
PMID:28343969	figure 1 E Thus, although Eso1, Wpl1, and Hrk1 all bind to the same surface of Pds5, we assume that they do not always compete for binding because of the excess amounts of Pds5 in the cells. Thus, HIM in Pds5 and PIM in Hrk1 are required solely for centromeric Hrk1 localization and its function, at least in the context of targeting the CPC to centromeres.
PMID:28343969	figure 1 E
PMID:28343969	Fig 2AB
PMID:28343969	Fig 2AB
PMID:28343969	Fig 2 B
PMID:28343969	Fig 2 B
PMID:28343969	Fig 2AB
PMID:28343969	Fig 2AB
PMID:28343969	"Fig 2C (vw: this represents Yoshi's suggestion"" An Ark1 reduction can become a reason of merotelic attachment, which is also caused by a defect in kinetochore structures.)"""
PMID:28343969	"Fig 2C this represents Yoshi's suggestion"" An Ark1 reduction can become a reason of merotelic attachment, which is also caused by a defect in kinetochore structures.)"" has_penetrance high , assayed_using ark1"
PMID:28343969	Fig 2F WT is about the same?
PMID:28343969	Fig 2F WT is about the same?
PMID:28343969	Fig 2E
PMID:28343969	Fig 2E
PMID:28343969	Fig 2 F
PMID:28343969	fig S4B
PMID:28343969	S4A
PMID:28343969	S4A
PMID:28343969	fig 4b
PMID:28343969	fig 4b
PMID:28343969	4C
PMID:28343969	4C
PMID:28343969	Fig 4E
PMID:28343969	Fig 4E
PMID:28343969	Fig 4f
PMID:28343969	Fig 4f
PMID:28343969	Fig 4f
PMID:28343969	Fig 4f
PMID:28343969	Fig 4G
PMID:28343969	Fig 4G
PMID:28343969	Fig S4A
PMID:28343969	Fig S4A
PMID:28343969	Fig S4A
PMID:28343969	(Figures S4D and S4E
PMID:28343969	(Figures S4D and S4E
PMID:28343969	Fig S4A
PMID:28343969	Fig S4A
PMID:28343969	(Figures S4D and S4E
PMID:28343969	(Figures S4D and S4E
PMID:28345447	restored by depletion of ammonium
PMID:28345447	restored by depletion of ammonium
PMID:28345447	restored by depletion of ammonium
PMID:28345447	restored by depletion of ammonium
PMID:28345447	restored by depletion of ammonium
PMID:28366743	Fig. 3 A/B present in interphase cells
PMID:28366743	Fig. 3 A/B present in interphase
PMID:28366743	Fig 1B
PMID:28366743	Fig 1B
PMID:28366743	Fig1B
PMID:28366743	Fig1b
PMID:28366743	Fig 1B
PMID:28366743	Fig S1G
PMID:28366743	Fig. 3B
PMID:28366743	Fig. 3B
PMID:28366743	Fig 4D
PMID:28366743	Fig. 4C
PMID:28366743	Fig. 4C
PMID:28366743	Fig. 4C
PMID:28366743	fig 4A
PMID:28366743	Fig 1B
PMID:28366743	synchronous mitotic cells fig 1c
PMID:28366743	Fig. 1C synchronous mitotic cells
PMID:28366743	Fig. 4A
PMID:28366743	figur 3A
PMID:28366743	figur 3A
PMID:28366743	figure 4C. synchronous mitotic cells
PMID:28366743	supp S1h
PMID:28366743	(Figure 1F
PMID:28366743	Figures 1FandS1H).
PMID:28366743	figure 4D. s
PMID:28366743	Figure S1e
PMID:28366743	Fig S3B
PMID:28366743	Figure S3B
PMID:28366743	Figure S3B
PMID:28366743	Figure S3B
PMID:28366743	Figure S3B
PMID:28366743	Figure S3B
PMID:28366743	Figure S3B
PMID:28366743	Fig. 2C/D, S2B,
PMID:28366743	Fig. 2C/D, S2B,
PMID:28366743	Figure 4D
PMID:28366743	Figure 4D
PMID:28366743	fig 3.a
PMID:28366743	fig 3a
PMID:28366744	Fig 1 A (checkpoint assay)
PMID:28366744	Deletion increases levels of mitotic checkpoint complex associated with the anaphase promoting complex in mitosis.
PMID:28366744	Required for mitotic checkpoint complex binding to the anaphase promoting complex.
PMID:28366744	vw I changed the genotype/ Fig 1 A (checkpoint assay)
PMID:28366744	vw; I changed the genotype here
PMID:28366744	"vw changed term from ""reduced ubiquitin ligase activity"""
PMID:28366744	Fig 1 A (checkpoint assay)
PMID:28366744	Fig 1 A (checkpoint assay)
PMID:28366744	Fig 1 A (checkpoint assay)
PMID:28366744	Fig 1 A (checkpoint assay)
PMID:28366744	fig 1 c
PMID:28366744	fig 1 c
PMID:28366744	fig S1
PMID:28366744	fig 2a
PMID:28366744	fig 1 c
PMID:28366744	fig 2a
PMID:28366744	fig 2a
PMID:28366744	fig 2a
PMID:28366744	figure 2b
PMID:28366744	Figures 3A and 3B
PMID:28366744	(Figure 3B).
PMID:28366744	(Figure 3A).
PMID:28366744	Figure 3A
PMID:28366744	(Figure 3A).
PMID:28366744	(Figure 3B).
PMID:28367989	S2P form
PMID:28377506	fig4
PMID:28377506	fig4
PMID:28377506	"fig 7: ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU"""
PMID:28377506	"fig 7: ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU"""
PMID:28377506	fig4D
PMID:2837764	assayed using mammalian proteins
PMID:28388826	data not shown
PMID:28388826	data not shown
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	uses histone H3 RNA immunoprecipitation
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	sequencing of Ago1-bound siRNA
PMID:28404620	uses Pol ii-RNA immunoprecipitation
PMID:28404620	also uses Pol ii-RNA immunoprecipitation
PMID:28404620	uses Pol ii-RNA immunoprecipitation
PMID:28404620	also uses Pol ii-RNA immunoprecipitation
PMID:28410370	stronger phenotype when crossed to fus1∆
PMID:28410370	wider localization at the shmoo tip
PMID:28410370	wider localization
PMID:28410370	phenotype more severe when crossed to fus1∆
PMID:28410370	Wider localization at shmoo tip
PMID:28410370	wider distribution along shmoo tip
PMID:28410370	wider localization
PMID:28410370	wider localization
PMID:28410370	Strong phenotype in crosses with fus1∆.
PMID:28410370	more severe phenotype when crossed to fus1delta
PMID:28410370	more severe phenotype when crossed to fus1∆
PMID:28410370	wider localization
PMID:28410370	wider localization
PMID:28432181	snRNA/ complementation of yeast pus1
PMID:28438891	type 2 cohesion (still bound)
PMID:28438891	type 2 cohesion (still bound) MITOTIC
PMID:28438891	MIOTOTIC
PMID:28438891	Fig 3C
PMID:28438891	Fig EV5
PMID:28438891	Fig 4E
PMID:28438891	Figure 5 B (exacerbates )
PMID:28438891	Fig 1D
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 3C
PMID:28438891	Fig 3C
PMID:28438891	Fig 3C
PMID:28438891	Fig 3C
PMID:28438891	fig 4
PMID:28438891	fig 7
PMID:28438891	Fig 5A
PMID:28438891	required for Rad21 dephosphorylation
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1C
PMID:28438891	Fig 1D
PMID:28467824	Mutations that are predicted to impair middle module sta- bility also lead to a general decrease in RNA synthesis (Extended Data Fig. 4d), showing that the middle module is globally required for transcription. (I use txn rather than RNA level because we know it is transcription)
PMID:28467824	Mutations that are predicted to impair middle module sta- bility also lead to a general decrease in RNA synthesis (Extended Data Fig. 4d), showing that the middle module is globally required for transcription. (I use txn rather than RNA level because we know it is transcription)
PMID:28469148	ura1 met5
PMID:28469148	ade6 arg1
PMID:28469148	lys3 ura1
PMID:28469148	ura1 met5
PMID:28469148	lys3 ura1
PMID:28469148	ura1 met5
PMID:28469148	lys3 ura1
PMID:28469148	ura1 met5
PMID:28469148	ura1 met5
PMID:28469148	lys3 ura1
PMID:28469148	lys3 ura1
PMID:28469148	lys3 ura1
PMID:28475874	in response to a single blocked replisome
PMID:28475874	in response to a single blocked replisome
PMID:28475874	In the absence of Rad51, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging
PMID:28475874	In the absence of Rad52, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging.
PMID:28475874	in response to a single blocked replisome
PMID:28475874	in response to a single blocked replisome
PMID:28475874	in response to a single blocked replisome
PMID:28475874	in response to a single blocked replisome
PMID:28476936	Fig4A, C, E, F no supplements added
PMID:28476936	Fig S1A, Fig1
PMID:28476936	Fig S1A, Fig1B,C
PMID:28476936	Fig 2, Fig3, Fig4B
PMID:28476936	Fig 2
PMID:28476936	Fig 2
PMID:28476936	Fig 2
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig 5 supplements added
PMID:28476936	Fig5 supplements added
PMID:28476936	FigS5 in this situation gad8 overexpression is unable to promote growth i. This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	FigS5 in this situation psk1 only causes a small increase in cell length increase compared to Sck2 . This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	Fig 2
PMID:28476936	Fig 2
PMID:28476936	Fig 2
PMID:28476936	Fig 2
PMID:28476936	FigS5 in this situation Sck1 only causes a small increase in cell length increase compared to Sck2 . This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	Fig S4A cell growth at G2/M1 arrest is dependent on transcription. no supplements added
PMID:28476936	Fig4D no supplements added
PMID:28479325	We find that the size dependent expression of Cdc25 does not require the 5′ UTR of its transcript, showing that this mechanism of translational regulation is not necessary for size dependent expression (Figure S3A).
PMID:28479325	mRNA quantitation was obtained by Nanostring experiments.
PMID:28479325	normal cell size. homeostasis
PMID:28479325	We propose that the size-dependent expression of the cdc25 transcript is the mechanism that allows cells to divide at a particular size, but it is not the mechanism which regulates what that size is.
PMID:28479325	During G2, the concentration of Cdc25 increases about 2 fold (Figure 1A)
PMID:28479325	arelatively constant concentration during G2, as previously observed [2mRNA quantitation was obtained by Nanostring experiments.
PMID:28479325	mRNA quantitation was obtained by Nanostring experiments.
PMID:28481910	same as cdc20-M10 alone
PMID:28481910	BrdU incorporation
PMID:28481910	BrdU incorporation
PMID:28481910	BrdU incorporation
PMID:28481910	BrdU incorporation
PMID:28497540	fig 1B
PMID:28497540	(Fig. 2B)
PMID:28497540	fig S2A
PMID:28497540	fig 4A
PMID:28497540	fig 1B, 1D
PMID:28497540	fig 1B
PMID:28497540	fig 1C
PMID:28497540	fig 1B
PMID:28497540	Fig. 3A,B
PMID:28497540	mph1Δ cells (Fig. 2B)
PMID:28497540	fig 1F
PMID:28497540	fig 1 B
PMID:28497540	fig 1C
PMID:28497540	S4
PMID:28497540	mph1Δ cells (Fig. 2B)
PMID:28497540	fig 1D
PMID:28497540	Fig. 5C
PMID:28497540	4B
PMID:28497540	fig 5
PMID:28497540	fig 5C
PMID:28497540	fig 4A
PMID:28497540	fig 5
PMID:28497540	Fig. E
PMID:28497540	Fig. S5
PMID:28497540	Fig. S5
PMID:28497540	fig 5
PMID:28497540	Fig. 5C
PMID:28497540	Fig 3C
PMID:28497540	Fig 3C
PMID:28497540	`s4
PMID:28497540	during interphase (not usually located then)
PMID:28497540	fig 2b
PMID:28497540	RECRUITS
PMID:28497540	Fig 2b
PMID:28497540	recruits
PMID:28497540	fig 1 EF
PMID:28497540	fig 1F
PMID:28497540	fig 1E
PMID:28513584	cut7D pkl1D ase1D lethal
PMID:28513584	Fig. 1
PMID:28513584	Fig. 2
PMID:28513584	Fig. 3
PMID:28513584	Fig. 3
PMID:28513584	Fig. 3
PMID:28513584	Fig. 3
PMID:28513584	Fig. 3
PMID:28513584	Fig. S4
PMID:28513584	Fig. S4
PMID:28513584	Fig. S3E
PMID:28513584	Fig. S3D and the fact that is required for bipolar spindle formation
PMID:28513584	cut7D pkl1D cls1off lethal
PMID:28513584	cut7D pkl1D klp9off does not elongate during anaphase B, cut7D pkl1D klp9D lethal, deleting all other kinesins except klp9 did not affect elongation after removing cut7
PMID:28513584	Fig. 1
PMID:28513584	Fig. S1
PMID:28513584	Fig. S1 Not really abnormal, should be just bipolar
PMID:28513584	Fig. 2
PMID:28513584	Fig. 2
PMID:28513584	Fig. 2 (main text)
PMID:28513584	Fig. 2
PMID:28513584	Fig. 2
PMID:28513584	Main text (Figure S2 seems wrongly labelled)
PMID:28513584	Fig. 2
PMID:28515144	Abolished ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	Reduced ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	Reduced ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28533364	Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B–D) through specific interaction between its YAG activation motif and Dcp2.
PMID:28533364	Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B–D) through specific interaction between its YAG activation motif and Dcp2.
PMID:28541282	fig 5d,e. Only in presence of cid14/16 does rrp6 degrade ago1 bound rnas. This mechanism protects the genome from uncontrolled small RNAs
PMID:28541282	see comment on cid14
PMID:28545058	Fig1D
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1C
PMID:28545058	Fig1C rpn15 is called dss1 in this paper
PMID:28545058	Fig2 A,B
PMID:28545058	Fig2 A,B
PMID:28545058	FigS1C,D
PMID:28545058	Fig2A
PMID:28545058	Fig3A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B
PMID:28545058	Fig1A,B In the paper this strain is called dss1
PMID:28545058	Fig1 D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	Fig1D
PMID:28545058	data not shown
PMID:28545058	Fig1A,B
PMID:28545058	Fig3B Table S4 mass spec used to show that there is bulk accumulation of nuclear localised protein rather than a few specific proteins
PMID:28545058	Fig2A, B
PMID:28545058	Fig3A
PMID:28545058	nuclear accumulation of mRNA ************S5 Table microarrays used
PMID:28545058	Fig2A
PMID:28545058	Fig2A
PMID:28545058	Fig 2A
PMID:28545058	Fig4 A,B
PMID:28545058	Fig4 A,B
PMID:28545058	Fig 4A
PMID:28545058	Fig 4C,D
PMID:28545058	Fig 4c
PMID:28545058	Fig4C cut6-621 partial suppresses the increased NC ratio of rae1-167 so not sure whether increased NC ration is the correct term
PMID:28545058	Fig 4D
PMID:28545058	Fig 4D
PMID:28552615	(Fig. S1B)
PMID:28552615	(Fig. S1C)
PMID:28552615	(Fig. S1C)
PMID:28552615	(Fig. S1C)
PMID:28552615	(Fig. S1E)
PMID:28552615	s2e
PMID:28552615	(Fig. 2h)
PMID:28552615	(Fig. 2h)
PMID:28552615	(Fig. 2h)
PMID:28552615	(Fig. 2i)
PMID:28552615	(Fig. 3a)
PMID:28552615	(Fig. S1C, 3A)
PMID:28552615	3F and G
PMID:28552615	(Fig. S1B)
PMID:28552615	(Fig. S1B)
PMID:28552615	(Fig. S1B)
PMID:28552615	(Fig. S1C)
PMID:28552615	"Is this translocase activaty or ""dislocase activity?"" Fig 5 (val, added substrate top2, this term will probably merge into displacement activityu). GO:0061995"
PMID:28552615	(Fig. S1C)
PMID:28552615	(Fig. S1C)
PMID:28552615	(Fig. S1C)
PMID:28572514	vw: made more specific, during copper starvation
PMID:28572514	fig7
PMID:28572514	fig7
PMID:28572514	Fig. 7
PMID:28572514	vw: moved down to new FYPO:0006212 before germ outgrowth, during copper starvation
PMID:28572514	fig7
PMID:28572514	vw: changed to match previous session terms RNA ...from cuf1􏰀 mutant spores showed loss of copper starvation-dependent induction of ctr4􏰁 and ctr5􏰁 gene expression, indicating that the copper-dependent reg ulation of ctr4􏰁 and ctr5􏰁 mRNAs required Cuf1 during germination and outgrowth.
PMID:28572514	see comment above
PMID:28572514	see comment above
PMID:28572514	vw: moved down to new FYPO:0006212
PMID:28572514	vw: moved down to new FYPO:0006212 before germ outgrowth, during copper starvation
PMID:28572514	fig7
PMID:28572514	fig 9
PMID:28572514	fig5
PMID:28572514	fig 6
PMID:28572514	fig 6
PMID:28586299	Figure 4A; decreased frequency of deletions and gene conversions at direct repeat recombination reporter
PMID:28586299	Figure 4C; increased frequency of deletions at direct repeat recombination reporter
PMID:28586299	Figure 2; decreased frequency of gene conversions but unaltered frequency of deletions at direct repeat recombination reporter; deletions in a rad51∆ mutant depend on Rad52
PMID:28586299	Figure 4B; decreased frequency of deletions at direct repeat recombination reporter
PMID:28586299	Figure 4C; decreased frequency of gene conversions at direct repeat recombination reporter
PMID:28600551	fig 1d
PMID:28600551	fig 2a
PMID:28600551	fig 2a
PMID:28600551	fig 4
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 2e
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 4
PMID:28600551	fig 4
PMID:28600551	fig 4
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 2a
PMID:28600551	fig 3c
PMID:28600551	fig 2a
PMID:28600551	fig 2a
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 4
PMID:28600551	fig 4
PMID:28600551	fig 4
PMID:28600551	fig 4
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 5
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 3d
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 - They say they use YES in methods and fig2
PMID:28600551	fig 1 c
PMID:28600551	I can never remember why e.g. sodium chloride isn't a child to salt stress
PMID:28600551	fig 1
PMID:28600551	fig 1
PMID:28600551	fig 1d
PMID:28600551	fig 1d
PMID:28600551	fig 5
PMID:28600551	fig 3d
PMID:28600551	fig 2c
PMID:28600551	fig 2c
PMID:28600551	fig 2d
PMID:28600551	fig 2d
PMID:28600551	fig 2e
PMID:28619713	Fig. S1 B
PMID:28619713	Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB inser- tion before the cell even enters mitosis.fig6
PMID:28619713	rename term https://github.com/geneontology/go-ontology/issues/14887 Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB inser- tion before the cell even enters mitosis.fig6
PMID:28619713	fig 6 C
PMID:28619713	Fig. S1 B
PMID:28619713	fig 6 C
PMID:28631612	"""poison"" product of shorter alternative transcript;assayed by expressing S.k. ortholog in S.p."
PMID:28631612	"""antidote"" product of longer alternative transcript; assayed by expressing S.k. ortholog in S.p."
PMID:28640807	Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1.
PMID:28640807	aerobic conditions
PMID:28640807	aerobic conditions
PMID:28640807	aerobic conditions
PMID:28640807	aerobic conditions
PMID:28640807	aerobic conditions
PMID:28640807	aerobic conditions
PMID:28640807	aerobic conditions
PMID:28640807	2 mM Glutathione restores aerobic growth.
PMID:28640807	2 mM Glutathione restores aerobic growth.
PMID:28640807	Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1.
PMID:28652406	Atf1.7M-HA are constitutively bound to the gpd1 and hsp9 promoters both before and after stress
PMID:28652406	As shown in Fig. 2B, the capacity of HA-Atf1.10M to activate hsp9 and gpd1 after stress imposition was abolished in the absence of Sty1,
PMID:28652406	allows stress-dependent activation of ctt1 and srx1 to the same extent as wild-type cells; however, it constitutively induces expression of gpd1 and hsp9 (Fig. 2A).
PMID:28652406	allows stress-dependent activation of ctt1 and srx1 to the same extent as wild-type cells; however, it constitutively induces expression of gpd1 and hsp9 (Fig. 2A).
PMID:28652406	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain atf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	2A,cells expressing the hypophosphorylation mutant HA-Atf1.10M are not able to fully trigger the ctt1 and srx1 genes after H2O2 stress
PMID:28652406	expression of HA-Atf1.10D fully suppressed all stress defects of cells lacking Sty1 (Fig. 2C).
PMID:28652406	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain atf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain atf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	atf1 expressing the mutant named HA-Atf1.6M, lacking sites 5 to 10 in Atf1, was as sensitive to growth on peroxide-containing plates as cells lacking Atf1.
PMID:28652406	Concomitantly, although expression of HA-Atf1.10M was not able to suppress the sensitivity to peroxides of strain atf1 (supplemental Fig. S1C and Fig. 1G), expression of HAAtf1.10D alleviated this phenotype (Fig. 1G).
PMID:28652406	Importantly, expression of the phospho-mimicking HA-Atf1.10D (Fig. 2B) or HA-Atf1.6D (Fig S3, C and D) bypasses the requirement for a MAP kinase in the transcription process, which questions the direct participation of the kinase in Pol II initiation and/or elongation.
PMID:28652406	Strains expressing wild-type Atf1 or Atf1.7M or Atf1.7D mutants displayed the same patterns of tolerance to peroxides and activation of stress genes as the constitutive amino-terminally tagged versions (supplemental Fig S4, B and C).
PMID:28652406	ditto
PMID:28652406	ditto
PMID:28652406	ditto
PMID:28652406	ditto
PMID:28652406	vw, I deleted Caludias annotation by mistake when comparing to the older partially completed session by Laura, so adding back !
PMID:28652406	ditto
PMID:28652406	whether Atf1 binding to DNA is dependent on the presence of Pcr1; as shown in Fig. 4D, Atf1-GFP is not recruited to DNA in pcr1 cells, with the only exception of srx1
PMID:28652406	expression of the Sty1-independent Atf1.7D-HA mutant cannot bypass the absence of Pcr1, as shown by the lack of transcription of stress genes (Fig. 4C).
PMID:28652406	ditto
PMID:28652406	ditto
PMID:28652406	that Pap1 is dispensable for the activation of gpd1 and hsp9 but required for ctt1 and srx1 (Fig. 5A)
PMID:28652406	ditto
PMID:28652406	Regarding the role of Pap1 and Atf1 at these genes, ChIP analysis indicates that the stress-dependent recruitment of Atf1 to ctt1 and srx1 promoters is dependent on Pap1 (Fig. 5C).
PMID:28652406	Atf1 is constitutively bound to srx1 and ctt1 in strain trr1....
PMID:28652406	....whereas it is never recruited to these promoters in cells expressing Pap1.C523D (Fig. 5D).
PMID:28652406	As shown in Fig. 2B, the capacity of HA-Atf1.10M to activate hsp9 and gpd1 after stress imposition was abolished in the absence of Sty1,
PMID:28656962	These data suggest that Bhd1 and Ypt71 (but not Ypt7) functionally interact and, in agreement with the mammalian cell data, negatively regulate TORC1 activity in response to amino-acid deprivation.
PMID:28656962	These data suggest that Bhd1 and Ypt71 (but not Ypt7) functionally interact and, in agreement with the mammalian cell data, negatively regulate TORC1 activity in response to amino-acid deprivation.
PMID:28656962	figure 5 b
PMID:28656962	figure 5 b
PMID:28656962	figure 5 b
PMID:28656962	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7).
PMID:28656962	We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7).
PMID:28656962	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28659415	Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo.
PMID:28659415	Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo.
PMID:28667014	idn1Δ loz1Δ – enhances gluconate accumulation when compared to idn1Δ cells LC-MS/MS and enzymatic assays were used to measure gluconate accumulation in wild-type, idn1Δ
PMID:28667014	LC-MS/MS
PMID:28667014	LC-MS/MS and enzymatic assays were used to measure gluconate accumulation in wild-type and idn1Δ
PMID:28674280	same as snf22delta alone
PMID:28674280	same as snf22delta alone
PMID:28674280	same as snf22delta alone
PMID:28765164	fig2e
PMID:28765280	Fig 1B
PMID:28765280	figure 1B
PMID:28765280	Fig 1A
PMID:28765280	figure 2
PMID:28765280	we could probly go to increased degradation because of the bortezombin exp
PMID:28765280	figure 1D
PMID:28765280	Fig. 7A
PMID:28765280	Fig. 7A
PMID:28765280	Fig 7A
PMID:28765280	Fig 7A
PMID:28765280	(Fig. 6G).
PMID:28765280	6 ef
PMID:28765280	Fig 6C
PMID:28765280	Fig 6C
PMID:28765280	Fig 6A
PMID:28765280	3b
PMID:28765280	3b
PMID:28765280	Fig 1B
PMID:28765280	Fig 2A
PMID:28765280	Fig. 1EF
PMID:28771613	1E
PMID:28771613	1E
PMID:28771613	1E
PMID:28771613	unfortunately no direct binding data, but physical interactions have been shown in other organisms
PMID:28771613	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C),
PMID:28771613	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C),
PMID:28771613	2B
PMID:28775153	Fig4D. DAPI staining. I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known)
PMID:28775153	Fig4C. DAPI staining. I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known)
PMID:28775153	Fig4B. DAPI staining. I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known)
PMID:28784611	fig 5 B CR slid- ing events no longer occurred in myo51Δ efr3Δ
PMID:28784611	Figure 3E
PMID:28784611	Figure 1B
PMID:28784611	phospholipid biosynthesis?
PMID:28784611	Fig. S1, C and D)
PMID:28784611	Fig 2 A-C
PMID:28784611	Fig 2 A-C
PMID:28784611	Fig 2 A-C
PMID:28784611	Fig. S2 D
PMID:28784611	Fig 3 A (in table, data not shown)
PMID:28784611	fig 5 B CR slid- ing events no longer occurred in myo51Δ efr3Δ
PMID:28784611	Figure 1A
PMID:28784611	fig 1 A&B
PMID:28784611	fig 5A
PMID:28784611	fig S2C
PMID:28784611	Fig 1B
PMID:28784611	Figure 1B
PMID:28784611	"i requested reduced plasma membrane PIP issues/3117 GFP-2xPH(Plc delta) ""localization The PI(4,5)P2 sensor GFP-2×PH(PLCδ) (Stefan et al., 2002) was reduced at the cell cortex and the division site in efr3Δ compared with WT (Fig. 1 D), indicating that PIP PM abundance is reduced in efr3Δ"""
PMID:28784611	Figure 3C
PMID:28784611	Figure 3B
PMID:28784611	Figure 3D
PMID:28784611	naintenence
PMID:28784611	Figure S1D
PMID:28784611	Figure S1C
PMID:28784611	Figure S2A-B
PMID:28784611	Figure S2A-B
PMID:28784611	Figure S2E
PMID:28784611	Figure 1C
PMID:28784611	Figure 1C
PMID:28784611	Fig. S1, C and D)
PMID:28806726	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
PMID:28806726	untreated (table S1)
PMID:28806726	replication forks slow independently of intra-S checkpoint (fig. 6)
PMID:28806726	inhibition of origin firing requires intra-S checkpoint (fig. 5)
PMID:28806726	inhibition of origin firing requires intra-S checkpoint (fig. 5)
PMID:28806726	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
PMID:28806726	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
PMID:28806726	inhibition of origin firing requires intra-S checkpoint (fig. 5)
PMID:28811350	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28811350	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28811350	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28811350	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated from MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28821619	generated by MMS mutagenesis
PMID:28825727	Cnd3 depletion following promoter shut-off and auxin-induced degron activation
PMID:28825727	Cnd3 depletion following promoter shut-off and auxin-induced degron activation
PMID:28825727	Supplementary Figs. 1b,f and 4a–c Cnd3 depletion following promoter shut-off and auxin-induced degron activation
PMID:28825727	(vw made more specific) Hi-C Supplementary Figs. 1b,f and 4a–c
PMID:28825727	fig 2b hi-C difference assay
PMID:28825727	hi C????? Supplementary Figs. 1b,f and 4a–c
PMID:28825727	hic and 3C pcr fig 2d increased mitotic intra centromere connection
PMID:28825727	fig 3 hi-C
PMID:28827290	fig 2
PMID:28827290	fig 2B
PMID:28827290	fig 5
PMID:28827290	fig 6
PMID:28827290	fig 6
PMID:28827290	fig 6
PMID:28827290	fig 6
PMID:28827290	fig 6
PMID:28827290	fig 6
PMID:28827290	fig 7
PMID:28827290	fig 8
PMID:28827290	fig 1B
PMID:28827290	fig 1B
PMID:28827290	fig 2
PMID:28827290	figure 2B
PMID:28827290	fig 2C
PMID:28827290	wt 68% fig 2C
PMID:28827290	fig 2D
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 3
PMID:28827290	fig 4
PMID:28827290	fig 4
PMID:28827290	fig 4
PMID:28827290	fig 5
PMID:28827290	fig 5
PMID:28841135	mRNA co-immunoprecipitated with ribosomes
PMID:28882432	fig 3
PMID:28904333	especially at centromere; also at other regions where Ino80 complex normally binds
PMID:28904333	30 degrees
PMID:28904333	especially at centromere; also at other regions where Ino80 complex normally binds
PMID:28904333	25 degrees
PMID:28914606	Furthermore, the FRET signal of mCherry-Cdc15 with two other F-BAR domains (GFP-Imp2 and GFP-Rga7) indicates that all three cytokinesis F-BARs are packed in close proximity upon the membrane
PMID:28914606	Furthermore, the FRET signal of mCherry-Cdc15 with two other F-BAR domains (GFP-Imp2 and GFP-Rga7) indicates that all three cytokinesis F-BARs are packed in close proximity upon the membrane
PMID:28914606	A strong FRET signal between mCherry-Cdc15 and Acyl-GFP is consistent with the binding of Cdc15’s F-BAR to anionic phospholipids within the plasma membrane
PMID:28924043	Cdr1-K41A remains in nodes; Cdr1+ not tagged
PMID:28924043	Cdr1-K41A remains unphosphorylated; Cdr1+ not tagged
PMID:28924043	combination of in vitro kinase assay and mutant phenotypes
PMID:28924043	Cdr2 does not exit nodes (unlike Cdr1) upon osmotic stress
PMID:28934464	fig 3E
PMID:28934464	I replaced GO:0090579 dsDNA loop formation as per https://github.com/geneontology/go-annotation/issues/3610
PMID:28934464	5D a bit tenuous but we don't have this annotated..
PMID:28934464	5D a bit tenuous but we don't have this annotated..
PMID:28934464	fig 3E
PMID:28934464	fig 3D
PMID:28934464	fig 3D
PMID:28934464	fig 3C
PMID:28934464	fig 3C
PMID:28934464	fig 3C
PMID:28934464	fig 3C
PMID:28934464	fig 3B
PMID:28934464	fig 3B
PMID:28934464	fig S2D
PMID:28944093	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28944093	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28944093	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28944093	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28947618	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	Intron-Specific pre-mRNA Splicing
PMID:28947618	Fig 8B in spliceosome
PMID:28947618	(Fig 7A)
PMID:28947618	(Fig 7A)
PMID:28947618	(Fig 7A)
PMID:28947618	Fig 4A
PMID:28947618	Fig 3E LysSde2-C (pro-obo/term-requests/119/), is N-end rule substrate
PMID:28947618	Fig 3E (N-end rule pathway substrate) assayed_using(LysSde2-C)
PMID:28947618	Fig 2D
PMID:28947618	Fig 2D
PMID:28947618	Fig 2A &B
PMID:28947618	Appendix Fig S2A
PMID:28947618	fig 1B
PMID:28947618	fig 1B
PMID:28947618	assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02
PMID:28947618	(endo) mutant does not cleave Sde2 precursor
PMID:28947618	(endo) mutant does not cleave Sde2 precursor
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	normal processing, complements partially sde2Δ
PMID:28947618	normal processing, complements partially sde2Δ
PMID:28947618	normal processing, complements partially sde2Δ
PMID:28947618	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig 5B; Appendix Fig S5A and B
PMID:28947618	Fig EV2B processing defective, does not complement sde2Δ
PMID:28947618	Fig EV2B processing defective, does not complement sde2Δ
PMID:28947618	Fig EV2B processing defective, does not complement sde2Δ
PMID:28947618	Fig EV2B processing defective, does not complement sde2Δ
PMID:28947618	does not grow at high temperature, defective pre-mRNA splicing, assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02
PMID:28947618	column_17 Sde2UBL
PMID:28947618	Intron-Specific pre-mRNA Splicing
PMID:28947618	decreased cell population growth at high temperature
PMID:28947618	does not complement sde2Δ, defective in telomeric silencing and genome stability
PMID:28947618	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	normal processing, complements partially sde2Δ
PMID:28947618	processing defective, does not complement sde2Δ
PMID:28947618	fig 1 D does not complement sde2Δ
PMID:28947618	fig 1 D complements partially sde2Δ
PMID:28947618	normal processing, protein very stable, does not complement sde2Δ
PMID:28947618	normal processing, protein unstable, complements partially sde2Δ
PMID:28947618	normal processing, protein unstable, complements partially sde2Δ
PMID:28947618	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	normal processing, complements partially sde2Δ
PMID:28947618	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	Fig 3C) decreased cell growth, normal processing, protein very stable, complements partially sde2Δ; over expression causes growth defect in hub1-1 strain, defective in telomeric silencing and genome stability
PMID:28947618	normal processing, complements partially sde2Δ
PMID:28947618	processing defective, does not complement sde2Δ
PMID:28947618	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	normal processing, protein unstable,complements partially sde2Δ
PMID:28947618	Fig EV2B normal processing, complements sde2Δ
PMID:28947618	Fig EV2B normal processing, complements sde2Δ
PMID:28947618	processing defective, does not complement sde2Δ
PMID:28947618	reduced processing, complements partially sde2Δ
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	Fig. S3
PMID:28974540	fig 1b
PMID:28974540	Fig. S2 B
PMID:28974540	fig1
PMID:28974540	5A
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 5 D-G nuclear envelope
PMID:28974540	fig 5 D-G nuclear envelope
PMID:28974540	fig 5b
PMID:28974540	fig 5b nuclear envelope
PMID:28974540	5A
PMID:28974540	(Fig. 4 G and see the Ubiquitin pull-down section of Materials and methods).
PMID:28974540	fig 4e
PMID:28974540	fig 4c
PMID:28974540	fig 4a
PMID:28974540	fig 3 G
PMID:28974540	fig 3
PMID:28974540	fig 3
PMID:28974540	added affected genes as extensions fig 3 E
PMID:28974540	added affected genes as extensions fig 3 E
PMID:28974540	Fig. S3 I additive, do we know %?
PMID:28974540	Fig. S3, G and H
PMID:28974540	s3 E
PMID:28974540	s3 C
PMID:28974540	fig S2
PMID:28974540	fig 1
PMID:28974540	fig 1C
PMID:28974540	fig 1a + others
PMID:28974540	vw: moved down to elongated (update fypo?) fig 1e
PMID:28974540	Fig. S2 A & 1E
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	added affected genes as extensions fig 3 A-C
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 2E
PMID:28974540	fig 6
PMID:28974540	fig 6
PMID:28974540	fig 6
PMID:28976798	fig1
PMID:28976798	fig 1 D
PMID:28976798	fig1
PMID:28976798	fig1
PMID:28976798	fig1
PMID:28977643	mhf1-L78R
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	affects tRNA-Ser UGA/CGA; suggests tRNA-Ser UGA/CGA misfolding due to decreased dimethylation of G26, but modification not assayed directly for this tRNA
PMID:28977649	affects tRNA-Ser UGA/CGA; suggests tRNA-Ser UGA/CGA misfolding due to decreased dimethylation of G26, but modification not assayed directly for this tRNA
PMID:28977649	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28977649	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28977649	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA
PMID:28977649	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28982178	40 fold less
PMID:29021344	(Supplemental Figure S1A).
PMID:29021344	Figure 1F
PMID:29021344	Figure 4A and Supplemental Figure S4
PMID:29021344	Figure 4A and Supplemental Figure S4
PMID:29021344	Figure 4A and Supplemental Figure S4
PMID:29021344	Figure 4A and Supplemental Figure S4
PMID:29021344	Figure 4B
PMID:29021344	Figure S5D
PMID:29021344	Figure S5D
PMID:29021344	fig3C
PMID:29021344	Figure 2E
PMID:29021344	Figure 2G
PMID:29032152	fig2 b,c
PMID:29032152	Table 3
PMID:29032152	fig 2
PMID:29032152	Table 3
PMID:29032152	Table 3
PMID:29032152	Table 3
PMID:29032152	Table 3
PMID:29032152	fig 4
PMID:29032152	fig 4
PMID:29032152	inferred from combined experiments
PMID:29032152	fig 4
PMID:29032152	fig 3b
PMID:29032152	fig2
PMID:29032152	fig 1
PMID:29032152	fig 2a
PMID:29032152	fig 3b
PMID:29032152	fig 3b
PMID:29032152	fig 3b
PMID:29032152	fig 1, 3b
PMID:29032152	fig 3b
PMID:29032152	fig 3e
PMID:29032152	fig 3e
PMID:29032152	fig 3e
PMID:29032152	fig 2
PMID:29032152	fig4
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig6
PMID:29079657	fig2 and supp table
PMID:29079657	To conclude, upon nutrient starvation, TORC2 functions as both an activator and an inhibitor of sexual differentiation, the latter being mediated by Taf12 phosphorylation.
PMID:29079657	fig1
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:29079657	fig2 and supp table
PMID:2908246	mild over expression of cdc2+ on multi copy plasmid rescues the cdc13-117 ts phenotype
PMID:2908246	mild over expression of cdc13+ on multi copy plasmid pYep13 causes slow growth
PMID:2908246	mild over expression of cdc13+ on multi copy plasmid pYep13 rescues the cdc13-117 ts phenotype. .
PMID:2908246	Fig 3
PMID:2908246	Fig 3
PMID:29084823	Fig3C
PMID:29084823	Fig6A
PMID:29084823	Fig6A
PMID:29084823	Fig6A
PMID:29084823	Fig5E
PMID:29084823	Fig5E
PMID:29084823	Fig5C,D
PMID:29084823	Fig5C,D
PMID:29084823	Fig6A,B
PMID:29084823	Fig6 A,B
PMID:29084823	Fig6A,B
PMID:29084823	Fig6A,B
PMID:29084823	Fig6A,B
PMID:29084823	Fig7A shows that puc1delta shows increased mating efficiency at nitrogen levels which suppress mating in wild type cells
PMID:29084823	RNA
PMID:29084823	Fig 5B, construct 3
PMID:29084823	Fig4A,B about 10%? of Zfs1 is phosphorylated during vegetative growth
PMID:29084823	Fig4D Sup Fig3 the hyperphosphoryated zfs1 (3rd band higest). Gad8 is required to hyperphosphorylate zfs1. In Fig4C they also show that TOR inhibition by Torin stimulates hyerphosphorylation of Zfs1
PMID:29084823	Fig4A,B Zfs is hyperphosphorylated in response to nitrogen depletion
PMID:29084823	Fig3C, Fig7A shows that zfs1delta shows high mating efficiency at nitrogen levels which suppress mating in wild type cells wild type cells
PMID:29084823	Fig6A,B
PMID:29084823	Fig3C
PMID:29084823	Fig3B varying the copy number of pJKpuc1+ leads to varying levels of sporulation efficiency in wild type cells increased puc1 mRNA causes reduced mating efficiency
PMID:29084823	Fig3A deletion of puc1 increases mating efficiency of zfs1 delta to WT
PMID:29084823	Fig3A
PMID:29084823	Fig 2D, E, Sup Fig 2
PMID:29084823	Fig 2B,C fig6a
PMID:29084823	Figure 1C
PMID:29084823	Figure 1C
PMID:29084823	"jack suggested ""up regulation of protein binding RNAs because normally bound by zfs1"" I'm using this to make the sequestering GO annotation."
PMID:29084823	Figure 1A Sup Fig1
PMID:29084823	Fig6A
PMID:29084823	Fig6A
PMID:29084823	Fig5E
PMID:29084823	Fig5E
PMID:29084823	Fig3A deletion of cig2 does not rescue mating efficiency zfs1delta
PMID:29084823	Fig3A deletion of cig1 does not rescue mating efficiency of zfs1 delta
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29109278	mat3M::ura4+
PMID:29109278	tel2L::ura4+
PMID:29109278	otr1R(SphI)::ura4+
PMID:29123917	S10 E and F
PMID:29123917	Later stage of meiotic prophase, observed by co-localisation with Taz1
PMID:29123917	Later stage of meiotic prophase, observed by co-localisation with Taz1
PMID:29123917	fig6
PMID:29134248	Fusion domain
PMID:29134248	plasma membrane fusion during conjugation
PMID:29134248	plasma membrane fusion during conjugation
PMID:29136238	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggest- ing that phosphorylation of H3Y41 counteracts the interac- tion of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	Fig4
PMID:29136238	Fig4
PMID:29136238	Fig4/5
PMID:29136238	Fig4/5
PMID:29136238	fig7
PMID:29136238	Fig1
PMID:29136238	Fig1
PMID:29136238	Fig2
PMID:29136238	Fig2
PMID:29136238	Fig2
PMID:29136238	Fig2
PMID:29136238	Fig2
PMID:29136238	Fig3
PMID:29136238	Fig3
PMID:29136238	Fig3
PMID:29136238	Fig3
PMID:29136238	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggest- ing that phosphorylation of H3Y41 counteracts the interac- tion of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggest- ing that phosphorylation of H3Y41 counteracts the interac- tion of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29149597	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29167352	~30% of the double mutant cells exhibited the monopolar spindle phenotype.
PMID:29167352	(Fig. 1C
PMID:29167352	28 celcius
PMID:29167352	(Fig. 1C 28 Celcius
PMID:29167352	(Fig. 1C
PMID:29167352	(Fig. 1C
PMID:29167352	(Fig. 1C
PMID:29167352	(Fig. 1C
PMID:29167352	fig 4. Klp2 is not required, but acts collaboratively with Pkl1, in anchoring the spindle microtubule to the mitotic SPB
PMID:29167352	often in a punctate manner
PMID:29167439	limit subtelomeric DNA amplification in G0
PMID:29167439	increase with telomere shortening and time in quiescence
PMID:29167439	require for subtelomeric DNA amplification in G0
PMID:29167439	increase with telomere shortening and time in quiescence
PMID:29167439	Require for subtelomeric DNA amplification in G0
PMID:29180432	fig 5f
PMID:29180432	fig 2G
PMID:29180432	fig 2G
PMID:29180432	figure 3
PMID:29180432	fig6
PMID:29180432	increased duration of metaphase Fig. 5E
PMID:29180432	Fig. 5 B and D
PMID:29180432	fig 5 (measured at 4 um spindle. WT has 6%)
PMID:29180432	fig 4
PMID:29180432	fig 3
PMID:29180432	figure 3
PMID:29180432	fig3
PMID:29180432	fig 6
PMID:29180432	fig 2G
PMID:29194511	fig 1b &C
PMID:29194511	fig 1b &C
PMID:29194511	fig 1b &C
PMID:29194511	Figure 2E-F, supplementary figure 5
PMID:29194511	Figure 2A,B,C
PMID:29194511	fig 4a
PMID:29194511	fig 4a
PMID:29194511	fig 4b
PMID:29194511	fig 4b
PMID:29194511	fig 5
PMID:29194511	Figure 3C-D, Supplementary Figure 8A-B
PMID:29194511	Figure 3E-F, Supplementary figure 8 C-D
PMID:29194511	Figure S1A and B
PMID:29194511	Figure S1A and B
PMID:29194511	Figure S1A and B
PMID:29194511	Figure S1A and B
PMID:29194511	fig 1b &C
PMID:29194511	fig 1b &C and 3H
PMID:29194511	fig 1b &C and 3H
PMID:29194511	fig 1b &C
PMID:29194511	fig 1b &C
PMID:29194511	fig 1b &C
PMID:29194511	Figure 2G, supplementary figure 4
PMID:29214404	at telomeres 1L, 1R, 2L, 2R
PMID:29214404	greater decrease at telomeres 1R and 2L than at 1L and 2R
PMID:29214404	at telomere 1R
PMID:29214404	at telomeres 1L, 2R
PMID:29215009	same as either single mutant
PMID:29215009	same as exo1delta alone
PMID:29215009	upstream reporter
PMID:29215009	upstream reporter
PMID:29216371	IMP evidence for part_of extension
PMID:29216371	IMP evidence for part_of extension
PMID:29249658	Fig 4F
PMID:29249658	fig 1B
PMID:29249658	fig 1B
PMID:29249658	figure 1c
PMID:29249658	fig 1 `D,E ~55%
PMID:29249658	fig 1
PMID:29249658	fig 1
PMID:29249658	fig 1
PMID:29249658	CHeCK phenotypes
PMID:29249658	fig 2A
PMID:29249658	fig 2A
PMID:29249658	figure 2D
PMID:29249658	fig 2A
PMID:29249658	fig 2A
PMID:29249658	fig 2A
PMID:29249658	fig 2A
PMID:29249658	fig 2
PMID:29249658	figure 2
PMID:29249658	figure 2
PMID:29249658	figure 2
PMID:29249658	fig 2A
PMID:29249658	fig 3A
PMID:29249658	fig 3B
PMID:29249658	fig 3c
PMID:29249658	fig S3A
PMID:29249658	fig 3D
PMID:29249658	fig 3
PMID:29249658	fig 3
PMID:29249658	Figure S-3F
PMID:29249658	Figure S-3F
PMID:29249658	Figure S-3F
PMID:29249658	Figure S-3F
PMID:29249658	Figure S-3F
PMID:29249658	Figure S-3F
PMID:29249658	Figure 3D
PMID:29249658	fig 3D
PMID:29249658	fig 3h
PMID:29249658	Figure 3H
PMID:29249658	Fig 4C D
PMID:29249658	Fig 4C D
PMID:29249658	figure S4C
PMID:29249658	figure S4C
PMID:29249658	figure S4C
PMID:29249658	figure S4C
PMID:29249658	Fig 4F (lasso)
PMID:29259000	Figure 3F
PMID:29259000	fig 2A abolished entry into meiosis (at pre meiosis?)
PMID:29259000	fig 2A abolished entry into meiosis (at pre meiosis?)
PMID:29259000	fig 7D,E,F
PMID:29259000	Figure 6
PMID:29259000	fig 5E
PMID:29259000	fig S5A
PMID:29259000	fig2A
PMID:29259000	fig 5D
PMID:29259000	fig 5
PMID:29259000	Figure 4
PMID:29259000	Figure 4A and B: MI NDJ
PMID:29259000	Figure 4A and B: MI NDJ
PMID:29259000	Figure S3C-E
PMID:29259000	Figure S3C-E
PMID:29259000	fig2
PMID:29259000	fig2 abolished asci formation
PMID:29259000	fig 3D
PMID:29259000	fig 3D
PMID:29259000	fig5
PMID:29290560	Fig 3D
PMID:29290560	fig1 ER plasma membrane tethering ER-PM contact removal OR abnormal ER-PM contact formation
PMID:29290560	fig1
PMID:29290560	Figures 1C and S1C ER-PM contact removal
PMID:29290560	Figures 1D and S1F ER-PM uncoupling *********lateral PM
PMID:29290560	Figures 1D and S1F
PMID:29290560	(Figure 1F) ER-PM uncoupling
PMID:29290560	Fig 2A
PMID:29290560	Figure 2E
PMID:29290560	FIg 3C
PMID:29290560	Figure 3C
PMID:29290560	Figure 3C
PMID:29290560	Fig 3D
PMID:29290560	Fig 3D
PMID:29292846	fig3
PMID:29292846	fig2
PMID:29292846	fig2
PMID:29292846	Deletion of LEM domain decreases the association of Lem2 at the centromere
PMID:29292846	fig2
PMID:29292846	fig5
PMID:29292846	fig5
PMID:29292846	fig 5
PMID:29292846	fig2
PMID:29292846	fig2
PMID:29292846	fig3
PMID:29292846	DNA binding site: 1-60 a.a.
PMID:29292846	fig5
PMID:29292846	fig5
PMID:29292846	fig3
PMID:29292846	fig4
PMID:29292846	fig4
PMID:29292846	fig5
PMID:29292846	fig5
PMID:29292846	fig4
PMID:29292846	fig 1a residues 200-307
PMID:29319508	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of life cycle of cell
PMID:29319508	A phenotype in which a cell lyses, i.e. the plasma membrane ruptures and cytoplasm is lost, in presence of higher concentration of 2-deoxyglucose.
PMID:29319508	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29330317	fig3
PMID:29330317	fig3
PMID:29343550	Figure 1C
PMID:29343550	Figure 4A LifeAct-mcherry
PMID:29343550	Figure 2C DAPI, methyl blue
PMID:29343550	Figure 4Cmcherry
PMID:29343550	Figure 4E tagged with GFP
PMID:29343550	Figure 3A allele tagged with mNeonGreen
PMID:29343550	Figure 5
PMID:29343550	Figure 5
PMID:29343550	Figure 4A LifeAct-mcherry issues/3215
PMID:29343550	Figure 4A LifeAct-mcherry
PMID:29343550	Figure 4E-F tagged with GFP
PMID:29343550	Figure 4C 4Cmcherry
PMID:29343550	Figure 3A allele tagged with mNeonGreen
PMID:29343550	Figure 5
PMID:29343550	Figure 5
PMID:29343550	Figure 4A LifeAct-mcherry
PMID:29343550	Figure 1A-B
PMID:29343550	Figure 2C DAPI, methyl blue
PMID:29352077	figure 4
PMID:29352077	figure 4F
PMID:29352077	figure 4
PMID:29352077	figure 4
PMID:29352077	figure 4
PMID:29352077	figure 4
PMID:29352077	figure 4
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 3
PMID:29352077	figure 2
PMID:29352077	figure 2
PMID:29352077	figure 3
PMID:29352077	figure 4
PMID:29414789	Northern blot and primer extension analysis
PMID:29414789	Primer Extension Analysis
PMID:29414789	8c
PMID:29414789	Primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	GONEW: negative regulation of cellular response to phosphate starvation
PMID:29414789	Northern blot and primer extension analysis
PMID:29414789	Northern blot and primer extension analysis
PMID:29414789	Northern blot and primer extension analysis
PMID:29414789	Primer extension analysis
PMID:29414789	Northern blot and primer extension analysis
PMID:29422501	fig 1c
PMID:29422501	fig 3a
PMID:29422501	fig 1c
PMID:29422501	fig1 c
PMID:29422501	fig1 c
PMID:29422501	fig 1 a
PMID:29422501	fig2
PMID:29422501	fig2
PMID:29422501	fig2
PMID:29422503	fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in ter1∆.
PMID:29422503	fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in ccq1∆.
PMID:29422503	Pof8 expression level is not affected in ccq1∆.
PMID:29422503	fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in trt1∆.
PMID:29422503	Pof8 expression level is not affected by trt1∆.
PMID:29422503	fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in est1∆.
PMID:29422503	Pof8 expression was not affected by est1∆.
PMID:29422503	Fig. 3a Pof8-TER1 interaction is reduced but not eliminated in ccq1∆.
PMID:29422503	Fig. 3a) Pof8-TER1 interaction is reduced but not eliminated in trt1∆ cells.
PMID:29422503	Fig. 3a Pof8-TER1 interaction is not affected by est1∆.
PMID:29422503	Trt1-TER1 interaction is reduced but not eliminated in pof8-∆[289-4020]. Extent of reduction in Trt1-TER1 is similar to pof8∆ cells.
PMID:29422503	fig 5
PMID:29422503	fig 5
PMID:29422503	fig 5
PMID:29422503	Fig. 4e
PMID:29422503	Fig. 4d
PMID:29422503	Lsm3 protein level was not affected by est1∆.
PMID:29422503	Fig. 4f Lsm3 binding to telomeres was not affected by est1∆.
PMID:29422503	Lsm3 protein level was not affected by trt1∆.
PMID:29422503	Fig. 4f Lsm3 binding to telomeres was not affected by trt1∆.
PMID:29422503	Lsm3 protein level was not affected by ter1∆.
PMID:29422503	Lsm3 binding was detected at ars2004, non-ARS, ade6+ and his1+ loci. In ter1∆ cells, Lsm3 binding to those non-telmeric sites were increased.
PMID:29422503	figs 1-3
PMID:29422503	(created to replace WT phenotype annotation)
PMID:29422503	(created to replace WT phenotype)
PMID:29422503	(created to replace WT phenotype)
PMID:29422503	(created to replace WT phenotype annotation) lsm3-myc chip
PMID:29422503	figure 1 a
PMID:29422503	fig1 Lose telomere signal, much like trt1∆ cells.
PMID:29422503	figure 1a Telomere shortening is similar to pof8∆ cells.
PMID:29422503	pof8∆ taz1∆ showed much shorter telomere length (almost like wild-type cells) than taz1∆ cells, but showed some rearrangement in sub-telomeres.
PMID:29422503	pof8∆ rap1∆ cells showed shortened telomeres, more similar to pof8∆, rather than highly elongated telomeres in rap1∆ cells.
PMID:29422503	pof8∆ poz1∆ cells showed very slightly shortend telomeres, rather than highly elongated telomeres in poz1∆ cells. (This strain showed longer telomere than pof8∆ cells.)
PMID:29422503	pof8∆ rif1∆ cells showed short telomeres, very similar to pof8∆ cells.
PMID:29422503	fig 1 c/d Trt1-myc ChIP
PMID:29422503	Based on ChIP, ter1∆ cause loss of telomerase (Trt1) localization at telomeres.
PMID:29422503	Trt1 expression level detected by western blot is reduced in ter1∆ cells.
PMID:29422503	moderately reduced less severe thanin ter1∆ cells.
PMID:29422503	Telomere binding of Est1 is reduced in pof8∆ cells.
PMID:29422503	Est1 showed similar expression level in pof8∆ cells as wild-type cells.
PMID:29422503	Fig. 3c Interaction between Est1 and TER1 was not affected by pof8∆.
PMID:29422503	fig 3 b
PMID:29422503	Est1 binding to telomeres is reduced to near no binding in ter1∆, based on ChIP assay.
PMID:29422503	Est1 expression level detected by western in ter1∆ cells was similar to Est1 level in ter1+ (wild-type) cells.
PMID:29422503	Pof8 expression level was not altered in ter1∆ cells.
PMID:29422503	Fig 4 a Expression level of telomerase RNA TER1 is reduced but not eliminated in pof8∆ cells. Expression level for telomerase RNA pre-cursor was not affected by pof8∆.
PMID:29422503	Fig. 4c Lsm3-TER1 interaction is abolished in pof8∆ cells.
PMID:29422503	Fig. 4f
PMID:29422503	(created to replace WT phenotype annotation)
PMID:29422503	(created to replace WT phenotype annotation) fig 3 b
PMID:29422503	(created to replace WT phenotype annotation) est1-myc chip
PMID:29422503	(created to replace WT phenotype annotation) trt1-myc chip
PMID:29422503	fig 3a (created to replace WT phenotype annotation)
PMID:29422503	fig 1 e
PMID:29422503	fig 1 e
PMID:29422503	fig 1 e
PMID:29422503	fig 1 c/d
PMID:29422503	fig 1 c/d
PMID:29422503	fig 1 c/d
PMID:29422503	(created to replace WT phenotype annotation) Fig. 1e
PMID:29422503	Fig 1
PMID:29422503	Trt1 binding is reduced to ~80% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	Trt1 binding is reduced to ~70% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	Trt1 binding is reduced to ~58% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	fig 6 b
PMID:29422503	fig 6
PMID:29422503	fig 6
PMID:29422503	fig 6 pof8-∆[289-402] cells show as short telomere as pof8∆ cells.
PMID:29422503	fig 6 pof8-∆[390-402] cells show as short telomere as pof8∆ cells.
PMID:29422503	fig 6 pof8-R343A cells show as short telomere as pof8∆ cells.
PMID:29422503	fig 6 pof8-Y330A cells show as short telomere as pof8∆ cells.
PMID:29422503	Fig. 4f Lsm3 binding at telomeres is increased by ter1∆.
PMID:29422503	fig 5
PMID:29422503	Lsm3 protein level was not affected by pof8∆.
PMID:29422503	Supplementary Fig. 4
PMID:29422503	fig 5
PMID:29422503	figs 1-3
PMID:29422503	Supplementary Fig. 4
PMID:29422503	Supplementary Fig. 4
PMID:29422503	Supplementary Fig. 4
PMID:29422503	Trt1 binding is reduced to ~69% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29424342	ts background fig5
PMID:29424342	ts background fig5
PMID:29424342	4
PMID:29424342	4
PMID:29424342	fig2
PMID:29424342	4b
PMID:29424342	4
PMID:29424342	4
PMID:29424342	4
PMID:29424342	fig5
PMID:29424342	fig5
PMID:29424342	6
PMID:29424342	6
PMID:29424342	6
PMID:29432178	Fig. 3A
PMID:29432178	the expression of most genes induced by amino acid starvation in wild-type cells was not up-regulated, confirming that Gcn2 is the major mediator of this response
PMID:29432178	Can we say somewhere - overexpresses genes involved by amino acid starvation, or something similar?
PMID:29432178	Fig. 3E
PMID:29432178	Fig. 3A
PMID:29432178	Fig. 3B during normal growth
PMID:29432178	Ribosome profiling and matching RNA-seq in gcn2Δ cells treated or untreated with 3-AT revealed that the majority of the translationally induced genes did not respond to amino acid starvation (Fig. 2B)
PMID:29432178	Fig. 3A
PMID:29453312	Active Ras1 is localized to cell poles during mitotic growth
PMID:29453312	Ste6 co-localizes with the actin fusion focus during the process of cell-cell fusion
PMID:29453312	Active Ras1 co-localizes with the actin fusion focus during the process of cell-cell fusion
PMID:29453312	Ative Ras1 localizes to septa during mitotic growth
PMID:29453312	Ras activity increases during the mating process and is maximum at the fusion site just before the fusion event.
PMID:29453312	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29453312	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29453312	In the absence of gap1 Ras activity increases and decorates the entire cortex of vegetative growing cells
PMID:29453312	Active Ras1 is localized to cell poles during mitotic growth
PMID:29453312	ras1 mutant cells undergo precocious fusion resulting in cell lysis
PMID:29453312	ras1 mutant cells undergo precocious fusion resulting in cell lysis
PMID:29453312	Active Ras1 is localized to cell poles during mitotic growth
PMID:29458562	fig4
PMID:29458562	fig2 (likey due to intron encoded maturase)
PMID:29458562	fig4
PMID:29458562	fig3 abolished
PMID:29458562	Fig. 2
PMID:29458562	Fig. 2
PMID:29458562	Fig. 2
PMID:29458562	Fig. 2
PMID:29458562	DNS
PMID:29458562	fig3
PMID:29458562	fig3
PMID:29458562	fig3
PMID:29458562	fig4
PMID:29458562	fig4
PMID:29458562	fig4
PMID:29514920	Fig 1A
PMID:29514920	fig 3A, fig 3B Fig. S2, A and B IN TRANSIENT BURSTS & progressive increase in the number of Wee1 nodes as a function of cell size, ... 20X in Wee1 nodes in large cells versus small cells (Fig. 4 B).
PMID:29514920	affecting Wee1
PMID:29514920	Affecting Wee1 vw Increased , term pending
PMID:29514920	fig 3D Affecting Wee1
PMID:29514920	affecting Cdr1 vw:ig. S2, F and G
PMID:29514920	figure 2D Epistatic to cdr2delta
PMID:29514920	Fig 2C protein localizes to cytoplasm, nucleus, and spindle-pole body.
PMID:29514920	figure 2D Epistatic to cdr2delta
PMID:29514920	figure 2B
PMID:29514920	figure 2B
PMID:29514920	Fig 1A
PMID:29514920	figure 2B
PMID:29514920	fig2B
PMID:29514920	Fig 1C
PMID:29514920	Fig 1B
PMID:29514920	Fig. 1A
PMID:29514920	Fig 1A
PMID:29514920	Fig 1A
PMID:29514920	Fig. 1A
PMID:29529046	"We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants"
PMID:29529046	Zhf1 is required for the rapid transport of zinc ions out of the cytosol during a zinc shock (a condition where there is a rapid influx of zinc into a cell)
PMID:29529046	A key finding of our work is that Zhf1 does NOT transport zinc out of the cytosol under conditions of zinc ion starvation
PMID:29529046	Fig 5A/B In this paper we used a high affinity zinc-responsive FRET sensor (ZapCY1) to measure zinc ion availability in the cytosol under conditions of zinc deficiency. Thus, in addition to accumulating high levels of total cellular zinc - this manuscript shows that loz1D cells also accumulate higher levels of zinc in the cytosol. This accumulation is also dependent upon Zrt1 as this phenotype is not observed in a loz1 zrt1 double mutant
PMID:29529046	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	The experiment performed was to measure total cellular zinc ion levels in a zrt1D strain during a zinc shock (Figure 4A)
PMID:29529046	"We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants"
PMID:29529046	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	The reporter genes used were the ZapCY1 high affinity and ZapCY2 low affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	Zrg17 also transports zinc out of the cytosol when zinc is available (as well as when it is limiting)
PMID:29529046	Fig 4 BE
PMID:29529046	Figure 1 (EDTA, zinc chelator)
PMID:29529046	Figure 1 (EDTA, zinc chelator)
PMID:29529046	fig6
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29529046	Fig 8
PMID:29549126	fig7
PMID:29549126	fig7
PMID:29549126	fig6
PMID:29549126	fig6
PMID:29549126	assayed using heme analog ZnMP
PMID:29549126	assayed using heme analog ZnMP
PMID:29549126	assayed using heme analog ZnMP
PMID:29549126	3B,C, We therefore concluded that Shu1 is required for hemin acquisition when hemin is present at very low concentrations (0.075 􏰄M), whereas its presence is dispens- able under conditions of high hemin concentrations
PMID:29549126	3B,C,
PMID:29596413	fig 7C supression of trm7-delta
PMID:29596413	fig 7C
PMID:29596413	fig 7C
PMID:29596413	fig 7C
PMID:29596413	fig 7
PMID:29596413	fig 7
PMID:29596413	fig 7C supression of trm7-delta
PMID:29596413	fig 7C supression of trm7-delta
PMID:29596413	fig 7
PMID:29596413	fig 7
PMID:29596413	fig 7C supression of trm7-delta
PMID:29596413	fig 7C supression of trm7-delta
PMID:29596413	fig 7C supression of trm7-delta
PMID:29596413	fig 7C
PMID:29610759	enriched at mat1 right border and cenH left border; fig 1
PMID:29610759	fig 5
PMID:29610759	at MPS1
PMID:29610759	fig 1
PMID:29610759	fig 1
PMID:29610759	fig 2
PMID:29610759	figs 1 & 4
PMID:29610759	figs 1 & 4
PMID:29632066	fig S1B
PMID:29632066	fig S1B
PMID:29632066	fig S1B
PMID:29641590	fig3
PMID:29641590	fig3
PMID:29641590	A1 cleavage
PMID:29641590	A2 cleavage
PMID:29641590	fig3
PMID:29641590	A0 cleavage
PMID:29641590	fig3
PMID:29689193	thicker and thinner, disrupted homeostasis
PMID:29689193	thicker and thinner, disrupted homeostasis
PMID:29689193	thicker and thinner, disrupted homeostasis
PMID:29689193	fig 3C
PMID:29689193	figure 3B
PMID:29689193	figure 3B
PMID:29689193	figure 2 F
PMID:29689193	Promotes cell wall thickness hoemostasis
PMID:29689193	Promotes cell wall thickness hoemostasis
PMID:29689193	Promotes cell wall thickness hoemostasis
PMID:29699848	abolished interaction with gad8
PMID:29699848	affect interaction with Tor1
PMID:29735656	fig 4b
PMID:29735656	fig 4b
PMID:29735656	S4
PMID:29735656	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	figure 1A, supp S1A
PMID:29735656	figure 1A, supp S1A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 1 A
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3c
PMID:29735656	fig 4e
PMID:29735656	figure 4d
PMID:29735656	S4
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	figure 3, figure S1B
PMID:29735656	fig 4b
PMID:29735745	Fig. 5 C
PMID:29735745	Fig. 5 B
PMID:29735745	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	Fig. 2 D
PMID:29735745	Fig 2 B
PMID:29735745	Fig 2 B
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 5 A, B, C; Fig. 7 C
PMID:29735745	Fig. 5 A, B, C; Fig. 7 C
PMID:29735745	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	Video S2
PMID:29735745	Video S2
PMID:29735745	Fig. 2 C
PMID:29735745	Fig. 2 C
PMID:29735745	Fig. 5 H
PMID:29735745	Fig. 5 H
PMID:29735745	Fig S2 F
PMID:29735745	Fig. S2 F
PMID:29735745	Fig S2 F
PMID:29735745	Fig. S2 F
PMID:29735745	Fig. S2 F
PMID:29735745	Fig. S2 F
PMID:29735745	Fig. S2 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig S2 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig 7 D
PMID:29735745	Fig. 7 C
PMID:29735745	Fig. 7 B
PMID:29735745	Fig. 7 B
PMID:29735745	Fig. 7 C
PMID:29735745	Fig. 7 B
PMID:29735745	Fig. 7 B
PMID:29735745	Fig. 7 B
PMID:29735745	Fig. 6 B
PMID:29735745	Fig. 5 G
PMID:29735745	Fig. 5G
PMID:29735745	Fig. 7 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig. S2 D
PMID:29735745	Fig. 1 D
PMID:29735745	Fig. 1 C
PMID:29735745	Fig. 1 C
PMID:29735745	Fig. 1 E
PMID:29735745	Fig. 5 B
PMID:29735745	Fig. 5 B
PMID:29735745	Fig. 5 B
PMID:29735745	Fig. 5 C
PMID:29735745	Fig. 6 D
PMID:29735745	Fig 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 6 B, C
PMID:29735745	Fig. 5 F
PMID:29735745	Fig. 1 E
PMID:29735745	Fig. 1 D
PMID:29735745	Fig. 1 E
PMID:29735745	Fig. 1 C
PMID:29735745	Fig. 2 D
PMID:29735745	Fig. 2 D
PMID:29735745	Fig. 2 D
PMID:29735745	Fig. 2 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 3 D
PMID:29735745	Fig. 5 A, 5 C
PMID:29735745	Fig. 5 A
PMID:29735745	Fig. 5 A
PMID:29735745	Fig. 5 A
PMID:29742018	in vitro, casein substrate
PMID:29742018	normal with and without spindle checkpoint activation
PMID:29742018	in vitro, casein substrate
PMID:29742018	in vitro, casein substrate
PMID:29742018	in vitro, casein substrate
PMID:29742018	Hhp1 accumulates at SPB when spindle checkpoint activated
PMID:29742018	in vitro, casein substrate
PMID:29742018	in vitro, casein substrate
PMID:29742018	in vitro, casein substrate
PMID:29742018	normal with and without spindle checkpoint activation
PMID:29742018	in vitro, casein substrate
PMID:29774234	Sensitive to HU, CPT and MMS
PMID:29774234	Exacerbated at high temperature
PMID:29774234	slightly better growth than stn1-226 alone
PMID:29774234	same as stn1-226 alone
PMID:29774234	loss of telomeric and subtelomeric sequences at high temperature
PMID:29804820	However, the interaction is significantly diminished when either L32 (Mis16D1–32), or both L32 (Mis16D1–32) and L32/W33 (Mis16D1–33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1–33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	A Homodimer of the Mis18 C-Terminal Domain Interacts with a Mis16-Eic1 Heterodimer
PMID:29804820	The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T
PMID:29804820	The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T
PMID:29804820	The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T
PMID:29804820	FIgure 4D
PMID:29804820	(Figures 6A and 6B).
PMID:29804820	However, the interaction is significantly diminished when either L32 (Mis16D1–32), or both L32 (Mis16D1–32) and L32/W33 (Mis16D1–33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1–33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	However, the interaction is significantly diminished when either L32 (Mis16D1–32), or both L32 (Mis16D1–32) and L32/W33 (Mis16D1–33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1–33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	However, the interaction is significantly diminished when either L32 (Mis16D1–32), or both L32 (Mis16D1–32) and L32/W33 (Mis16D1–33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1–33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	However, the interaction is significantly diminished when either L32 (Mis16D1–32), or both L32 (Mis16D1–32) and L32/W33 (Mis16D1–33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1–33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29813053	Fig S3D. The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR unconventional type II myosin Myp2 is compromised.
PMID:29813053	Fig 7. The spindle and the proximity of the nucleus to the division site are required for proper septum synthesis activation in fission yeast. (A) Scheme of the steps required to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or from the division site. (A-1 and C) Nucleus and division site are maintained in the cell middle; cells were treated for 90 min and imaged with methyl 2-benzimidazolecarbamate (or carbendazim, MBC, 50 μg ml-1) to avoid spindle assembly and nuclear separation. (A-2 and D) Nucleus and division site are relocated to a cell end; cells were treated for 45 min, centrifuged to displace the nucleus, treated 45 more min and visualized with MBC. (A-3 and E) The nucleus is relocated and separated from the division plane; cells were treated for 90 min, centrifuged and examined with MBC. (B) mad2Δ cells were grown and imaged without MBC as in Fig 1. The mad2Δ cells were used to avoid a delay caused by the activation of the spindle assembly checkpoint. (C-E) The premature and uncoupled septation start caused by the absence of the spindle depends on the position of the nucleus. mad2Δ cells were processed as in A to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or the division site. (C) The nucleus and division site are maintained in the cell middle. (F) The nucleus and division site are relocated to a cell end. (E) The nucleus is relocated and separated from the division plane. MBC-treated cells were imaged as in B. Anaphase A onset was considered as time zero. Graphs to the right are as in Fig 4. Dashed lines and arrowheads: green, anaphase A onset; dark blue, septum synthesis start; light blue, septum ingression onset. White arrowhead: first CW-stained septum synthesis detection. White arrow: first CW-staining increase showing septum ingression. A.U., arbitrary units. (F) Uncoupled septum synthesis and ingression timing with MBC is restored to wild-type levels when the undivided nucleus is separated from the division site. Table showing the time between anaphase A (green) and septum synthesis start (dark blue) or septum ingression onset (light blue) in the indicated cells. Parenthesis: n, number of experiments and cells; T, delay in septum synthesis and ingression start with respect to control cells with MBC as in C.
PMID:29813053	Fig 7. The spindle and the proximity of the nucleus to the division site are required for proper septum synthesis activation in fission yeast. (A) Scheme of the steps required to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or from the division site. (A-1 and C) Nucleus and division site are maintained in the cell middle; cells were treated for 90 min and imaged with methyl 2-benzimidazolecarbamate (or carbendazim, MBC, 50 μg ml-1) to avoid spindle assembly and nuclear separation. (A-2 and D) Nucleus and division site are relocated to a cell end; cells were treated for 45 min, centrifuged to displace the nucleus, treated 45 more min and visualized with MBC. (A-3 and E) The nucleus is relocated and separated from the division plane; cells were treated for 90 min, centrifuged and examined with MBC. (B) mad2Δ cells were grown and imaged without MBC as in Fig 1. The mad2Δ cells were used to avoid a delay caused by the activation of the spindle assembly checkpoint. (C-E) The premature and uncoupled septation start caused by the absence of the spindle depends on the position of the nucleus. mad2Δ cells were processed as in A to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or the division site. (C) The nucleus and division site are maintained in the cell middle. (F) The nucleus and division site are relocated to a cell end. (E) The nucleus is relocated and separated from the division plane. MBC-treated cells were imaged as in B. Anaphase A onset was considered as time zero. Graphs to the right are as in Fig 4. Dashed lines and arrowheads: green, anaphase A onset; dark blue, septum synthesis start; light blue, septum ingression onset. White arrowhead: first CW-stained septum synthesis detection. White arrow: first CW-staining increase showing septum ingression. A.U., arbitrary units. (F) Uncoupled septum synthesis and ingression timing with MBC is restored to wild-type levels when the undivided nucleus is separated from the division site. Table showing the time between anaphase A (green) and septum synthesis start (dark blue) or septum ingression onset (light blue) in the indicated cells. Parenthesis: n, number of experiments and cells; T, delay in septum synthesis and ingression start with respect to control cells with MBC as in C.
PMID:29813053	S5 Fig. The establishment of SIN asymmetry and the timely activation of septum synthesis do not depend on each other. (A, B) Early log-phase wild-type and thermosensitive cps1-191 (Bgs1) mutant cells were grown in YES at 25ÊC, shifted to 28ÊC for 1 h (A) or 32ÊC for 30 min (B) to produce a gradual delay in the onset of septum synthesis of cps1-191 mutant, and imaged as in Fig 5C. Anaphase B onset is considered as time zero (T = 0). White arrow: first CWstained detection of septum synthesis. Arrowheads: green, anaphase B onset; blue, septum deposition start (time immediately before septum detection with CW); red, complete asymmetry of SIN Cdc7, being Cdc7-GFP completely lost from one SPB. The data of this figure are developed in S2 Table. (C) The timing of septation onset is not related to the asymmetry of SIN. Early log-phase wild-type cells were grown in YES at 25ÊC, 28ÊC or 32ÊC, imaged as in Fig 5C and the timings of SIN asymmetry and of septation onset were determined with respect to the anaphase B onset (see also the data in S2 Table).
PMID:29813053	Fig 3
PMID:29813053	Fig 3
PMID:29813053	Fig 4D & E
PMID:29813053	Fig 5B, Table 1; also inferred from localization timing
PMID:29813053	Fig 56A-D; also inferred from localization timing
PMID:29813053	Fig 56E; also inferred from localization timing
PMID:29813053	Fig 2. The start of septation scales with anaphase B progression and cell size in fission yeast and correlates linearly with the cell length.
PMID:29813053	Fig 2. The start of septation scales with anaphase B progression and correlates linearly with the cell length.
PMID:29813053	Fig 4E and F. Inactivation of Cdc2 kinase in early mitosis induces a very premature septation onset. ATP-analogue sensitive cdc2-asM17 mutant cells carrying Cdc13-GFP were G2-arrested by growth in the presence of 1 μM1-NP-PP1 for 3.5 h at 32C. Then, the cells were G2-released by transfer to a fresh medium and imaged to detect the entry into mitosis. Cdc2 was inactivated during early mitosis transferring the cells to a fresh medium containing either DMSO or 10 μM1-NP-PP1.
PMID:29813053	Fig 5E. Timely activation of septum synthesis does not depend on SIN asymmetry. Defective SIN-Inhibitory Phosphatase (SIP) complex csc2Δ cells were examined. The data of cells of C, D and E are developed in S2 Table.
PMID:29813053	Fig 6. The levels of Etd1 and Rho1 regulate the timing of septation start. (A) The timing of septum deposition onset correlates with the start of increase of Etd1 in the cell middle. Cells were grown inMMwithout thiamine (GFP-etd1+ induced) at 25ÊC for 24 h and imaged as in Fig 1. (B) The increase of Etd1 in the cell middle and concomitant initiation of septation are delayed in long cells. Cells were analyzed as in A after 3.5 h of cell cycle arrest at 36ÊC. Graphs to the right show the total fluorescence of GFP-Etd1 at the cell poles and middle in the series to the left. A.U., arbitrary units. Arrow, cortical localization of Etd1 in the cell middle. Dashed outlines indicate the ROIs used to measure the total fluorescence of GFP-Etd1 in the corresponding regions of the cell. (C) The timing of septation onset is dependent on the level of etd1+. Cells expressing endogenous etd1+ and 41X-GFP-etd1+ grown at 32ÊC for 24 h either in the absence (ON, high etd1+ level; n = 4, 34 cells) or in the presence of thiamine (OFF, wild-type etd1+ level; n = 2, 11 cells), and cells expressing etd1Δ 81X-etd1+ grown for 15 h with thiamine (OFF, very low etd1+ level; n = 3, 23 cells), just before the emergence of SIN phenotype were analyzed as in A.
PMID:29813053	Fig 6. The levels of Etd1 and Rho1 regulate the timing of septation start. (A) The timing of septum deposition onset correlates with the start of increase of Etd1 in the cell middle. Cells were grown inMMwithout thiamine (GFP-etd1+ induced) at 25ÊC for 24 h and imaged as in Fig 1. (B) The increase of Etd1 in the cell middle and concomitant initiation of septation are delayed in long cells. Cells were analyzed as in A after 3.5 h of cell cycle arrest at 36ÊC. Graphs to the right show the total fluorescence of GFP-Etd1 at the cell poles and middle in the series to the left. A.U., arbitrary units. Arrow, cortical localization of Etd1 in the cell middle. Dashed outlines indicate the ROIs used to measure the total fluorescence of GFP-Etd1 in the corresponding regions of the cell. (C) The timing of septation onset is dependent on the level of etd1+. Cells expressing endogenous etd1+ and 41X-GFP-etd1+ grown at 32ÊC for 24 h either in the absence (ON, high etd1+ level; n = 4, 34 cells) or in the presence of thiamine (OFF, wild-type etd1+ level; n = 2, 11 cells), and cells expressing etd1Δ 81X-etd1+ grown for 15 h with thiamine (OFF, very low etd1+ level; n = 3, 23 cells), just before the emergence of SIN phenotype were analyzed as in A.
PMID:29813053	Fig 6. The levels of Etd1 and Rho1 regulate the timing of septation start. (D, E) The start of septum synthesis does not dependent on cortical Etd1. Cells expressing a functional Etd1 version that is absent from the cortex from etd1Δ 41X-GFP-etd1-Δ9 strain grown at 32ÊC either for 6 to 9 h without thiamine (ON; n = 2, 37 cells) or with thiamine (OFF; n = 2, 17 cells) were analyzed.
PMID:29813053	Fig 6. The levels of Etd1 and Rho1 regulate the timing of septation start. (F) The start of septum deposition is dependent on the level of rho1+. Cells expressing endogenous rho1+ and 3Xrho1+ grown at 32ÊC for 16 h either without (ON, high rho1+ level; n = 2, 14 cells) or with thiamine (OFF, wild-type rho1+ level; n = 2, 16 cells) were analyzed.
PMID:29813053	Fig 2. The start of septation scales with anaphase B progression and cell size in fission yeast. and correlates linearly with the cell length.
PMID:29813053	Fig 5B. Septation start is delayed when the function of Sid2 is compromised. Cells were grown in YES at 25C, shifted to 28C for 4 h and imaged as in Fig 1. The data are developed in Table 1 and Table 3.
PMID:29813053	Fig S3E. The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR F-BAR protein Cdc15 is compromised.
PMID:29813053	Fig 2. The start of septation scales with anaphase B progression and cell size in fission yeast and correlates linearly with the cell length.
PMID:29844133	Beware using aged colonies, cell size recovery observed.
PMID:29844133	beware using old strains, phenotypic changes observed.
PMID:29851556	in the presence or absence of Nbs1
PMID:29851556	localization of mutated protein assayed
PMID:29866182	FLAG-Ago1, Arb1-Myc
PMID:29866182	FLAG-Ago1
PMID:29866182	Myc-Ago1
PMID:29866182	Myc-Ago1
PMID:29866182	FLAG-Ago1
PMID:29866182	Tas3-Myc
PMID:29866182	FLAG-Ago1, Arb1-Myc
PMID:29898918	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	slightly worse than srs2delta alone
PMID:29898918	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	slightly worse than srs2delta alone
PMID:29898918	Epistatic genetic interaction (same as eme1delta alone)
PMID:29898918	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	Epistatic genetic interaction (same as eme1delta alone)
PMID:29898918	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	Required for cellular resistance to MMS and CPT.
PMID:29898918	present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.
PMID:29899453	Extended Data Fig 4a Cdk9 inhibition increased chromatin recruitment of Dis2
PMID:29899453	Extended Data Fig 4d Added Dis2 extension
PMID:29899453	Extended Data Fig 4d (vw: fixed allele)
PMID:29899453	Extended Data Fig 5a vw: fixed allele and target
PMID:29899453	Extended Data Fig 5a vw: fixed allele and target
PMID:29899453	Extended Data Fig 5a vw: based on EXP and comment changed allele from psf2 to cdk9 (P.P. Core CPF recruitment to chromatin is unaffected by Cdk9 inhibition). pfs2 pla1 cft1
PMID:29899453	Fig 3e
PMID:29899453	Fig 1b
PMID:29899453	fig 1c
PMID:29899453	Fig 1c, Extended Data Fig 2a
PMID:29899453	fig 1c
PMID:29899453	Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	check this addition Fig. 2a, Extended Data Fig. 2a
PMID:29899453	Fig S2, Extended Data Fig. 2c
PMID:29899453	Fig S2, Extended Data Fig. 2d
PMID:29899453	Fig. 2d,
PMID:29899453	Extended Data Fig 2f
PMID:29899453	Extended Data Fig 2f
PMID:29899453	Extended Data Fig 3a ig. 2c, Extended Data Fig. 3b–d)
PMID:29899453	Fig. 2e, Extended Data Fig. 4b
PMID:29899453	Fig. 2e, Extended Data Fig. 4c
PMID:29899453	fig 6a.b
PMID:29899453	fig 6a.b
PMID:29899453	FIgure 3d. Extended fig 8d (vw: some suppression?)
PMID:29899453	extended data figure 9 decreased RNA pol2 localization to chromatin (occurs at termination sites)
PMID:29899453	Extended data figure 9
PMID:29899453	Extended Data Fig 3a ig. 2c, Extended Data Fig. 3b–d)
PMID:29899453	figure 3 e Also increased termination index Fig. 4e
PMID:29899453	figure 3 e
PMID:29899453	fig 1d
PMID:29899453	fig 1d
PMID:29899453	fig 1d
PMID:29899453	Fig 5c.
PMID:29899453	Extended Data Fig 10
PMID:29899453	Extended Data Fig 10
PMID:29899453	Extended Data Fig 10
PMID:29899453	Extended Data Fig 6e Cdk9 does not restrict chromatin recruitment of Sds21.
PMID:29899453	Extended Data Fig 6a,b ChIP–qPCR analysis at the rps17a+ gene. Comparison of pSpt5:Spt5 ratio in the indicated strains upstream and downstream of the CPS at 30 °C (left) and comparison of the ratio between dis2+ and dis2-11 cells at 18 °C (right). Extended Data Fig 6a,b
PMID:29899453	Extended Data Fig 5d .
PMID:29899453	Extended Data Fig 2f .(cdk9as, cdk9as ssu72C13S, ssu72C13S)
PMID:29899453	vw: I changed the allele to the multi gene genotype to reflect the comment. Extended Data Fig 2c Fcp1 inactivation stabilizes Rpb1 Ser2 phosphorylation after Lsk1 inhibition. Fission-yeast strains, lsk1as or lsk1as fcp1-452, were grown at 30 °C and shifted to 37 °C (or not shifted), treated for the indicated time with 20 μM 3-MB-PP1, and analysed by immunoblotting for Pol II Ser2 phosphorylation
PMID:29899453	Fig 3e
PMID:29899453	fig 1b
PMID:29899453	Fig 1B vw: corrected back to dis2 not cdk9!
PMID:29899453	fig 1b
PMID:29914874	Supplementary Fig. S3
PMID:29914874	Supplementary Fig. S3
PMID:29914874	Supplementary Fig. S3
PMID:29914874	Supplementary Fig. S3
PMID:29914874	Supplementary Table S3
PMID:29914874	Supplementary Fig. S3
PMID:29914874	Supplementary Fig. S3
PMID:29914874	Supplementary Figure S3
PMID:29930085	Figure 5, Figure S4, Movie 5
PMID:29930085	Figure 6, Figure S6, Movie 7
PMID:29930085	Figure 4, Movie 4
PMID:29930085	Figure 4, Figure S3, Movie 4
PMID:29930085	Figure 4, Movie 4
PMID:29930085	Figure 3, Movie 2
PMID:29930085	Figure 3, Figure 4, Figure S2, Movie 2, Movie 3, Movie 4
PMID:29930085	Figure 2
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 1
PMID:29930085	Figure 5, Figure S4, Movie 5
PMID:29930085	fig 7c
PMID:29930085	figure 7d
PMID:29930085	figure 7D
PMID:29930085	Portli Figure 7, Movie 9 https://github.com/pombase/fypo/issues/3339
PMID:29930085	PORTLI Growth Figure 6, Figure S6, Movie 7 https://github.com/pombase/fypo/issues/3339
PMID:29930085	(PORTLI GROWTH) fig 6 c https://github.com/pombase/fypo/issues/3339
PMID:29930085	PORTLI GROWTH Fig S6 https://github.com/pombase/fypo/issues/3339
PMID:29930085	PORTLI GROWTH Fig S6 https://github.com/pombase/fypo/issues/3339
PMID:29930085	Fig. 5B
PMID:29930085	Fig. 5B
PMID:29930085	Figure 4, Movie 4
PMID:29930085	Figure S3
PMID:29930085	Figure 4,AB
PMID:29930085	PORTLI GROWTH (Figs 3B and 4B; Movie 2) https://github.com/pombase/fypo/issues/3339
PMID:29930085	PORTLI GROWTH (Figs 3B and 4B; Movie 2) https://github.com/pombase/fypo/issues/3339
PMID:29930085	fig 3
PMID:29930085	fig 3
PMID:29930085	(PORTLI GROWTH) fig 2 interphase arrest https://github.com/pombase/fypo/issues/3339
PMID:29930085	fig 2 interphase arrest
PMID:29930085	fig 1 interphase arrest
PMID:29930085	fig 1 interphase arrest
PMID:29930085	fig 1 interphase arrest (requested during interphase)
PMID:29930085	fig 1 interphase arrest (requested during interphase)
PMID:29930085	fig 1 interphase arrest (requested during interphase)
PMID:29930085	fig 1 interphase arrest (requested during interphase)
PMID:29930085	fig 1 interphase arrest
PMID:29930085	fig2 movie1
PMID:29930085	S1
PMID:29930085	Figure 7, Figure S8
PMID:29930085	Figure 7, Figure S8
PMID:29930085	Figure S6, Movie 8
PMID:29930085	Figure S6, Movie 8
PMID:29930085	Figure S3
PMID:29930085	Figure S3
PMID:29930085	Figure 7, Movie 9
PMID:29975113	Figures 1B and S1A Dma1-mNeonGreen became enriched at SPBs prior to SPB separation. It appeared to transiently leave SPBs during anaphase B, returning before telophase and then leaving again after cell division. Dma1 SPB transient loss happens before the development of Cdc7 SPB localiztion asymmetry. Dma1 failed to return to SPBs in late anaphase in cdc7-24 cells at restrictive temperature. Dma1 could be detected on majority SPBs in cdc16-116 cells at restrictive temperature, suggesting high SIN activity promote Dma1 SPB re-accumulation at the end of anaphase.
PMID:29975113	Figure 1B and S1B Dma1-mNeonGreen forms a ring at cell division site during early mitosis. Then it leaves and returns to cell division site during mitosis. Dma1 transiently leaves cell division site before Sid2 appears at the cell division site.
PMID:29975113	Figure 1B and S1B
PMID:29975113	(DNS) Dma1-I194A constitutively localizes to SPB throughout the cell cycle. Dma1-I194A localizes more intensely at one of the two SPBs for most of mitosis
PMID:29975113	Figure 2B and C
PMID:29975113	Figure S2B
PMID:29975113	(Vw, because mutants are related to WT, I changed this to 'normal'), Dma1-I194A-mNeonGreen displays transient loss from SPB during anaphase, just like wildtype Dma1.
PMID:29975113	[ dma1 unubiquitinated, sid4 phosphorylated] When Dma1-GFP is permanently tethered to SPBs by Sid4-GBP-mCherry, cells displayed multi-nucleate and kissing nuclei indicative of SIN and cytokinesis failure.
PMID:29975113	Figure S2D dma1-GFP sid4-GBP-mCherry cells are very sick, if not die. ppc89-DUB rescued the synthetic sick phenotype of dma1-GFP sid4-GBP-mCherry. The cells have reduced levels of multi-nucleate and kissing nuclei compared with dma1-GFP sid4-GBP-mCherry.
PMID:29975113	Figure 2D in vivo
PMID:29975113	Figure S2A
PMID:29975113	Figure S2D
PMID:29975113	temporal localization pattern Figure S2B
PMID:29975113	Figure 2D
PMID:29975113	Figure 2G
PMID:29975113	These data are consistent with auto-ubiquitination triggering Dma1 destruction.
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. S2A
PMID:29975157	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	Fig. 4D; live cell imaging
PMID:29975157	Fig. 4C; live cell imaging
PMID:29975157	Fig. 4B; live cell imaging
PMID:29975157	Fig. 4A; live cell imaging
PMID:29975157	Fig. 3; live cell imaging
PMID:29975157	Fig. 2D; live cell imaging
PMID:29975157	Fig. 2A-C; live cell imaging
PMID:29975157	Fig. 2A-C; live cell imaging
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. S2A-D
PMID:29975157	Fig. S2C,D
PMID:29975157	Fig. 1B
PMID:29975157	Fig. S2E
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	Fig. 1B; DAPI and methyl blue staining
PMID:30003614	fig 4 normal level of free fatty acid
PMID:30003614	fig 4
PMID:30003614	fig 4
PMID:30003614	fig 5 = cerulenin
PMID:30003614	fig 4
PMID:30003614	increased number of lipid droples/cell fig 3b/c
PMID:30044717	Fig S2,E
PMID:30044717	Fig S3 DE
PMID:30044717	Fig S3 DE
PMID:30044717	fig 2a
PMID:30044717	fig 2b
PMID:30044717	fig S4E
PMID:30044717	fig S4E
PMID:30044717	Fig S2,E
PMID:30044717	fig 5B
PMID:30044717	fig 5b
PMID:30044717	Fig5D and Movie 5
PMID:30044717	Fig. S6B
PMID:30044717	Figure 1
PMID:30044717	Fig 7E
PMID:30044717	Fig 7E
PMID:30044717	Figure 7
PMID:30044717	Fig 5C
PMID:30044717	Figure 6E
PMID:30044717	Supp S1F
PMID:30044717	Supp S1G
PMID:30044717	fig S2
PMID:30044717	fig S2
PMID:30044717	Fig S2C,E
PMID:30044717	Fig 5
PMID:30044717	fig 5B
PMID:30044717	fig 5B
PMID:30044717	Fig S4C
PMID:30044717	fig1
PMID:30044717	Figure 1
PMID:30044717	Fig 2B
PMID:30044717	Fig S4C
PMID:30044717	Fig2a (vw: average survival ~ 7 cell cycles)
PMID:30044717	fig 6A
PMID:30044717	Fig S4C
PMID:30044717	Fig S4C
PMID:30044717	Fig 5C
PMID:30044717	fig 4
PMID:30053106	requires long flap (binding affinity much higher with 27-nt than 15-nt flap)
PMID:30072377	Fig. 4A,B
PMID:30072377	Fig. 3C, D; Fig. 4A,B
PMID:30072377	Fig. 4C. Resistant to 1mM spermidine at 37C.
PMID:30072377	Fig. 3B, Fig. 4A,B
PMID:30072377	Fig. 4C Resistant to 1 mM spermidine at 37C.
PMID:30072439	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30072439	decreased cellular diphosphoglycerate level
PMID:30072439	Sorbitol addition partly suppresses beta-glucan accumulation in cwh43-G753R mutant cells
PMID:30072439	Drastic changes in antioxidants, sugar derivatives, amino acid derivatives, organic acids, coenzyme A (CoA), and nucleotide derivatives. Most of these compounds are biomarkers for nutritional starvation (low-glucose or nitrogen-starvation).
PMID:30072439	Partial suppression of growth defect in the presence of sorbitol
PMID:30072439	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	Partial suppression of growth defect in the presence of sorbitol
PMID:30072439	However, in scs2Δ scs22Δ double deletion mutant cells, localization of both Cwh43–GFP and AHDL– mCherry at the plasma membrane disappeared, and, instead, accumulated in the cytoplasm
PMID:30072439	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	Normal glucose consumption, but cell division is sensitive to low glucose condition
PMID:30072439	increased cellular dimethyl-histidine level during vegetative growth
PMID:30072439	Revealed by lipidomic analysis using mass spectrometry, thin layer chromatography, and lipid droplet staining
PMID:30072439	Revealed by thin layer chromatography
PMID:30072439	Lack of lipid droplet formation
PMID:30072439	Lack of lipid droplet formation
PMID:30072439	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30076928	transcription read through by PCR
PMID:30076928	RT-PCR
PMID:30076928	transcription read through by PCR
PMID:30076928	RT-PCR
PMID:30076928	mini-chromosome loss assay
PMID:30089114	Heterochromatin structure protects native CENP-A from ubiquitin-mediated degradation.
PMID:30089114	polyubiquitylated
PMID:30089908	Fig. 1g
PMID:30089908	Regulation of asymmetric gene expression from parental genomes
PMID:30089908	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	Regulation of asymmetric gene expression from parental genomes
PMID:30089908	Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies
PMID:30089908	Homothalic pak2∆ partners exhibit fusion efficiency decrease of ~20% as compared to wildtype partner fusion. Homothalic pak2∆ cells undergo transient fusion with frequency of ~10%, which is absent in wildtype matings.
PMID:30089908	fig 1 II
PMID:30089908	Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies
PMID:30089908	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	M-cells
PMID:30089908	P-cells (rapid) M-cells (delayed)
PMID:30089908	Extended Data Fig. 3b, Supplementary Video 5a
PMID:30089908	GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329
PMID:30089908	GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329
PMID:30089908	(Fig. 1a, type IIIa
PMID:30089908	Fig. 1a, type IIIb
PMID:30089908	abolished karyogamy with transient cytogamy (this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	abolished karyogamy with transient cytogamy (this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	Figure 1c
PMID:30089908	Extended data figure 1 F dominant over shk2 downstream sporulation phenotypes
PMID:30089908	in M-cell
PMID:30089908	Fig. 1a, type IIIb
PMID:30089908	******abolished, in M cells*******Fig. 2a, Supplementary Video 5, Fig. 2b, Supplementary Video 2a Importantly, mei3 was also asymmetrically expressed in WT...zygotes first express the meiotic inducer Mei3 from the P genome.
PMID:30089908	go-ontology/issues/16327
PMID:30089908	*******to nucleus of opposite mating type cell******
PMID:30089908	Fig. 3d, Supplementary Video 5b
PMID:30089908	Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b
PMID:30089908	Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b
PMID:30089908	Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b
PMID:30089908	Fig. 2c never ending search for mating partner
PMID:30089908	never ending search for mating partner by P cell
PMID:30102332	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	Figures 4 & 5.
PMID:30102332	Figures 4 & 5.
PMID:30102332	Figure 5.
PMID:30102332	Figure 5.
PMID:30102332	Figure 5.
PMID:30102332	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	Figures 4 & 5.
PMID:30104346	evidence is combination of ChIP in this paper plus data in other publications showing that Ctp1 binds DNA directly
PMID:30104346	evidence is combination of ChIP in this paper plus data in other publications showing that Rad50 orthologs (and therefore almost certainly Sc Rad50) binds DNA directly
PMID:30104346	evidence is combination of ChIP in this paper plus data in other publications showing that Rad52 binds DNA directly
PMID:30110338	H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331
PMID:30110338	H3 K9me3
PMID:30110338	H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331
PMID:30110338	H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331
PMID:30116786	Fig 4C
PMID:30116786	Fig 4E
PMID:30116786	fig 3B
PMID:30116786	fig 3B
PMID:30116786	fig 3C *********during G0
PMID:30116786	Fig. 3F loss of mitotic competence
PMID:30116786	Fig 3
PMID:30116786	Fig 3
PMID:30116786	Fig 3
PMID:30116786	Fig 3
PMID:30116786	Fig 4A,E
PMID:30116786	Fig S3
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E *******during quiesence
PMID:30116786	Fig 4E
PMID:30116786	Fig 4E
PMID:30116786	Fig. 3F loss of mitotic competence
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30134042	assayed at cdc18 and cdc22
PMID:30201262	SFig5
PMID:30201262	fig6
PMID:30201262	fig6
PMID:30201262	fig 1.
PMID:30201262	Temperature was shifted at prophase or metaphase.
PMID:30201262	Temperature was shifted at anaphase B.
PMID:30201262	fig6
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30212894	correlation with gel shift assays
PMID:30217891	S14
PMID:30217891	fig3
PMID:30217891	fig3
PMID:30279276	Cdc42-GTP assayed with CRIB; broad zones of activity
PMID:30280012	Fig 6
PMID:30280012	Fig 6
PMID:30280012	Figure S5A, S5B,
PMID:30280012	Fig 6
PMID:30280012	Fig 6
PMID:30280012	Fig S5C, S6
PMID:30280012	Fig 6
PMID:30280012	Fig 6
PMID:30282034	at transcription_termination_signal
PMID:30282034	at transcription_termination_signal
PMID:30282034	at transcription_termination_signal
PMID:30282034	at transcription_termination_signal
PMID:30332655	inferred from phenotypes and from direct assay using human calcineurin
PMID:30348841	deletion of Brc1 significantly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	Nse4 foci gone in nse6 mutant cells; Nts1 overexpression background to mitigate nse6Δ genotoxin sensitivity
PMID:30348841	MMS-induced Nse4 SUMOylation was also reduced in brc1􏰀 cells but was similar to wild-type in rhp18􏰀 cells, which support normal Nse4-GFP focus formation (Fig. 4B)
PMID:30348841	As anticipated, the MMS-induced SUMOylation of Nse4-TAP in wild-type cells was detectable upon immunoprecipitation (IP) of Nse4 without overexpression or initial enrichment of SUMO (Fig. 4A)
PMID:30348841	Notably, however, deletion of either Nse5 or Nse6 strongly reduced Nse4 residence at all binding sites tested, which was most evident under conditions of genotoxic stress that stimu- late de novo Smc5-Smc6 loading
PMID:30348841	Notably, however, deletion of either Nse5 or Nse6 strongly reduced Nse4 residence at all binding sites tested, which was most evident under conditions of genotoxic stress that stimu- late de novo Smc5-Smc6 loading
PMID:30348841	nse2-SA brc1􏰀 cells are more sensitive to genotoxins than either single mutant (Fig. 4C).
PMID:30348841	mutations in brc1 weaken interaction with nse6
PMID:30348841	Nse4 sumoylation at wild type level
PMID:30348841	Nse4 sumoylation reduced in brc1Δ
PMID:30348841	Nse4 sumoylation undetectable in nse6Δ
PMID:30348841	deletion of Nse5 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	deletion of Nse6 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	Nse4 foci gone in nse6 mutant cells; Nts1 overexpression background to mitigate nse6Δ genotoxin sensitivity
PMID:30348841	physical interaction between brc1-T672A and Smc5
PMID:30348841	physical interaction between brc1-T672A and Nse6
PMID:30348841	fig 1 a: brc1 mutant abolishes Nse4 nuclear foci in HU/MMS treated cells
PMID:30348841	fig 1 brc1 mutant cells expressing brc1-T672A are deficient in Nse4 foci formation
PMID:30355493	S3C
PMID:30355493	2d
PMID:30355493	2d
PMID:30355493	3c
PMID:30355493	2d
PMID:30355493	2d
PMID:30355493	2d
PMID:30355493	fig4
PMID:30355493	2d
PMID:30355493	2d
PMID:30355493	2d
PMID:30355493	2d
PMID:30355770	Fig. 2B
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. S6
PMID:30355770	Fig. S6
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2B
PMID:30355770	Fig. 7D
PMID:30355770	Fig. S8
PMID:30355770	Fig. 4B
PMID:30355770	Fig. S8
PMID:30355770	Fig. S8
PMID:30355770	Fig. 7D
PMID:30355770	Fig. 2B
PMID:30355770	Fig. 2B
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 4B
PMID:30355770	Fig. 4B
PMID:30355770	Fig. 4B
PMID:30355770	Fig. S5
PMID:30355770	Fig. S5
PMID:30355770	Fig. S5
PMID:30355770	Fig. S6
PMID:30355770	Fig. 2B
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 2A
PMID:30355770	Fig. 7D
PMID:30355770	Fig. 7D
PMID:30355770	Fig. 7D
PMID:30355770	Fig. 7D
PMID:30389790	fig 6
PMID:30389790	fig 10
PMID:30389790	fig 10
PMID:30389790	fig S4
PMID:30389790	fig S4
PMID:30389790	fig 6
PMID:30389790	fig 5b
PMID:30389790	fig 5b
PMID:30389790	fig 2b
PMID:30389790	fig 2b
PMID:30389790	figure 5 and 11 (no loss of viability )
PMID:30389790	figure 5c hypoglycosylation
PMID:30389790	figure 5c
PMID:30389790	figure 5c
PMID:30389790	figure 5b and S2
PMID:30389790	fig 10
PMID:30389790	Glucosidase 1, a type II membrane protein with a luminal hydrolytic domain, removes the outermost glucose from protein-linked Glc3Man9GlcNAc2 in the endoplasmic reticulum
PMID:30389790	fig 3b
PMID:30389790	fig 5b
PMID:30389790	fig 5b
PMID:30393157	fig 4
PMID:30393157	Fig. 5A
PMID:30393157	Fig. 5A
PMID:30393157	Fig. 5A
PMID:30393157	Fig. 5A
PMID:30393157	Fig. 5A
PMID:30393157	Fig. 5A
PMID:30393157	Fig. 5A
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	Fig. 2B
PMID:30393157	Fig. 2B
PMID:30393157	Fig. 2B
PMID:30393157	Fig. 2C/D
PMID:30393157	Fig. 2C/D
PMID:30393157	Fig. 2C/D
PMID:30393157	Fig. 2C/D
PMID:30393157	fig 2E/F
PMID:30393157	fig 2E/F
PMID:30393157	fig 2E/F
PMID:30393157	fig 2E/F
PMID:30393157	figure 3D
PMID:30393157	Fig. 2C/D
PMID:30393157	figure 3D
PMID:30393157	Fig. 2B
PMID:30393157	fig 1C/D
PMID:30393157	fig 1A
PMID:30393157	fig 4
PMID:30393157	fig 4
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:30393157	table2
PMID:3040264	table1
PMID:3040264	table1
PMID:3040264	table1
PMID:3040264	fig 2 b (uncondensed chromosomes)
PMID:3040264	fig 2 B
PMID:3040264	fig 2 b (uncondensed chromosomes)
PMID:3040264	fig 2 a no spindle rod like chromsomes
PMID:3040264	2b
PMID:3040264	fig 2 a
PMID:3040264	fig 2 a no spindle rod like chromsomes
PMID:3040264	fig 2 a no spindle rod like chromsomes
PMID:30427751	figure 2 A with increased loc to spb
PMID:30427751	figure 2 B
PMID:30427751	figure 2 A with increased loc to spb
PMID:30427751	figure6AC
PMID:30427751	figure 1
PMID:30427751	figure6AC
PMID:30427751	figure 1 G/H (from preexisting microtubules)
PMID:30427751	figure6D
PMID:30427751	figure 5I
PMID:30427751	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	figure 5GH
PMID:30427751	fig 5A (recruitment)
PMID:30427751	figure 5A
PMID:30427751	figure 5A
PMID:30427751	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	figure 2 B
PMID:30427751	figure 2 B
PMID:30451685	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	Figure 2—figure supplement 1D
PMID:30451685	Figure 2D and Figure 2—figure supplement 2
PMID:30451685	Figure 2—figure supplement 2
PMID:30451685	Figures 4C and 4D; assayed_using cpy1
PMID:30451685	Figure 4E
PMID:30451685	Figure 4E
PMID:30451685	Figure 2D and Figure 2—figure supplement 2
PMID:30451685	Figure 2D and Figure 2—figure supplement 2
PMID:30451685	Figure 2—figure supplement 2
PMID:30451685	Figure 2D and Figure 2—figure supplement 2
PMID:30451685	Figure 2D and Figure 2—figure supplement 2
PMID:30451685	Figure 2—figure supplement 2
PMID:30451685	Figure 2D and Figure 2—figure supplement 2
PMID:30451685	Figure 3—figure supplement 1
PMID:30451685	Figure 2—figure supplement 1A
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A
PMID:30451685	Figure 3—figure supplement 1B
PMID:30451685	Figure 3—figure supplement 2
PMID:30451685	Figure 3—figure supplement 2
PMID:30451685	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	Figure 3—figure supplement 2
PMID:30451685	Figure 3—figure supplement 2
PMID:30451685	Figure 3—figure supplement 2
PMID:30451685	Figure 4A; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4—figure supplement 1C; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4A; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4A; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	Figure 4B
PMID:30451685	Figure 4B
PMID:30451685	Figure 4B
PMID:30451685	Figure 4B
PMID:30451685	Figure 4B
PMID:30451685	Figure 4B
PMID:30451685	Figure 4B
PMID:30451685	Figure 4C,D
PMID:30451685	Figures 2A and 2B; assayed_using cpy1
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	Figure 4C,D
PMID:30451685	Figure 4C,D
PMID:30451685	Figure 4C,D
PMID:30451685	Figure 4C,D
PMID:30451685	Figure 4C,D
PMID:30451685	Figure 4C,D
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1A, 2B
PMID:30451685	Figure 3—figure supplement 1B, 2B; assayed__using cpy1
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	Figures 2A and 2B; assayed_using cpy1
PMID:30451685	Figure 1 (direct assay for vacuolar membrane) and Figure 1-figure supplement 1 (sequence feature evidence for transmembrane)
PMID:30451685	when SpHfl1 was overexpressed from a strong nmt1 promoter, the cytosolic signal of mYFP-SpAtg8 disappeared and the vacuole membrane localization of mYFP-SpAtg8 became much more conspicuous (Figure 1F).
PMID:30451685	Figure 2
PMID:30451685	Figure 2 and Figure 2-figure supplement 1
PMID:30462301	Figure 3B and Supplementary Figure S6
PMID:30462301	Figure 2C, D, Supple- mentary Figure S3A and C
PMID:30462301	Figure 2C, D, Supple- mentary Figure S3A and C
PMID:30462301	suggested by Junko
PMID:30462301	Figure 6B and Supplementary Figure S8C
PMID:30462301	Figure 6B and Supple- mentary Figure S8B
PMID:30462301	Figure 6B and Supple- mentary Figure S8B
PMID:30462301	Figure 6B and Supplementary Figure S8C)
PMID:30462301	Figure 6B and Supplementary Fig- ure S8B
PMID:30462301	Figure 6B and Supplementary Fig- ure S8B
PMID:30462301	Figure 6B and Supplementary Fig- ure S8B
PMID:30462301	competatively with lem2
PMID:30462301	Figure 4F and Supplementary Figure S7F
PMID:30462301	Supplementary Figure S7E
PMID:30462301	Supplementary Figure S7E
PMID:30462301	Figure 4A
PMID:30462301	Supplementary Figure S7E
PMID:30462301	Figure 4A
PMID:30462301	Figure 4A
PMID:30462301	Figure 4A
PMID:30462301	competatively with sad1
PMID:30462301	Supplementary Figure S7A-D)
PMID:30462301	Figure 3
PMID:30462301	Figure 3
PMID:30462301	Figure 3
PMID:30462301	Figure 3
PMID:30462301	Figure 3B and Supplementary Figure S6
PMID:30462301	Figure 3B and Supplementary Figure S6
PMID:30462301	Figure 3B and Supplementary Figure S6
PMID:30462301	Figure 3A
PMID:30462301	Figure 3A
PMID:30462301	Figure 3A
PMID:30462301	Figure 3A
PMID:30462301	Supple- mentary Figure S5B
PMID:30462301	Supple- mentary Figure S5B
PMID:30462301	Supple- mentary Figure S5B
PMID:30462301	Supple- mentary Figure S5B
PMID:30462301	Supple- mentary Figure S5B
PMID:30462301	Supple- mentary Figure S4A)
PMID:30462301	Figure 2E and Supple- mentary Figure S4B
PMID:30462301	Supple- mentary Figure S4A)
PMID:30462301	Supple- mentary Figure S4A)
PMID:30462301	Supple- mentary Figure S4A)
PMID:30462301	Supplementary Figure S1A-E
PMID:30462301	Figure 2C, Supplementary Figure S3A and C
PMID:30462301	Figure 2C, Supplementary Figure S3A and C
PMID:30462301	Figure 2C, Supplementary Figure S3A and C
PMID:30462301	(Fig- ure 2D, Supplementary Figure S3B and C
PMID:30462301	(Fig- ure 2D, Supplementary Figure S3B and C
PMID:30463883	at 33 degrees Celsius
PMID:30463883	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	at 36 degrees Celsius
PMID:30463883	at 36 degrees Celsius
PMID:30463883	at 36 degrees Celsius
PMID:30463883	at 33 degrees Celsius
PMID:30463883	at 36 degrees Celsius
PMID:30463883	at 33 degrees Celsius
PMID:30463883	at 33 degrees Celsius
PMID:30463883	figure 2 AB
PMID:30463883	figure 2 AB
PMID:30463883	figure 2 AB
PMID:30463883	at 36 degrees Celsius
PMID:30463883	at 36 degrees Celsius
PMID:30463883	figure 2 AB
PMID:30463883	figure 2 AB
PMID:30471998	Dip1 activates Arp2/3 complex to nucleate linear actin filaments analogous to branched actin filaments created by Wsp1-mediated Arp2/3 complex activation. These Dip1-Arp2/3 complex nucleated filaments act as seeds for Wsp1-mediated Arp2/3 complex branching nucleation.
PMID:30475921	wtf13 driver, wtf18 suppressor
PMID:30475921	wtf13 driver, wtf18 suppressor
PMID:30475921	wtf18-2 allele assayed
PMID:30475921	when wtf13 antidote not present (homozygous, wtf13poison/wtf13+, or wtf13poison/wtf13Δ
PMID:30475921	suppresses wtf13 drive
PMID:30475921	wtf13 driver, wtf18 suppressor
PMID:30475921	wtf13 driver, wtf18 suppressor
PMID:30503780	fig 2 D
PMID:30503780	(transeferred from Junk's session PMID:30462301)
PMID:30503780	(transeferred from Junk's session PMID:30462301)
PMID:30503780	(transeferred from Junk's session PMID:30462301)
PMID:30503780	(transeferred from Junk's session PMID:30462301)
PMID:30503780	Figures 5C
PMID:30503780	Figures 5C
PMID:30503780	Figures 5A and 5B
PMID:30503780	Figures 5A and 5B
PMID:30503780	fig S5B
PMID:30503780	fig S5B
PMID:30503780	fig S5B
PMID:30503780	fig S5B (southern blot)
PMID:30503780	fig S5B
PMID:30503780	fig S5B
PMID:30503780	incompatible with DNA binding
PMID:30503780	fig4
PMID:30503780	fig4
PMID:30503780	figure3 (incompatible with rap1 binding)
PMID:30503780	figure 2D
PMID:30503780	figure 2D
PMID:30503780	figure 2D
PMID:30503780	Figures 5A and 5B
PMID:30528393	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30528393	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30528393	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30528393	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30530492	glycosphingolipid transport
PMID:30530492	glucosylceramide, galactosylceramide
PMID:30573453	(Figure 2c)
PMID:30573453	FIgure S4
PMID:30573453	(Figure 2c)
PMID:30573453	(Figure 2c)
PMID:30573453	2d
PMID:30573453	(Figure 3a)
PMID:30573453	(Figure 3a)
PMID:30573453	fig6
PMID:30573453	fig6
PMID:30573453	(figure S8)
PMID:30573453	(Figure S8)
PMID:30573453	FIgure S8
PMID:30573453	FIgure S8
PMID:30573453	fig6
PMID:30573453	(Figure 2c)
PMID:30573453	(Figure S7)
PMID:30573453	fig5
PMID:30573453	(Figure 3a)
PMID:30573453	(Figure S7)
PMID:30573453	FIgure S7
PMID:30573453	fig6
PMID:30573453	2d
PMID:30573453	fig6
PMID:30573453	fig6
PMID:30573453	fig6
PMID:30573453	fig6
PMID:30573453	fig6
PMID:30573453	fig6
PMID:30573453	fig5
PMID:30573453	fig5
PMID:30573453	fig5
PMID:30573453	fig5
PMID:30573453	fig5
PMID:30573453	(Figure 4c)
PMID:30573453	(Figure 4d)
PMID:30573453	FIgure 4C
PMID:30601114	Figure 2A and Figure 2–figure supplement 1B-E
PMID:30601114	Non-adenosine residues upstream of the poly(A) tail were also rapidly removed by Ccr4-Not when Puf3 or Zfs1 were present
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	Figure 1–figure supplement 1A
PMID:30601114	Figure 1–figure supplement 1A
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	figure 2
PMID:30601114	figure 2 B
PMID:30601114	figure 2 B
PMID:30601114	ADD DOMAIN WHEN SO TERM AVAILABLE Figure 2A and Figure 2–figure supplement 1B-E
PMID:30601114	Figure 2A and Figure 2–figure supplement 1B-E
PMID:30601114	Figure 1–figure supplement 1B/Figure 1–figure supplement 1C
PMID:30601114	PRE element Figure 1–figure supplement 1B/Figure 1–figure supplement 1C
PMID:30601114	Figure 1A and Figure 1–figure supplement 1D- E)
PMID:30601114	Figure 1A and Figure 1–figure supplement 1D- E)
PMID:30601114	Figure 1A and Figure 1–figure supplement 1D- E) (I think it is correct to describe as an enzyme regulator (MF, because it increases processivity.)
PMID:30601114	Figure 1B and Figure 1–figure supplement 1D-E (I think it is correct to describe as an enzyme regulator (MF, because it increases processivity.)
PMID:30601114	Non-adenosine residues upstream of the poly(A) tail were also rapidly removed by Ccr4-Not when Puf3 or Zfs1 were present
PMID:30602572	Fig 1C observed that Klp5􏰀/Klp6􏰀 contained only 2.3 􏰁 0.4 (mean 􏰁 S.E.).
PMID:30602572	Figure 6C-D Increased mitochondrial numbers and decreased mitochondrial sizes with overall mitochondrial volume same as what is observed in wild-type cells
PMID:30602572	Figure 1C-D
PMID:30602572	(Fig. S5B) Furthermore, in Klp4􏰀 cells, which typically contain sev- eral short mitochondria (Fig. 1A), absence of Dnm1 results in a single large, fused mitochondrion
PMID:30602572	Figure 6B
PMID:30602572	Figure 1B the anti-parallel microtubule bundles are only about half the length of wild-type bundles
PMID:30602572	Figure 2C the mitochondria have a fission frequency that is almost double that of wild-type
PMID:30602572	Klp5􏰀/Klp6􏰀 cells exhibited a fission frequency that was half that of WT
PMID:30602572	WT cells highly overex- pressing Dnm1 had 11.6 􏰁 0.2 mitochondria (mean 􏰁 S.E.), which is twice that of WT cells
PMID:30602572	We counted 23.3 􏰁 1.4 (mean 􏰁 S.E.) mitochondria in Klp5􏰀/Klp6􏰀 cells lacking Mmb1􏰀 (Fig. 6C), which was not significantly different from Mmb1􏰀 cells
PMID:30626735	75 J/m^2; Andres SN et al. (2019)
PMID:30626735	200 Gy; Andres SN et al. (2019)
PMID:30626735	Andres SN et al. (2019)
PMID:30635402	This phenotype is observed in the presence of ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], a catalytic topo II inhibitor.
PMID:30635402	Identified by mass spectrometry
PMID:30635402	Identified by mass spectrometry
PMID:30635402	Identified by mass spectrometry
PMID:30635402	Identified by mass spectrometry
PMID:30635402	Identified by mass spectrometry
PMID:30635402	also assayed directly using human CKII
PMID:30635402	Identified by mass spectrometry
PMID:30635402	These phosphorylation sites were identified by the phos-tag analysis, phospho-specific antibodies, and in vitro phosphorylation assay
PMID:30635402	ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], is a catalytic topo II inhibitor
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Cellular fractionation; affecting Rec25
PMID:30640914	Rec25 visualization
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	Cellular fractionation; affecting Rec25
PMID:30640914	Cellular fractionation; affecting Rec25
PMID:30640914	Rec25 visualization
PMID:30640914	Rec25 visualization
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	S1A
PMID:30640914	S1A
PMID:30640914	S1A
PMID:30640914	S1A
PMID:30640914	S2
PMID:30640914	S2
PMID:30640914	S2
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	fig8
PMID:30640914	S4
PMID:30640914	fig8
PMID:30640914	fig s4
PMID:30640914	S2
PMID:30640914	s1
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30640914	mbs1 hotspot quantification
PMID:30640914	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	Recombination assay; assayed region: ade6 gene
PMID:30646830	trm401 (Trm4a) methylates C34 of tRNA-Leu (CAA) and tRNA-Pro (CGG) as well as all C48 tRNA methylation sites. Methylates C34 only on intron-containing tRNA.
PMID:30646830	Abolished tRNA cytosine-5 methylation of C49 and C50 (tRNA bisulphite sequencing)
PMID:30646830	trm402 (Trm4b) methylates C49 and C50 of tRNAs
PMID:30646830	abolished tRNA C34, C48 methylation (trna bisulphite sequencing)
PMID:30649994	S3
PMID:30649994	3E
PMID:30649994	3E
PMID:30649994	3E
PMID:30649994	3E
PMID:30649994	4b
PMID:30649994	Supplemental Figure S2
PMID:30649994	Supplemental Figure S2
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	tfs1∆ reduced centromere noncoding RNA in the clr4∆ strain. Northern blot assay
PMID:30652128	rpd1-S7A reduced centromere noncoding RNA in the clr4∆ strain. Northern blot assay
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	rpd1-S7A increased the rate of gross chromosomal rearrangement in the otherwise wild-type background. Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL
PMID:30652128	Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL
PMID:30652128	Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30652128	Monitoring an extra-chromosome ChL
PMID:30658998	fig 1B
PMID:30658998	fig 1B
PMID:30658998	fig 1B
PMID:30658998	fig 1D
PMID:30658998	fig 1C
PMID:30658998	fig 1B
PMID:30658998	fig 1B
PMID:30658998	fig 1B
PMID:30658998	supressed dna fragmentation
PMID:30658998	supressed dna fragmentation
PMID:30658998	fig 1D supressed by hexestrol or clomifene
PMID:30658998	fig 1C supressed by hexestrol
PMID:30659798	fig2
PMID:30659798	fig 2f
PMID:30667359	Figure 6C
PMID:30667359	Figure 6C
PMID:30667359	Figure 6C
PMID:30667359	Figure 6c
PMID:30667359	Figure 6B
PMID:30667359	Figure 6C
PMID:30667359	Figure 6B
PMID:30667359	Figure 6C
PMID:30667359	Figure 2B
PMID:30667359	Figure 2B
PMID:30667359	Figure 2B
PMID:30667359	Figure 2B
PMID:30667359	Figure 6C
PMID:30715423	... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe.
PMID:30715423	... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe.
PMID:30715423	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	No queuosine-mediated reduction of translational errors at GGC (Gly) and UGC (Tyr) codons
PMID:30715423	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30726745	Figure S5
PMID:30726745	Figure 7A
PMID:30726745	Figure 2, Figure 3
PMID:30726745	Figure 1
PMID:30726745	Figure 2, Figure 3.
PMID:30726745	Figure 6
PMID:30726745	Figure 7A
PMID:30726745	Figure 7C, 7D
PMID:30726745	Figure 7C, 7D
PMID:30726745	Figure 7A
PMID:30726745	Figure 7C, 7D
PMID:30726745	Figure 7C, 7D
PMID:30726745	Figure 7A
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Fig6 The nuclear envelope is marked with Cut11-GFP
PMID:30759079	data not shown
PMID:30759079	data not shown
PMID:30759079	data not shown
PMID:30759079	Fig6 The nuclear envelope is marked with Cut11-GFP
PMID:30759079	Fig6 The nuclear envelope is marked with Cut11-GFP
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30773398	Fig 1a
PMID:30773398	Fig 3
PMID:30773398	homodimer
PMID:30773398	Figure S2
PMID:30773398	Figure S2
PMID:30773398	Fig 1a
PMID:30773398	Figs 1C, S1
PMID:30773398	Figure 1E
PMID:30773398	Figure 1E
PMID:30773398	Figure S2
PMID:30773398	Figure 1E
PMID:30773398	Figure 1E
PMID:30773398	Figure S2
PMID:30773398	Figure S2
PMID:30773398	Figure S2
PMID:30773398	Figs 1B, 1D, 1F, S1, S2
PMID:30773398	Figs 1B, 1D, 1F, S1, S2
PMID:30773398	Figs 1B, 1D, 1F, S1, S2
PMID:30796050	Fig EV2
PMID:30796050	also inferred from orthology and various genetic interactions
PMID:30796050	Fig EV3; restrictive temperature for cdc2-M68
PMID:30796050	Fig EV3
PMID:30796050	Fig EV3
PMID:30796050	Fig 3
PMID:30796050	Fig 2
PMID:30796050	Fig 1
PMID:30796050	Fig 4
PMID:30796050	Fig 1
PMID:30796050	Fig S3
PMID:30796050	Fig S3
PMID:30796050	Fig S3
PMID:30796050	Fig S3
PMID:30796050	Fig S3
PMID:30796050	Fig S3
PMID:30796050	Fig 4
PMID:30796050	Fig 4
PMID:30796050	Fig 3
PMID:30796050	Fig 2
PMID:30796050	Fig 2
PMID:30796050	Fig S2
PMID:30796050	Fig S2
PMID:30796050	Fig S2
PMID:30796050	Fig S2
PMID:30796050	Fig S1
PMID:30796050	Fig S1
PMID:30796050	Fig 1
PMID:30796050	Fig 1
PMID:30796050	Fig 4
PMID:30796050	Fig 4
PMID:30796050	Fig 3; less intense Y arc in 2D gel
PMID:30796050	Fig 3; less intense Y arc in 2D gel
PMID:30796050	Fig 3
PMID:30796050	Fig 2, S2
PMID:30796050	Fig 2
PMID:30796050	Fig 1
PMID:30796050	Fig 1
PMID:30796050	Fig 1
PMID:30806623	Fig. 6
PMID:30806623	Fig. 6
PMID:30806623	Fig. 6
PMID:30806623	Fig. 1
PMID:30806623	Fig. 5
PMID:30806623	Fig. 1
PMID:30806623	Fig. 1
PMID:30806623	Fig. 1
PMID:30806623	Fig. 6
PMID:30806623	Fig. 3
PMID:30806623	Fig. 3
PMID:30806623	Fig. 6
PMID:30806623	Fig. 1
PMID:30806623	Fig. 1
PMID:30810475	fig7
PMID:30810475	figS6,7
PMID:30810475	figS6,7
PMID:30810475	figS6,7
PMID:30810475	figS6,7
PMID:30810475	fig7
PMID:30810475	fig7
PMID:30810475	fig7
PMID:30810475	fig7
PMID:30810475	fig7
PMID:30810475	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30810475	fig4
PMID:30810475	fig6
PMID:30810475	fig6
PMID:30810475	fig7
PMID:30810475	fig7
PMID:30810475	fig7 they say fragmented nucleus but they stained chromosomes, not nuclear envelope
PMID:30810475	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	fig1
PMID:30810475	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	fig1b
PMID:30810475	fig1b
PMID:30810475	fig1b
PMID:30810475	fig1
PMID:30810475	fig1b
PMID:30810475	fig4
PMID:30810475	fig4
PMID:30810475	fig4
PMID:30810475	fig4
PMID:30810475	fig1
PMID:30810475	fig1
PMID:30810475	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30810475	Required for the splicing of several genome-wide transcripts. Inferred from transcriptome sequencing of the mutant strain prp16F528S. Splicing defects in transcripts validated by RT-PCR assays.
PMID:30810475	Required for splicing of introns with strong 5' splice site - U6 snRNA and branch site - U2 snRNA interactions
PMID:30810475	fig1
PMID:30810475	fig1
PMID:30810475	fig1
PMID:30810475	fig1
PMID:30840879	MEMBRANE LIPID BINDING Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	fig 4e
PMID:30840879	MEMBRANE LIPID BINDING Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	fig 2A Figure 2A
PMID:30840879	2b normal lpid binding
PMID:30840879	1F
PMID:30840879	1F Defining the Rga7-binding motif within Rng10 further, we found that Rng10(751–950) bound Rga7(1–320) with a similar Kd of 0.69 μM (Figures 1F, 1G, and S2B)
PMID:30840879	To test for a direct interaction, we performed in vitro binding assays using recombinant Rng10 C terminus and the Rga7 F-BAR (Figures 1D and S2A). GST- Rng10(751–1,038) efficiently bound His6-Rga7(1–320) with a dissociation constant (Kd) of 0.43 μM (Figures 1D, 1E, and S2B).
PMID:30840879	F-BAR/BAR domain adaptors Rng10(751–950) interacts directly with the Rga7 F-BAR domain
PMID:30840879	GFP-Rga7(277–695) alone, lacking the majority of the F-BAR domain, could not localize to the PM, resulting in massive cell lysis
PMID:30840879	fig 4
PMID:30840879	fig 2b
PMID:30840879	fig 3c
PMID:30840879	fig 3 c
PMID:30840879	fig 3 c
PMID:30840879	fig 3e
PMID:30840879	fig 3 e
PMID:30840879	fig 3e
PMID:30840879	Figure 2A
PMID:30840879	fig 1B
PMID:30840879	fig 2A Figure 2A
PMID:30840879	fig 1B
PMID:30853434	Figure 3C-D
PMID:30853434	Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging)
PMID:30853434	Figure 3A-B (Live-cell time-lapse imaging)
PMID:30853434	Figure 3A-B (Live-cell time-lapse imaging)
PMID:30853434	Figure S4F and G (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC)
PMID:30853434	Figure S4C-D
PMID:30853434	Figure 3D (live cell DIC)
PMID:30853434	Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging)
PMID:30853434	Figure S1
PMID:30853434	Figure S1
PMID:30853434	Figure S1
PMID:30853434	Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging)
PMID:30853434	Figure S1
PMID:30853434	Figure 4I (Live-cell time-lapse imaging)
PMID:30853434	Figure 4G (live cell DIC)
PMID:30853434	Figure 4G (live cell DIC)
PMID:30853434	Figure 1H-I (live cell imaging)
PMID:30853434	Figure 1C
PMID:30853434	Figure S2C (live cell imaging)
PMID:30853434	FIg 1 D
PMID:30853434	Figure S2A-B (live cell imaging)
PMID:30853434	Figure 4G (live cell DIC)
PMID:30853434	Figure 4H (vw moved down to FYPO:0003481) (live cell DIC)
PMID:30853434	Figure S4F & H (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC)
PMID:30853434	FIg 1 D
PMID:30853434	FIg 1 D
PMID:30853434	Figure 3C-D (live cell DIC)
PMID:30853434	Figure 1H-I (live cell imaging)
PMID:30853434	Figure S3C-D (live cell imaging)
PMID:30853434	Figure S3A (live cell imaging)
PMID:30853434	Figure S4A (live cell imaging)
PMID:30853434	Figure S4A (live cell imaging)
PMID:30853434	Figure S4G (vw moved down to FYPO:0003481) (live cell DIC)
PMID:30853434	Figure S4A
PMID:30853434	Fig 2 E-F
PMID:30853434	Figure 4A-B (live cell imaging)
PMID:30853434	Figure 2E-F (live cell imaging)
PMID:30853434	Figure 4G (live cell DIC)
PMID:30853434	Figure S3A (live cell imaging)
PMID:30853434	Figure S4F&H (live cell DIC)
PMID:30853434	Figure S3C-D (live cell imaging)
PMID:30853434	Figure S1
PMID:30853434	Figure S1
PMID:30853434	Figure S4F and G (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC)
PMID:30853434	Figure 4E (moved from wee) (skewed towards small, low severity)
PMID:30853434	increased binding by about 2 fold from Figure 4C-D
PMID:30853434	Figure 3A-B (Live-cell time-lapse imaging)
PMID:30853434	Figure 1D-G (live cell imaging)
PMID:30853434	Figure 2A-B (vw changed to cell division site during M-phase from septum) (live cell imaging)
PMID:30862564	converted from bp by cc
PMID:30862564	converted from bp by cc
PMID:30967422	figure2b
PMID:30967422	figure2b
PMID:30967422	figure2b
PMID:30967422	figure2b
PMID:30973898	Fig 1D
PMID:30973898	figure1 B
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure1 A
PMID:30973898	figure 4 DAPI staining
PMID:30973898	figure 4 C mini-chromosome Ch16 loss assay
PMID:30973898	figure 5A
PMID:30973898	mini-chromosome Ch16 loss assay
PMID:30973898	figure 1B
PMID:30973898	Fig 1D
PMID:30973898	figure 3A
PMID:30973898	figure S2A
PMID:30973898	figure S2B
PMID:30973898	figure 2B (two hybrid)
PMID:30973898	figure 2B (two hybrid)
PMID:30973898	figure 2B (two hybrid)
PMID:30973898	figure 2B (two hybrid)
PMID:30973898	figure 2C
PMID:30973898	figure 2C
PMID:30973898	figure 2C
PMID:30973898	figure 2C
PMID:30973898	Figure 2D
PMID:30973898	Figure 2D
PMID:30973898	figure 2D
PMID:30973898	figure 2D
PMID:30973898	figure 3A
PMID:30973898	figure 3A
PMID:30973898	figure 3A
PMID:30973898	figure 3A
PMID:30973898	figure 4C
PMID:30973898	figure 4C
PMID:30973898	figure 5A
PMID:30973898	figure 5A
PMID:30973898	figure 5A
PMID:30973898	figure S2A
PMID:30973898	figure S2B
PMID:30973898	figure 5A
PMID:30973898	figure 5A
PMID:30975915	Fig 4
PMID:30975915	Fig. 4B
PMID:30975915	Fig. 4B
PMID:30975915	Figure 3
PMID:30975915	Figure 1
PMID:30975915	Figure 3
PMID:30975915	Fig. 4A
PMID:30975915	Fig. 4B
PMID:30975915	Fig 4
PMID:30975915	Figure 1
PMID:30975915	Figure 1
PMID:30975915	Figure 1
PMID:30975915	figure 1A
PMID:30975915	figure3
PMID:30975915	Fig. 2B
PMID:30992049	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	same as nmt81-vid21 alone
PMID:30992049	25 degrees; same as mst1-L344S alone
PMID:30992049	hhf2 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	same as swi1delta alone
PMID:30992049	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	hhf2 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 3
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 2
PMID:30996236	Fig 3
PMID:31000521	(vw 3B? changed from normal to lagging, added penetrance) dfp1-CFP-2CD rescues minichromosome loss in the absence of Swi6.
PMID:31000521	) Rad21 locates to centromere in dfp1-3A mutants.
PMID:31000521	(vw: changed genotype to add swi6 delt) dfp1-CFP-2CD restores lagging chromosomes in the absence of Swi6. Rad21 locates to centromere in dfp1-CFP-2CD mutants.
PMID:31000521	(Figure 3B Chp1 fails to accumulate at noncentromeric location in the absence of Chp2 and Swi6.
PMID:31000521	(Figure 3B vw changed more specific to lagging chromosmes) Increase the frequency of mitotic cells showing lagging chromosomes. Rad21 fails to accumulate at centromere in the absence of Swi6.
PMID:31000521	Fig 7 using minichromosome
PMID:31000521	Fig 7 using minichromosome
PMID:31000521	Fig 7 using minichromosome
PMID:31000521	fig 7 B
PMID:31000521	fig 7B
PMID:31000521	fig 7 B
PMID:31000521	fig 7 B
PMID:31000521	Rad21-GFP enrichment at the centromere is unaffected in swi6-sm1 (Figure S4C)
PMID:31000521	The swi6-sm1 allele disrupts silencing without lagging chro- mosomes (Yamagishi et al. 2008) (Figure S4, A and B). We observed a similar frequency of lagging chromosomes in wild-type (1%) and swi6-sm1 mutants (1.03%).
PMID:31000521	Fig 7 using minichromosome
PMID:31000521	5C
PMID:31000521	5E
PMID:31000521	5B
PMID:31000521	SUPP S1
PMID:31000521	Figure 3B
PMID:31000521	Figure 3B
PMID:31000521	Figure 3B
PMID:31000521	fig 3B
PMID:31000521	Figure 3B
PMID:31000521	Fig-2C
PMID:31000521	Fig-2C
PMID:31000521	Fig-2C
PMID:31000521	Fig-2A Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.
PMID:31000521	Fig-2A Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.
PMID:31000521	(VW changed to multi allele) The delay of m-to-G1/S phase transition in swi6∆ and dfp1-3A was abolished after deleting mad2.
PMID:31000521	5B abolish Swi6 protein localization to centromere during vegetative growth
PMID:31000521	Fig 7B
PMID:31015410	Fig4 a,c
PMID:31015410	Fig 4a,c
PMID:31015410	Fig 4,b,c ENHANCER OF N/C ratio of lem2/rae1
PMID:31015410	Fig4 a,c
PMID:31015410	Supp Fig6
PMID:31015410	supp Fig6a
PMID:31015410	Fig3f
PMID:31015410	Fig3c,d, OE SUPRESSOR OF NEM1delta lem2 supresses the increased NC ratio of nem1 delta
PMID:31015410	Fig 3c
PMID:31015410	Fig3a,b
PMID:31015410	Fig2 d,e,f,g,h supp fig6b
PMID:31015410	Fig2a,b,c
PMID:31015410	Fig 1a shows the lem2 chromatin binding domain is not required to restrict enhancement of the NC ratio of rae1-167
PMID:31015410	Fig 1a,b,c
PMID:31015410	Fig 1
PMID:31015410	Fig1 supp data
PMID:31015410	Fig1 supp data
PMID:31015410	Fig1 supp data
PMID:31015410	Fig1 supp data
PMID:31015410	Fig1 supp data
PMID:31015410	Fig1 supp data
PMID:31015410	Fig3f
PMID:31015410	Fig 3c
PMID:31015410	Fig 3c
PMID:31015410	supp Fig 7 supression of lem2delta
PMID:31015410	supp data Fig 1b,c
PMID:31015410	Fig1 and Fig1supp data
PMID:31015410	Fig3d
PMID:31015410	Fig3d, OE lem2 supresses the increased NC ratio of rae1-167
PMID:31015410	Fig3e suppression of nem1delta
PMID:31015410	Fig 3e
PMID:31015410	Fig 1 (normal compaction)
PMID:31015410	Fig 4a,c
PMID:31030285	fig8
PMID:31030285	not shown
PMID:31030285	Fig7
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	Fig7
PMID:31030285	Fig7
PMID:31030285	Fig7
PMID:31030285	Fig7
PMID:31030285	Fig6
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	cell growth is slower than wild type in glycerol and ethanol medium
PMID:31030285	Coq4 protein is decreased but Dlp1, Coq3, Coq5 and Coq8 are not
PMID:31030285	Coq4 protein is increased but Dlp1, Coq3, Coq5, and Coq8 are not
PMID:31030285	cell growth is faster than wild type in glycerol and ethanol medium
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	fig S1
PMID:31030285	Fig7
PMID:31030285	Fig7
PMID:31030285	Fig7
PMID:31041892	Figure 3; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 2; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	fig1
PMID:31041892	fig1
PMID:31041892	fig1
PMID:31041892	blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 3; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 2; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 4
PMID:31041892	Figure 4
PMID:31041892	Figure 5
PMID:31041892	Figure 3
PMID:31041892	Figure 3
PMID:31041892	Figure 2
PMID:31041892	Figure 2
PMID:31041892	Figure 5
PMID:31041892	Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	Figure 3
PMID:31041892	Figure 3
PMID:31041892	Figure 2
PMID:31041892	Figure 2
PMID:31053915	catechol O-methyltransferase activity
PMID:31053915	catechol O-methyltransferase activity (Vw I kept this as o-methytransferase since no report of catachols in fission yeast)
PMID:31072933	figure 1G
PMID:31072933	fig 2
PMID:31072933	figure 1G
PMID:31072933	figure 1G
PMID:31072933	Figure 1G/ figur2
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S4
PMID:31072933	figure S3
PMID:31072933	figure S4
PMID:31072933	figure S4
PMID:31072933	fig 3 B
PMID:31072933	fig 3 B
PMID:31072933	fig 3 B
PMID:31072933	figure 1c
PMID:31072933	figure 2C
PMID:31072933	figure2
PMID:31072933	figure 1e
PMID:31072933	figure 1e
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3A
PMID:31072933	figure 3F
PMID:31072933	figure 1e
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	figure 1c
PMID:31072933	(Rescued to WT level) Rad21 phosphorylation level in cohesin hinge cs mutants is rescued by Δwpl1, while the loss of the Rad21 protein level in cohesin hinge ts mutants cannot be rescued by Δwpl1
PMID:31072933	figure S7A
PMID:31072933	figure S7A
PMID:31072933	figure S7A
PMID:31072933	figure S7A
PMID:31072933	figure 6c
PMID:31072933	figure 6c
PMID:31072933	figure 6c
PMID:31072933	figure 6c
PMID:31072933	figure 6c
PMID:31072933	figure 6c
PMID:31072933	figure 4 AB
PMID:31072933	figure 4 AB
PMID:31072933	figure 4 AB
PMID:31072933	figure 4 AB
PMID:31072933	figure 4 AB
PMID:31072933	figure 4D-H
PMID:31072933	figure 4D-H
PMID:31072933	figure 4D-H
PMID:31072933	figure 5C
PMID:31072933	Fig 5C
PMID:31072933	figure 5C
PMID:31072933	figure S8
PMID:31072933	figure S8
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure S3
PMID:31072933	figure 6c
PMID:31072933	figure 1G
PMID:31072933	figure 6c
PMID:31072933	figure 1G
PMID:31089172	fig 4
PMID:31089172	Fig. 6
PMID:31089172	Fig. 6
PMID:31089172	Fig. 6
PMID:31089172	fig 6
PMID:31089172	Figure 6C-E
PMID:31089172	Figure 6C-E
PMID:31089172	Figure 5E
PMID:31089172	Figure 5E
PMID:31089172	Figure 5E
PMID:31089172	Figure 5E
PMID:31089172	Fig. 5D and Supplementary Fig. S2A,C
PMID:31089172	Fig. 5D and Supplementary Fig. S2A,C
PMID:31089172	Fig. 5D and Supplementary Fig. S2A,C
PMID:31089172	Fig. 5D and Supplementary Fig. S2A,C
PMID:31089172	Fig. 5B,C)
PMID:31089172	Fig. 5B,C)
PMID:31089172	Fig. 5B,C)
PMID:31089172	Fig. 5B,C)
PMID:31089172	Figure 4A
PMID:31089172	fig 4
PMID:31089172	fig 4
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Figure 4AB
PMID:31089172	Fig. 4A
PMID:31089172	Fig. 4A
PMID:31089172	Fig. 4A
PMID:31089172	Figure 4A
PMID:31089172	Figure 4A
PMID:31089172	Figure 4A
PMID:31089172	Figure 4A
PMID:31089172	Figure 4A
PMID:31089172	Figure 4A
PMID:31089172	Fig. 4A
PMID:31089172	Fig. 3
PMID:31089172	Fig. 3
PMID:31089172	Fig. 3
PMID:31089172	Fig. 3
PMID:31089172	Fig. 3
PMID:31089172	Fig. 3A top
PMID:31089172	fig 2 E
PMID:31089172	fig 2 E
PMID:31089172	fig 2 E
PMID:31089172	fig 2 C/D
PMID:31089172	fig 2 C/D
PMID:31089172	fig 2 C/D
PMID:31089172	fig 2 A/B
PMID:31089172	fig 2 A/B
PMID:31116668	1d (vw: localized by the secretory pathway)
PMID:31116668	1e
PMID:31116668	fig4
PMID:31116668	5c
PMID:31116668	fig 5
PMID:31131414	Southern blot; same as rap1-7A single mutant
PMID:31149897	Fig 5
PMID:31149897	Fig 4
PMID:31149897	Fig 4
PMID:31149897	Fig 4
PMID:31149897	Fig 6
PMID:31149897	Fig 4; very small difference from fbh1delta alone
PMID:31149897	Fig 3
PMID:31149897	Fig 6
PMID:31149897	elg1∆ exhibits reduced direct repeat recombination associated with replication fork collapse at the RTS1 replication fork barrier
PMID:31149897	Figure 3A; increased spontaneous direct repeat recombination
PMID:31149897	PCNA foci persist longer than normal, and form large bright patches before disappearing (Fig 2).
PMID:31149897	Fig 5
PMID:31178220	SpTam41 interacts strongly with cardiolipin (CL)
PMID:31201205	Fig.3
PMID:31201205	Fig. 2BC
PMID:31201205	Figure 5 (vw: changed to pear, descendent of spherical)
PMID:31201205	Figure 5, (VW: I made this more specific- figure 1E (36) this phenotype in increased in the presence of magnesium
PMID:31201205	Figure 4
PMID:31201205	Figure 4
PMID:31201205	Figure 6
PMID:31201205	Figure 6
PMID:31201205	figure 7
PMID:31201205	figure 7B small viable
PMID:31201205	figure 7B
PMID:31201205	figure 7B small, viable
PMID:31201205	Figure 4
PMID:31201205	Figure 4
PMID:31201205	figure 7B
PMID:31201205	Fig.3
PMID:31201205	Fig.3
PMID:31201205	Figure 4
PMID:31201205	Fig. 2BC
PMID:31201205	Figure 4
PMID:31201205	Figure 4
PMID:31201205	Fig.3
PMID:31201205	Fig.3
PMID:31201205	Fig. 2BC
PMID:31201205	Fig. 2BC
PMID:31201205	small viable
PMID:31201205	Figure 6
PMID:31201205	The resulting cwh43 pdt1Δ 201 double mutant partly recovered colony formation capacity at 36°C, compared to that of the 202 cwh43 single mutant (Fig. 2D).
PMID:31201205	Fig. 2BC
PMID:31201205	Fig.3
PMID:31239353	consistent with Loz1 facilitating the repression of pho8 gene expression in high zinc (Figure 2A)
PMID:31239353	Pho8 abundance is increased in high zinc in a loz1 deletion strain (Figure 2B and 2C)
PMID:31239353	figure 4 hat although processing of Pho8 is dependent upon the growth phase of cells, zinc is the major factor that limits Pho8 activity in vivo
PMID:31239353	fig1
PMID:31239353	fig1 abolished?
PMID:31239353	abolished ?
PMID:31239353	Figure 1B and 1C
PMID:31239353	figure 4 hat although processing of Pho8 is dependent upon the growth phase of cells, zinc is the major factor that limits Pho8 activity in vivo
PMID:31239353	Figure 5D
PMID:31239353	Figure 5D
PMID:31239353	figure 8
PMID:31239353	(DIRECTLY_ACTIVATES pho8 GO:0004035) As zinc did not affect Pho8 stability, processing, or dimerization, we hypothesized that the activity of Pho8 is directly affected by cellular zinc status. .. .....Taken together these results are consistent with yeast maintaining an inactive 5 Zinc-dependent alkaline phosphatase activity pool of Pho8 in low zinc, which can be rapidly activated as soon as zinc is available.
PMID:31239353	Figure 1B and 1C
PMID:31239353	pho8 transcript and protein levels are increased in high zinc BUT ZINC DEPENDENT CHAnges are independent of transcript levels
PMID:31239353	10-100 micromolar
PMID:31239353	fig1
PMID:31239353	Figure 1A
PMID:31239353	fig1
PMID:31239353	Figure 1A Zinc-dependen
PMID:31239353	figure 7
PMID:31239353	Figure 5B
PMID:31239353	figure 5B
PMID:31239353	Figure 2B
PMID:31239353	reduced during conditions of zinc shock (Figure 8 and Figure 9). (as Pho8 binds its zinc cofactors inside of the secretory pathway, it activity is dependent upon zinc transporters that supply zinc ions to the secretory pathway
PMID:31239353	reduced alkaline phosphatase activity and Pho8 dimerization (assayed via an EGS cross linking experiment - see Figures 6C and 6D)
PMID:31239353	reduced alkaline phosphatase activity and Pho8 dimerization (assayed via an EGS cross linking experiment - see Figures 6C and 6D)
PMID:31239353	figure 7
PMID:31239353	figure 7
PMID:31257143	Figures S3B and S3D
PMID:31257143	Figure 2B demonstrates robust arres 3b 80% 12 hours
PMID:31257143	figure 2d
PMID:31257143	figure 2d
PMID:31257143	Figure 2B demonstrates robust arres
PMID:31257143	3b 80% 12 hours
PMID:31257143	Figures S3B and S3C
PMID:31257143	Figure S4
PMID:31257143	figure 2D
PMID:31257143	Figure S4
PMID:31260531	chromatin association at MCBs is part of positive regulation of G1/S transition of mitotic cell cycle
PMID:31260531	Rep2 locates SAGA complex at MBF-regulated promoters.
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	non-canonical termination sites
PMID:31269446	non-canonical termination sites
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	non-canonical termination sites
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31269446	18 °C
PMID:31276301	fig 6
PMID:31276301	Furthermore, abnormally elon- gated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	Table 3
PMID:31276301	Figure 7b
PMID:31276301	Fig 4a
PMID:31276301	(Table 3)
PMID:31276301	Table 2 Figures 5a–d and S2)
PMID:31276301	Fig 4e
PMID:31276301	Figure S1a
PMID:31276301	Figure S1a
PMID:31276301	Fig 4b
PMID:31276301	fig 6
PMID:31276301	Furthermore, abnormally elon- gated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	Fig 4a
PMID:31276301	fig 4d
PMID:31276301	fig. 4e
PMID:31276301	fig. 4e
PMID:31276301	Figure S1a
PMID:31276301	Figure S1a
PMID:31276301	Figure S1a
PMID:31276588	Figure 1F
PMID:31276588	Figure 1D
PMID:31276588	Figure 1B
PMID:31276588	Figure 1C
PMID:31276588	Figure 1B
PMID:31276588	Figure 1C
PMID:31276588	Figure 1F.
PMID:31276588	Figure 1E
PMID:31276588	Figure 1E
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2C
PMID:31276588	Figure 2A
PMID:31276588	reporter system
PMID:31276588	Octo phosphatase IP8 is a relevant substrate for the Aps1 pyrophos- phatase with respect to phosphate homeostasis.
PMID:31276588	Figure 1B
PMID:31276588	Figure 1C
PMID:31276588	Figure 1D
PMID:31276588	Figure 1D
PMID:31276588	Figure 1D
PMID:31276588	Figure 1B
PMID:31276588	Figure 1C
PMID:31276588	Figure 1D
PMID:31276588	Figure 1D
PMID:31278118	cells revealed that H3K9me2 was notably decreased at cen- tromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	cells revealed that H3K9me2 was notably decreased at cen- tromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	Figure 4A https://github.com/pombase/fypo/issues/3693
PMID:31278118	Compared to the single ago1D or pds5D deletion mutants, the ago1D pds5D double mutant showed severe loss-of-silencing of Kint2::ura4+ (Figure S2C).
PMID:31278118	Figure 6B
PMID:31278118	However, the localization of Pds5 to euchromatic locations was unaffected in hetero- chromatin-deficient cells (Figure 5E)
PMID:31278118	However, the localization of Pds5 to euchromatic locations was unaffected in hetero- chromatin-deficient cells (Figure 5E)
PMID:31278118	ue to their antagonistic roles in cohesion establish- ment, the lethality of eso1D can be suppressed by deletion of wpl1 (Feytout et al. 2011; Kagami et al. 2011). Whereas wpl1D did not show defects in heterochromatic silencing, the eso1D wpl1D double mutant showed derepression of mat2P::ura4+ and haploid meiosis similar to pds5D cells (Figure 6A)
PMID:31278118	fig 2B (Figure S1B and Table S2). This variegated staining pattern is a char- acteristic of mutants that are known to be defective in the main- tenance of heterochromatin and that show a reduction, but not loss, of H3K9me levels (Taneja et al. 2017). Indeed, ChIP anal- yses of H3K9 di- and trimethylation (H3K9me2/3) showed a reduction in heterochromatic H3K9 marks at or near mat2P in pds5D (Figure 2B).
PMID:31278118	Fig 5 B vw: moved pds5 to assayed target
PMID:31278118	Figure 6A)
PMID:31278118	fig1 d
PMID:31278118	fig7
PMID:31278118	table 1
PMID:31278118	table1
PMID:31278118	fig 1D/E
PMID:31278118	Figure 6B
PMID:31278118	Figure S5 Moreover, when we deleted pds5 in cells lacking Eso1 and/or Wpl1, the levels of haploid meiosis displayed by double or triple mutants were comparable to that of single-mutant pds5D
PMID:31278118	Figure S5
PMID:31278118	fig 1D/E
PMID:31278118	fig 1D/E
PMID:31278118	Figure 6B
PMID:31278118	fig7
PMID:31278118	ue to their antagonistic roles in cohesion establish- ment, the lethality of eso1D can be suppressed by deletion of wpl1 (Feytout et al. 2011; Kagami et al. 2011). Whereas wpl1D did not show defects in heterochromatic silencing, the eso1D wpl1D double mutant showed derepression of mat2P::ura4+ and haploid meiosis similar to pds5D cells (Figure 6A)
PMID:31285271	Fig.2 gus1 associates with polysomes
PMID:31285271	Fig.2 Asc1 associates with polysomes.
PMID:31285271	fig4
PMID:31285271	fig4h
PMID:31285271	fig4h
PMID:31285271	6
PMID:31285271	6f
PMID:31285271	cytoplasmic translation is a parent to this term
PMID:31285271	3e
PMID:31285271	3e
PMID:31285271	3a
PMID:31285271	3a
PMID:31285271	2d
PMID:31285271	2d
PMID:31285271	2d
PMID:31285271	2d
PMID:31285271	2d
PMID:31285271	1e
PMID:31285271	1d
PMID:31285271	Fig2. rar1 associates with polysomes
PMID:31285271	Fig.2 Asc1 associates with polysomes.
PMID:31285271	Fig5. Asc1 colocalized with stress granule proteins in response to heat shock.
PMID:31289327	S2
PMID:31289327	S2
PMID:31289327	S2
PMID:31289327	4a
PMID:31289327	5
PMID:31289327	S2
PMID:31289327	5
PMID:31294478	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	4
PMID:31294478	4
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	fig 1 A and F
PMID:31294478	fig 1b We have shown using ChIP-seq experiments that Sen1 associates with all types of RNA polymerase III-transcribed genes. This includes tRNA_genes, 5S rRNA_genes, snu6 and srp7 but not the TFIIIC-bound COC sites.
PMID:31294478	COINCIDENT WITH 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	Figure 5B
PMID:31294478	2c, 5d
PMID:31294478	2c, 5d
PMID:31294478	2c, 5d
PMID:31294478	2b
PMID:31294478	2b
PMID:31294478	2b
PMID:31294478	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	4
PMID:31294478	AL fig 4. vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	2c, 5d
PMID:31294478	ChIP-qPCR of Dbl8 indicates that Dbl8 is enriched at the rDNA and at highly-expressed RNAPII-transcribed genes
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	AL fig 4. vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	2b
PMID:31294478	2b
PMID:31294478	2b
PMID:31294478	2b
PMID:31294478	2b
PMID:31294478	3
PMID:31294478	3
PMID:31294478	4
PMID:31294478	AL fig 4. vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294478	AL fig 4. and 5c vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.
PMID:31294800	UAAU motif
PMID:31315658	Additional file 1: Fig. S1b, c
PMID:31315658	Additional file 1: Fig. S1b, c
PMID:31315658	(Fig. 1c)
PMID:31315658	n sharp contrast, the H3K9me2 levels remained constant in leo1∆ cells throughout G0 phase (Fig. 2; Additional file 2: Fig. S2
PMID:31315658	Additional file 1: Fig. S1b, c
PMID:31332096	reduced chk1 phosphorylation
PMID:31332096	elimination of Rad3-specific phosphorylation
PMID:31341193	Increased co-localization with Cfr1
PMID:31341193	Reduced co-localyzation with the PI3P probe Cherry-FYVE
PMID:31341193	fig 1 Increased colocalization with Cfr1
PMID:31341193	28ºC
PMID:31341193	37ºC
PMID:31341193	Evaluated by measuring the size of Vps10-GFP foci
PMID:31341193	Microscopy
PMID:31341193	Fig 1 a-c
PMID:31341193	Fig 1 a-c
PMID:31341193	Dot-Blot assay
PMID:31341193	fig5
PMID:31341193	fig 1d
PMID:31341193	this is in a mutant but I guess it occurs physiologicall?
PMID:31341193	fig1
PMID:31341193	fig1
PMID:31341193	fig5
PMID:31341193	fig1
PMID:31341193	fig1
PMID:31341193	fig1
PMID:31341193	Fig1 (major)
PMID:31341193	Fig1 (minor)
PMID:31341193	isp6 delta supresses the abnormal Vps10 processing detected in vps35 delta strain
PMID:31341193	Microscopy
PMID:31341193	Microscopy
PMID:31341193	isp6 delta supresses the abnormal Vps10 processing detected in ent3 delta gga21 delta gga22 delta strain
PMID:31341193	isp6 delta suppresses Vps10 abnormal processing observed in ent3 delta gga22 delta strain
PMID:31341193	isp6 delta supresses the abnormal Vps10 proessing detected in gga21 delta gga22 delta strain
PMID:31341193	Reduced growth on 0.6M KCl plates
PMID:31341193	Reduced growth at 37ºC on YES agar plates
PMID:31341193	fig 7
PMID:31341193	fig 7 Syb1 co-localizes with late endosome markers
PMID:31341193	Dot-Blot test
PMID:31341193	Increased co-localization with Cfr1
PMID:31341193	Reduced co-localization with the PI3P probe Cherry-FYVE
PMID:31341193	Reduced co-localization with the PI3P probe Cherry-FYVE
PMID:31341193	FIg 3 Increased co-localization with Cfr1
PMID:31341193	Co-localization with TGN marker
PMID:31350787	fig1
PMID:31350787	fig1
PMID:31350787	fig4B
PMID:31350787	fig1
PMID:31350787	Fig. 3
PMID:31350787	Fig. 3
PMID:31350787	fig6
PMID:31350787	fig5
PMID:31350787	fig5
PMID:31350787	"fig 1A """
PMID:31350787	fig1
PMID:31350787	fig1
PMID:31350787	"fig 1A they say it is dramatically reduced....between med/low severity... ""dramatically reduced on glycerol medium, which requires high mitochondrial respiratory activity at 30 °C"""
PMID:31350787	fig2A The Dmti2 mutant was not able to grow at all on medium containing glycerol at the restrictive temperature of 37 °C
PMID:31350787	figb
PMID:31350787	fig1
PMID:31350787	fig1
PMID:31350787	"fig 1A """
PMID:31350787	"fig 1A """
PMID:31366733	fig7
PMID:31366733	fig7
PMID:31366733	fig7
PMID:31366733	fig7
PMID:31366733	fig7
PMID:31371524	inhinits hhf4 binding
PMID:31371524	figure 2
PMID:31371524	figure 2
PMID:31371524	figure 2
PMID:31371524	figure 6
PMID:31371524	figure 4
PMID:31371524	figure 6
PMID:31427431	2
PMID:31427431	4
PMID:31427431	5
PMID:31427431	7
PMID:31427431	5
PMID:31427431	2f
PMID:31427431	2f
PMID:31427431	5
PMID:31427431	6
PMID:31427431	6
PMID:31427431	6
PMID:31427431	7
PMID:31427431	s2
PMID:31427431	2f
PMID:31427431	2f
PMID:31427431	2
PMID:31427431	2
PMID:31427431	s2
PMID:31427431	2
PMID:31427431	2
PMID:31427431	2
PMID:31427431	1f
PMID:31427431	1e
PMID:31427431	1e
PMID:31427431	S1
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1b
PMID:31427431	1
PMID:31427431	7
PMID:31427431	7
PMID:31427431	6
PMID:31427431	6
PMID:31427431	6
PMID:31427431	6
PMID:31427431	6
PMID:31427431	7
PMID:31427431	6
PMID:31427431	7
PMID:31427431	7, type II cells
PMID:31456006	leucine auxotroph background
PMID:31456006	bunch of auxotrophic backgrounds shown - indicative of a.a. starvation
PMID:31456006	leucine auxotroph background
PMID:31468675	measured by cell growth spot assay
PMID:31468675	partial derepression of marker gene at silent mating-type cassette; measured by cell growth spot assay
PMID:31468675	measured by cell growth spot assay
PMID:31468675	spot assay
PMID:31468675	colocalizes with H3K9me2
PMID:31468675	measured by cell growth spot assay
PMID:31468675	colocalizes with H3K9me2
PMID:31468675	colocalizes with H3K9me2
PMID:31477575	fig2b
PMID:31477575	fig2b
PMID:31477575	fig1
PMID:31477575	S3B
PMID:31477575	S3B
PMID:31477575	S3B
PMID:31477575	S1
PMID:31477575	S1
PMID:31477575	3c
PMID:31477575	3c
PMID:31477575	fig1
PMID:31477575	S1
PMID:31477575	fig1
PMID:31477575	fig1
PMID:31477575	S1
PMID:31477575	S1
PMID:31477575	S1
PMID:31477575	S1
PMID:31477575	S1
PMID:31477575	S1
PMID:31477575	fig2b
PMID:31477575	fig2b
PMID:31477575	fig2b
PMID:31483748	Figure 2C
PMID:31483748	fig2
PMID:31483748	fig2
PMID:31483748	fig2
PMID:31483748	Figure 2A
PMID:31483748	Figure S1A
PMID:31483748	Figure S1A
PMID:31483748	Figure 3, A and B . number and intensity
PMID:31483748	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	Reduced Rad21 binding to chromosome arms
PMID:31483748	issues/3588 decreased
PMID:31483748	fig1 B–G
PMID:31483748	fig2
PMID:31483748	Figure 3, A and B
PMID:31483748	fig2
PMID:31483748	fig2
PMID:31483748	fig2
PMID:31483748	fig2
PMID:31483748	fig2
PMID:31483748	We examined whether Mto1 localizes to DNA repair factories and found that Mto1-mCherry was not detectable within the nucleus, as previously shown (Sawin et al., 2004; Venkatram et al.)
PMID:31483748	issues/3588 Figure 5, A–E
PMID:31483748	Figure 2C No increase in severity to mto1 delete
PMID:31483748	Figure 2C
PMID:31495586	Figure 2
PMID:31495586	Figure 3
PMID:31495586	Figure 6
PMID:31495586	Figure 6
PMID:31495586	Figure6
PMID:31495586	Figure 6
PMID:31495586	Figure 4
PMID:31495586	Figure 4 and 6
PMID:31495586	Figure 4 and 6
PMID:31495586	Figure 4 and 6
PMID:31495586	Figure1
PMID:31495586	Figure6
PMID:31495586	Figure6
PMID:31495586	Figure6
PMID:31495586	Figure6
PMID:31495586	Figure 4
PMID:31495586	Figure 3
PMID:31495586	Figure2, Increased 1.5-fold, assayed using CHD
PMID:31495586	FigureS5, assayed using LifeAct
PMID:31495586	FigureS5, assayed using LifeAct
PMID:31495586	Figure S6
PMID:31495586	Figure S6
PMID:31495586	Figure S6
PMID:31495586	Figure S6
PMID:31495586	1.1 fold, Figure S2
PMID:31495586	Figure S3
PMID:31495586	Figure S3
PMID:31495586	Figure S3
PMID:31495586	Figure S3
PMID:31495586	Figure S1, assayed using CHD
PMID:31495586	Figure3, S4, assayed using Myo52 and Fus1
PMID:31495586	Figure S5, assayed using LifeAct
PMID:31495586	FigureS3
PMID:31495586	FigureS3
PMID:31495586	FigureS3
PMID:31495586	FigureS3
PMID:31495586	assayed using CHD, FigureS1
PMID:31495586	Figure 3, assayed using Myo52
PMID:31495586	Figure 5
PMID:31495586	Figure 5, assayed using Myo52
PMID:31495586	Figure 5, assayed using Myo52
PMID:31495586	Figure 5, assayed using Myo52
PMID:31495586	Figure 4 and 6
PMID:31495586	Figure5
PMID:31495586	Figure5
PMID:31495586	Figure 2
PMID:31495586	Figure 2
PMID:31495586	Figure 2
PMID:31495586	Figure 2
PMID:31495586	Figure 2
PMID:31495586	Figure 2
PMID:31495586	Figure 2
PMID:31495586	Figure 3, assayed using Myo52
PMID:31495586	Figure 3
PMID:31495586	Figure 3
PMID:31495586	Figure 3
PMID:31495586	Increased 4-fold, Figure2
PMID:31495586	Increased 4-fold, FigureS1
PMID:31495586	Figure 2
PMID:31495586	Figure 1
PMID:31495586	Figure 3
PMID:31495586	Figure 3
PMID:31495586	Increased 4-fold, Figure2
PMID:31495586	Figure1
PMID:31509478	figS3C
PMID:31509478	fig6
PMID:31509478	fig 1
PMID:31509478	figure1
PMID:31509478	fig3
PMID:31509478	fig3
PMID:31509478	Figure 3E)
PMID:31509478	fig3
PMID:31509478	fig3
PMID:31509478	3F
PMID:31509478	Figure 3E)
PMID:31509478	Figure 6A
PMID:31509478	fig1
PMID:31509478	fig2
PMID:31509478	synonym =ring collapse fig3F
PMID:31509478	figS3C
PMID:31509478	figS3C
PMID:31509478	fig3
PMID:31509478	figS3C
PMID:31515876	When Loz1 is expressed at a constant level inside of cells, it binds to the zrt1 promoter in high zinc conditions and not in low zinc conditions (consistent with its role in gene repression in high zinc conditions
PMID:31515876	Loz1 represses gene expression when zinc is in excess and growth in zinc deficient media leads to de-repression of its target genes. Expression from the pgk1DTATA promoter leads to higher levels of Loz1 accumulating inside of cells, which in turn leads to higher levels of gene repression under low zinc conditions (Figure 1B)
PMID:31515876	When Loz1 is expressed at a constant level inside of cells, it binds to the adh4 promoter in high zinc conditions and not in low zinc conditions (consistent with its role in gene repression in high zinc conditions
PMID:31515876	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	ChIP-seq, RNA-seq and reporter gene analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 4)
PMID:31515876	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	ADD SO TERM WHEN AVAILABLE Mutagenesis of 3 Loz1 response elements in the SPBC1348.06c promoter resulted in the promoter no longer being repressed in high zinc in a manner that is dependent upon Loz1 (see Figure 4). The minimal Loz1 DNA binding domain (amino acids 426-522) also binds to this motif in vitro (supplemental Fig 2), and multiple copies of this element are able to confer Loz1-mediated gene repression in a minimal reporter system - see figure 6)
PMID:31532702	Figure 5E
PMID:31532702	Figure S6
PMID:31532702	Figure 5G (this term referes to initial
PMID:31532702	Figure 5H
PMID:31532702	Figure 5I
PMID:31532702	Figure 6A
PMID:31532702	Figure 6D, E
PMID:31532702	meiotic . The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31532702	top, Figure 3B, C)
PMID:31532702	meiosis I inital Figure 3B, C
PMID:31532702	Figure 2A
PMID:31532702	Figure S3B, C pentrance, frequently like quadruple
PMID:31532702	Figure S5
PMID:31532702	28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B)
PMID:31532702	28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B)
PMID:31532702	The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31532702	figure 1B
PMID:31532702	figure 1B
PMID:31532702	single nucleus
PMID:31532702	Figure 1D, E . monopolar?
PMID:31532702	Figure figure 1B, D
PMID:31532702	Figure 2A
PMID:31532702	I didn't check the supp, but probably can only make this annotation?
PMID:31532702	Figure 5B
PMID:31532702	Figure 5C, D
PMID:31532702	Figure 5E
PMID:31538680	Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31562247	figure 4c
PMID:31562247	figure 4ab
PMID:31562247	figure 4ab
PMID:31562247	figure 4c
PMID:31562247	Indeed, no noticeable change in mitochondrial morphology or altered mitochondrion numbers were found in the three mutant cells cultured in glucose-rich EMM (Fig. 5, C and D).
PMID:31562247	As shown in Fig. 6, A and B, ROS production under glucose starvation was reduced, but not abolished, in the absence of Dnm1 because only 􏰆25% of dnm1􏰇 cells were DCDHF-DA– positive after glucose starvation.
PMID:31562247	As shown in Fig. 5A, the changes in mitochondrial morphology were similar within 40 min of glucose starvation in the three mutant and WT cells
PMID:31562247	fig 3a
PMID:31562247	(with decreased total volume -. new term requested) Throughout the period of glucose starvation, mito- chondria in dnm1􏰇 cells did not appear to fragment but shrunk over time (Fig. 3A). mitochondrion numbers remained largely unchanged during glucose starvation (Fig. 3B)
PMID:31575705	Figure 1A
PMID:31575705	Figure 1A
PMID:31575705	fig1
PMID:31575705	constitutive
PMID:31575705	decreased replciation restart fig1 indicating that only one-third of forks arrested at the RTS1-RFB are efficiently restarted in the absence of Fft3.
PMID:31575705	normal replciation restart/ HR-mediated fork restart RTS1-RFB assay. urprisingly, the induction of downstream RS in fft3-K418R-myc strain was similar to the one observed in wild-type cells (Fig 4D, bottom panel). This finding indicates that the lack of the ATPase activity does not impact the efficiency of HR-mediated fork restart.
PMID:31575705	Fig 2 C RTS1-RFB assay
PMID:31575705	The fft3-K418R-myc strain exhibited similar sensitivity to CPT and MMS than fft3Δ cells, indicating that the ATPase activity is required to promote cell re- sistance to replication stress.
PMID:31575705	Fig 1A growth inhibited by 0.005% MMS after 4 days
PMID:31575705	RTS1-RFB assay
PMID:31582398	Figure. 5C, D normal (increased mitochondrial segregation during meiosis)
PMID:31582398	To verify that the attachment to microtubules was not necessary for segregation during meiosis, we employed parental cells lacking the microtubule-mitochondrial linker protein Mmb1 (Fu et al., 2011). Additionally, one of the parental cells had its mitochondria fluorescently labeled. In zygotes and asci resulting from this cross, we observed that parental mito- chondria continued to remain segregated (Fig. S2, C and D).
PMID:31582398	Figure. 3C, D, E, F and Video 5 mitochondrial mixing during meiosis
PMID:31582398	"tetrad dissection ""in the absence of Mcp5 in rho+ parental strain (strain PHP4xVA074; see Table S1), only 31.3% of the tetrads dissected (n = 16 tetrads) exhibited mtDNA segregation similar to that observed in Fig. 6 D."""
PMID:31582398	Figure. 3C, D, E, F and Video 5 mitochondrial mixing during meiosis
PMID:31584934	fig. 3,4
PMID:31584934	"""Consistent with this, we found that the deletion of pcf1 is synthetic lethal with the deletion of hip1, the gene encoding one subunit of the fission yeast HIRA complex (S4A Fig). T"""
PMID:31584934	"""Reciprocally, H3-H113D-HA association with wt H3 and H4 were severely reduced"""
PMID:31584934	fig. 2
PMID:31584934	"changed to decreased from abolished based on ""H3-FLAG association with H3-H113D-HA was severely reduced"""
PMID:31584934	fig. 7
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	fig. 6
PMID:31584934	coincident with replication fork barrier but dependent on JM formation - not sure if we can be more specific here than nuclear chromatin?
PMID:31584934	fig. 3c
PMID:31584934	fig. 3
PMID:31584934	fig. 3
PMID:31615333	Figure 2 and S3
PMID:31615333	Figure 2 and S3
PMID:31615333	Figure 1c
PMID:31615333	Figure S3
PMID:31615333	Figure 2 and 3
PMID:31615333	Figure S3
PMID:31615333	Figure 2 and 3
PMID:31615333	Figure S3
PMID:31615333	Figure S1
PMID:31615333	Figure 2, detected by northern blot analysis
PMID:31615333	Figure 2 and S3
PMID:31615768	fig 3
PMID:31615768	fig 3I
PMID:31615768	S2A
PMID:31615768	fig 4
PMID:31615768	fig 4
PMID:31615768	1E unbundled microtubules seen in early mitosis
PMID:31615768	S2A/4
PMID:31615768	S2A/4
PMID:31615768	S1
PMID:31615768	fig3a by cen2-GFP observation
PMID:31615768	1E unbundled microtubules seen in early mitosis
PMID:31615768	S2
PMID:31615768	1A
PMID:31615768	figureS4
PMID:31615768	fig 1C
PMID:31615768	fig 1C
PMID:31615768	fig 3
PMID:31615768	fig 3
PMID:31618856	Figure 2D
PMID:31618856	defective in microtubule growth during both interphase and mitosis
PMID:31618856	appears to retain normal microtubule nucleation activity
PMID:31618856	fig1
PMID:31618856	fig 3
PMID:31618856	fig 4
PMID:31618856	fig 4
PMID:31618856	fig 4
PMID:31641022	fig2
PMID:31641022	"chnaged from ""increased rate of sporulation"""
PMID:31644361	Figure 1H (in vitro) Cdr1 directly phosphory- lated Wee1, but Cdr1(K41A) did not ().
PMID:31644361	Cdr1 directly phosphory- lated Wee1, but Cdr1(K41A) did not (Figure 1H).
PMID:31644361	Figure 1 D Phosphorylation of Wee1 in fission yeast cells was reduced in the catalytically inactive mutant cdr1(K41A)
PMID:31644361	Fig1 In contrast, Cdr2 overexpression induced hyperphosphoryla- tion of Wee1 but no change in Cdk1-pY15
PMID:31644361	Fig 1C overexpression of Cdr1 but not of Cdr2 re- sulted in reduced cell size in cdr1∆cdr2∆ cells (Figure 1C
PMID:31644361	Fig1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity,
PMID:31644361	Fig1B. In contrast, Cdr2 overexpression induced hyperphosphoryla- tion of Wee1 but no change in Cdk1-pY15
PMID:31644361	Fig1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity,
PMID:31644361	Fig 1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity,
PMID:31644361	Figure 3 B
PMID:31644361	Along with enhanced Wee1 hyperphosphorylation, these cells di- vided at a smaller size than wild-type cells. These results show that Cdr1 localization to nodes is a limiting factor for phosphorylation of Wee1 and cell size at division
PMID:31644361	deed, cdr1∆ wee1(4A) cells divided at the same size as cdr1∆ cells
PMID:31644361	(Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD
PMID:31644361	(Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD
PMID:31644361	(Figure 3, A and D). We confirmed that wee1(4A) protein level does not increase and still localizes to cortical nodes
PMID:31644361	Accordingly, the size of wee1(4A) cells was largely (but not entirely) insensitive to Cdr1 overexpression (Figure 3G).
PMID:31644361	(Figure 4A). We confirmed that S. pombe Cdk1- asM17 directly thiophosphorylates Wee1 and Wee1(K596L)
PMID:31644361	Figure 5B) We tested the effects of artificially recruiting mEGFP-cdr1(∆460-482) back to nodes using cdr2-GFP- binding peptide (GBP)-mCherry, which contains the GBP. In this system, mEGFP-cdr1(∆460-482) colocalized with cdr2-GBP-mCherry at nodes.
PMID:31644361	Figure 3 A onsistent with this model, wee1(4A) phosphorylation was reduced when compared with wild type, and its phosphorylation was not altered by cdr1∆ or cdr2∆ (
PMID:31657618	Fig. 4
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Table
PMID:31657618	Fig. 3
PMID:31657618	Fig. 3
PMID:31657618	Fig. 3
PMID:31657618	Fig. 3
PMID:31657618	Fig. 3
PMID:31657618	Fig. 3
PMID:31657618	Fig. 4
PMID:31657618	Fig. 4
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31712578	Table S3
PMID:31712578	Table S3
PMID:31712578	Table S3
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31712578	Table S3
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31712578	Table S3
PMID:31712578	Table S3
PMID:31712578	Table S3
PMID:31712578	Table S3
PMID:31712578	Table S3; spore viability lower than wild type (~50% of wild-type viability)
PMID:31712578	Table S3; spore viability similar to wild type
PMID:31719112	temperature permissive for mcm4/cdc21-M68
PMID:31719112	temperature restrictive for cdc22-M45
PMID:31719163	localizes to division site after Gef1 and Scd2, but before contractile ring constriction begins
PMID:31719163	localizes to division site before Scd1, and before contractile ring constriction begins
PMID:31719163	localizes to division site before Scd1, and before contractile ring constriction begins
PMID:31777937	A novel 5′-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes
PMID:31811152	Figure 1b, (live cell observation)
PMID:31811152	Figure 4b (live cell observation)
PMID:31811152	Figure 1c
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 1b, Figure 4b (live cell observation)
PMID:31811152	Figure 4a
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 1b (live cell observation)
PMID:31811152	Figure 4a. homologous pairing examined at C24 locus
PMID:31811152	Figure 4b (live cell observation)
PMID:31811152	Figure 4b,
PMID:31811152	C24 locus. fig2
PMID:31811152	C24 locus. fig2
PMID:31811152	fig2
PMID:31811152	fig2
PMID:31811152	Figure 1c
PMID:31833215	same as maf1delta alone
PMID:31837996	RNA-seq
PMID:31837996	similar to pob3delta alone
PMID:31837996	RNA-seq
PMID:31837996	similar to pob3delta alone
PMID:31837996	assayed using bulk histones
PMID:31837996	assayed using bulk histones
PMID:31837996	RNA-seq
PMID:31837996	RNA-seq
PMID:31837996	RNA-seq
PMID:31848341	binds H3-H4 dimer; assayed in vitro using Xenopus histones
PMID:31895039	Fig.1b
PMID:31895039	Psm1 and Mis4 are found in Pef1 immunoprecipitates (Fig. 5AB)
PMID:31895039	Fig. 7. The phenotype is exacerbated by pph3 deletion and rescued by pef1 deletion
PMID:31895039	Figure 2—figure supplement 1
PMID:31895039	36.5°C
PMID:31895039	Fig.1 36.5°C
PMID:31895039	Fig. 2
PMID:31895039	Fig. 1 36.5°C
PMID:31895039	fig1c
PMID:31895039	Fig.1
PMID:31895039	Fig.1
PMID:31895039	Figure 1—figure supplement 1
PMID:31895039	Figure 1—figure supplement 1
PMID:31895039	"Figure 1—figure supplement 1. ""although colonies were tiny and grew very slowly"""
PMID:31895039	Fig.5
PMID:31895039	Phosphorylates Rad21 on threonine 262. Fig.5
PMID:31895039	Fig.7
PMID:31895039	Fig.7
PMID:31895039	Fig.7 34°C
PMID:31895039	Fig.7
PMID:31895039	Fig.7. Phenotype suppressed by the deletion of pef1
PMID:31895039	Fig.7. Phenotype suppressed by the deletion of pef1
PMID:31895039	34°C, Fig.7
PMID:31895039	34°C, Fig.7
PMID:31895039	Fig.5
PMID:31895039	Fig.8
PMID:31895039	Fig.8
PMID:31895039	Fig.8
PMID:31895039	Fig.8
PMID:31895039	Fig.8
PMID:31895039	Fig.8
PMID:31895039	Fig.8
PMID:31895039	Fig.1
PMID:31895039	Fig.1
PMID:31895039	Pef1 ablation or chemical inactivation of its kinase activity stimulates Rad21 and Mis4 binding to their cognates sites on chromosomes. The effect in most prominent in the G1 phase of the mitotic cycle.
PMID:31895039	Fig.1
PMID:31895039	Fig.6
PMID:31895039	Fig.7
PMID:31895039	Fig.7
PMID:31895039	Fig.4
PMID:31895039	Fig.4
PMID:31895039	Fig.7. Phenotype suppressed by the deletion of the pef1 gene
PMID:31895039	Fig.7. Phenotype suppressed by the deletion of the pef1 gene
PMID:31895039	Fig.2 supp1
PMID:31895039	"Figure 5Dm : ""In vitro Rad21 phosphorylation was abolished when Pef1 was purified from psl1 deleted cells"""
PMID:31895039	(Figure 5E and Figure 5—figure supplement 1). Replacement of T262 by an alanine abolished in vitro Rad21 phosphorylation by Pef1-GFP
PMID:31895039	fig 5g
PMID:31895039	antagonises pef1
PMID:31911490	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
PMID:31911490	fig 5C
PMID:31911490	fig 5e
PMID:31911490	Fig. 5B
PMID:31911490	Fig. 4B
PMID:31911490	fig2C
PMID:31911490	Fig. 1B cell length at division either of pmk1􏰂 cells or in a mutant strain lacking the dual-specificity phos- phatase Pmp1 that dephosphorylates and inactivates Pmk1 in vivo (14), ... was similar to that of wild-type cells (Fig. 1B)
PMID:31911490	fig 1B
PMID:31911490	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
PMID:31911490	Fig. 1B
PMID:31911490	(Fig. 1B)
PMID:31911490	fig 4h
PMID:31911490	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
PMID:31911490	Pyp2 protein levels increased 􏰁2 times in the mutant background (Fig. 5C), but they were of a lower magnitude than that in rnc1􏰂 versus wild-type cells (􏰁8 to 9 times) (Fig. 2C
PMID:31911490	12.13 + 0.1
PMID:31911490	FIg2
PMID:31911490	fig 3f
PMID:31911490	(Fig. 1D). In addition, basal Sty1 activity was significantly higher in exponentially growing rnc1􏰂 cells ex- pressing a genomic C-terminal hemagglutinin (HA)-tagged version of the MAP kinase, compared to wild-type cells or a pmk1􏰂 mutant
PMID:31911490	Fig 2B
PMID:31911490	These results suggest that while T50 is a main phosphorylation site for Sty1 within Rnc1, other phosphosites are likely targeted by this kinase in vivo.
PMID:31911490	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
PMID:31911490	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	and enhanced expression of Wak1, Wis1, and Pyp1 proteins during unperturbed growth (Fig. 5C) a
PMID:31911490	(Fig. 1B)
PMID:31911490	Fig. 1B Fig. 1C (14.04􏰃0.25 versus 11.98􏰃0.29􏰋m, respectively)
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	Fig. 2
PMID:31932483	Fig. 3
PMID:31932483	Fig. 4A
PMID:31932483	Fig. 7E
PMID:31932483	Fig. 6E
PMID:31932483	Fig. 6F
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 1 M KCl in agar
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	Fig 4B; 0.5 mM H2O2 in agar
PMID:31941401	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	Figure 1B
PMID:31941401	Fig. S2
PMID:31941401	Fig. S2)
PMID:31941401	Pho8Δ60 assay (Fig. S3A).
PMID:31941401	Fig. S2)
PMID:31941401	In contrast, Pho8Δ60 activity was only restored to about half of the wild-type level when expressing Atg38[AIM mut]. AND Tdh1-YFP processing assay
PMID:31941401	Figure 3A,B
PMID:31941401	Figure 2A Pho8Δ60 autophagy assay
PMID:31941401	Pho8Δ60 assay (Fig. S3A).
PMID:31941401	Figure 1E
PMID:31941401	Figure 1F
PMID:31941401	Figure 1G)
PMID:31941401	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	Figure 1G)
PMID:31941401	Figure 1G)
PMID:31941401	Figure 1G)
PMID:31941401	Figure 1G)
PMID:31980821	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4􏰀 ter1􏰀 for vegetative and qui- escent cells (Supplementary Figure S3D and E).
PMID:31980821	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4􏰀 ter1􏰀 for vegetative and qui- escent cells (Supplementary Figure S3D and E).
PMID:31980821	3D We confirmed that telomere foci moved from nuclear periphery to a more central area (zone 1 to zone 2 or 3) in bqt4􏰀 Vg cells
PMID:31980821	2B
PMID:31980821	Figure 2D We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clus- terization did not reach WT level in ter1􏰀 cells after 3 days in G0.
PMID:31980821	2D althouh also the percentage of cells that contain a unique telomeric cluster in G0 after streaks 3 and 4 (Fig- ure 2D). We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clus- terization did not reach WT level in ter1􏰀 cells after 3 days in G0.
PMID:31980821	accumulation of TERRA depends on Cid14, a RNA poly adenyl-transferase, (Supplementary Figure S5)
PMID:31980821	When ter1+ gene was deleted in bqt4􏰀 cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumula- tion of TERRA in Vg cells and this robust increase in tran- scription is even stronger after 48H in quiescence
PMID:31980821	As previously shown, we ob- served that telomere erosion and STEEx formation in ter1􏰀 cells correlates with defects to exit properly from G0 (22)
PMID:31980821	Indeed, in bqt4􏰀 ter1􏰀 cells the percentage of cells that are unable to form a colony increased in correlation with the massive accumulation of STEEx at D1 and D3 of senes- cence
PMID:31980821	When ter1+ gene was deleted in bqt4􏰀 cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumula- tion of TERRA in Vg cells and this robust increase in tran- scription is even stronger after 48H in quiescence
PMID:31980821	TERRA level was higher in bqt4􏰀 than WT in vegetative cells and this difference was substantially inten- sified after 48H in quiescence (Figure 6A),
PMID:31980821	TERRA level was higher in bqt4􏰀 than WT in vegetative cells and this difference was substantially inten- sified after 48H in quiescence (Figure 6A),
PMID:31980821	In contrast to ter1􏰀 cells in which the loss of growth capacity was progressive, the growth of bqt4􏰀 ter1􏰀 cells was severely impaired (Figure 4A and Supplementary Fig- ure S2).
PMID:31980821	5A. bqt4delta/ telomerase + cells exhibited wild-type telomeres that were stable in post-mitotic cells
PMID:31980821	STEEx were readily detected as two bands at 1500 and 900 bp, the highest one being prevalent (Figure 5A, right panel). Strikingly, we observed a massive accumulation of STEEx in quiescent bqt4􏰀 ter1􏰀 cells at early time points of quiescence (Figure 5A).
PMID:32012158	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	The interaction between these proteins was abolished in the absence of red1 (Fig 3A), suggesting that Red1 physically links Mmi1 with the exosome. and Fig 4B The direct binding of Red1 with Rrp6 was also observed (Fig 4B).
PMID:32012158	figure 3A
PMID:32012158	figure 1 a
PMID:32012158	figure 5B
PMID:32012158	figure 5B
PMID:32012158	figure 5A
PMID:32012158	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED IN GENOME
PMID:32012158	figure 1 a
PMID:32012158	figure 5A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure S3A
PMID:32012158	figure 2
PMID:32012158	figure 1 a
PMID:32012158	figure 2
PMID:32012158	figure 1 a
PMID:32012158	figure 1 a
PMID:32012158	figure 1 a
PMID:32012158	figure 6 a
PMID:32023460	increased cortical ER remodeling dynamics
PMID:32023460	(Figure 4 S4B).
PMID:32023460	Pil1 lacking the C terminus failed to interact with Scs2 (Figure S5F
PMID:32023460	cortical
PMID:32023460	decreased Pil1 protein abundance Figure S1F
PMID:32023460	resulting in the formation of fewer punctate eisosomes (Figure S1B).
PMID:32023460	(Figure S1F). increased Pil1 phosphorylation was detected in these cells
PMID:32023460	PMID:32023460 Of note, the PM coverage of eisosomes was also reduced in scs2Dscs22D cells (Figure S1B), implicating VAPs in the regulation of eisosome assembly.
PMID:32023460	(Figures 1A and 1B) (EM) data also confirmed that eisosomes/MCC associated with the cER, especially with curved cER rims, over the lateral cell cortex in WT (Figures 1C and S1A). Such an asso- ciation was abolished in scs2Dscs22D cells lacking ER-PM con- tacts.(the Exp says more but I don't know how to capture that)
PMID:32023460	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	increased cortical ER remodeling dynamics the cortical tubular ER pattern changes faster than wild type
PMID:32023460	increased cortical ER remodeling dynamics
PMID:32023460	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	(Figure 3A) decreased cortical ER remodeling dynamics the cortical tubular ER pattern changes slower than wild type
PMID:32023460	(Figure S3C). the cortical tubular ER pattern changes slower than wild type
PMID:32023460	(Figure 3A) the cortical tubular ER pattern changes slower than wild type
PMID:32023460	(Fig- ure S5G). the cortical tubular ER pattern changes faster than wild type
PMID:32023460	fig2 increased cortical ER remodeling dynamics
PMID:32023460	fig2 increased cortical ER remodeling dynamics
PMID:32023460	fig2 the cortical tubular ER pattern changes faster than wild type
PMID:32023460	(Figure S1F). Pil1 mis-assembled into fewer and longer filaments
PMID:32023460	Figure S3D) VW CHANGED GENOTYPE TO INCLUDE pil1 delta background. sey1 deleta is impled
PMID:32023460	decreased Pil1 protein abundance Figure S1F
PMID:32023460	(Figure 4 S4B).
PMID:32023460	(Figure 4 S4B).
PMID:32023460	(Figure 4 S4B).
PMID:32023460	(Figure 4 S4B).
PMID:32032353	inferred from crosses involving hemizygous diploids
PMID:32032353	assayed by expressing S.k. ortholog in S.p.
PMID:32032353	S.p. wtf13 assayed; doesn't specify which isoform (or if it's both)
PMID:32032353	Both wtf21 alleles were found at equal frequency in the viable spores.
PMID:32032353	inferred from crosses involving hemizygous diploids
PMID:32032353	S.p. wtf13 assayed; doesn't specify which isoform (or if it's both)
PMID:32032353	assayed by expressing S.k. ortholog in S.p.
PMID:32032353	assayed by expressing S.k. ortholog in S.p.
PMID:32047038	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32047038	(Fig. 5G) The IP6-binding pocket formed between CSN2 and Rbx1 is remarkably conserved from yeasts to plants and humans (Figs. 2D and 3D). Deleting ipk1, the yeast IP6 synthase, abolishes Csn2 interaction with Cul1 in Schizosaccharomyces pombe,
PMID:32047038	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32047038	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32053662	figure5 a-c
PMID:32053662	6bc
PMID:32053662	6bc
PMID:32053662	6bc
PMID:32053662	6d
PMID:32053662	6d
PMID:32053662	figure5 a-c
PMID:32053662	figure5 a-c
PMID:32053662	figure5 a-c
PMID:32053662	figure5 a-c
PMID:32053662	figure5 a-c
PMID:32053662	figure5 a-c
PMID:32053662	figure5 a-c
PMID:32053662	6d
PMID:32053662	6bc
PMID:32053662	6bc
PMID:32062975	Figure 6A
PMID:32062975	fig 6B
PMID:32062975	Figure 6A
PMID:32062975	Figure 6A
PMID:32071154	fig 5C
PMID:32071154	fig 5C
PMID:32071154	fig 5C
PMID:32071154	fig 4
PMID:32071154	fig4
PMID:32071154	fig 4
PMID:32071154	fig4
PMID:32071154	figure 2C
PMID:32071154	fig 2B
PMID:32071154	polysome profile
PMID:32071154	vw: changed from slow growth (6hr)
PMID:32071154	fig 4
PMID:32071154	fig 4
PMID:32071154	fig 4
PMID:32071154	polysome profile
PMID:32071154	Fig 7B
PMID:32071154	Fig 7B
PMID:32071154	Fig 7B
PMID:32071154	Fig 7B
PMID:32071154	Fig 7
PMID:32071154	Fig 7
PMID:32071154	Fig 7
PMID:32071154	Fig 7
PMID:32071154	figure 6F
PMID:32071154	figure 6F
PMID:32071154	Figure 6E
PMID:32071154	Figure 6E
PMID:32071154	Fig 6a
PMID:32071154	Fig 6a
PMID:32071154	Fig 6a
PMID:32071154	Fig 6a
PMID:32071154	fig 5C
PMID:32075773	37 C is a moderate heat shock for fission yeast, which does not slow growth nor exerts toxicity to wild-type cultures, but significantly affects the viability of cells lacking stress signaling components, such as the MAP kinase Sty1 (Figures 1E and S1B).
PMID:32075773	Fig S2A
PMID:32075773	Fig S2
PMID:32075773	fig2B S2B-D
PMID:32075773	fig2B S2B-D
PMID:32075773	fig2B S2B-D
PMID:32075773	fig2B S2B-D
PMID:32075773	fig2B S2B-D
PMID:32075773	fig2B S2B-D
PMID:32075773	fig2B S2B-D
PMID:32075773	Fig S2
PMID:32075773	Figure 1B
PMID:32075773	Figure 1B.
PMID:32075773	fig 4D
PMID:32075773	fig 4D
PMID:32075773	fig 3D) Lack of Mas5 abolishes both PAC formation and the assembly of stress granules.
PMID:32075773	Fig S2
PMID:32075773	Fig S2
PMID:32084401	FigS1A,C cells arrested G1 in low nitrogen then released into S phase at restrictive temperature cells the tested for viability at 25°C after S phase with only ccdc13hpm
PMID:32084401	Fig1B cells blocked in G1 by nitrogen starvation and released in presence of nitrogen into S phase with cdc13+ switched off
PMID:32084401	Fig S1D cdc13+ and cdc13HPM are not differentially sensitive to rum1. S phase same in both strains in absence of rum1
PMID:32084401	Fig2A cells expressing only cdc13HPM are unable to form colonies
PMID:32084401	Fig2B-D Endogenous untagged nmt 41cdc13+ is expressed to allow cells to proceed into mitosis tagged exogenous cdc13HPM or cdc13+ control can be seen at SPB
PMID:32084401	Fig2A cells are unable to enter mitosis in absence of cdc13+ expression-no septated cells
PMID:32084401	cdc13HPM mutant can localise to SPB in mitosis
PMID:32084401	Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	Fig 2H when plo1 kinase is inactivated at the restrictive temperature the HPM mutant does not bind to the SPB after release into mitosis
PMID:32084401	Fig2H cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
PMID:32084401	Fig3A when an integrated copy of cdc13HPM (at leu1 locus) is expressed from the cdc13 promoter the endogenous cdc13+ cells are advanced into mitosis. This suggests cdc13HPM can do some of events required for mitotic entry. This is independent of the G1/S cyclins
PMID:32084401	cdc13HPM mutant fails to localise to the SPB during G2
PMID:32084401	Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FIGURE S1E Wee1-dependent CDK-Y15 phosphorylation was similar between Cdc13HPM-CDK and Cdc13WT-CDK
PMID:32084401	Fig2H cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
PMID:32084401	FigS1-E cdc2 Y15 phosphorylation same in cdc13+ control and cdc13HPM strain endogenous cdc13+ is completely degraded so does not contribute in the HPM mutant
PMID:32101481	Figure 6, A and B
PMID:32101481	Figure 1A and 1B
PMID:32101481	4B?
PMID:32101481	Though the length of CR formation (node appearance to complete ring) was similar in wild type, cdc15-22A, and cdc15-22D, the periods of maturation (interval between CR formation and constriction initiation) and constriction (start to end of CR diameter decrease) were shorter in cdc15-22A and longer in cdc15-22D (Figure 4F).
PMID:32101481	Indeed, the percentage of tip septa was significantly reduced in mid1Δ pom1as1 cdc15-22D cells (Figure 4G).
PMID:32101481	Figure 6E
PMID:32101481	Figure 6D Indeed, deleting components of the CR scaffolded by Cdc15 (e.g., pxl1 or fic1) suppressed tip septation in mid1Δ pom1as1cells to a similar degree as cdc15-22D (Figure 6, D and E).
PMID:32101481	Figure 2D
PMID:32101481	(Figure 2, C and
PMID:32101481	the slow-migrating, phosphorylated forms of Cdc15 were reduced in pom1Δ cells (Figure 3B), and recombinant Pom1 efficiently phosphorylated recombinant N-terminal (Cdc15N; amino acids [aa]1–460) ||||||. later....We conclude that Cdc15 is a key substrate in the Pom1-mediated tip occlusion pathway.
PMID:32101481	Figure 6, A and B
PMID:32101745	fig 4g & S4. /Figure 5A)
PMID:32101745	figure 3A
PMID:32101745	figure 3A/B
PMID:32101745	Figure 5B the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	figure 3E
PMID:32101745	figure 3F
PMID:32101745	3' mrna extension figure Figure 4C; Figure S3 Although the percentage of total reads was relatively small, the iss1-DC mutation caused a reproducible and statistically sig- nificant extension of the 30 end of transcripts by about 200 nt.
PMID:32101745	fig 4e The 73 genes with increased expression in the iss1-DC mutant were evaluated for common functions and were strongly enriched for factors important for iron assimilation GO:0033212.
PMID:32101745	fig 4g & S4. /Figure 5A)
PMID:32101745	Figure 5B the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	Figure 5F the iss1-DC truncation did disrupt its interaction with Mmi1.
PMID:32101745	Figure S5 However, the truncation did not reduce Iss1 interaction with Rrp6
PMID:32101745	Figure 5H. We found that Iss1 assembles into nuclear dots, and these co-localized with Pla1, indicating that Iss1 also assembles in vivo with RNA elimination factors
PMID:32142608	plate-based screen
PMID:32142608	spot assay
PMID:32142608	spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	spot assay
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	Phosphorylated during growth in media containing heavy water.
PMID:32142608	spot assay
PMID:32142608	spot assay
PMID:32142608	spot assay
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	spot assay
PMID:32142608	plate-based screen
PMID:32142608	spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen, spot assay
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32142608	plate-based screen
PMID:32168916	Figure 4 (ALSO TFIIH but not sure which sunbunit)
PMID:32168916	Figure 3 & S4(ALSO TFIIH but not sure which sunbunit)
PMID:32168916	Figure 3 & S4(ALSO TFIIH but not sure which sunbunit)
PMID:32168916	fig3
PMID:32168916	fig3
PMID:32168916	Figure S4
PMID:32168916	Figure S4
PMID:32168916	Figure S4
PMID:32168916	Figure S4
PMID:32168916	Figure 4 (ALSO TFIIH but not sure which sunbunit)
PMID:32168916	Figure 4 SAP155K700E restopred splicing to prp10-1
PMID:32204793	Figure 1D, Figure 1—figure supplement 1; spot test and survival assay
PMID:32204793	Figure 1D, Figure 1—figure supplement 1; spot test and survival assay
PMID:32204793	Figure 6—figure supplement 1
PMID:32204793	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	Figure 6—figure supplement 1
PMID:32204793	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	Figure 7A,B; spot test and survival assay
PMID:32204793	Figure 7—figure supplement 1B; spot test
PMID:32204793	Figure 7—figure supplement 1B; spot test
PMID:32204793	Figure 7—figure supplement 1B; spot test
PMID:32204793	Figure 7A,B; spot test and survival assay
PMID:32204793	actually inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	actually inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	in complex with Sfr1; Figure 6
PMID:32204793	in complex with Swi5; Figure 6
PMID:32204793	Figure 1—figure supplement 1A; spot test
PMID:32204793	Figure 1—figure supplement 1A; spot test
PMID:32204793	Figure 1—figure supplement 1A, Figure 7C,D, Figure 7—figure supplement 1A; spot test and survival assay
PMID:32204793	Figure 7A,B; spot test and survival assay
PMID:32204793	Figure 7C,D; spot test and survival assay
PMID:32204793	Figure 7C,D; spot test and survival assay
PMID:32204793	Figure 7C,D; spot test and survival assay
PMID:32269268	Fig 5
PMID:32269268	Fig 1
PMID:32269268	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	Fig 1
PMID:32269268	Fig 1
PMID:32269268	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	Fig 1
PMID:32269268	Fig 1
PMID:32269268	Fig 1
PMID:32269268	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	Fig 1
PMID:32269268	Fig 1
PMID:32269268	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	Fig 1
PMID:32269268	Fig 4
PMID:32269268	Fig 4
PMID:32269268	Fig 5
PMID:32269268	Fig 5
PMID:32269268	Fig 5
PMID:32269268	Fig 2
PMID:32269268	Fig S2
PMID:32269268	Fig 2, S1
PMID:32277274	figa
PMID:32277274	figb
PMID:32277274	fig2
PMID:32282918	Figure 9C
PMID:32282918	Figure 9C
PMID:32282918	Figure 7B
PMID:32282918	Figure 7B and 8B
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 1
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 8B
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S2
PMID:32282918	Figure S1
PMID:32282918	Figure S1
PMID:32282918	Figure S1
PMID:32282918	Figure S1
PMID:32282918	Figure S1
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 9B
PMID:32282918	Figure 9C
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 9C
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 1
PMID:32282918	Figure 2
PMID:32282918	Figure 2
PMID:32282918	Figure 2
PMID:32282918	Figure 2
PMID:32282918	Figure 2
PMID:32282918	Figure 2
PMID:32282918	Figure 2
PMID:32282918	Figure 3A
PMID:32282918	Figure 3A and 9C
PMID:32282918	Figure 3A
PMID:32282918	Figure 3B
PMID:32282918	Figure 3B
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S7
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure S3
PMID:32282918	Figure 1
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 7A
PMID:32282918	Figure 7A
PMID:32282918	Figure 5C
PMID:32282918	Figure 3B
PMID:32282918	Figure 3B
PMID:32282918	Figure 3B
PMID:32282918	Figure 3B
PMID:32282918	Figure 3B
PMID:32282918	Figure 3B
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5A
PMID:32282918	Figure 5B
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 11
PMID:32282918	Figure 11
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 5B
PMID:32282918	Figure 5B
PMID:32282918	Figure 5B
PMID:32282918	Figure 5B
PMID:32282918	Figure 6B
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 6B
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 6B
PMID:32282918	Figure 6B
PMID:32282918	Figure 6B
PMID:32282918	Figure 6A
PMID:32282918	Figure 6A
PMID:32282918	Figure 6A
PMID:32282918	Figure 6A
PMID:32282918	Figure 6A
PMID:32282918	Figure 6B
PMID:32282918	Figure 6B
PMID:32282918	Figure 6B
PMID:32282918	Figure 6B
PMID:32282918	Figure 6B
PMID:32282918	Figure 7A
PMID:32282918	Figure 7A, pin∆ rescues the lethality of aps1∆ asp1-H397A
PMID:32282918	Figure 7B
PMID:32282918	Figure 7A
PMID:32282918	Figure 7A
PMID:32282918	Figure 7A
PMID:32282918	Figure 7A
PMID:32282918	Figure 8A
PMID:32282918	Figure 8A
PMID:32282918	Figure 8A
PMID:32282918	Figure 8A
PMID:32282918	Figure 8A
PMID:32282918	Figure 8B
PMID:32282918	Figure 8B
PMID:32282918	Figure 8B
PMID:32282918	Figure 8B
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 10
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 9B
PMID:32282918	Figure 8B
PMID:32295063	compared to Lsd1-ao single mutant
PMID:32295063	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	compared to lsd1-ao single mutant
PMID:32295063	Loss of the HMG domain of Lsd2 (but not Lsd1) produces inviable cells (lethal).
PMID:32295063	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	KΔ::ade6+ monitored by qRT-PCR
PMID:32319721	CFU counts
PMID:32320462	Sterols do not accumulate in endosomes
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Sterols do not accumulate in endosomes after treatement with CK-666
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Sterols do not accumulate in endosomes after treatement with CK-666
PMID:32320462	Sterols accumulate in endosomes
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Eisosomes protruding towards cell interior
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor; internal structures
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32320462	Evaluated with D4H sterol sensor
PMID:32327557	Fig. 3
PMID:32327557	Fig. 2
PMID:32327557	5ug/mL
PMID:32327557	Small rescue of cut7D pkl1D
PMID:32327557	Fig. 4
PMID:32327557	Fig. 4
PMID:32327557	Fig. 4
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 2
PMID:32327557	Fig. 2
PMID:32327557	Fig. 2
PMID:32327557	Fig. 2
PMID:32327557	Fig. 2
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32327557	Fig. 3
PMID:32341083	HU absent
PMID:32341083	HU absent
PMID:32341083	HU absent
PMID:32341083	HU absent
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	PFGE; An extrachromosome ChLC
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	PFGE; An extrachromosome ChLC
PMID:32355220	PFGE; An extrachromosome ChLC
PMID:32355220	PFGE; An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at cen1
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	ade6B/ade6X at the ura4 locus
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	An extrachromosome ChLC
PMID:32355220	PFGE; An extrachromosome ChLC
PMID:32361273	fig 2D length is 10.299 micron cf WT 12.7 in same conditions
PMID:32361273	fig 2D length is 7.5 micron cf WT 6.2 in same conditions
PMID:32361273	fig 2 This conserved inhibitory phosphorylation occurs as the Cdc2-Cdc13 complex is being formed to prevent its premature activation during G2 phase
PMID:32361273	fig 2
PMID:32361273	fig 2
PMID:32361273	fig 1C (i.e normal TOR signalloing)
PMID:32361273	fig S1A
PMID:32361273	fig S1A
PMID:32361273	fig1
PMID:32361273	fig1
PMID:32361273	fig1
PMID:32361273	Delay in the dephosphoryaltion of Ste9 and defect in the degradation of the cyclin Cdc13 in nitrogen starvation
PMID:32361273	fig7A
PMID:32361273	fig1
PMID:32361273	1D. The cells also presented a defect in the degradation of the cyclin Cdc13 and a delay in the dephosphorylation of Ste9
PMID:32361273	2G. the use of cdc10 mutant backgrounds is common for checking the ability of cells to arrest in G1
PMID:32361273	fig 7
PMID:32361273	protein phophatase substrate adaptor
PMID:32361273	(TAP-Par1F314Q), this interaction was reduced (Figure 6C)
PMID:32361273	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype corre- lated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype corre- lated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	fig 4 Notably, loss of cig1 and cig2 utterly overrode these defects,
PMID:32361273	fig 2
PMID:32361273	Figure S4D
PMID:32361273	Figure S4D
PMID:32361273	Figure S4D
PMID:32361273	Figure S4D
PMID:32361273	deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B).
PMID:32361273	deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B).
PMID:32361273	fig3
PMID:32361273	fig3b
PMID:32361273	fig 2F
PMID:32361273	fig 3
PMID:32361273	fig3
PMID:32361273	fig 2F
PMID:32361273	fig S2 B
PMID:32361273	fig 2E, S2A
PMID:32414915	The Meu13-Mcp7 complex activates the initiation step of DNA strand exchange by Dmc1. The Meu13-Mcp7 complex also stimulates Rad51-driven strand exchange to a much less extent in the presence of the Swi5-Sfr1 complex.
PMID:32414915	The Meu13-Mcp7 complex activates the initiation step of DNA strand exchange by Dmc1. The Meu13-Mcp7 complex also stimulates Rad51-driven strand exchange to a much less extent in the presence of the Swi5-Sfr1 complex.
PMID:32441227	using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	decreased cell population viability under overexpession of Mal3(Q89R) fragment using the nmt1 promoter
PMID:32441227	decreased cell population viability under overexpession of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	overexpression of Mal3(Q89R) mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-197) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-197) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-197) fragment using the nmt1 promoter
PMID:32441227	wild type under the nmt1 promoter
PMID:32441227	wild type under the nmt1 promoter
PMID:32441227	wild type under the nmt1 promoter; DAPI staining
PMID:32441227	wild type under the nmt1 promoter
PMID:32441227	overexpression of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-308) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-308) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-241) fragment using the nmt1 promoter
PMID:32441227	Overexpession of Mal3(Q89R) mutant using the nmt1 promoter
PMID:32441227	overexpression of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	Overexpession of Mal3(Q89R) mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-308) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter
PMID:32441227	overexpression of Mal3(Q89R) mutant using the nmt1 promoter
PMID:32441227	Overexpession of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3(Q89R) mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-241) fragment using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (135-308) fragment using the nmt1 promoter
PMID:32441227	Overexpession of Mal3(1-241) fragment using the nmt1 promoter
PMID:32441227	wild type under the nmt41 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	Overexpression of Mal3 (1-197) fragment using the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	wild type under the nmt41 promoter
PMID:32441227	using the nmt1 promoter
PMID:32441227	Overexpression of Mal3(Q89R) mutant using the nmt1 promoter
PMID:32441227	wild type under the nmt1 promoter
PMID:32441227	using the nmt1 promoter
PMID:32496538	Figure 5; rbp1 also Figure 7
PMID:32496538	Strand-specific RT-qPCR; Figure 2
PMID:32496538	Strand-specific RT-qPCR; Figure 2
PMID:32496538	Strand-specific RT-qPCR; Figure 2
PMID:32496538	Strand-specific RT-qPCR; Figure 2
PMID:32496538	Strand-specific RT-qPCR; Figure 2
PMID:32496538	Strand-specific RT-qPCR; Figure 2
PMID:32496538	Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5
PMID:32496538	Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5
PMID:32496538	Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Figure 5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	Supplementary Fig S8
PMID:32496538	Supplementary Fig S8
PMID:32496538	Supplementary Fig S8
PMID:32496538	Figure 6 and Supplementary Fig S8
PMID:32496538	Figure 6 and Supplementary Fig S8
PMID:32496538	Figure 6 and Supplementary Fig S8
PMID:32496538	Supplementary Fig S7
PMID:32496538	Supplementary Fig S7
PMID:32496538	Supplementary Fig S7
PMID:32496538	Supplementary Fig S7
PMID:32496538	Supplementary Fig S7
PMID:32496538	Supplementary Fig S7
PMID:32496538	Figure 5; rbp1 also Figure 7
PMID:32496538	Figure 5; rbp1 also Figure 7
PMID:32496538	Figure 5; rbp1 also Figure 7
PMID:32496538	Figure 5
PMID:32499400	at different lncRNA polyadenylation sites
PMID:32499400	EMM -U agar plates, supplemeted with 6AU concentration ranging from 3.6 to 150 ug/mL
PMID:32499400	100 ug/mL MPA
PMID:32499400	at tgp1 promoter
PMID:32499400	at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1)
PMID:32499400	at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1)
PMID:32499400	also assayed genome-wide
PMID:32499400	also assayed genome-wide
PMID:32499408	We then examined how the altered protein level of Tas3 affects the RITS complex formation in vivo. Notably, the low level of Tas3 in hsp90-G84C cells could only recruit minimal amount of Ago1 detected by co-immunoprecipitation assay at elevated temperatures (Figure 4C). (Figure 4B)
PMID:32499408	It is noteworthy that the amount of Arb1 was also drastically decreased in hsp90-G84C cells at high temperatures (Figure 4E)
PMID:32499408	Figure 3
PMID:32499408	fig 5e
PMID:32499408	Figure 7A
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	even at 25 °C, Arb1-associated Ago1 in the immunoprecipitates from hsp90-G84C cells was much reduced compared to wild-type samples (Figure 4E),
PMID:32499408	Figure 2E
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	Figure 1B-E and supplementary Figure S1B
PMID:32499408	Figure 3
PMID:32499408	that the amount of Tas3 but not Ago1 was significantly reduced once the hsp90-G84C cells were shifted to restrictive temperature of 37 °C for 4 hours (Figure 4B)
PMID:32499408	(Figure 4B)
PMID:32502403	A failed mitotic nuclear division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus.
PMID:32502403	Consistently, these cells showed a higher fre- quency of asymmetric NE divisions (Figure S2C)
PMID:32502403	Apq12 localized in tubules con- nected to or in close proximity to the MMD and at spindle pole regions, mirroring ER tubules marked with Yop1-GFP, Rtn1- GFP, or the artificial ER luminal marker mCherry-ADEL
PMID:32502403	A failed mitotic nuclear division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus.
PMID:32502403	When these cells were left in this con- dition, daughter nuclei began to move closer to each other until they finally merged into one single nucleus (Figure 4E). This phenotype can be promoted if spindles are forced to disas- semble by treating the cells with 30 mg/mL MBC, resulting in 35% (n = 34) of nuclear coalescence events.
PMID:32502403	ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B
PMID:32502403	ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B
PMID:32502403	The coalescence of daughter nuclei was also observed in apq12D cells that failed to undergo nuclear division (Figure 4F).
PMID:32502403	Apq12 localized in tubules con- nected to or in close proximity to the MMD and at spindle pole regions, mirroring ER tubules marked with Yop1-GFP, Rtn1- GFP, or the artificial ER luminal marker mCherry-ADEL
PMID:32502403	causally upstreasm of?
PMID:32502403	A failed mitotic nuclear envelope division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus. We found that wild-type cells showed timed NE division in the absence of actomyosin ring (Figures 4A and 4B), demon- strating that NE division is independent of cell division. However, 100% of imp1D cells (n = 126) completely failed to undergo NE division, resulting in cells with two nuclei linked by a long NE bridge (Figures 4A and 4B; Video S4). This result demonstrates that Imp1 is required for NE division.
PMID:32502403	We found that, in imp1D cells, NPCs were detected at the MMD and the peripheral NPC component Nup60 was removed from this domain (Figure 4C); however, the removal of structural components such as Nup107 and the membrane nucleoporin Cut11 was not observed (Figures 4C, S3A, and S3B).
PMID:32502403	Figure 1A
PMID:32518066	We conclude that the carboxy-terminal 12 amino acids of Lsm1 are important for the binding specificity of Lsm1–7.
PMID:32518066	Lsm1Δ56C–7 can only bind tightly to the RNA with a 5′ stem–loop and single stranded 3′ end (Kd = 70 and 32 nM, respectively) (Fig. 5C).
PMID:32518066	These data indicate that high affinity binding sites for the Lsm1–7 complex must be at the 3′ termini of RNA. On
PMID:32546512	Figure 5
PMID:32546512	a scenario in which Erh1 acts as a brake on Mmi1’s ability to promote CPF-de- pendent termination during prt lncRNA synthesis.
PMID:32546512	suggest ... Erh1 acts as a brake on Mmi1’s ability to promote CPF-de- pendent termination during prt lncRNA synthesis.
PMID:32546512	In addition, using the prt–pho1 reporter plas- mid to gauge Pho1 acid phosphatase expression, we found that Pho1 activity was lower in mmi1Δ cells than in wild-type cells (Fig. 6C)
PMID:32546512	Figure 4B
PMID:32546512	Figure 4B
PMID:32546512	Figure 4B
PMID:32546512	Figure 4B
PMID:32546512	Figure 4B
PMID:32546512	Figure 4B
PMID:32546512	(Normal compared to WT) The instructive findings were that the de-repression of Pho1 by erh1Δ was effaced in rhn1Δ, ssu72-C13S, ctf1Δ, ppn1Δ, and swd22Δ cells and was attenuated in dis2Δ cells (Fig. 4B
PMID:32546512	(Normal compared to WT) The instructive findings were that the de-repression of Pho1 by erh1Δ was effaced in rhn1Δ, ssu72-C13S, ctf1Δ, ppn1Δ, and swd22Δ cells and was attenuated in dis2Δ cells (Fig. 4B
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 2 We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the double- mutant was slow-growing on YES agar and cold-sensitive: he de-re- pression of Pho1 activity by erh1Δ was erased in the asp1-D333A back- ground
PMID:32546512	Figure 2 We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the double- mutant was slow-growing on YES agar and cold-sensitive: he de-re- pression of Pho1 activity by erh1Δ was erased in the asp1-D333A back- ground
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 2 vw changed from decreased to normal (compared to WT)
PMID:32546512	Figure 2 vw changed from decreased to normal (compared to WT)
PMID:32546512	Figure 4
PMID:32546512	Figure 2A
PMID:32546512	Figure 2A
PMID:32546512	Figure 2
PMID:32546512	Figure 2
PMID:32546512	Figure 2C the fivefold de-repression of Pho1 in the aps1Δ strain was enhanced additively to 12- fold in the erh1Δ aps1Δ background
PMID:32546512	Figure 2C the fivefold de-repression of Pho1 in the aps1Δ strain was enhanced additively to 12- fold in the erh1Δ aps1Δ background
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Figure 5
PMID:32546512	Northern blotting and primer extension, Figure 6
PMID:32546512	Northern blotting, Figure 6
PMID:32546512	Figure 2A
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 4
PMID:32546512	Figure 2B
PMID:32546512	Figure 2C
PMID:32546512	Figure 2B
PMID:32546512	Figure 2C
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure S1
PMID:32546512	Figure 8
PMID:32546512	Figure 8
PMID:32546512	Figure 8
PMID:32546512	Figure 8
PMID:32546512	Figure 8
PMID:32546830	Figure 2
PMID:32546830	linker
PMID:32546830	Figure 2E tetrad analysis
PMID:32571823	figure3D
PMID:32571823	figure 2d
PMID:32571823	figure3C
PMID:32571823	figure3B
PMID:32571823	figure 2d
PMID:32571823	figure3A (increased cacineurin signalling)
PMID:32571823	figure 2d
PMID:32571823	figure 1
PMID:32571823	figure 1
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2d
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2d
PMID:32571823	figure 1
PMID:32571823	FIG 4 Ccr1 is a molecular target of TAM.
PMID:32571823	figure 2c
PMID:32571823	figure 2
PMID:32571823	figure 2
PMID:32571823	figure 2d
PMID:32571823	figure 2d
PMID:32571823	figure 2d
PMID:32571823	figure 2d
PMID:32571823	figure 2d
PMID:32571823	figure 2
PMID:32571823	figure 2b
PMID:32571823	figure 2b
PMID:32571823	fig5
PMID:32571823	figure 2
PMID:32594847	DNS
PMID:32594847	DNS
PMID:32594847	DNS
PMID:32650974	figures 1,2,4. These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	M-Pol I complex
PMID:32650974	split YFP and affinity capture
PMID:32650974	M-Pol I complex
PMID:32650974	swollen
PMID:32650974	figure 4. These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	figures 1,2,4 These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32692737	regulates pathway choice
PMID:32723864	Figure S1.
PMID:32723864	Figure S1.
PMID:32723864	Figure S1. In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A)
PMID:32723864	Figure S1.
PMID:32723864	Figure 7
PMID:32723864	Figure 7
PMID:32723864	Figure 7
PMID:32723864	Figure 7
PMID:32723864	Figure 7
PMID:32723864	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	Figure 6
PMID:32723864	Figure 6
PMID:32723864	Figure 6
PMID:32723864	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	Figure 5
PMID:32723864	Figure 5 Three typical types of plots are shown: (I) WTlike metaphase spindle length (maintenance), (II) spindle regression (regression), and (III) continuous spindle elongation (lacking metaphase).
PMID:32723864	Figure 5
PMID:32723864	Figure 5
PMID:32723864	Figure S1. In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A)
PMID:32723864	3F. The results show that the absence of Klp2 affects the localization of Ase1-GFP to the meiotic spindles and leads to a decrease of the Ase1-GFP intensity on the meiotic spindles.
PMID:32723864	In both mitotic and meiotic cells, the absence of Klp2 slightly but significantly prolonged the duration of preanaphase (Fig. 2, F and G).
PMID:32723864	absence of Klp2 did not significantly affect spindle elongation during prophase I and only slightly lengthened the maximal spindle length during metaphase I (Fig. 2G).
PMID:32735772	Figures 2G and 2H
PMID:32735772	fig 6b
PMID:32735772	Figure 6A
PMID:32735772	fig 6b
PMID:32735772	ER- autophagosome anchor requested https://github.com/geneontology/go-ontology/issues/19873
PMID:32735772	Figure 7B We found that DTT-induced increase of Epr1 was severely diminished in ire1D (Figure 7B), indicating that Epr1 upregulation requires Ire1.
PMID:32735772	Figure S1E
PMID:32735772	Figure S1E nitrogen starvation-induced ER-phagy appeared to be normal in epr1D
PMID:32735772	Figure 2B, 2G, 2H
PMID:32735772	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	Figure 1C AIM-mutated Epr1- C was pulled down as efficiently as wild-type Epr1-C by Scs2 but did not support the pull-down of Atg8 PLUS more experiments We hypothesized that the main role of Epr1 in ER-phagy is to mediate a connection between Atg8 and VAPs. requirement of Epr1 in ER-phagy can be by- passed by an artificial soluble tether that bridges an Atg8-VAP connection.Figure 4D).
PMID:32735772	The abilities of Epr1-C to bind Atg8 and VAPs using separate motifs suggest that one Epr1-C molecule may be able to interact with both an Atg8 molecule and a VAP molecule simultaneously and thereby bridge an Atg8-VAP association. To test this possi- bility, we performed an in vitro GST pull-down experiment using three proteins expressed in Escherichia coli: GST-tagged Scs2(1-126) corresponding to the FFAT-binding MSP domain, HA-tagged Atg8, and Smt3-tagged Epr1-C (Figure 4C). GST- Scs2(1-126) alone did not pull down Atg8. However, in the pres- ence of Epr1-C, GST-Scs2(1-126) efficiently pulled down both Epr1-C and Atg8, indicating that Epr1-C can bridge an indirect interaction between Scs2 and Atg8. Together, our results demonstrate that the main role of Epr1 in ER-phagy is to bridge an Atg8- VAP connection.
PMID:32735772	Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D).
PMID:32735772	Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D).
PMID:32735772	Remarkably, Epr1-C, but not Epr1-N, could completely rescue the defects of epr1D in DTT-induced ER- phagy
PMID:32735772	Figures S3B and S3D Epr1-C showed ER localization in vegetatively growing cells, whereas Epr1-N was diffusely distributed in the cytoplasm and the nucleus
PMID:32735772	Figures S3B and S3D Epr1-C showed ER localization in vegetatively growing cells, whereas Epr1-N was diffusely distributed in the cytoplasm and the nucleus
PMID:32735772	figure 3D
PMID:32735772	(Figure 3D) As expected, in cells lacking both Scs2 and Scs22, Epr1 became diffusely distributed in the cytoplasm
PMID:32735772	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	check with Dan **** Thus, Epr1 is an ER-phagy receptor required for ER stress-induced selective autophagy of both the nuclear envelope and the peripheral ER.
PMID:32735772	Figure 2a
PMID:32735772	Figure 1C
PMID:32735772	Figure 1C
PMID:32735772	Figure 1C
PMID:32735772	Fig. S1B
PMID:32735772	Figure 6A
PMID:32735772	Figure 6A
PMID:32735772	Figure 6A
PMID:32735772	Figure 6A
PMID:32735772	Figure 6A
PMID:32735772	Figure 6A
PMID:32735772	Figure 3D ******check with DAN, is this an overexpression allele?
PMID:32735772	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	Figures 1B and S1C
PMID:32735772	Figure 2a
PMID:32735772	Figure 7E the ER-phagy defect of ire1D was largely rescued (Figure 7E).
PMID:32735772	Figures 1B and S1C
PMID:32735772	Figure 3C Epr1 interacted with both Scs2 and Scs22 in the Y2H assay
PMID:32735772	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	(Figure S6B), indicating that Ire1 is dispensable for DTT-induced bulk autophagy but is essential for DTT-induced ER-phagy.
PMID:32735772	Fig 3
PMID:32735772	Fig. S1B
PMID:32735772	Fig. S1B
PMID:32735772	ER- autophagosome anchor requested https://github.com/geneontology/go-ontology/issues/19873
PMID:32790622	viable spore yield assay
PMID:32790622	viable spore yield assay
PMID:32790622	viable spore yield assay
PMID:32790622	viable spore yield assay; 16% of the surviving spores had inherited two copies of chromosome 3 and were thus aneuploid/diploid.
PMID:32790622	viable spore yield assay; 30% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid.
PMID:32790622	viable spore yield assay; 20% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid.
PMID:32790622	viable spore yield assay
PMID:32817556	Phenotype is greatly enhanced by mutation of the IR-R boundary element
PMID:32841241	UAC codon/GUA anticodon tRNA
PMID:32841241	CCU codon/AGG anticodon tRNA
PMID:32841241	UAC codon/GUA anticodon tRNA
PMID:32841241	CCU codon/AGG anticodon tRNA
PMID:32841241	UAC codon/GUA anticodon tRNA
PMID:32841241	CCU codon/AGG anticodon tRNA
PMID:32841241	UAC codon/GUA anticodon tRNA
PMID:32841241	ACU codon/AGU anticodon tRNA
PMID:32841241	CCU codon/AGG anticodon tRNA
PMID:32841241	UAC codon/GUA anticodon tRNA
PMID:32841241	CCU codon/AGG anticodon tRNA
PMID:32841241	UAC codon/GUA anticodon tRNA
PMID:32841241	CCU codon/AGG anticodon tRNA
PMID:32848252	Fig. 4, Extended Data Fig. 7
PMID:32848252	Extended Data Figure 2 (nucleoplasmic side)
PMID:32848252	Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	extended data 6 c,d
PMID:32848252	Fig. 4a, b. Daughter nuclei in the les1Δ strain also suffered transient leakages at the time of maximum spindle elongation, as measured by loss of nuclear NLS–GFP (;
PMID:32848252	fig 3g
PMID:32848252	lem2 (which encodes Lem2, the binding partner of Cmp7) is also SL with les1
PMID:32848252	nstead, the repair process was associated with recruitment of the ESCRTIII protein Cmp7 (Fig. 4d) to sites of local NEB20 (Fig. 4d, Extended Data Fig. 8b, c).
PMID:32848252	causally upstream?
PMID:32848252	fig 3b
PMID:32848252	Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	Extended Data Figure 8
PMID:32848252	Les1 stalks functionally isolate daughter nuclei from the process of Imp1-dependent local NEB at the centre of the bridge prob- ably acts to create a seal by gathering the inner nuclear envelope tightly around the spindle,
PMID:32848252	fig 4/6
PMID:32848252	extended fig4
PMID:32848252	fig 4/6
PMID:32878942	Fig 4H&I and S3F&G
PMID:32878942	fig4
PMID:32878942	Fig. S3A
PMID:32878942	Fig. S3A
PMID:32878942	Fig. S3A
PMID:32878942	Fig S3B&C
PMID:32878942	Fig. S3A
PMID:32878942	Fig 3D
PMID:32878942	Fig 3D
PMID:32878942	Fig 3D
PMID:32878942	Fig S3F&G
PMID:32878942	Fig S3B,C,&D
PMID:32878942	Fig 4D,E&F
PMID:32878942	Fig S3E
PMID:32878942	Fig S3E
PMID:32878942	Fig S3E
PMID:32878942	Fig S3E
PMID:32878942	Figure 2D&E
PMID:32878942	Figure 2F-H
PMID:32878942	Figure 2I (vw changed tp FYPO:0002559)
PMID:32878942	Fig S3B&C
PMID:32878942	Fig S3F
PMID:32878942	Fig 4H&I and S3F&G
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	arg3-GFP fusion localisation in minimal media (EMM)
PMID:32896087	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	Data from screening of prototroph deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	EMM media with arginine
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototrophic deletion library
PMID:32896087	solid media screen using prototroph deletion library.
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32896087	EMM media with arginine
PMID:32908306	Cup1-GFP immunofluorescence
PMID:32909946	in vitro autophosphorylation activity of Atg1 from atg11D mutant was almost undetectable (Figure 1D
PMID:32909946	Figure 1C). Such a band was not observed for D193A and T208A mutants, confirming that they are indeed kinase dead (
PMID:32909946	Fig 1a
PMID:32909946	Fig 1 a
PMID:32909946	we found that in S. pombe, Atg1 from atg13D, atg17D, or atg101D mutant exhibited autophosphorylation activities simi- lar to that of Atg1 from wild type
PMID:32915139	cells lacking Sty1 grew in these low LatA concentrations (Figure 1B).
PMID:32915139	replaces wt annotation
PMID:32915139	replaces wt annotation
PMID:32915139	fig 4d
PMID:32915139	fig1 SuppF
PMID:32915139	Figure 1C
PMID:32915139	upstream elements of this signaling cascade shared this phenotype... Mcs4, the redundant MAPKKK´s Wak1 and Win1, and MAPKK Wis1 (Figure 1A, Figure 1—figure supplement 1
PMID:32915139	Cells expressing a mutant allele Mcs4(D512N) that does not activate the SAPK pathway upon stimulation with hydro- gen peroxide (Shieh et al., 1997), displayed Sty1 activation during LatA treatment,
PMID:32915139	fig 5c
PMID:32915139	50%
PMID:32915139	figure 5B
PMID:32915139	Figure 2A and C) check, has synonym increased stability (better than increased length?)
PMID:32915139	(Figure 2—figure supplement 5). ngs formed and constricted correctly in >85% of sty1D cells (Figure 2D).
PMID:32915139	Overexpression under the control of B-estradiol promoter (vw: I added an allele synonym, later these will be searchable and visible)
PMID:32915139	fig3b
PMID:32915139	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—figure supplement 3).
PMID:32915139	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—figure supplement 3).
PMID:32915139	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—figure supplement 3).
PMID:32915139	fig2-supp1
PMID:32915139	fig 5b
PMID:32915139	fig 5b
PMID:32915139	Figure 5—figure supplement 4
PMID:32915139	fig 1F
PMID:32915139	Figure 5—figure supplement 4
PMID:32915139	25%
PMID:32915139	explicit delay in ring constriction and disassembly (21 ± 0.6 min in wild-type cells vs 36 ± 1.6 min in for3D cells; Figure 2—figure supplement 5
PMID:32915139	fig 3a
PMID:32915139	Figure 1C
PMID:32915139	fig3c
PMID:32915139	Figure 1C
PMID:32915139	fig 3a
PMID:32915139	fig1 SuppF
PMID:32915139	upstream elements of this signaling cascade shared this phenotype... Mcs4, the redundant MAPKKK´s Wak1 and Win1, and MAPKK Wis1 (Figure 1A, Figure 1—figure supplement 1
PMID:32915139	fig1 SuppF
PMID:32915139	fi1 supp5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 1, Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 3
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 4
PMID:33010152	Fig. 8
PMID:33010152	Fig. 8
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 5
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 6
PMID:33010152	Fig. 1
PMID:33010152	Fig. 4
PMID:33010152	Fig. 1
PMID:33010152	Fig. 1
PMID:33010152	Fig. 1
PMID:33010152	Fig. 1
PMID:33010152	Fig. 1
PMID:33010152	Fig. 1
PMID:33010152	Fig. 1
PMID:33010152	Fig. 8
PMID:33049028	Further analysis revealed that the levels of intron-retaining cox1 and cob1 tran- scripts were increased in 􏰀ppr10 cells in the intron-containing background (Fig. 1A–C)
PMID:33049028	fig4
PMID:33049028	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[􏰀i] and 􏰀ppr10[􏰀i] cells (Fig. 1E–G
PMID:33049028	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[􏰀i] and 􏰀ppr10[􏰀i] cells (Fig. 1E–G
PMID:33049028	Further analysis revealed that the levels of intron-retaining cox1 and cob1 tran- scripts were increased in 􏰀ppr10 cells in the intron-containing background (Fig. 1A–C)
PMID:33108274	The wtf4poison proteins is distributed throughout asci and spores in the absence of the wtf4antidote. The antidote assembles with the poison and then both proteins are localized to the vacuole in spores.
PMID:33108274	The wtf4poison proteins is distributed throughout asci and spores in the absence of the wtf4antidote. The antidote assembles with the poison and then both proteins are localized to the vacuole in spores.
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33109728	Fig. 4B
PMID:33125111	(Fig. 3).
PMID:33125111	(Fig. 1A).
PMID:33125111	(Fig. 1B). decreasing slows after 6 hours
PMID:33125111	(Fig. 1C).
PMID:33125111	(Fig. 1C).
PMID:33125111	(Fig. 3).
PMID:33131769	*****(abnormal distribution in...) inhomogeneous contractile Rng2 ring An inhomogeneous contractile Rng2 ring is an abnormal actomyosin contractile ring that show an uneven distribution of 2mYFP-Rng2-12A over the ring.
PMID:33131769	An fragile actomyosin contractile ring is an abnormal actomyosin contractile ring that disassemble by treatment with a low dose of Latrunculin A, an actin depolymerizing agent.
PMID:33131769	An fragile actomyosin contractile ring is an abnormal actomyosin contractile ring that disassemble by treatment with a low dose of Latrunculin A, an actin depolymerizing agent.
PMID:33137119	affecting substrate Fkh2 in vitro
PMID:33137119	pREP81-gad8-T260C fig1a
PMID:33137119	Fig3C. we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	7B.
PMID:33137119	Fig3A. affecting substrate Fkh2 in vitro
PMID:33137119	pREP81-gad8-T260C fig 2B
PMID:33137119	figure 3d. I CHANGED THIS ONE< IS IT CORRECT?
PMID:33137119	fig 3b
PMID:33137119	fig 3b
PMID:33137119	fig 3B
PMID:33137119	Following release from campthotecin
PMID:33137119	Fig3A.Gad8-K263C was also phosphorylated at S546 under conditions that compromise Tor1 activity, such as osmotic or low glucose stress (S3A Fig), further supporting Tor1-independent phosphorylation of Gad8-K263C by an as yet unknown kinase.
PMID:33137119	affecting Gad8-S546 phosphorylation
PMID:33137119	fig1c
PMID:33137119	fig1c
PMID:33137119	fig 6b
PMID:33137119	fig 6b
PMID:33137119	pREP81-gad8-T260C. fig1a
PMID:33137119	pREP81-gad8-K263C figure 2
PMID:33137119	pREP81-gad8-K263C
PMID:33137119	pREP81-gad8-T260C fig2
PMID:33137119	pREP81-gad8-K263C
PMID:33137119	pREP81-gad8-K263C
PMID:33137119	pREP81-gad8-T260C fig 2B
PMID:33137119	fig2
PMID:33137119	pREP81-gad8-Q298L fig 5a
PMID:33137119	pREP81-gad8-Q298L fig6D
PMID:33137119	pREP81-gad8-Q298L
PMID:33137119	Fig3A. affecting substrate Fkh2 in vitro
PMID:33137119	affecting substrate Fkh2 in vitro
PMID:33137119	affecting Gad8-S546 phosphorylation
PMID:33137119	affecting Gad8-S546 phosphorylation
PMID:33137119	Fig3A. To our surprise, Gad8-K263C was phosphorylated at S546 in wild type cells, as well as in Δtor1 cells (S546-P, Fig 3A).This finding suggests that the Gad8-K263C mutant is phosphorylated by a kinase that normally does not recognize Gad8 as a substrate.
PMID:33137119	Fig3A. affecting substrate Fkh2 in vitro
PMID:33137119	fig 6c L fig6D
PMID:33137119	Additionally, the phosphorylation sites of Gad8 are required for genotoxic stress, since gad8-S527A/S546A mutant alleles are also sensitive to DNA damage and DNA replication stress (S5B Fig).
PMID:33137119	fig 6c dominent negative effect
PMID:33137119	(S5A Fig)
PMID:33137119	Fig3C. The wild type Gad8 is not phosphorylated at T387 in the absence of Tor1 and is only weakly phosphorylated under low-glucose conditions (Fig 3C).
PMID:33137119	Fig3C. we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	As previously described [33], mutating both Tor1-dependent phosphorylation sites, S546 and S527, to alanine, abolished the ability of cells to grow at high temperature or in the presence of osmotic stress (Fig 3B)
PMID:33137119	The only conditions under which we did not detect phosphorylation of Gad8-K263C were in Δtor1 cells in the presence of hydroxyurea or camptothecin (S3B Fig), a finding that may suggest that the activity of the kinase responsible for Gad8-K263C phosphorylation is inhibited under genotoxic stress conditions.
PMID:33137119	affecting substrate Fkh2 in vitro
PMID:33137119	affecting substrate Fkh2 in vitro
PMID:33138913	figure 6B
PMID:33138913	By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D)
PMID:33138913	Therefore, we propose that a major role of Atg43 in the mitophagy process is to tether Atg8 to mitochondria through direct interaction with Atg8 via the AIM region.
PMID:33138913	figure 2F, 2G, 2H
PMID:33138913	fig1
PMID:33138913	fig1D
PMID:33138913	2A
PMID:33138913	Fig- ure 5—figure supplement 1F
PMID:33138913	In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C
PMID:33138913	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C
PMID:33138913	Fig- ure 5—figure supplement 1F
PMID:33138913	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	fig1a
PMID:33138913	fig1
PMID:33138913	fig1
PMID:33138913	fig 2.
PMID:33138913	fig 3b
PMID:33138913	fig 3b/4b
PMID:33138913	check genotype. ***********figure 3c
PMID:33138913	figure 3D
PMID:33138913	figure 3D
PMID:33138913	figure 3D
PMID:33138913	fig 3H
PMID:33138913	fig 3H
PMID:33138913	fig 3H
PMID:33138913	figure 3I
PMID:33138913	fig 3i
PMID:33138913	fig 3K
PMID:33138913	fig 4D
PMID:33138913	fig 4D
PMID:33138913	figure 4B
PMID:33138913	fig3 supp1b&c
PMID:33138913	whereas Atg43 with a truncation of the 60 C-terminal aa was defective in mitophagy (Figure 4B)
PMID:33138913	figure 4B Atg43 lacking the 20 C-terminal aa exhibited only a partial defect in mitophagy,
PMID:33138913	fig 4c
PMID:33138913	figure 4G
PMID:33138913	The interaction between full-length Atg43 and Mim2 was confirmed using reciprocal immunoprecipitation experi- ments (Figure 5A and Figure 5—figure supplement 1B).
PMID:33138913	MIM complex (requrested)
PMID:33138913	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fis- sion yeast (Figure 5—figure supplement 1H
PMID:33138913	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fis- sion yeast (Figure 5—figure supplement 1H
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I)
PMID:33138913	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	figure 6B,D
PMID:33138913	figure 6B
PMID:33153481	Fig.1a,d,e,f,S3; 3D quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, Shortened the distance between genomic loci
PMID:33153481	Fig.S2; G2 arrested cells by cdc2-asM17
PMID:33153481	Fig.2,3,S4; Hi-C, G2 arrested cells by cdc2-asM17
PMID:33153481	Fig.4,S5; G2 arrested cells by cdc2-asM17
PMID:33153481	Fig.6e; 3D quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17
PMID:33153481	Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FISH; same as nup132delta alone
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FISH
PMID:33159083	pmt3-D81R pmt3-KallR
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33172987	Figure S2
PMID:33172987	Figure S3
PMID:33172987	Figure S2
PMID:33172987	Figure S2
PMID:33172987	Figure1C (requested normal membrane lipid binding)
PMID:33172987	I changed the function annotation to this process annotation because it precisely negates the SGD annotation
PMID:33172987	Opy1 PH1 (aa1-128) can directly bind phospholipids in vitro Figure 1
PMID:33172987	Figure 3
PMID:33172987	Figure S3
PMID:33172987	Figure S3
PMID:33172987	Figure S2
PMID:33172987	Figure S2
PMID:33172987	Figure S2
PMID:33172987	Figure S2
PMID:33172987	(Fig. S2B).
PMID:33172987	Figure S2
PMID:33172987	Figure S1
PMID:33172987	Figure S1
PMID:33172987	Figure S1
PMID:33172987	Figure S1
PMID:33172987	Figure 4E-F
PMID:33172987	Figure 3A
PMID:33172987	(Fig. 1F-G
PMID:33172987	Fig. 1D-E
PMID:33172987	Figure S2
PMID:33172987	Figure S2
PMID:33172987	Figure S2
PMID:33172987	THIS IS A GUESS I COULD NOT ACCESS THE SUPP SO ANNOTATED TO THE Snider ITS3-1 growth phenotype
PMID:33172987	PH1 domain Fig. 2A, Table S2
PMID:33172987	Figure 1C
PMID:33176147	Figures 4E and 4F
PMID:33176147	Figures 4E and 4F
PMID:33176147	Figures 4E and 4F
PMID:33176147	figS2A
PMID:33176147	fig1E
PMID:33176147	fig1E
PMID:33176147	fig1E
PMID:33176147	fig1F
PMID:33176147	fig1F
PMID:33176147	fig1F/figS2A
PMID:33176147	fig1F
PMID:33176147	fig 2A
PMID:33176147	fig 2A
PMID:33176147	figure 2c Figures 3B and S3B Figures 4C and 4D
PMID:33176147	figure 2c Figures 3B and S3B Figures 4C and 4D
PMID:33202882	intron 2
PMID:33225241	Background Sty1-GFP
PMID:33225241	same as mas5delta alone
PMID:33225241	background: Pyp1-GFP
PMID:33225241	same as mas5delta alone
PMID:33357436	Figure 3A
PMID:33357436	Figure S2E
PMID:33357436	These results indicate that the Cdc15 F-BAR domain can position Cdc12 directly at the PM by binding membrane and Cdc12 simultaneously.
PMID:33357436	moved down from abnormal localization
PMID:33357436	Figure S2C
PMID:33357436	Figure S2B electron microscopy of purified Cdc15 F-BAR domain
PMID:33357436	Figure 4F
PMID:33357436	In vitro binding assay with Cdc15 F-BAR domain and full length Pxl1
PMID:33357436	Figures 3C and 3D
PMID:33357436	additional cewlll. poles
PMID:33357436	fig 2B in vitro binding assay with Cdc15 F-BAR domain and Cdc12 peptide aa20-40
PMID:33378674	at pericentromeric regions
PMID:33378677	inferred from abolished interaction between Pof8 and Lsm subunits
PMID:33378677	inferred from abolished interaction between Pof8 and Lsm subunits
PMID:33378677	inferred from decreased interaction between Pof8 and Lsm subunits
PMID:33386485	Background Rho1.C17R-mCherry
PMID:33386485	background Hsp104-GFP and Rho1.C17R-mCherry
PMID:33386485	background Hsp104-GFP and Rho1.C17R-mCherry
PMID:33386485	background Hsp104-GFP and Rho1.C17R-mCherry
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	3a glucose starve
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	figure 4b
PMID:33400299	3a glucose starve
PMID:33400299	3a glucose r excess
PMID:33400299	Figure 2n
PMID:33400299	Figure 2n
PMID:33400299	Figure 2n
PMID:33400299	figure 4b
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	Table1
PMID:33400299	Table1
PMID:33400299	Table1
PMID:33400299	(Figure 2k–m).
PMID:33400299	To further examine whether ROS and NO mediated increased Rst2 transcriptional activity caused by mitochondrial complex III/IV inhibitors, we examined the effect of antioxidant N-acetyl-L-cysteine (NAC) which aids in ROS detoxification and 2-(4-Carboxyphenyl)-4,4,5,5-tetramethy-limidazo-line-1-oxyl-3- oxide (Carboxy-PTIO), a NO-specific scavenger on the Rst2 transcriptional activity stimulated by mitochondrial complex III/IV inhibitors. The results showed that NAC and Carboxy-PTIO significantly inhibited mitochondrial complex III/IV inhibitors-induced activation of Rst2 in a dose-dependent manner (Figure 2e–j), suggesting that ROS and NO were involved in mitochondrial respiratory chain complex III/IV inhibitors-induced activation of Rst2. To further prove this result, we also examined the effect of a mammalian NO synthesis (NOS) inhibitor, N G-nitro-l-arginine methyl ester (NAME) on the Rst2 transcriptional activity stimulated by mitochondrial complex III/IV inhibitors, since it was reported that NAME treatment can reduce NO formation by more than 60% in yeast cells (Astuti et al., 2016a). As expected, NAME dose-dependently decreased mitochondrial complex III/IV inhibitors- induced Rst2 activation (Figure 2k–m).
PMID:33400299	Figure 1m
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	Figure 1m
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	figure 4b
PMID:33410907	Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5.
PMID:33410907	Figure 1
PMID:33410907	Figure 2c (this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	Figure 2c (this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	( Figure 5D **I moved this from a WT phenotype)
PMID:33410907	(is thsi |+h2os, check) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H),
PMID:33410907	(is this +H2o2, check) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H),
PMID:33410907	Ssu72, but not with the GST control in the pull down experiment. These results suggested that Pin1 directly interacted with and recruited Ssu72 for pSer5 dephosphorylation to facilitate progression of transcription important for cellular response to oxidative stress
PMID:33410907	2B
PMID:33410907	Figure 1
PMID:33410907	2B
PMID:33410907	2B
PMID:33410907	These results suggested that, in addition to the binding to theRpb1-CTD, the isomerization activity was also required for the fu
PMID:33410907	Intriguingly, upon oxidative stress, the association between Rpb1 and Sty1 was decreased in wild type cells and up regulated in the pin1 mutant with reduced phosphorylation of Ser2 (Figure 4B).
PMID:33410907	PHOSPHORYLATED CTD Following H2O2 stress, Pin1 bound phosphorylated CTD to promote Sty1 dissociation from it to facilitate oxidative stress induced transcription.
PMID:33410907	Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5.
PMID:33410907	Sty1 associated with Rpb1 in S. pombe as demonstrated by co-immunoprecipitation beforeH2O2 stress. This result suggested that the interaction between Sty1 andRpb1 did not require the activation of Sty1
PMID:33410907	In line with these results, Ser2 phosphorylation of Rpb1-CTD, which facilitated transcription elongation, was reduced in pin1 mutant as a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5.
PMID:33410907	6c
PMID:33410907	As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5.
PMID:33410907	In the absence of Pin1, Ser5 phosphorylated Rpb1 was associated and accumulated at the promoter region following H2O2 stress but was defective in entering elongation to generate transcripts of the corresponding genes (Figure 1C)
PMID:33410907	Figure 5
PMID:33410907	In line with these results, Ser2 phosphorylation of Rpb1-CTD, which facilitated transcription elongation, was reduced in pin1 mutant as a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	Figure 5
PMID:33410907	Figure 5e
PMID:33410907	Figure 1
PMID:33410907	Figure 1
PMID:33410907	In line with theseresults, Ser2 phosphorylation of Rpb1-CTD, which facilitatedtranscription elongation, was reduced in pin1 mutantas a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	Figure 1
PMID:33410907	fig2a
PMID:33410907	fig? (under calf alkaline phosphatase treated)
PMID:33410907	Figure 1C
PMID:33410907	Figure 1C
PMID:33410907	Figure 1C
PMID:33410907	Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5.
PMID:33419777	Fig1B, C Table 1
PMID:33419777	Fig1A
PMID:33419777	Fig 2, Table 2
PMID:33419777	Fig 2, Table 2
PMID:33419777	negative regulation (check relationship to membrane reassembly)
PMID:33419777	Fig4A.
PMID:33419777	Fig5A
PMID:33419777	Fig5 E,F abnormal protein localisation in multinucleated cells
PMID:33419777	Fig5C Table 3
PMID:33419777	Fig5C compare16 and 17 Table 3 I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	increased cell size variability. cellular phenotype of variable cell size at division may be further increased in the absence of another cellular protein Fig5 compare 14 and 15 Table 3 I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	Fig5C compare 7 and 9 When cdc2 is not tyrosine phosphorylation mga2 delta does not increase the cell size variability any further.
PMID:33419777	Fig5C compare 4 and 6 the variability of cdc2cdc13 fusion protein is increased in mga2 delta. I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	Fig5A
PMID:33419777	Fig5A
PMID:33419777	Fig4 B,C, D. A cellular phenotype found in multinucleated cells where nuclear division is no longer synchronous and cells with an odd number of nuclei are observed
PMID:33419777	FigS1. delayed septation, Cellular phenotype where cells initiate growth before septation has taken place, resulting in variable cell size at division.
PMID:33419777	Fig4A
PMID:33419777	Fig 3I same in wild type background
PMID:33419777	Fig3H same in wild type background
PMID:33419777	Fig 3A-F same result in Wild type background
PMID:33419777	Fig3A-F same result in wild type background
PMID:33419777	negative regulation (check relationship to membrane reassembly)
PMID:33419777	Fig1B, C Table 1
PMID:33419777	Fig1B, C Table 1
PMID:33419777	Fig1B, C Table 1
PMID:33419777	Fig1B, C Table 1
PMID:33434270	Figure. 6A
PMID:33434270	Figure. 5A
PMID:33468217	inferred from silencing and H3-K9 methylation phenotypes
PMID:33468217	inferred from silencing and H3-K9 methylation phenotypes
PMID:33483504	figure 3a
PMID:33483504	figure 3a
PMID:33483504	fig. 3d
PMID:33483504	fig 4 significantly decreased the number of Mdm12 (a constitutive component of the ERMES complex) foci
PMID:33483504	fig 4d though the expression levels of Mdm12 were comparable in WT and emr1Δ Cells
PMID:33483504	fig 5
PMID:33483504	As shown in Fig. 6b, c, Emr1-FL and Emr1-ΔN, but not Emr1-ΔC, restored the normal number of Mdm12 foci, confirming that the C-terminus of Emr1 is required for regulating the number of ERMES foci.
PMID:33483504	er to mitochondria
PMID:33483504	fig 1c
PMID:33483504	fig. 1b n=344
PMID:33483504	fig. 1b n=344
PMID:33483504	integral 2a,b,c,d
PMID:33483504	fig1 (cox4-GFP to label Mt)
PMID:33483504	fig. 1a
PMID:33483504	fig 1d. Despite the multiple types of abnormalities observed in emr1Δ cells, mitochondria of emr1Δ cells were still able to undergo fission and fusion (Fig. 1d), but improperly segregated into daughter cells after mitosis (Fig. 1e). This phenotype of defective mitochondrial segregation is consistent with the previous finding that spherical/giant mitochondria in mutant cells compromise mitochondrial movements, inheritance, and segregation7,8,2
PMID:33483504	figure 3b
PMID:33483504	fig. 3b
PMID:33496728	Figure S1
PMID:33496728	Figure S3
PMID:33496728	Figure S1
PMID:33496728	Figure S3
PMID:33496728	Figure S3
PMID:33496728	Figure 1E, F. VW instead of abnormal, I did increased and decreased rate with low penetrance (i.e the rate is variable within the population, someincreased and some decrreased, although there see to be 2 distinct sub-populations we can't capture this effectively)
PMID:33496728	Figure 1E, F. The average constriction rate of Δmid1 contractile rings is 0.27 μm/min (Saha and Pollard, 2012a), but the distribution of constriction rates appears bimodal with fast and slow subpopulations. The type of strand that builds the contractile ring strongly correlates with its constriction rate, with contractile rings made from nascent strands constricting faster (0.32 μm/min) and contractile rings made from enduring strands constricting more slowly (0.20 μm/min; Fig. 1 E).
PMID:33496728	Figure 1A, B
PMID:33496728	(Fig. 4 C). Cdc12p distributed in a smaller zone in the R-nodes of Δmid1 cells...node dimensions in the R-nodes of constricting contractile rings.....
PMID:33496728	Figure 1E, F. We generated Δmid1 Δmyp2 double-mutant cells and found that the distribution of constriction rates of their contractile rings is still bimodal, albeit with both populations constricting 25–50% more slowly than the Δmid1 populations, consistent with Myp2p being responsible for ∼50% of the constriction rate
PMID:33496728	Figure 3 Figure 4 Figure S2
PMID:33496728	Figure 1
PMID:33496728	Figure 2 Figure 3 Figure 4 Figure S2
PMID:33496728	Figure 1E, F
PMID:33496728	Figure 5 (VW: changed severity from high to low as this seems to partially rescue mid1-delta?)
PMID:33496728	Figure 5
PMID:33496728	Figure 1, Figure 5. +5 min, a 15-min delay compared with wild-type cells
PMID:33496728	Figure 5
PMID:33496728	Figure 5
PMID:33496728	Figure 6
PMID:33496728	Figure 1
PMID:33496728	Figure S1
PMID:33496728	Figure S1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig4
PMID:33506191	"fig4 If possible, please add the following comment - “The nucleus is retained in the center of the cell during mitosis."""
PMID:33506191	Fig 7 These results indicate that first, the main reason for lethality of cut7 is derived from the cut phenotype; second, some cells could escape from cut by displacing the nucleus from the middle of the cell axis; and finally, these cut7 survivors could resume cell division as diploid progenies at the permissive temperature.
PMID:33506191	fig2 live cell imaging
PMID:33506191	fig2 live cell imaging
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig4
PMID:33506191	fig6
PMID:33506191	Fig7
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33506191	fig1
PMID:33511417	genome-wide average; slightly increased amplitudes of the -2, -1, +1 nucleosome peaks (relative to NDR)
PMID:33511417	genome-wide average
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure 2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure2
PMID:33526714	figure 2
PMID:33529549	Figure 1. Increased equational segregation in sgo1∆ background.
PMID:33529549	FIgure 1. Decreased equational segregation in the sgo1∆ rec12∆ background or the haploid sgo1∆ background.
PMID:33529549	Figure 1. Increased equational segregation in sgo1∆ background.
PMID:33529549	The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids.
PMID:33529549	Figure 1. Increased equational segregation in the sgo1∆ background.
PMID:33529549	Decreased equational segregation in the diploid sgo1∆ rec12∆ background or the haploid sgo1∆ background.
PMID:33529549	Furthermore, the dam1Δ mutation increased equational segregation of sister chromatids in rec12+ cells (figure 5b, left) but it decreased equational segregation in sgo1Δ rec12Δ or haploid meiotic sgo1Δ cells (figure 5b,c)
PMID:33529549	Importantly, the dam1Δ mutation impaired disjunction of homologous chromosomes (figure 5a), as seen in mad2Δ and ark1-so mutants [25,52].
PMID:33529549	Anaphase A chromosome movement is completely abolished and only anaphase B chromosome movement occurs.
PMID:33529549	***** increased bi-oriented attachment of sister chromatids in meiosis I*****The frequencies of sister centromere splitting varied (electronic supplementary material, figure S2A), but the mean splitting frequencies per centromere obtained by the bootstrap method were signifi- cantly higher in rec12Δ cells than in rec12+ cells (the difference was also significant in the usual t-test, p < 0.01; figure 2d, +). The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids.
PMID:33529549	FIgure 1. These results indicate that the error correction mechanism decreases bi-oriented attachment of sister chromatids in the presence of chiasmata, but conversely increases bi-oriented attachment (thereby decreasing mono-oriented attachment) in the absence of chiasmata. In our previous study, the equational segregation frequencies of cen1 were somewhat higher in the rec12Δ background [28], although the reason for this is unknown. However, the mad2Δ mutation similarly decreased equational segregation, being consistent with our current results.
PMID:33534698	On the other hand, Iml1 and Sea3 were co-immunoprecipitated even in the absence of Seh1, Sea2, and Sea4 (Figure 3E), implying that Sea3 directly binds to GATOR1 and anchors the other GATOR2 components to GATOR1.
PMID:33534698	Figure 2g
PMID:33534698	Figure 2e (sea3 rescued by gtr1 GDP-locked)
PMID:33534698	Figure 2f
PMID:33534698	Figure 2e (sea3 rescued by gtr1 GDP-locked)
PMID:33534698	Figure 2b (any1 rescues)
PMID:33534698	Figure 2b (any1 reescues)
PMID:33534698	Figure 2b
PMID:33534698	Figure 1
PMID:33534698	Figure 1
PMID:33534698	Figure 1
PMID:33534698	Figure 1, Supp 1
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Figure 1, Supp 1
PMID:33534698	Figure 1, Supp 1
PMID:33534698	Figure 1, Supp 1
PMID:33534698	Figure 1, Supp 1
PMID:33534698	Figure 1, Supp 1
PMID:33534698	Figure 1, Supp 1
PMID:33534698	vw I edited to make the response the extension to GCN2 mediated signalling, but I hope to improve these GO terms.
PMID:33534698	Autophagy in response to leucine starvation was abrogated by the gcn1D, but not gcn20D, mutation (Figure 4D),
PMID:33534698	We found that autophagy after leucine starvation was severely impaired in cells lacking Cpc2 and in those overexpressing a fission yeast ortholog of Yih1/IMPACT (Figure 4—figure supplement 1G), confirming the essential role of the Gcn2 activity in autophagy induction upon amino acid starvation.
PMID:33534698	fig 4 a Though much less than that in wild-type cells, autophagy was still detectable in the tsc2D iml1D double mutant, indicating that, in addition to the GATOR1 and TSC complexes, there must be an additional mechanism to attenuate TORC1 upon nitrogen starvation for autophagy induction.
PMID:33534698	fig4a
PMID:33534698	Figure 2a
PMID:33534698	Figure 2a
PMID:33534698	Gcn2-dependent induction of autoph- agy was also observed in cells treated by 3-amino-1,2,4-triazole (3-AT) or methionine sulfoximine (MSX), inhibitors of histidine and glutamine biosynthesis, respectively (Figure 4—figure supplement 1D,E).
PMID:33534698	fig 4e In order to test whether the Gcn2 kinase induces autophagy through phosphorylation of eIF2a, we constructed a strain that expresses eIF2a with its phosphorylation site Ser52 substituted by ala- nine (eIF2a-S52A).
PMID:33534698	Moreover, S. pombe cells lacking Gcn3 (Figure 4D) or Fil1 (Figure 4F) displayed autophagy defects during leucine starvation.
PMID:33534698	Indeed, we observed that, after leucine starvation, the Fil1 protein increased, which was dependent on Gcn2 and the phosphorylation of eIF2a (Fig- ure 4—figure supplement 1H).
PMID:33534698	Figure 1
PMID:33534698	Figure 1
PMID:33534698	Figure 1
PMID:33534698	Figure 1
PMID:33534698	In the gnc2D iml1D tsc2D triple mutant, a trace of released GFP was detected only after 14 hr of nitrogen starvation (Figure 6C), while autophagy takes place within 2 hr in wild-type cells after the starvation (Figure 4B).
PMID:33534698	Moreover, the autophagy defect of the gcn2D mutant was complemented by TORC1 inactivation by the TORC1 inhibitors, rapamycin and caffeine (Figure 5B).
PMID:33534698	5A). In contrast, Psk1 remained phosphorylated even after the starvation in the gcn2D, eIF2a-S52A, and fil1D mutant strains (Figure 5A), suggesting that TORC1 inactivation in leucine-starved cells is medi- ated by the Gcn2-eIF2a-Fil1 pathway.
PMID:33534698	(ARginine starvation) Similarly, in cells of arginine auxotrophy, Gcn2-dependent autophagy was detectable after incubation in the growth medium without arginine (Figure 4—figure supplement 1C).
PMID:33534698	However, no GFP accumulation was detected in gcn2D cells under leucine starvation (Figure 4C), demonstrating that the autophagy induced by leucine starvation is dependent on the Gcn2 kinase.
PMID:33534698	(DIRECTLY INHIBITS) Recently, another conserved arginine residue in mammalian GATOR1, Arg78 of the Nprl2 subunit,was proposed to serve as an arginine finger that promotes GTP hydrolysis by RagA/B (Shen et al.,2019, Figure 3—figure supplement 3B). To assess the role of the equivalent residue in the S.pombe GATOR1, Arg98 in Npr2 was substituted with alanine to construct an npr2R98A mutantstrain. The mutant cells exhibited a compromised growth phenotype that was rescued by rapamycinor the gtr1SN mutation, an indicative of compromised GAP activity of GATOR1 (Figure 3—figuresupplement 3C). Though the npr2R98A phenotype was not as severe as that of the npr2 nullmutant, these observations are in line with the model that the conserved Arg residue in Npr2, butnot the one in Iml1, acts as an arginine finger of GATOR1 also in fission yeast.
PMID:33534698	(DIRECTLY INHIBITS) Recently, another conserved arginine residue in mammalian GATOR1, Arg78 of the Nprl2 subunit,was proposed to serve as an arginine finger that promotes GTP hydrolysis by RagA/B (Shen et al.,2019, Figure 3—figure supplement 3B). To assess the role of the equivalent residue in the S.pombe GATOR1, Arg98 in Npr2 was substituted with alanine to construct an npr2R98A mutantstrain. The mutant cells exhibited a compromised growth phenotype that was rescued by rapamycinor the gtr1SN mutation, an indicative of compromised GAP activity of GATOR1 (Figure 3—figuresupplement 3C). Though the npr2R98A phenotype was not as severe as that of the npr2 nullmutant, these observations are in line with the model that the conserved Arg residue in Npr2, butnot the one in Iml1, acts as an arginine finger of GATOR1 also in fission yeast.
PMID:33534698	(Figure 3—figure supplement 3A), indicating that Arg854 of S. pombe Iml1 is not essential for the GATOR1 function.
PMID:33534698	On the other hand, immuno- precipitation of the GATOR1 subunit Iml1 found that the physical interaction between GATOR1 and the Gtr1 GTPase was reduced in the sea3D mutant (Figure 3M).
PMID:33534698	(Figure 3—figure supplement 2E,F and G),
PMID:33534698	(Figure 3—figure supplement 2E,F and G),
PMID:33534698	In the case of the sea3D mutant, Iml1, Npr2, and Npr3 were all detectable on vacuoles (Figure 3—figure supplement 2E,F and G),
PMID:33534698	(Figure 3—figure supplement 1C–E).
PMID:33534698	(Figure 3—figure supplement 1C–E).
PMID:33534698	Furthermore, consi tent with the essential role of Sea3 in the interaction between GATOR1 and the other GATOR2 sub- units, the vacuolar localization of Sea2, Sea4, and Seh1 ( was abrogated in the sea3D background (Figure 3—figure supplement 1C–E).
PMID:33534698	Consis- tently, in the absence of intact GATOR1, the vacuolar localization of Sea3 (Figure 1E) was lost and the protein diffused throughout the cytosol (Figure 3I, Figure 3—figure supplement 1A),
PMID:33534698	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3–GATOR1 association (Figure 3F,G and H).
PMID:33534698	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3–GATOR1 association (Figure 3F,G and H).
PMID:33534698	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3–GATOR1 association (Figure 3F,G and H).
PMID:33536395	As expected, Och1-EGFP expressed in the wild type strain showed strong fluorescence as a typical Golgi-like dots, but faint fluorescent dots were confirmed in gmn2∆ cells (Fig. 4A).
PMID:33536395	As expected, Och1-EGFP expressed in the wild type strain showed strong fluorescence as a typical Golgi-like dots, but faint fluorescent dots were confirmed in gmn2∆ cells (Fig. 4A).
PMID:33536395	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These re- sults indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	changed from protein retention in ER lumen
PMID:33536395	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These re- sults indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	The Gmn2-EGFP protein was recycled back into the ER just as Gms1-EGFP, indicating that Gmn2-EGFP localized mostly to the Golgi membranes (Fig. 6B).
PMID:33536395	The gmn2∆ cells were found to be viable despite growing slightly slower than the wild type (Fig. 3A MM (leu-)) and exhibited the same phenotypes as those of the original gmn2 mutant.
PMID:33536395	The gmn2∆ cells were highly sen- sitive to hygromycin B, being unable to grow on YES plates containing 25 μg/ml of the drug (Fig. 3A)
PMID:33536395	Fig. 3B
PMID:33536395	Fig. 3C
PMID:33536434	GI Redundancy
PMID:33568651	Rnh201-RED mutant, based on the S. cerevsiae equivalent, is unable to remove single rNMPs from DNA but, buy genetic analysis, is able to remove runs of rNMPs.
PMID:33568651	Polymerase usage sequencing
PMID:33568651	replication dynamic analysis demonstrates that the priming strand is stable in the absence of Ku (previous work has shown resection is increased behind the arrested fork). Replication restart is slightly delayed, confirming previous work. Assayed by polymerase usage sequencing
PMID:33568651	Polymerase usage sequencing
PMID:33568651	Polymerase usage sequencing
PMID:33574613	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g). and Fig. 4g).
PMID:33574613	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	Intriguingly, cells expressing Pir1-SD, but not Pir1-WT or Pir1-SA, continued to divide on nutrient-limiting medium at a low temperature (Fig. 4a), suggesting that stabilized Pir1 supports cell proliferation under suboptimal growth conditions.
PMID:33574613	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	Fig 1 a
PMID:33574613	Fig 1 a
PMID:33574613	figure 1e
PMID:33574613	figure 1c
PMID:33574613	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g).
PMID:33574613	The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g).
PMID:33574613	Fig 1 b (me2)
PMID:33574613	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	which?
PMID:33574613	which?
PMID:33574613	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	Moreover, loss of the ubiquitin ligase-associated Cullin-RING finger family protein Cul4, a component of ClrC35,36 that interacts with MTREC15, also stabilized Pir1 in both tor2-ts6 and nitrogen-starved cells (Fig. 3c
PMID:33574613	Moreover, loss of the ubiquitin ligase-associated Cullin-RING finger family protein Cul4, a component of ClrC35,36 that interacts with MTREC15, also stabilized Pir1 in both tor2-ts6 and nitrogen-starved cells (Fig. 3c
PMID:33574613	ubi4 gene, which encodes polyubiquitin implicated in sexual development34, was upregulate in tor2-ts6 cells (Fig. 3a).
PMID:33574613	Interestingly, the expression of Pir1-SD in tor2-ts6 cells restored the levels of Red1 (Extended Data Fig. 2e), suggesting that the reduction in Red1 in the tor2 mutant cells (Fig. 1c) is linked to the degradation of its interaction part- ner Pir1
PMID:33574613	Figure 6B DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	Figure 6B DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	Figure 6B DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	cells showed impaired oscillation of chromosomes and a prolonged horsetail stage (approximately 160min compared with approximately 120min; Fig. 7a,b).
PMID:33574613	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g). and Fig. 4g).
PMID:33574613	Fig 1 b (1.5x) (me2)
PMID:33574613	Extended data Fig 1 b c (also at MTREC independent islands)
PMID:33574613	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	Fig 1 b (me2)
PMID:33574613	Fig 1 a
PMID:33574613	he Tor2-containing TORC1 complex phosphorylated Pir1 in vitro and mutation of the 12 serine residues to alanine attenu- ated Pir1 phosphorylation (Extended Data Fig. 2a,c).
PMID:33574613	Extended Data Fig. 2a,c
PMID:33574613	Replacement of the 12 phospho-serine residues with the phospho-mimic aspartic acid residue (Pir1-12SD) indeed conferred stability in tor2-ts6 cells (Extended Data Fig. 2d)
PMID:33574613	Replacement of the 12 phospho-serine residues with the phospho-mimic aspartic acid residue (Pir1-12SD) indeed conferred stability in tor2-ts6 cells (Extended Data Fig. 2d); Deletion of ubi4 in tor2-ts6 cells cells indeed stabilized Pir1 (Fig. 3b)
PMID:33574613	Consistently, ubiquitination of Pir1-SD in the tor2-ts6 mts2-1 mutant was reduced (Fig. 2e).
PMID:33574613	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	abnormal asci containing fewer than four, or no, spores were frequently generated (Fig. 7c).
PMID:33574613	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1–3)
PMID:33574613	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1–3)
PMID:33574613	Fig 1 a
PMID:33574613	Similar to pir1∆, tor2-ts6 cells showed a severe growth defect at a semi-permissive temperature (29°C) on minimal medium but not on rich medium (Fig. 4d).
PMID:33574613	Similar to pir1∆, tor2-ts6 cells showed a severe growth defect at a semi-permissive temperature (29°C) on minimal medium but not on rich medium (Fig. 4d).
PMID:33574613	Notably, Pir1 was depleted during early meiosis (Fig. 5a) but gradually recov- ered by middle meiosis.
PMID:33574613	Whereas Pir1-WT disappeared, Pir1-SD per- sisted during meiosis as multiple nuclear foci coinciding with Mmi1 and Erh1 foci (Fig. 5b,c).
PMID:33574613	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	Moreover, ubiquitination of Pir1 was detected in tor2-ts6 cells and increased in the tor2-ts6 mts2-1 mutant (Fig. 1h)
PMID:33574613	figure 1h
PMID:33574613	Fig. 1f,g
PMID:33579781	Fig. 2
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 5A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 5B
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 2 However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, includ- ing the rump, in the context of the full-length CTD (Fig. 2), signifying that reduced proline content is tolerated and that Pro3 and Pro6 need not be present in consecutive heptads
PMID:33579781	Need to add modified version
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 4A
PMID:33579781	Fig. 2 However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, includ- ing the rump, in the context of the full-length CTD (Fig. 2), signifying that reduced proline content is tolerated and that Pro3 and Pro6 need not be present in consecutive heptads
PMID:33658433	vw:added nucleosome assembly
PMID:33670267	ATPase assay
PMID:33670267	TAP co-purification, Western blot for histone H3
PMID:33670267	TAP co-purification, Western blot for histone H3
PMID:33670267	ATPase assay
PMID:33670267	TAP co-purification, Western blot for histone H3
PMID:33670267	ATPase assay
PMID:33670267	ATPase assay
PMID:33670267	TAP co-purification, Western blot for histone H3
PMID:33683349	fig3 (i.e wee?)
PMID:33683349	fig 5
PMID:33683349	fig3
PMID:33683349	fig3
PMID:33683349	fig 5a
PMID:33683349	figure 6b
PMID:33683349	fig2 (30 degrees) wee1-50ts mik1D cells divide at a smaller size than wee1-50ts mik1D cig2D cells
PMID:33683349	fig3
PMID:33683349	figure 4
PMID:33683349	High temp - 30 degrees. (VW I changed this from a cell phenotype term to a population phenotype term) fig1 We interpret this suppression to indicate that the lethal mitoses, which occur in the smallest cells, require Cig2/CDK activity instead of, or in addi- tion to, Cdc13/CDK activity.
PMID:33683349	"fig1 &2 Nick suggested ""mitotic catastrophe""We would make this a related synonym?"
PMID:33683349	figure 4
PMID:33683349	fig 6a
PMID:33683349	QUESTION ig 5b (I only curated the red line temp inc at tome zero, becase it would be difficult to specify at 60 mins, I could not think of a way to do this). I'm assuming these cells do not enter mitosis, is that correct
PMID:33711009	20°
PMID:33711009	20°
PMID:33711009	20°
PMID:33711009	20°
PMID:33711009	20°
PMID:33711009	Neither the N-terminal segment from aa 1–496 nor the C-terminal fragment from 578–710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A)
PMID:33711009	Neither the N-terminal segment from aa 1–496 nor the C-terminal fragment from 578–710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A)
PMID:33723569	25ºC
PMID:33723569	25ºC
PMID:33723569	25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	25ºC, live-cell imaging, cell length at septation
PMID:33723569	25ºC, live-cell imaging, cell length at septation
PMID:33723569	25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	25ºC
PMID:33723569	25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	32ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	25ºC
PMID:33723569	25ºC
PMID:33723569	25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33723569	live-cell imaging, 25ºC
PMID:33754639	temperature sensitive 37°
PMID:33771877	fig3.
PMID:33771877	fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	Fig 2
PMID:33771877	Fig 2
PMID:33771877	fig 1
PMID:33771877	fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	fig 2b Importantly, the accumulation of condensin in sen1Δ cells could not be caused by an accumulation of either TFIIIC or Tbp1 because their levels on chromatin remained largely unaffected in the absence of Sen1, as shown by ChIP with a GFP-tagged version of Tbp1 and a myc-tagged version of the TFIIIC component Sfc6 (Figs 2B and S1).
PMID:33771877	Fig 2b
PMID:33771877	fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	fig 1
PMID:33771877	fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	fig3.
PMID:33771877	fig3.
PMID:33771877	fig3.
PMID:33775921	highest overexpression level
PMID:33788833	Affecting Cps1 carboxypeptidase
PMID:33788833	Affecting Cps1 carboxypeptidase
PMID:33788833	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	Affecting Vps10 and the PI(3) probe Cherry-FYVE
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	same as vps35delta alone
PMID:33788833	same as vps35delta alone
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	same as fsv1delta alone
PMID:33788833	Affecting Cps1 carboxypeptidase
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	Affecting Cps1 carboxypeptidase
PMID:33788833	Affecting Cps1 carboxypeptidase
PMID:33788833	Affecting Cps1 carboxypeptidase
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	The mutant protein is observed at the vacuolar surface
PMID:33788833	In the null mutant and the mutant without SNARE domain the fluorescence of prevacuolar endosome markers is reduced, and Cps1 processing is abnormal
PMID:33788833	co-localization with Vps35 and with Vps27
PMID:33788833	co-localization with Cfr1
PMID:33788833	80 mM MgCl2
PMID:33788833	1.0 M KCl
PMID:33823663	DNS
PMID:33823663	DNS
PMID:33823663	figure9
PMID:33823663	figure 9 modified form is activated for sexual differentiation
PMID:33825974	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	Figure s2 (c); live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	Figure 4d, 4e; Figure s3b; live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33836577	figure 3D
PMID:33836577	figure 2
PMID:33836577	figure 2 requires phosphorylated T89, T154, T155 to bind Nbs1 FHA domain
PMID:33836577	figure 2
PMID:33836577	figure 3D
PMID:33836577	figure 3D
PMID:33836577	figure 3D
PMID:33836577	figure 3B
PMID:33836577	figure 3B
PMID:33836577	figure 3B
PMID:33836577	figure 3B
PMID:33836577	figure 3B
PMID:33836577	figure 3C
PMID:33836577	figure 3C
PMID:33836577	figure 3C
PMID:33836577	figure 3D
PMID:33836577	We therefore introduced a synthetic CT15 peptide into an endonuclease assay containing the MR complex, but lacking Nbs1 (Fig. 4A). Strikingly, the CT15 peptide stimulated the endonuclease activity of MR similarly to the unphosphorylated, full-length Ctp1 (Fig. 4B). Moreover, stimulation of MR at higher concentrations of the CT15 peptide (100 μM) was comparable to the maximal levels achieved with the MRN complex and phosphorylated full-length Ctp1 (Ctp1p in Fig. 4C).
PMID:33836577	figure 1
PMID:33836577	figure 1
PMID:33836577	figure 1
PMID:33836577	figure 2D
PMID:33836577	figure 2D
PMID:33836577	figure 2E
PMID:33836577	figure 3C
PMID:33836577	figure 3C
PMID:33836577	figure 3D
PMID:33836577	figure 2E
PMID:33888556	Figure 2A cohesion protection defect
PMID:33888556	Figure 2D
PMID:33888556	Figure 3AB vw repurposed this as it was essentially the same as the other annotation to this genotype (suggesting that Rec8-2A was properly expressed but not protected at centromeres during anaphase I.)
PMID:33888556	Figure 3
PMID:33888556	figure 4
PMID:33888556	Figure 3BC Strikingly, the phenotype of rec8-2E was completely suppressed by sgo1Δ indicating that Rec8-2E was protected by Sgo1 not only at centromeres but also along the chromosome arm.
PMID:33888556	Figure 1C
PMID:33888556	Figure 1C
PMID:33888556	Figure 1C
PMID:33888556	Figure 1C
PMID:33888556	Figure 1C
PMID:33888556	refer to model in figure 4. Therefore, consistent with the genetic analyses, this biochemical analysis supports the notion that phosphorylation at Rec8-S450 and the adjacent site plays a role in promoting the PP2A-dependent removal of CK1-dependent phosphorylation of Rec8 (Fig. 4B).
PMID:33888556	Figure 2A
PMID:33888556	Figure 2F
PMID:33888556	Figure 3D. phosphomimetic rec8
PMID:33888556	Figure 3D.
PMID:33888556	Figure 3D.
PMID:33888556	Figure 3D. phosphomimetic rec8
PMID:33888556	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	figure 4 (no rescue by sgo3)
PMID:33888556	figure 4
PMID:33888556	Figure (we modelled this increased duration of cohesion in mitotic anaphase, and the ectopic rec8 expression is now part of the genotype,does that sound OK?)
PMID:33888556	Figure 1B/C
PMID:33888556	Figure 1C
PMID:33909078	alpha-1,3-galactosylation of O-linked glycan
PMID:33909078	alpha-1,2-galactosylation of N-linked glycan
PMID:33909078	alpha-1,2-galactosylation of N-linked glycan
PMID:33909078	alpha-1,2-galactosylation of N-linked glycan
PMID:33909078	alpha-1,2-galactosylation of O-linked glycan
PMID:33909078	alpha-1,2-galactosylation of O-linked glycan
PMID:33909078	alpha-1,3-galactosylation of O-linked glycan
PMID:33909078	alpha-1,3-galactosylation of O-linked glycan
PMID:33925026	Assays were done in the MDR-sup (multi-drug resistance-suppressed) genetic background together with nda3-TB101
PMID:33925026	same as klp6delta alone
PMID:33925026	same as klp6delta alone
PMID:33925026	same as alp14delta alone
PMID:33925026	same as alp14delta alone
PMID:33925026	same as alp14delta alone
PMID:33925026	same as alp14delta alone
PMID:33925026	same as alp14delta alone
PMID:33925026	reduced frequency of microtubule rescue
PMID:33925026	reduced frequency of microtubule catastrophe
PMID:33946513	Figure 4a
PMID:33946513	Figure 2D
PMID:33946513	Figure 2A,B
PMID:33946513	Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT)
PMID:33946513	Figure 2D
PMID:33946513	to pac
PMID:33946513	to pac
PMID:33946513	Figure 6. We found that the dri1∆ cells acquired tolerance to high temperature, as they could form colonies at 39 ◦C, whereas wild-type cells could not (Figure 6C).
PMID:33946513	fig 1c dri1 supresses cut7
PMID:33946513	SHOULD THIS BE NORMAL? However, the Mal3 protein levels did not change in the presence or absence of Dri1 (Supplementary Figure S3A). Similarly, the levels of Mal3-GFP on the spindle MTs were almost the same both in wild-type and dri1∆ cells (Supplementary Figure S3B).
PMID:33946513	Figure 2A,B
PMID:33946513	fig1
PMID:33946513	fig1a
PMID:33946513	fig S4a
PMID:33946513	to pac
PMID:33946513	to pac
PMID:33946513	Figure 3A
PMID:33946513	Figure 3A
PMID:33946513	Figure 3A
PMID:33946513	Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT)
PMID:33970532	only amino acid auxotrophic cell
PMID:33970532	only amino acid auxotrophic cell
PMID:33970532	The control strain ED668 expressed ecl1+ when Mg2+ was depleted but not in a strain lacking fil1+ (Figure 2a)
PMID:33970532	to capture target of ecl1
PMID:33970532	only amino acid auxotrophic cell
PMID:34010645	Figure 2.
PMID:34010645	Figure 2.
PMID:34010645	Figure 2
PMID:34010645	H3K9me3 levels at pericentric dh repeats and dh RNA levels in hht3-K9MK14R cells are similar to those in wild-type cells, comparing with hht3-K9M.
PMID:34019809	fix catalytic activity
PMID:34019809	structure, fig2
PMID:34019809	fix catalytic activity
PMID:34028542	After cultivation in low glucose MM for 10 h, medium was replaced with low-glucose nitrogen-starved MM, and cells were further cultivated for 4 h.
PMID:34028542	top panel, Fig. 6A; Fig. S3B,C).
PMID:34028542	Cytoplasmic Ght5-GFP was observed within the vacuolar membrane stained with FM4-64.
PMID:34028542	Proliferation defect of gad8ts rod1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	Proliferation defect of gad8ts mutant in low glucose was restored by SPCC584.15c deletion.
PMID:34028542	fig6
PMID:34028542	fig6
PMID:34028542	Fig1 aly3 rescues
PMID:34028542	Proliferation defect of gad8ts aly2 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	Proliferation defect of gad8ts aly1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	although not shown directly , genetic interactions are consistent with this activity
PMID:34028542	fig6 (phenocopies WT)
PMID:34028542	fig 5
PMID:34080538	Fig. 4
PMID:34080538	Fig. 5
PMID:34080538	Fig. 5
PMID:34080538	Fig. 5
PMID:34080538	Fig. 5
PMID:34080538	Fig. 5 supp 3
PMID:34080538	Fig. 5 supp 3
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 5 -Phosph form (From other publications, we know bona-fide that the localisation observed here is the kinetochore, but here they study how it changes)
PMID:34080538	Fig. 5 - Dephosph form
PMID:34080538	Fig. 5 - Dephosph form
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34080538	Fig. 4
PMID:34086083	YES, YES (low-glucose)
PMID:34086083	YES, YES (low-glucose)
PMID:34086083	ALERTED FROM A LATER PAPER Rst2 regulates the expression of ste11, which encodes a transcription factor to regulate sexual development (Sugimoto et al. 1991); fbp1, which encodes fructose-1,6-bisphosphatase (Hoffman and Winston 1990); and mug14, which encodes an adducin homolog (Inamura et al. 2021).
PMID:34133210	Although there was a small difference in CR formation between pxl1(9A) (13.6 +/- 2.5; 33 cells) and pxl1(9D) (12.2 +/- 2.3 min; 41 cells), formation was similar in pxl1(9D) and pxl1+ (12.4 +/- 3.0; 32 cells), and there were no significant differences in the durations of CR maturation.
PMID:34133210	Figure 4, A and B
PMID:34133210	Cdk1 phosphorylation of Pxl1 reduced binding to the F-BAR domain of Cdc15 (Figure 5A), but not to Cdc15C (Figure 5B).
PMID:34133210	Although there was a small difference in CR formation between pxl1(9A) (13.6 +/- 2.5; 33 cells) and pxl1(9D) (12.2 +/- 2.3 min; 41 cells), formation was similar in pxl1(9D) and pxl1+ (12.4 +/- 3.0; 32 cells), and there were no significant differences in the durations of CR maturation.
PMID:34133210	fig1
PMID:34133210	although not IDA, there is experimental data to support this inference
PMID:34133210	Constriction took longer in pxl1(9A)
PMID:34169534	also assayed using Pil1 co-tethering with microscopy
PMID:34169534	also assayed using Pil1 co-tethering with microscopy
PMID:34209806	We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2  89.4 or 1558.2  159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively),
PMID:34209806	Need to curate ref42 for earlier part of this story, but this can be. inferred here from the interactions
PMID:34209806	We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2  89.4 or 1558.2  159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively),
PMID:34209806	i added as good to have multiple support.
PMID:34209806	The interactions of the Nrl1(NRDE-2) and the Nrl1(C-term) domain constructs with Mtl1 were significantly lower
PMID:34228709	equivalent substitution to cdc20-P287R
PMID:34228709	Cds1 is partially phosphorylated
PMID:34228709	Chk1 is partially phosphorylated
PMID:34228709	hypermutator
PMID:34228709	DNA combing
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:34250083	Phenotype determined with robotics-based CFU assay.
PMID:3428262	mitotic G2/M transition delay
PMID:34292936	worse than rad51delta alone
PMID:34292936	worse than rad51delta alone
PMID:34296454	This result indicates that the immediate decrease in protein synthesis rates upon TOR inhibition is not dependent upon the S6Ks or their downstream targets.
PMID:34296454	hese observations are consistent with the idea that the essential TORC1 is the major complex responsi- ble for the rapid inhibition of protein synthesis and that changes in phosphorylation levels relevant to regulating protein synthesis should be detectable within 20 min and significant by 40 min of TOR inhibition.
PMID:34296454	Please refer to Fig. 5E&F from paper for partial inhibition protein synthesis phenotype
PMID:34296454	For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course
PMID:34296454	For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course
PMID:34309513	in vitro (Figure 4A, Video 1).
PMID:34309513	in vitro (Figure 4A, Video 1).
PMID:34309513	in vitro (Figure 4A, Video 1).
PMID:34309513	in vitro (Figure 4A, Video 1).
PMID:34309513	in vitro (Figure 4A, Video 1).
PMID:34309513	in vitro (Figure 4A, Video 1).
PMID:34346498	Figure 2F
PMID:34346498	Figure 5 To confirm this, we evaluatedthe behaviour of bqt1Δ sad1.2 alp4-GFP cells harbouring the SPBmarkers Sid4–mCherry and Sad1.2–mCherry, effectively showingthat Alp4–GFP molecules located far from the nucleus wereassociated with the SPBs (Fig. 5C,D)
PMID:34346498	figure 7C
PMID:34346498	Figure 7
PMID:34346498	Figure 2F
PMID:34346498	Figure 6 Remarkably, we found that, in the case of bqt1Δ sad1.2 alp14-26 meiocytes, despite clear dysfunction of alp14-26, self-assembled spindles were still able to form and behaved normally (Fig. 6C,D). However, they formed in a smaller percentage of meiocytes (from ∼80% to ∼30%, Fig. 6F), indicating that the contribution of Alp14 to self-assembled spindle formation and behaviour is substantial.
PMID:34346498	analysis of bqt1Δ sad1.2 dis1Δ meiocytes showed that the percentage of selfassembled spindles with normal formation and function was similar to that in the bqt1Δ sad1.2 setting (Fig. 6F,H).
PMID:34346498	figure7 maximum length of self-assembled spindles increased upon deletion of klp6 (from 7.9±3.8 μm to 12.9±4.7 μm; Fig. 7E).
PMID:34346498	figure7 C
PMID:34346498	decreased abnormal SPB-independent meiosis II
PMID:34346498	figure 7C
PMID:34346498	Figure 7
PMID:34346498	Figure 2
PMID:34346498	Figure 3A
PMID:34346498	Figure 5 To confirm this, we evaluatedthe behaviour of bqt1Δ sad1.2 alp4-GFP cells harbouring the SPBmarkers Sid4–mCherry and Sad1.2–mCherry, effectively showingthat Alp4–GFP molecules located far from the nucleus wereassociated with the SPBs (Fig. 5C,D)
PMID:34346498	Figure 1
PMID:34346498	Figure 1 (see above)
PMID:34346498	Figure 1 (see above)
PMID:34346498	Figure 2E
PMID:34346498	Figure 2E
PMID:34346498	Figure 3
PMID:34346498	figure7 maximum length of self-assembled spindles increased upon deletion of klp6 (from 7.9±3.8 μm to 12.9±4.7 μm; Fig. 7E).
PMID:34346498	Figure 6B
PMID:34346498	Figure 2F
PMID:34346498	late spindle elongation (move down /when GO reflect stages of meiotic spindle elongation)
PMID:34352089	Supplementary Figure S5B
PMID:34352089	Pac1 strain (Pac1-AA) that allowed rapid rapamycin-dependent nuclear exclusion of Pac1 (Figure 1B).
PMID:34352089	we observed a sharp decline in RNAPII occupancy inside the gene body, directly downstream of the Pac1- bound region located in the first half of the genes (Fig- ure 2B, blue profile). In contrast, Pac1 nuclear exclusion resulted in extended RNAPII occupancy throughout the entire ORFs (Figure 2B, red profile). Such differences in RNAPII profiles are suggestive of Pac1-dependent prema- ture termination.
PMID:34352089	waiting for GO:NEW.inferred from association with prremature termination sites
PMID:34352089	we observed a sharp decline in RNAPII occupancy inside the gene body, directly downstream of the Pac1- bound region located in the first half of the genes (Fig- ure 2B, blue profile). In contrast, Pac1 nuclear exclusion resulted in extended RNAPII occupancy throughout the entire ORFs (Figure 2B, red profile). Such differences in RNAPII profiles are suggestive of Pac1-dependent prema- ture termination.
PMID:34352089	Figure 3A and Supplementary Fig- ure S5A
PMID:34352089	MOVE DOWN
PMID:34352089	MOVE DOWN
PMID:34352089	NEW TERM REQUESTED CHILD OF BOTH termination of RNA polymerase II transcription, poly(A)-independent We showed pac1-dependent poly(A)-independent RNA polymerase II termination for 2 mRNA genes (mfs2 and SPBC530.02), 4 snRNA genes (snU1, snU2, snU4 and snU5), and 2 snoRNA genes (snU3 and snU32) . Can this be added in the annotation extension ?
PMID:34352089	Figure 3A and Supplementary Fig- ure S5A
PMID:34352089	figure 1c
PMID:34352089	5' extended precursors, C/C box (but not H/ACA box). Pac1 nuclear exclusion specifically led to the accumulation of 5′-extended precursors of Pac1-bound C/D box snoRNAs (Supplementary Figure S3A). This ac- cumulation was confirmed by Northern blot assays on three C/D box snoRNAs (sno16, snoU14 and snr79), whereas a control H/ACA box snoRNA (sno12) was unaffected
PMID:34352089	5' extended precursors, C/C box (but not H/ACA box)
PMID:34352089	5' extended precursors, C/C box (but not H/ACA box)
PMID:34352089	waiting for GO:NEW. We show this for only two mRNA: mfs2 and SPBC530.02. Can this be added in the annotation extension ?
PMID:34382912	figure 2
PMID:34382912	fig4
PMID:34382912	fig 5
PMID:34382912	fig 5
PMID:34382912	fig 5
PMID:34382912	fig4
PMID:34382912	fig 5
PMID:34382912	fig 5
PMID:34382912	fig 5
PMID:34382912	fig4
PMID:34382996	Only when gpd1∆ is in h- cell
PMID:34382996	Stronger phenotype in h+ than h- cell
PMID:34382996	figure5
PMID:34382996	figure5
PMID:34382996	Fig. 6 E and Fig. S4 D. By LM, Myo52 and Exo84 also showed strong signal reduction in fus1Δ .
PMID:34382996	Interestingly, the reduction in local secretion correlates with a strong loss of the wPM phenotype (Fig. 6, A and B; Fig. S4, E and F; and Fig. S5): only 4% of h+ fus1Δ cells (1/27) showed wPM, whereas 73% (16/22) and 20% (4/20) of h+ WT showed wPM in WT × WT and WT × fus1Δ crosses, respectively
PMID:34382996	no assembly of vesicles by electron microscopy (Because cell fu- sion completely fails when both partner cells lack fus1)
PMID:34382996	Fig. 6, A–C The density of vesicles was strongly reduced in the fus1Δ cells, whether this was h+ or h−, while WT h+ cells showed slightly higher vesicle density than h− cells, as in previous analysis ()
PMID:34382996	Fig. 6, A–C The density of vesicles was strongly reduced in the fus1Δ cells, whether this was h+ or h−, while WT h+ cells showed slightly higher vesicle density than h− cells, as in previous analysis ()
PMID:34389684	Fig 7A
PMID:34389684	Fig 7a
PMID:34389684	Fig 7 compared to WT
PMID:34389684	Fig 7 compared to WT
PMID:34389684	compared to WT
PMID:34389684	compared to WT
PMID:34389684	compared to WT
PMID:34389684	Random spore analysis
PMID:34389684	Although seb1- G476S asp1-H397A cells grew slowly in liquid medium at 30 °C, an assay of acid phosphatase showed that the double mutant expressed threefold higher levels of Pho1 than the seb1-G476S single mutant (Fig. 6B). (NOTE ABOUT 20 FOLD HIGHE TTHAN WT)
PMID:34389684	similar to wt
PMID:34389684	Figure 1A (vw changed to increased with low serverity as we compare to WT)
PMID:34389684	Random spore analysis (DNS)
PMID:34389684	Random spore analysis (DNS)
PMID:34389684	Random spore analysis (DNS)
PMID:34389684	Figure 1A
PMID:34389684	Figue 1C
PMID:34389684	this can be inferred from the experiments
PMID:34389684	Random spore analysis
PMID:34389684	The seb1-G476S and aps1Δ alleles were synthetically lethal;
PMID:34389684	Here, we found that tgp1 promoter–driven acid phosphatase expression was increased 30-fold in seb1-G476S cells versus seb1-WT cells and that this derepression was effaced by mutating the promoter-proximal nc- tgp1 PAS (Fig. 4D).
PMID:34389684	(Fig. 4B), Pho1 expression from the wild-type plasmid was increased sevenfold in seb1-G476S cells versus seb1-WT cells thereby echoing the derepressive effect of seb1-G476S on pho1 expression from the chromosomal prt–pho1 locus.
PMID:34389684	..... while rhn1Δ rescued the cs growth defect of seb1-G476S at 20 °C
PMID:34389684	Figue 3A Notable findings were that seb1-G476S rescued the ts growth defect of rhn1Δ at 37 °C......
PMID:34389684	Random spore analysis
PMID:34389684	Random spore analysis
PMID:34389684	Random spore analysis
PMID:34389684	Random spore analysis
PMID:34389684	Random spore analysis
PMID:34389684	Figure 1c
PMID:34389684	NorthernBlotting
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	RNA-seq poly(A) tail reads. (Figs. 3–5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	Fig 7A
PMID:34402513	Figure S2A and C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure S2A-B
PMID:34402513	Figure S2A-B
PMID:34402513	Figure S2A-B there was no detectable defect in morphology or cell division in imp2-11A, imp2-11E, imp2-17E, imp2-28A or imp2-28E cells although some imp2-17A cells failed to separate, forming chains (Fig. S2A and B).
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 3. Imp2-11A-mNG was recruited to the CR earlier (ca. 4 minutes) than Imp2-mNG (Fig. 3A, B, and C).
PMID:34402513	Figure SA and C
PMID:34402513	Figure S2D and F
PMID:34402513	Figure S2D-E
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	vw added extensions to link MF to BP & phase
PMID:34402513	This phenotype suggests that phosphorylation of the 17 CK1 consensus sites in Imp2 promotes the medial anchoring of the CR on the membrane, possibly by stabilizing an unknown interaction involving the Imp2 IDR.
PMID:34402513	Figure S2A-B
PMID:34402513	Together these findings implicate Cdk1 in modulating the timing of Imp2 localization to the CR, and are consistent with the general theme of Cdk1 inhibiting cytokinesis until chromosome segregation is complete
PMID:34402513	Imp2 was phosphorylated by Hhp1 in vitro, and mutation of the 15 identified and two more CK1 consensus sites eliminated this phosphorylation (Fig. 2B)
PMID:34402513	Figure S4A
PMID:34402513	Figure S4A
PMID:34402513	Figure S4B
PMID:34402513	Figure 2E
PMID:34402513	Figure 3
PMID:34402513	Figure S2D-E
PMID:34402513	Figure 4
PMID:34402513	Figure 4
PMID:34402513	Figure 4
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure S3B-C
PMID:34402513	Figure 4
PMID:34402513	Figure 4
PMID:34402513	Figure 4
PMID:34402513	Figure 2D
PMID:34402513	Figure S2D and F
PMID:34402513	Figure S2A and C
PMID:34402513	Figure S3B-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 1A-C
PMID:34402513	Figure 2F
PMID:34402513	Figure S2A-C
PMID:34402513	Figure S2A-B
PMID:34402513	Figure S4B
PMID:34402513	Figure S4B
PMID:34402513	Figure S3A Interestingly, we noticed during imaging that imp2-17A rlc1-mNG sid4-mNG cells displayed CR sliding events where the CR formed in the middle of the cell but then slid towards one cell tip (6/18 cells) (Fig. S3A).
PMID:34402513	Figure S3B-C
PMID:34402513	Figure S2D-E
PMID:34402513	Figure 4A-B
PMID:34402513	Figure 4A-B
PMID:34402513	Figure 4A-B
PMID:34402513	Figure 2G
PMID:34402513	Figure S2D-E
PMID:34402513	Figure S2F
PMID:34402513	Figure S2C
PMID:34402513	Figure S3B-C
PMID:34402513	Figure 4
PMID:34402513	Figure 4
PMID:34402513	Figure 4. However, imp2-17E cells exhibited slower CR constriction. In fact, CR remnants remained in 62% of imp2-17E cells for the duration of our observation.
PMID:34402513	Figure 3. Imp2-11E-mNG was not recruited to the CR later than Imp2-mNG but its peak accumulation was delayed compared to wildtype (Fig. 3A, B, and C)
PMID:34402513	Figure 2G However, mutation of 3 additional Cdk1 consensus sites abolished Imp2 phosphorylation by Cdk1 (Imp2-11A, Fig. 2C).
PMID:34402513	Figure 2G, H
PMID:34402513	Figure S4A
PMID:34402513	Figure S4A
PMID:34402513	Figure S2A and C
PMID:34402513	Figure S2A and C
PMID:34402513	Figure S2A-B
PMID:34402513	Figure S2A-B
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence was from RNA-seq not from microarray
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence was from RNA-seq data
PMID:34460892	Evidence from RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence code was RNA-seq
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34460892	Evidence form RNA-seq data
PMID:34464389	S7A Fig A re-analysis of RNA-seq data from non-dividing cells [68] revealed a subtle increase in tlh2 expression during chronological ageing
PMID:34464389	Fig 5A Given the increased lifespan of rnh1Δ rnh201Δ cells
PMID:34464389	5B Notably, in aged cells the double mutant showed an ~3-fold increase in chro- mosomal junctions on average, albeit with large variation, but no increase in indels
PMID:34464389	Figure 4B Accordingly, our smFISH experiment showed that tlh2 was de-repressed in sir2 deletion cells
PMID:34464389	Based on DNA breakpoint junctions in genome sequence data (Fig 5B While wild-type cells showed a substantial increase of indels in aged cells, sir2Δ cells showed only a subtle increase
PMID:34464389	Figure S7C Moreover, the tlh2 overexpression strain was substantially shorter-lived than wild-type cells
PMID:34464389	Figure 5A Cells lacking Sir2 showed a subtle extension of chronological lifespan compared to wild-type, especially at later timepoints
PMID:34464389	Figure S7B The proportion of junctions down- stream of tlh2 was higher in the tlh2 overexpression strain compared to wild-type
PMID:34464389	during stationary phase. Figure 6C In fact, the protein levels of Scw1 markedly decreased in ageing cells.
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:34499159	Figure 3c
PMID:34499159	Figure 4c
PMID:34499159	Figure 5A
PMID:34499159	Figure 2
PMID:34499159	Figure 3d
PMID:34499159	Figure 2
PMID:34499159	Figure 3C
PMID:34499159	Figure 2
PMID:34499159	Figure 3c
PMID:34499159	Figure 4b
PMID:34499159	Figure 4B
PMID:34499159	Figure S2B
PMID:34499159	Figure 5E
PMID:34499159	Thus, in addition to Psk1, Atg13 also appears to be phosphorylated by TORC1 in a manner dependent on Mip1 Tyr-533, a residue critical for the TOS motif-mediated recruitment of TORC1 substrates.
PMID:34499159	Figure 5D These observations indicate that the mip1 mutation does not affect the TORC1-dependent phosphorylation of Sck1, Sck2 and Maf1.
PMID:34499159	Figure 5A
PMID:34499159	Figure 4B
PMID:34499159	Figure 1
PMID:34524082	Figure 3F / fig1 These experiments confirm the observation by Oya et al., 2019 that the H3K14ub substrate triggers a dramatic and specific increase in the methyltransferase activity of Clr4. However, in contrast to the previous study, we observe that the KMT domain is sufficient to mediate this regulatory mechanism.
PMID:34524082	consistent with Clr4’s KMT domain mediating the crosstalk between H3K14ub and H3K9me2/3 as an essential step in heterochromatin formation and maintenance.
PMID:34524082	Figure 3F /fig1
PMID:34524082	Figure 3F /fig1
PMID:34524082	hht-ub14 substrate which both manifest a similar degree of strong stimulation by H3K14ub (Figure 1C, Figure 1—figure supplement 1E–H).
PMID:34524082	Fig. 4E
PMID:34524082	Fig. 4E
PMID:34524082	Fig. 4E
PMID:34524082	Fig. 4E
PMID:34524082	Fig. 4D
PMID:34524082	Fig. 4D
PMID:34524082	Fig. 4D
PMID:34524082	Fig. 4E REQUESTED ABOLISHED
PMID:34524082	Fig. 4A
PMID:34524082	Fig. 4D
PMID:34524082	Fig. 4D
PMID:34524082	Fig. 4D (Currently, we cannot explain why the dg transcripts in the 3FA mutant are only slightly elevated while completely losing H3K9me2/3.)
PMID:34524082	VW REQUESTED ABOLISHED Fig. 4E Both H3K9me2 and H3K9me3 were completely abolished in clr4-GS253 and clr4-3FA strains at centromeric dg/dh repeats, being indistinguishable from clr4Δ
PMID:34524082	Fig. 4A
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34580178	figure 1B
PMID:34608864	presence or absence of HU
PMID:34608864	presence or absence of HU
PMID:34608864	presence or absence of MMS
PMID:34608864	presence or absence of MMS
PMID:34608864	presence or absence of HU
PMID:34608864	presence or absence of HU
PMID:34608864	presence or absence of MMS
PMID:34608864	in presence or absence of MMS
PMID:34613787	Contractile rings of adf1-M3 mutant cells accumulated actin twice as fast over a similar period of time as wild-type cells (Table 2).
PMID:34613787	In prior work the mutant cells appeared to assemble normal contractile rings, but our quantitative measurements revealed that the cdc12-4A mutation reduced by about half both the rate of accumulation and the peak numbers of polymerized actin in the ring (Fig. 2E and Table 1).
PMID:34613787	Figure 2B
PMID:34613787	(Fig. 3C) The number of Cdc12-3GFP molecules in the contractile rings of adf1-M3 mutant cells was on average about twice that of wild-type cells and much more variable
PMID:34613787	Therefore, mature rings of the mutant had on average about 1.9 times as much actin as wild-type cells
PMID:34613787	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	Second, the normalized disassembly rate, which took the number of actin molecules in the ring into consideration, was 40% lower in the mutant than wild-type cells.
PMID:34613787	In contrast, these myosins persisted at nearly their highest levels for an hour and the time course of the process was much more variable in the adf1-M3 mutant cells (Fig. 4C and D). In a few cofilin mutant cells, the myosins dwelled at the cell division site for more than 10 minutes after the completion of the ring constriction (Fig. 5A).
PMID:34613787	Figure 2B
PMID:34613787	(Fig. 3A-B and Table 2). Contractile rings of adf1-M3 mutant cells that were able to constrict had twice as many myosin molecules as the wild-type cells, translating to one myosin motor domain for every 70 nm of filament
PMID:34613787	(Fig. 3A-B and Table 2). Contractile rings of adf1-M3 mutant cells that were able to constrict had twice as many myosin molecules as the wild-type cells, translating to one myosin motor domain for every 70 nm of filament
PMID:34613787	Mutations of either type II myosin gene in the myo2-E1 or myp2Δ strains reduced the numbers of actin molecules in contractile rings by more than half compared with wild-type cells at the end of 10 the maturation period and the onset of constriction (Fig. 6A-B and Table 1).
PMID:34613787	Mutations of either type II myosin gene in the myo2-E1 or myp2Δ strains reduced the numbers of actin molecules in contractile rings by more than half compared with wild-type cells at the end of 10 the maturation period and the onset of constriction (Fig. 6A-B and Table 1).
PMID:34613787	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization
PMID:34613787	WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization
PMID:34613787	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	mechanoreceptor. Together, these results indicate that Wsc1 clustering may be triggered by local surface compression, independently of puta- tive ‘‘trans’’ homotypic interactions between extracellular sensors from neighbor cells or general cell-to-cell signaling.
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	increased lateral diffusion in membrane. Finally, Wsc1DWSC-GFP and Wsc1DSTR-GFP, which are incapable of clustering, exhibited much smaller half-times—closer to that of mCherry-Psy1 (Figures 6A, 6B, and S6A).
PMID:34666001	(vw: 25% cell death)
PMID:34666001	In microchannels, where clusters form at high frequency, due to larger and more frequent compressive mechanical stresses onto the CWs, the survival behavior was markedly different. First, wsc1D cells exhibited a much higher yield of death of $28%. Second, all alleles exhibited a high yield of death around $25% including wsc1DWSC
PMID:34666001	n these videos, we did not detect any lysis in WT red cells, but a high incidence of dying wsc1DCC-GFP of $26%
PMID:34666001	increased lateral diffusion in membrane. Finally, Wsc1DWSC-GFP and Wsc1DSTR-GFP, which are incapable of clustering, exhibited much smaller half-times—closer to that of mCherry-Psy1 (Figures 6A, 6B, and S6A).
PMID:34666001	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at con- tacts close to $2 (Figures 5D, 5E, and S2F–S2H).
PMID:34666001	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at con- tacts close to $2 (Figures 5D, 5E, and S2F–S2H).
PMID:34666001	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at con- tacts close to $2 (Figures 5D, 5E, and S2F–S2H).
PMID:34666001	Remarkably, the Wsc1DCC-GFP lacking a large fraction of the cytoplasmic C-ter- minal tail, and thus presumably defective in downstream signal transduction was dispensable for clustering. This finding rein- forces the notion that Wsc1 clustering occurs independently of downstream CWI signaling.
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34666001	figure 5
PMID:34674264	in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2
PMID:34674264	Fig. 2B). Almost abolished Dma1 auto-ubiquitination by in vitro assay
PMID:34674264	Decreased Dma1 auto-ubiquitination by in vitro assay
PMID:34674264	in vitro assay
PMID:34674264	Although this assay is not quantitative, we found that Sid4 was ubiquitinated to similar levels as in wild-type in both dma1-6A and dma1-6D/E but was not ubiquitinated in dma1D (Fig. 2A).
PMID:34674264	(Fig.3A–C). Reduced contractile ring localization during mitosis. However, we observed that Dma1-6A was significantly more difficult to detect at the first instance of CR localization early in mitosis than either Dma1 or Dma1-6D/E
PMID:34674264	in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2
PMID:34674264	in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2
PMID:34674264	Normal localization to medial cortical nodes, SPB, and division septum as wildtype
PMID:34674264	Normal localization to medial cortical nodes, mitotic contractile ring, SPB, and septum as wildtype
PMID:34674264	Fig 4a We observed that nda3-km311, dma1- 6A nda3-km311, and dma1-6D/E nda3-km311 cells delayed septation relative to wild-type cells and that dma1Δ cells did not
PMID:34674264	Fig 4a
PMID:34674264	Localization to SPBs at the same level as wildtype during spindle stress
PMID:34674264	Localization to SPBs at the same level as wildtype during spindle stress
PMID:34674264	CHECK ALLELELS we combined analog-sensitive (cdc2-as, orb5-as) and temperature- sensitive (plo1-1) alleles. Despite these kinases targeting Dma1 in vitro, we found no evidence that inhibiting any of them singly (not shown) or together (Fig. 1G) chan- ged Dma1 phosphostatus as monitored by SDS/PAGE mobility suggesting that these kinases are not responsible for regulating Dma1 phosphostatus in cells.
PMID:34674264	Normal localization to medial cortical nodes, SPB, and division septum as wildtype
PMID:34674264	(Fig.2B). Dma1-6D/E auto-ubiquitination was modestly but reproducibly reduced relative to wild- type. Specifically, while 82% of wild-type Dma1 became ubiquitinated on at least one site, 71% of Dma1-6D/E did.
PMID:34674264	in vivo phosphorylation sites identified by mass spectrometry
PMID:34674264	in vivo phosphorylation site identified by mass spectrometry
PMID:34674264	in vitro kinase assay showed S166 is phosphorylated by Cdk1
PMID:34674264	in vitro kinase assay showed S251 is phosphorylated by Plo1
PMID:34731638	(figure 1 f)
PMID:34731638	(fig1G) (fig1G ) vw changed to increased (compared to WT)
PMID:34731638	(fig1G ) vw changed to increased (compared to WT)
PMID:34731638	Moreover, epe1Δ reduced the expression of several subtelomeric genes in pob3Δ, suggesting that it also counteracts heterochromatin spreading (Figure 3G)
PMID:34731638	Partial suppression of pob3∆ silencing phenotype.
PMID:34731638	To test this more directly, we performed the HSS assay in the double spt16–1epe1Δ mutant. Indeed, heterochromatin spreading was completely restored (Figure 3H, compare with Figure 2D)
PMID:34731638	(Figures 1E and S1D) we found increased signals of elongating RNAPII (RNAPII Ser2P) and H2B ubiquitination (H2Bub), a histone mark associated with active transcription
PMID:34731638	(Figure S1E)
PMID:34731638	Figures S2C–S2E in chromatin/euchromatin
PMID:34731638	Figures S2C–S2E in chromatin/euchromatin
PMID:34731638	Although degradation of Epe1 still occurs in pob3Δ in S phase, we found increased steady-state levels of Epe1 in cycling cells (Figure S3A).
PMID:34731638	found reduced Swi6 binding in spt16–1 at subtelomeric genes close to the heterochromatin boundary (SPAC212.12, SPAC212.06c; Figure 4D).
PMID:34731638	(Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	(Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	(Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	synthetic defect in the silencing of dg and tlh1/2 transcripts (Figure 4C)
PMID:34731638	ntriguingly, while H3K9me2 levels were unaltered in spt16–1, H3K9me3 levels were reduced at several loci at the TEL1L subtelomeric region (i.e., SPAC212.09c, SPAC212.08c, and SPAC212.06c; compare Figure 4B with 4A)
PMID:34731638	Figure 4E
PMID:34731638	Figure 4E
PMID:34731638	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
PMID:34731638	(Figures 1E and S1D) we found increased signals of elongating RNAPII (RNAPII Ser2P) and H2B ubiquitination (H2Bub), a histone mark associated with active transcription
PMID:34731638	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
PMID:34731638	Nonetheless, the pob3Δ mutant exhibited increased incorporation of H3-T7 at the TEL1L region (Figure 4G), implying that the H3 turnover rate is increased at subtelomeric heterochromatin.
PMID:34731638	(Figure 2C) Conversely, in the pob3Δ strain, the orange reporter was also fully derepressed in the majority of cells, yet the green reporter remained silenced or mildly derepressed. This result implies that pob3Δ cells have a heterochromatin spreading defect
PMID:34731638	(Figures 1B, 1C, S1D) only a subtle change of H3K9me2 at pericentromere
PMID:34731638	(Figure 1B) In contrast, there was a substantial reduction of H3K9me2 at the mating-type locus, in agreement with a previous study (Holla et al., 2020) (Figure S1A), and at the subtelomeres
PMID:34731638	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
PMID:34731638	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
PMID:34731638	(Figure S2F)
PMID:34731638	vw changed from decreased to normal because look WT?
PMID:34731638	(figure 1 f)
PMID:34731638	Figure 4E
PMID:34731638	Figure 4E
PMID:34731638	(Figure 1 G)
PMID:34731638	(Figure 1 G)
PMID:34738170	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34738170	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34738170	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34798057	(weird!) Intriguingly, the double nda2noD nda3noD mutant was less sensitive than the single ones. OK!Therefore, a possible explanation for the lower sensitivity of the double mutant is that defects resulting from the elevated level of one monomer are compensated for by a similar overexpression of the second monomer.
PMID:34798057	Both mutants displayed meiosis defects with a reduction in gamete numbers and viability more marked in the nda2noD mutant (Figures 6A, 6B, and 6C).
PMID:34798057	Figures 6I and 6J
PMID:34798057	Figure 6E When dus3D diploids were induced to enter meiosis, the time needed in prophase for spindle assembly in MI was increased, while a marked in- crease in the duration of metaphase was noted in both MI and MII (Figures 6D–6H).
PMID:34798057	V348A
PMID:34798057	Figure S1 D
PMID:34798057	(Figure S7A),
PMID:34798057	(Figure S7A)
PMID:34805795	during amino acid starvation
PMID:34805795	BFC augments TORC1 activation in response to amino acid stimulation
PMID:34805795	during amino acid supplementation. (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation.
PMID:34805795	during amino acid supplementation. (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation.
PMID:34805795	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid star- vation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	(Figure S1A)
PMID:34805795	Figure 5
PMID:34805795	Figure S1A
PMID:34805795	Figure S1A
PMID:34805795	results in a significant growth advantage of BFC mutant over wild-type strains when equal number of log phase cells are grown on rapamycin-containing EMM plates supplemented with amino acids (Figures S1A and S1B). Moreover, treating cells with 125 or 150 ng/mL of rapamycin for 90 min revealed that the growth advantage of BFC mutants correlates with an increase in P-Rps6 levels compared to wild-type cells (Figure S5C). Together, these data support a model in which BFC participates in TORC1 repression.
PMID:34805795	Bhd1 and Fnp1 appear diffusely distributed throughout the cytoplasm in amino acid replete conditions, but localize to vacuoles in response to amino acid starvation evidenced by the strong overlap between Bhd1-/Fnp1-GFP and the FM4-64 dye under amino acid starvation conditions (Figures 2A–2F)
PMID:34805795	(figure 4d) (vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	(figure 4d) (vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	Figure 5
PMID:34805795	(Figure 4F) (vw: ph9)
PMID:34805795	(Figure 4F) (vw: ph9)
PMID:34805795	(Figure S1A)
PMID:34805795	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid star- vation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	during amino acid starvation
PMID:34810257	We next checked the distribution of CENP-TCnp20-GFP in ccp1Δ and found that its centromere localization was unaffected in the mutant (Fig. 2 G–I).
PMID:34810257	Yeast two hybrid The yeast two-hybrid assays showed that the Ccp1 homodimer mutant, Ccp1-4A, was unable to interact with CENP-TCnp20 (Fig. 3A and SI Appendix, Fig. S8)
PMID:34810257	But most cnp20-14A cells display mitotic delay, and more than 12% of mutant cells failed to complete chromosome segregation within 30 min (Fig. 6 E and F)
PMID:34810257	(ndc80 receptor) These co-IP experiments showed that the interaction between Ndc80 and CENP-TCnp20 is drastically increased during mitosis (Fig. 7C), supporting the idea that the presence of Ccp1 interferes with the interaction between Ndc80 and CENP-TCnp2
PMID:34810257	These data demonstrate that CDK1 is capable of phosphorylating the CIM domain of CENP-TCnp20. Various slow migrating bands were observed in the assay with Cnp201-55 (Fig. 7D), indicating that the domain contains multiple phosphorylation sites, consistent with our point mutation analysis. (ASSAYED USING HUMAN CDK1)
PMID:34810257	But GFP-Ccp1 is completely disassociated from centromeric regions in cnp20-ΔCIM at all stages of the cell cycle (Fig. 4 C and D and SI Appendix, Fig. S13).
PMID:34810257	(Fig. 4 E and F).
PMID:34810257	We found that cnp20-14A is highly sensitive to TBZ, even more strongly than the cnp20-ΔCIM mutant (Fig. 6D and SI Appendix, Fig. S16),
PMID:34810257	fig 3 Our results indicate that the first 55 amino acids of CENP-TCnp20 are the minimal interaction domain with Ccp1, which we named the Ccp1- interacting motif (CIM).
PMID:34810257	However, we found that Spc25-GFP appeared not to attach to microtubules in ∼20% of cnp20-14A mitotic cells, indicating that dephosphorylation of the CIM domain leads to mislocalization of Ndc80C during mitosis (Fig. 7A). Importantly, our co-IP results indicated that the interaction between Cnp20-14A and Ndc80 is significantly reduced during mitosis (Fig. 7B).
PMID:34810257	Cnp20-14A showed a strong interaction with Ccp1 (Fig. 5F)
PMID:34810257	In addition, we found that CENP-ACnp1-GFP partially reduced its centromere localization in cnp20-9 at the restrictive temperature (SI Appendix, Fig. S6).
PMID:34810257	Yeast two hybrid To investigate how phosphorylation of the CIM domain affects the interaction between Ccp1 and CENP-TCnp20, we conducted yeast two-hybrid assays with Cnp20-14D and Ccp1. We found that the interaction between Cnp20-14D and Ccp1 was dramatically reduced (Fig. 5F).
PMID:34810257	whereas the localization of GFP-Ccp1 at centromeres only has a mild reduction in the CENP-A ts mutant, cnp1-1 (SI Appendix, Fig. S4).
PMID:34810257	during mitotc M-phase. In contrast, we found that GFP-Ccp1 in all cnp20-14A mutant cells remains associated with centromeres during all the stages of the cell cycle (Fig. 6 B and C).
PMID:34810257	(These data suggest that phosphorylation of the CIM domain leads to disassociation of Ccp1 from centromeres. CIM domain) Together,our data indicate that CENP-TCnp20 is required for Ccp1 centromere localization
PMID:34810257	fig 3 Our results indicate that the first 55 amino acids of CENP-TCnp20 are the minimal interaction domain with Ccp1, which we named the Ccp1- interacting motif (CIM). Yeast two hybrid
PMID:34810257	Consistent with the key role of CENP-TCnp20 in the assembly of the Ndc80 complex, we found that the association of Ndc80-GFP with centromeres is lost in cnp20-9 at the restrictive temperature (Fig. 2 C and D).
PMID:34810257	We found that GFP-Ccp1 was delocalized from centromeres at the restrictive temperature in cnp20-9 at all stages of the cell cycle (Fig. 2 E and F and SI Appendix, Fig. S3)
PMID:34810257	whereas the localization of GFP-Ccp1 at centromeres only has a mild reduction in the CENP-A ts mutant, cnp1-1 (SI Appendix, Fig. S4).
PMID:34849791	Figure 3B
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S3B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S2B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S1B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S6B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Supplemental Figure S4B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Figure 3B
PMID:34849791	Figure 3A
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Figure 4
PMID:34849791	Figure 4
PMID:34849791	Supplemental Figure S5B
PMID:34849791	Supplemental Figure S5B
PMID:34851403	Non-separated signals were found to be significantly or nearly significantly wider than in wild-type cells (Fig. 3E,F;)
PMID:34851403	In mrc1Δ cells, sister kinetochores and centromere cores separated at a low, but significant, level (Fig. 3A–D; Figs S2C and S3A,B), and non-separated signals were significantly wider in shape (Fig. 3E,F; Fig. S3C,D).
PMID:34851403	Additionally, the DNA replication checkpoint function of Mrc1 is not required for sister kinetochore association, because deletion of cds1, which encodes an effector kinase functioning downstream of Mrc1 in the DNA replication checkpoint pathway (Alcasabas et al., 2001; Murakami and Okayama, 1995; Tanaka and Russell, 2001), did not affect the kinetochore association state or sister chromatid segregation (Fig. 3C,E; Fig. S2C).
PMID:34851403	In cells lacking Sgo1 (sgo1Δ), which protects centromeric cohesin during anaphase, no separated kinetochore signals were observed (Fig. 3A,C), although sister chromatids frequently underwent equational segregation in the absence of chiasmata (Fig. S2B).
PMID:34910579	ogether, these results confirmed that Sbg1 is specific to Bgs1, while Smi1 regulates the levels of both Bgs4 and Bgs1 at the division site, with a more important role for Bgs4 (Figure 7, A–C).
PMID:34910579	36 degrees
PMID:34910579	36 degrees
PMID:34910579	36 degrees
PMID:34910579	Supplemental Figure S2, A–D
PMID:34910579	Supplemental Figure S2, A–D
PMID:34910579	36 degrees
PMID:34910579	36 degrees
PMID:34910579	36 degrees
PMID:34910579	36 degrees
PMID:34910579	Figure 1, C and D restrictive temperature mutant.
PMID:34910579	36 degrees
PMID:34910579	see above
PMID:34910579	We confirmed the defects in septa using electron microscopy. In cells with closed septa, the primary septum was uneven (Figure 3, red arrows) and thinner in smi1-1 cells than in WT (Figure 3A).
PMID:34910579	Figure 2A
PMID:34910579	recruits glucanases and glucan synthases to division site
PMID:34910579	36 degrees
PMID:34910579	36 degrees
PMID:34910579	38.5% cf WT 11.5% Figure 1F
PMID:34910579	recruits glucanases and glucan synthases to division site
PMID:34951983	Microtubule dynamics required for spindle repair following laser ablation
PMID:34951983	Not required for spindle repair following laser ablation
PMID:34951983	required for spindle repair following laser ablation
PMID:34951983	required for spindle repair following laser ablation
PMID:34958661	Fig S1A; 27 micron
PMID:34958661	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C–E; and Fig. S3 M).
PMID:34958661	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C–E; and Fig. S3 M).
PMID:34958661	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C–E; and Fig. S3 M).
PMID:34958661	(actually mid1-Nter)
PMID:34958661	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	Thus, Arf6 and Mid1 are partially over- lapping anchors for Cdr2 nodes.
PMID:34958661	We combined arf6Δ with the mid1(400–450Δ) mu- tant that cannot bind Cdr2. In the resulting cells, Cdr2 was ab- sent from the cell cortex and formed large cytoplasmic puncta (Figs. 4 A and S2 J).
PMID:34958661	o explain this connection, we examined the localization of Wee1 and Cdr1 at cortical nodes in arf6Δ mutants. Wee1 localized to nodes in arf6Δ, but Cdr1 did not (Fig. 3, D and E; and Fig. S3 D)
PMID:34958661	"Modified form is indirect because GDP bound does not localize to nodes) ""These defects indicate that Arf6 anchors Cdr2 stably at nodes, meaning that Arf6 and Cdr2 reciprocally promote each other’s node localization."""
PMID:34958661	rf6Δ cells had cytoplasmic Cdr2 clusters that were absent in wild-type cells (Figs. 3 A and S2 J), indicating defects in cortical anchoring.
PMID:34958661	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	Ucp3-mNG localized to spots at the cell tips, which likely represent endocytic actin patches due to colocalization with actin patch component Pan1 (Fig. S2, E and F)
PMID:34958661	Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G)
PMID:34958661	Further, Arf6 localization to nodes was lost upon deletion of its GEF Syt22 (Fig. 2 G
PMID:34958661	but the GTP-locked allele arf6(Q75L)-mNG remained at nodes (Fig. 2 F)
PMID:34958661	A GDP-locked mutant arf6(T52N)-mNG lost node localization, (Fig. 2 F)
PMID:34958661	Arf6 node localization required Cdr2 but not other node proteins (Figs. 2 E and S2 B).
PMID:34958661	trongly enriched at cortical nodes in the cell middle (Fig. 2 A). Arf6 and Cdr2 colocalized at nodes (Figs. 2 B and S2 A)
PMID:34958661	Arf6 localizes stably to Cdr2 nodes during interphase in a manner that depends on nucleotide binding, membrane binding, and Cdr2 itself.; strongly enriched at cortical nodes in the cell middle (Fig. 2 A). Arf6 and Cdr2 colocalized at nodes (Figs. 2 B and S2 A)
PMID:34958661	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	The cell length at division phenotype for arf6Δ was minor, but these cells were wider than wild type (Fig. S1 E).
PMID:34958661	This is from GIs, phenocopy, PLUS If the Arf6 localization defect in syt22Δ is due to loss of the GTP-bound state, then it should be suppressed by arf6(Q75L). Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G)
PMID:34958661	Fig S1A; 24.6 micron
PMID:34958661	Fig S1A; 26.6 micron
PMID:34958661	Figure 1
PMID:34958661	Figure 1
PMID:34959732	(Sub lethal and lethat doese) Figure 5 and Figure S3. Also in the Table 3.
PMID:34959732	Table 5 and Figure S3, and Figure S4C. Vegetative cell lysis caused by lethal and sublethal concentrations of micafungin is suppressed in the pbr1-8
PMID:34959732	(Sub lethal and lethat doese) Figure 5 and Figure S3. Also in the Table 3.
PMID:34959732	Figure 4B and Figure S2B. Also in the Table 3. The pbr1-8 mutation partially suppresses the slowing cytokinesis caused by lethal concentrations of caspofungin, suggesting that besides Bgs4, this drug affects other Bgs subunits (Bgs1 and/or Bgs3)
PMID:34959732	Figure 3A and Figure S1A. Table 3. Suppression of the lytic phenotype at cytokinesis
PMID:34959732	Figure 3B and Figure S1B. Also in the Table 3. Cytokinesis is blocked in both wild-type and pbr1-8 strains treated with lethal concentrations of the echinocandin drug anidulafungin, suggesting that this drug affects the function of Bgs4 and Bgs1 and/or Bgs3
PMID:34959732	Figure 4A and Figure S2A Sublethal concentrations of caspofungin
PMID:34959732	Table 5 and Figure S3, and Figure S4C. Vegetative cell lysis caused by lethal and sublethal concentrations of micafungin is suppressed in the pbr1-8
PMID:34959732	Figure 4B and Figure S2B. Also in the Table 3. The pbr1-8 mutation partially suppresses the slowing cytokinesis caused by lethal concentrations of caspofungin, suggesting that besides Bgs4, this drug affects other Bgs subunits (Bgs1 and/or Bgs3)
PMID:34959732	Figure 4A and Figure S2A Sublethal concentrations of caspofungin
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	Northern Blotting, RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:34967420	RNA-Seq
PMID:35008733	Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	(thin-layer chromatography) Additionally, the pattern of complex sphingolipids in Lac1-depleted cells shows a strong accumulation of IPC and the appearance of new bands that might correspond to different IPC species
PMID:35008733	fig 5 b. (thin-layer chromatography) We detected an accumulation of PHS and sphingoid bases-1-phosphate levels (PHS-1P or DHS-1P)
PMID:35008733	Fig 3. Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	Fig 3. Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35011726	Nse1- R188E mutant shows synthetic lethality with smc6-74
PMID:35011726	Nse1- R188E mutant shows synthetic lethality with smc6-74
PMID:35011726	Among the Nse1-bound factors, we repeatedly ob- served the Ubc13, Mms2, and Uba1 (Data File S1A,B, Data File S2A–C—ProteomeXchange: PXD029573, and Table S3).
PMID:35011726	(Figure 2D
PMID:35011726	Figure 1A The MS analysis of the Nse1/3/4- and Ubc13/Mms2-containing in vitro ubiquitination assay led to the identification of Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	(Figure 3A) ubiquitin ligase mutant
PMID:35011726	severe growth defects with smc6-X and nse6∆
PMID:35011726	Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	Figure 1A
PMID:35011726	Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	(Figure 3A) ubiquitin ligase mutant
PMID:35011726	Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome.
PMID:35011726	These synthetic phenotypes were again suppressed by the nse1-C216S mutation (Figure S5).
PMID:35011726	severe growth defects with smc6-X and nse6∆
PMID:35011726	Figure 1A
PMID:35011726	severe growth defects with smc6-X and nse6∆
PMID:35011726	The Nse1 ubiquitin ligase mutant showed a synthetic relationship with the Nse2 SUMO ligase mutant (C195S, H197A), indicating their separate roles in SMC5/6 function
PMID:35011726	Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome.
PMID:35011726	severe growth defects with smc6-X and nse6∆
PMID:35011726	Figure 1A The MS analysis of the Nse1/3/4- and Ubc13/Mms2-containing in vitro ubiquitination assay led to the identification of Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35012333	Fig 13
PMID:35012333	Fig 4B
PMID:35012333	Fig 4B
PMID:35012333	Fig 4B
PMID:35012333	Fig 4B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 5A
PMID:35012333	Fig 6B
PMID:35012333	Fig 6B
PMID:35012333	Fig 6A
PMID:35012333	Fig 6A
PMID:35012333	Fig 7A
PMID:35012333	Fig 7A
PMID:35012333	Fig 7A
PMID:35012333	Fig 7B
PMID:35012333	Fig 7B
PMID:35012333	Fig 7B
PMID:35012333	Fig 7B
PMID:35012333	Fig 7B
PMID:35012333	Fig 7B
PMID:35012333	Fig 7A
PMID:35012333	Fig 4A
PMID:35012333	Fig 7A
PMID:35012333	Fig 7A
PMID:35012333	Fig 7A
PMID:35012333	Fig 8B
PMID:35012333	Fig 8B
PMID:35012333	Fig 8A
PMID:35012333	Fig 8A
PMID:35012333	Fig 4
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 4A
PMID:35012333	Fig 10B
PMID:35012333	Fig 2A
PMID:35012333	Fig 2B
PMID:35012333	Fig 2A
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 2A
PMID:35012333	Fig 2A
PMID:35012333	Fig 2B
PMID:35012333	Fig 2B
PMID:35012333	Fig 2B
PMID:35012333	Fig 1A
PMID:35012333	Fig 1A
PMID:35012333	Fig 1A
PMID:35012333	Fig 1A
PMID:35012333	Fig 1A
PMID:35012333	Fig 1A
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 1A
PMID:35012333	Fig 1A
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 10B
PMID:35012333	Fig 4
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig 10A
PMID:35012333	Fig S7
PMID:35012333	Fig S7
PMID:35012333	Fig S7
PMID:35012333	Fig S7
PMID:35012333	Fig S7
PMID:35012333	Fig S7
PMID:35012333	Fig S6
PMID:35012333	Fig S6, new term suggested
PMID:35012333	Fig 12B
PMID:35012333	Fig 12B
PMID:35012333	Fig 12B
PMID:35012333	Fig S5A
PMID:35012333	Fig S5A
PMID:35012333	Fig S5B
PMID:35012333	Fig S5B
PMID:35012333	Fig S4
PMID:35012333	Fig S4
PMID:35012333	Fig S4
PMID:35012333	Fig S4
PMID:35012333	Fig S4
PMID:35012333	Fig S4
PMID:35012333	Fig S3
PMID:35012333	Fig S3
PMID:35012333	Fig S3
PMID:35012333	Fig S3
PMID:35012333	Fig S2
PMID:35012333	Fig 12A
PMID:35012333	Fig 13
PMID:35012333	Fig 13
PMID:35012333	Fig 13
PMID:35012333	Fig 13, new term suggested
PMID:35012333	Fig 13, new term suggested
PMID:35012333	Fig 13, new term suggested
PMID:35012333	Fig 13, new term suggested
PMID:35012333	Fig 13, new term suggested
PMID:35012333	Fig 13
PMID:35012333	Fig 13
PMID:35012333	Fig 13
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11A
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Fig 11B
PMID:35012333	Described in Garg et al. (NAR 2020) -PMID: 33010152
PMID:35012333	Described in Garg et al. (NAR 2020) -PMID: 33010152
PMID:35012333	Fig 10A
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35012333	Fig 5B
PMID:35024575	Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508.
PMID:35024575	Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508.
PMID:35075549	(Fig. S1) The results showed that Fzo1 protein was not degraded at late time points only in the Δubc8 mutant (Fig. 4). Fzo1 protein was not degraded in ∆rsv2 and Δubc8 mutants after longer incubation times (60 and 72 h)
PMID:35075549	(Fig. 3). We found that Fzo1 protein was not degraded at late time points in the ∆rsv2 mutant
PMID:35075549	****STATIONARY PhASE**** the protein level of Fzo1 is unstable during the stationary phase.
PMID:35075549	(Fig. 5) We found that when Fzo1 protein was overexpressed, it was no longer degraded at late time points
PMID:35075549	-ve regulation stat phase
PMID:35075549	-v regulation, stationary phase
PMID:35079912	We found that only Δfio1 cells were sensitive to Cu2+
PMID:35079912	(Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM.
PMID:35079912	(Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM.
PMID:35079912	(Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition.
PMID:35079912	(Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition.
PMID:35082773	(Figure 5A) In addition, the Cdc25 protein level decreased in 􏰀ppk21 and 􏰀cdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level .
PMID:35082773	It should be noted that cdr2+ overexpressed wild-type cells showed a shorter cell length at 27◦C, but a longer cell length at 35◦C than cdr2+ non-overexpressed wild-type cells (Figure 3B).
PMID:35082773	(Figure 3C). In addition, the cdr2+ overexpressed wild-type cells showed a higher septation index than cdr2+ non-overexpressed wild-type cells at 35◦C
PMID:35082773	(Figures 3A,B) overexpression of cdr2+ also reversed the defects in the cell length and the septation index of ksg1-208 cells
PMID:35082773	(Figure 2D and Supplementary Figure 1) The results showed that the septation ring of the ksg1-208 delta-ppk21 double mutant was off-centered at 33◦C, which was more severe than that of ksg1-208 cells
PMID:35082773	(Figures 2D,E) results showed that ksg1-208 􏰀ppk21 cells exhibited a longer cell length than either ksg1-208 or 􏰀ppk21 cells at both 27 and 33◦C
PMID:35082773	(Figure 2C) 33 degrees
PMID:35082773	Figure 2B...which was recovered by the overexpression of ppk21+
PMID:35082773	(Figure 2B) ...which was recovered by the overexpression of ppk21+
PMID:35082773	(Figure 2A) significantly longer than that of wild-type cells at 27◦C
PMID:35082773	Figure 1A
PMID:35082773	Figure 4c In contrast, a fraction of ksg1-208 cells showed septum or division site localized Cdr2-mEGFP in the dividing cells at 27◦C, indicating the cortex dissociation of Cdr2 was hindered.
PMID:35082773	(Figure 5A) Western blot analysis showed that the level of Cdc25 protein was dramatically lower in ksg1-208 cells than that in wild-type cells, indicating that Ksg1 played a crucial role in the accumulation of Cdc25 protein
PMID:35082773	(Figure 5A). we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells (Figures 4A,B),
PMID:35082773	Figure 1A
PMID:35082773	(Figure 5A). In addition, the Cdc25 protein level decreased in 􏰀ppk21 and 􏰀cdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level
PMID:35082773	(Figures 4A,B) we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells
PMID:35099006	pkd2 mutants show temporary deflation followed by reinflation. pkd2-B42 has 50% lower spring constant as measured by Atomic Force Microscopy implicating reduced cellular stiffness. This indicates a reduced ability of this mutant at maintaining cellular turgor.
PMID:35099006	The growth rate of pkd2-B42 at the restrictive temperature of 36C or higher is 80% lower than wild-type cells.
PMID:35099006	Increased percentage of septated cells at both permissive and restrictive temperature.
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure 4B,D
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2A-C
PMID:35108037	Figure S2A-C
PMID:35108037	Figure S2A-C
PMID:35108037	Figure S2A-C
PMID:35108037	Figure S2A-C
PMID:35108037	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	Figure 1B, 1D-F, 2B-E, 3A-B, S1A-B
PMID:35108037	Figure S3B (25C)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Figure S3A
PMID:35108037	Figure S3A (25C)
PMID:35108037	Figure S2E
PMID:35108037	Figure 4B,D
PMID:35108037	Figure 4B,D
PMID:35108037	Figure 4A,C
PMID:35108037	Figure 4A,C
PMID:35108037	in vitro binding assay with purified Cdc15 F-BAR domain and purified Pxl1 (Fig 1E)
PMID:35108037	in vitro binding assay, Figure 3B
PMID:35108037	Figure S1D-E
PMID:35108037	Figure S2D (19c)
PMID:35108037	Figure S2D
PMID:35108037	Figure S2D(25,29,32)
PMID:35108037	Figure S2D
PMID:35108037	Fig S2D
PMID:35108037	Figure S2D
PMID:35108037	Figure S2D
PMID:35108037	Figure S2D
PMID:35108037	Figure S2D
PMID:35108037	Figure S2D (25,29,32)
PMID:35108037	Figure S2D (25,29,32)
PMID:35108037	Figure S2D
PMID:35108037	Figure S2D
PMID:35108037	Fig S2D
PMID:35108037	Fig S2D
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Figure S2E
PMID:35108037	Pxl1-AxxA1-3 bound Cdc15C1(aa600-end) just as well as wild type Pxl1 (Figure S1A)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Pxl1-P18A reduced binding to full-length Cdc15 compared to wild-type Pxl1 (Figure 3A)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Figure S3A (25C)
PMID:35108037	Mutant bound Cdc15C1(aa600-end) as well as wildtype Pxl1 (Figure S1A)
PMID:35108037	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	Pxl1-P18A+AxxA6 reduced binding to full-length Cdc15 compared to wild type Pxl1 (Figure 3A)
PMID:35108037	Pxl1-AxxA6 reduced binding to full-length Cdc15 (Figure 3A) and Cdc15 C1 (Figure S1A)
PMID:35108037	Pxl1 (aa177-188 P181A, P184A) abolished binding to Cdc15 SH3 and Cdc15C1(aa600-end), Figure 2D
PMID:35108037	Figure 2B - Pxl1(AxxA1-6) reduced binding to Cdc15C(aa441-end) compared to wildtype Pxl1
PMID:35108037	Figure S2A-C
PMID:35157728	Significantly, Δbdf2 restores low levels of Gcn5 binding at MBF promoters in Δtor1 cells under normal growth conditions and also restores the normal pattern of an increased level of Gcn5 in response to HU (Fig 6C).
PMID:35157728	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	Figure2 A
PMID:35157728	We detected a markedly higher level of Gcn5 binding at subte- lomeric genes in Δtor1 cells, compared with wild type cells (Fig 4A).
PMID:35157728	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	Figure2 A
PMID:35157728	Tor1 inhibits the binding of Gcn5 at sub-telomeric genes and MBF promoters
PMID:35157728	no supression
PMID:35157728	Figure2 A
PMID:35157728	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	Figure2 A
PMID:35157728	The Δbdf2 muta- tion also suppresses the elevated levels of Gcn5 at the subtelomeric chromatin in Δtor1 cells (Fig 4E).
PMID:35157728	30 fold. Fig 2
PMID:35157728	120 fold. Fig 2
PMID:35157728	280 fold. Fig 2
PMID:35157728	25%
PMID:35157728	24%
PMID:35157728	Significantly, Δbdf2 restores low levels of Gcn5 binding at MBF promoters in Δtor1 cells under normal growth conditions and also restores the normal pattern of an increased level of Gcn5 in response to HU (Fig 6C).
PMID:3516412	activated_by(CHEBI:18420)
PMID:35171902	. Interestingly, although git3Δ nmt41-epe1+ cells form heterochromatin at pericentric repeats,
PMID:35171902	polysome profiling
PMID:35171902	nterestingly, we found that Epe1 protein levels are significantly reduced in git3Δ nmt41-epe1+ and pka1Δ nmt41-epe1+ cells (Fig 2F)
PMID:35171902	H3K9me2 levels at dh repeats are restored close to wild-type levels in git3Δ nmt41-epe1+ cells (Fig 1E).
PMID:35171902	Consistent with the results of the genetic screen, serial dilution analyses show that git1Δ, git3Δ, git5Δ, gpa2Δ, pka1Δ, and cyr1Δ all rescue silenc- ing defects of otr::ura4+ caused by Epe1 overexpression, as indicated by better growth on EMM medium containing 5-FOA (Fig 1D)
PMID:35171902	polysome profiling
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35194019	TBZ 15ug/ml
PMID:35194019	TBZ 15ug/ml
PMID:35194019	TBZ 15ug/ml
PMID:35194019	Figur 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	Figur 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35194019	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	Figur 5D
PMID:35194019	Figur 5D
PMID:35194019	TBZ 15ug/ml
PMID:35194019	TBZ 15ug/ml
PMID:35194019	Fig S10 (tetrad analysis)
PMID:35277511	growth >48 hrs, growth to exponential phase
PMID:35277511	telomere southern (experiment)
PMID:35277511	telomere southern (experiment)
PMID:35286199	Fig. 1
PMID:35286199	Fig. 5
PMID:35286199	Fig. 5
PMID:35286199	Fig. 4
PMID:35286199	Fig. 4
PMID:35286199	Fig. 4
PMID:35286199	Fig. 4
PMID:35286199	Fig. 4
PMID:35286199	Fig. 4
PMID:35286199	Fig. 3
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 2
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 1
PMID:35286199	Fig. 2
PMID:35293864	Fig. 2 - Figure supplement 2F
PMID:35293864	Fig. 2 - Figure supplement 1 klp5Δklp6Δ cells exhibited slightly longer microtubule growth events
PMID:35293864	Fig. 5F,G The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion
PMID:35293864	Note: not sure about the term name and the child. Fig. 3 supp 1 A, C
PMID:35293864	Fig. 5 supp 3E
PMID:35293864	Fig. 5F,G The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion
PMID:35293864	Fig. 5E Ase1 is required for normal rescue distribution
PMID:35293864	Fig. 4 - figure supplement 2 We found that in both les1Δ and nem1Δ cells microtubule growth speed inside the nuclear bridge was faster than in wild-type cells
PMID:35293864	Fig. 4 - figure supplement 2 We found that in both les1Δ and nem1Δ cells microtubule growth speed inside the nuclear bridge was faster than in wild-type cells
PMID:35293864	mal3Δ cells exhibited lower microtubule growth speed throughout anaphase B Fig. 2G
PMID:35293864	Fig. 2 - Figure supplement 2E
PMID:35300005	100 ug/ml canavanine
PMID:35314193	Figure 10
PMID:35314193	Figure 12
PMID:35314193	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 4
PMID:35314193	Figure 10
PMID:35314193	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 1
PMID:35314193	Figures 1 and 3
PMID:35314193	Figures 1 and 3
PMID:35314193	Figure 12
PMID:35314193	Figure 12
PMID:35314193	Figure 8
PMID:35314193	Figure 12
PMID:35314193	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 3
PMID:35314193	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 4
PMID:35314193	Figure 12
PMID:35314193	Figure 8
PMID:35314193	Figure 8
PMID:35314193	Figure 8
PMID:35314193	Figure 8
PMID:35320724	Figure 4
PMID:35320724	Figure S4
PMID:35320724	Figure 5
PMID:35320724	Figure 4
PMID:35320724	Figure 5
PMID:35320724	Figure 4
PMID:35320724	Figure 4
PMID:35320724	Figure 4
PMID:35320724	Figure 4
PMID:35320724	Figure 4
PMID:35320724	Figure 1B, 2D, 5B, 6C, 7B, 7C
PMID:35320724	Figure S5
PMID:35320724	Figure S7
PMID:35320724	Figure 6
PMID:35320724	Figure 5
PMID:35320724	Consistent with the low levels of separase, we found that sister chromatid separation was delayed in cdc48- 353 mutant cells relative to the decline in CDK1 activity at mitotic exit (Figure 1C).
PMID:35320724	Figure 4
PMID:35320724	Figure 1B, 5B
PMID:35320724	Figure 1B, 5B
PMID:35320724	figure 3a However, the cellular degradation kinetics of securin-GFP were indistinguishable in cdc48+ and cdc48-353 mutant cells after normalizing for the reduced level (Figure 3A), suggesting that se- curin degradation was unaffected in the cdc48-353 mutant.
PMID:35320724	Figure 3a Similar results were obtained for Cdc13-GFP (Figure S1). Hence securin and Cdc13 are still efficiently targeted for proteasomal degradation in the cdc48-353 mutant.
PMID:35320724	Figure S6G
PMID:35320724	Figure S5
PMID:35320724	Figure 6
PMID:35320724	Figure 6
PMID:35320724	Figure 5
PMID:35320724	Figure S6B
PMID:35320724	Figure 6
PMID:35320724	Figure 3, S1
PMID:35320724	Figure 6
PMID:35320724	Figure 6
PMID:35320724	Figure 6
PMID:35320724	Figure 6
PMID:35320724	Figure 7
PMID:35320724	Figure 7
PMID:35320724	Figure 4
PMID:35320724	Figure 4
PMID:35320724	Figure 4
PMID:35320724	Figure 5
PMID:35320724	Figure 7
PMID:35320724	Figure 7
PMID:35320724	Figure 7
PMID:35320724	Figure 7
PMID:35320724	Figure S6D
PMID:35320724	Figure 3, S1
PMID:35320724	Figure 5
PMID:35320724	Figure 2C
PMID:35320724	Figure 2C
PMID:35320724	Figure S1
PMID:35320724	Figure 2A even if securin levels were elevated to only about eight times the wild-type level (Kamenz et al., 2015) (Figure 2A
PMID:35320724	Figure 2C
PMID:35320724	Figure 4
PMID:35325114	TERM REQUESTED growth auxotrophic for valine
PMID:35325114	TERM REQUESTED growth auxotrophic for isoleucine
PMID:35333350	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination
PMID:35333350	These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure.
PMID:35333350	(Figure S5B)
PMID:35333350	(Figure S5B)
PMID:35333350	during horsetail/ prophase
PMID:35333350	These results sugest that in the rec8-F204S mutant, as in rec8Δ, the Rec8- dependent meiosis-specific short chromatin loop structures are lost, resulting in a concomitant loss of the structural property of the chromosome required for proper alignment.
PMID:35333350	rec8-S552P and rec8Δ, which showed the cohesion defect, were used as a control strain (see Supplementary Figure S5C, S5D, and S5E for details of the rec8-S552P mutant)
PMID:35333350	These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure.
PMID:35333350	(Figures 2A and B) Hi-C analysis for rec10Δ and rec12Δ cells showed X-shaped contacts similar to wild-type cells AND (Figure 3A).... punctate Hi-C interactions observed in the wild-type were mostly lost in rec8Δ
PMID:35333350	(Figures 2A and B) Hi-C analysis for rec10Δ and rec12Δ cells showed X-shaped contacts similar to wild-type cells AND (Figure 3A).... punctate Hi-C interactions observed in the wild-type were mostly lost in rec8Δ
PMID:35333350	Supplementary Figure S4B) wpl1Δ rarely showed torsional turning (Supplementary Figure S4C, Supplemen- tal Movies 1, and 2) during horsetail movements that is important for the alignment of homologs
PMID:35333350	figure 4c,e also supported by (Figure 4A), Fluorescence images of Rec8- GFP showed that axial structures in meiotic chromosomes were more prominent in wpl1Δ than in the wild-type
PMID:35333350	Figure S4B
PMID:35333350	DECREASED NUMBER (figure 6 and figure 5e, S6BC) defective loop formation also supported by increased distance between the telomere-ade8 distance was longer in the rec8-F204S mutant than in the wild-type, suggesting that the chromatin of the rec8-F204S mutant was flexible and was abnormally stretched by the traction of the horsetail movement
PMID:35333350	(Figure 5D, Supplemental Movies 1, and 3) In the rec8-F204S mutant, only the leading edge of the nucleus followed the horsetail movement, while the bulk of chromosomes were left behind, similar to rec8Δ
PMID:35333350	(Figure 7)
PMID:35333350	(Figure 6B). The alignment index of chromosome 1 at meiotic prophase (2.5 h) decreased in rec8-F204S (1.6) compared with the wild-type (rec8-wt, 2.6)
PMID:35333350	(Figure 5C) The rec8-F204S mutant maintained sister chromatid cohesion as assessed at the cut3 gene locus
PMID:35333350	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination (Rec10-mCherry forms aberrant dotty or filamentous aggregates within the nucleus, similar to rec8∆.)
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35416247	in presence of tschimganine
PMID:35512546	RRM3
PMID:35536002	Fig. 7
PMID:35536002	Fig. 12
PMID:35536002	Fig. 12
PMID:35536002	Fig. 8
PMID:35536002	Fig. 8
PMID:35536002	Fig. 12
PMID:35536002	Fig. 8 & 12
PMID:35536002	Fig. 12 (Note how the levels are the same as when the pyrophosphatase is inactivated in the full-length protein)
PMID:35536002	Fig. 7
PMID:35536002	Fig. 8 and text
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 8
PMID:35536002	Fig. 8
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35536002	Fig. 7
PMID:35609605	and is already defective in actomyosin  17 compaction at the permissive temperature of 24 C (Figure S1C, video S2) and (Figures 3A, 3B, and S3A))
PMID:35609605	COMPACTION Figures 3A, 3B, and S3A (inhibiting exocytosis rescues defect of compaction)
PMID:35609605	"Figures 3A, 3B, and S3A (no rescue) dan says ""FigS3A (bottom panel) shows that ring compaction completely failed in scs2Δscs22Δmyo2-E1(aaG345R) at 36 degree. In fact, we did not directly show that these cells failed ring contraction similarly as myo2-E1(aaG345R) at high temperature (which is well known) in the paper, as we mainly focused on ring compaction process. But we have implied that in the context."""
PMID:35609605	COMPACTION I asked is this the correct genotype? Dan answered Our quantification in FigS3C (bottom panel) shows that ring compaction is slightly faster in scs2Δscs22Δmyo2-E1(aaG345R) than wt at 24 degree, although such a difference is not significant quantitatively. Qualitatively, compaction (in terms of mobility) of individual nodes was indeed faster. So, I felt reluctant to use either “normal” or “abnormal” to describe that.
PMID:35609605	figure 4D
PMID:35609605	figure 4D
PMID:35609605	(partial rescue) Incomplete ring compaction was still observed in myo2- E1pil1D, although such fraction was reduced as compared with myo2-E1 (Figure 3B I don't see the images - this is from the bar chart))
PMID:35609605	COMPACTION Figures 3A, 3B, and S3A
PMID:35609605	Figure 3 COMPACTION
PMID:35622906	OLD SPB
PMID:35639710	Figure 2A
PMID:35639710	Second, Any1R175C does not show an increase but rather a strong decrease in its ubiquiti- nation level.
PMID:35639710	Figure1
PMID:35639710	Increased protein ubiquitination.
PMID:35639710	Fig 1
PMID:35639710	Figure3 confirms dominance of can1-1
PMID:35639710	Fig 1
PMID:35639710	Figure 1 (same as WT)
PMID:35673994	Fig. 5F
PMID:35673994	Fig. 5
PMID:35673994	Fig. 6
PMID:35673994	Fig. 6
PMID:35673994	Fig. 5
PMID:35673994	Fig. 5
PMID:35673994	Fig. 5
PMID:35673994	Fig. 5
PMID:35673994	Fig. 5
PMID:35673994	Fig. 6
PMID:35673994	Fig. 2B
PMID:35673994	Fig. 5
PMID:35673994	Fig. 4E
PMID:35673994	Fig. 2B
PMID:35673994	Fig. 2B
PMID:35673994	Fig. 2B
PMID:35673994	Fig. 2A
PMID:35673994	Fig. 2B
PMID:35673994	chimera expressed from the ura4 locus (@ura4) - kept because not assayed from fus1 locus
PMID:35673994	Fig. 2H
PMID:35673994	Fig. 2C
PMID:35673994	Fig. 6
PMID:35673994	Fig. 3
PMID:35673994	Fig. 3
PMID:35673994	Fig. 2D
PMID:35673994	Fig. 6
PMID:35673994	Fig. 6
PMID:35673994	Fig. 6
PMID:35673994	Fig. 4E
PMID:35673994	Fig. 4E
PMID:35673994	Fig. 5C
PMID:35673994	Fig. 5
PMID:35673994	Fig. 4E
PMID:35673994	Fig. 5
PMID:35673994	Fig. 5
PMID:35673994	Fig. 5
PMID:35781263	"The Δght5 strain is always in 27 a ""low glucose state"" even when cultured in high glucose medium, and this may be the reason why the 28 lifespan extension phenotype appears."
PMID:35781263	decreased
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Figure 7
PMID:35924983	Figure 7
PMID:35924983	Figure 7
PMID:35924983	Figure 7
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Fig. 6
PMID:35924983	Fig. 6
PMID:35924983	Figure 3
PMID:35924983	through nuclear exclusion
PMID:35924983	through nuclear exclusion
PMID:35924983	through degradation by ubiquitination
PMID:35924983	through degradation by ubiquitination
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 6
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Figure 3
PMID:35924983	Figure 3
PMID:35924983	Figure 6
PMID:35924983	Figure 6
PMID:35924983	Figure 6
PMID:35924983	Figure 6
PMID:35924983	Figure 6
PMID:35924983	Figure 6
PMID:35924983	Figure 7
PMID:35924983	Figure 7
PMID:35924983	Figure 7
PMID:35924983	Figure 7
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4, Table 1
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35924983	Supplemental Figure 4
PMID:35940128	term requested Queuosine nucleosidase activity
PMID:35940128	Queuosine absent from tRNA when cells are supplied with queuosine nucleoside, but not when supplied with queuine nucleobase
PMID:35970865	(during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcrip- tion at the central core region.
PMID:35970865	(during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcrip- tion at the central core region.
PMID:35970865	during M-phase Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)
PMID:35970865	(during M-phase) Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)
PMID:35970865	Figure 2a (during M-phase)
PMID:35970865	Fig. 2a The resultant mis6-302 cut9-665 double mutant exhibited severe growth defects, even at the semi-restrictive temperature (Fig. 2a). This suggests that the mitotic function of Mis6 is crucial for prolonged metaphase.
PMID:35970865	Fig. 2a The resultant mis6-302 cut9-665 double mutant exhibited severe growth defects, even at the semi-restrictive temperature (Fig. 2a). This suggests that the mitotic function of Mis6 is crucial for prolonged metaphase.
PMID:35970865	Note that an increase of transcript levels from centromeres has not been demonstrated in the paper. What has been exactly demonstrated is an increased association of RNA polII to the cnt region of centromeres.
PMID:35970865	Note that an increase of transcript levels from centromeres has not been demonstrated in the paper. What has been exactly demonstrated is an increased association of RNA polII to the cnt region of centromeres.
PMID:35970865	normal CENP-A maintenance
PMID:35970865	normal CENP-A maintenance
PMID:35970865	normal CENP-A maintenance
PMID:35970865	Fig. 2a
PMID:35970865	normal CENP-A maintenance
PMID:35970865	figure4
PMID:35970865	decreased CENP-A maintenance
PMID:35970865	When we followed the temporal kinetics of GFP- Cnp1 intensity during metaphase, the reduction of GFP-Cnp1 intensity seen in mis6-302 and mis15-68 cells was rescued by the additional knockout of Fft3 (mis6-302 fft3Δ, Supplementary Fig. 11a–c; mis15-68 fft3Δ, Supplementary Fig. 11d–f), confirming that Fft3 removes Cnp1 upon transcription at centromeres.
PMID:35970865	Defective in CENP-A maintenance. Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)In the mis15-68 mutants, signal intensities of Cnp1 at centromeres during mitotic arrest were decreased like in the mis6-302 mutant, whereas not in the mis12-537 and nuf2-2 mutants (Fig. 2h–j and Supplementary Figs. 5b–d and 7)
PMID:35970865	Fig. 2a
PMID:35970865	"Fig. 2c, d).""decreased CENP-A maintenance during M-phase"". defective in CENP-A maintenance during M phase, as well as defective in CENP-A loading during interphase The GFP-Cnp1 intensity at centromeres decayed more rapidly in mis6-302 cells than in WT cells (Fig. 2f, g and Supplementary Figs. 4 and 5a). Taken together, these results suggest that Mis6, but not Scm3, is responsible for the maintenance of Cnp1 at centromeres during metaphase."
PMID:35970865	Fig. 2a
PMID:35970865	figure4
PMID:35970865	Fig. 2a
PMID:36006032	figure 1 D
PMID:36006032	Overexpression of Par2 suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Par2 suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Par1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Par1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of all Ppa1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Overexpression of all Ppa1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest- and-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
PMID:36006032	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest- and-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
PMID:36006032	Our in vitro dephosphor- ylation assay results demonstrated that individually overexpressing PP2A subunits indeed boosted the over- all phosphatase activity compared to expressing endog- enous subunits alone (Figure 3B).
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36006032	figure 1 D
PMID:36090151	1.6 mM
PMID:36090151	1.6 mM
PMID:36108046	Surprisingly, Slp1Cdc20 was slightly, but appreciably and reproducibly, less abundant (ranging from roughly 20% to 50% at different time points) in dnt1Δ cells than in wild-type cells (Fig 3B), suggesting Dnt1 may indeed positively regulate the levels of intact Slp1Cdc20. In addition, this regulation of Slp1Cdc20 stability by Dnt1 is Dma1-independent, as the dnt1Δ dma1Δ double mutant has a similar level and degradation profile of Slp1Cdc20 as dnt1Δ single mutant (S5 Fig).
PMID:36108046	I changed to decreased. becasue the phenotype is compared to WT,
PMID:36108046	I changed to decreased. becasue the phenotype is compared to WT,
PMID:36108046	inefficient anaphase initiation upon SAC inactivation/ persistent MCC-APC/C binding upon SAC activation The SAC was first robustly activated by the nda3-KM311 mutant then inactivated by shifting mitotically arrested cells back to permissive temperature(30˚C)/ We found that dnt1Δ cells retained high amounts of SPB-localized Cdc13-GFP and nuclear Cut2-GFP for much pro- longed period compared to wild-type cells, almost to the same degree as previously identified SAC-inactivation defective mutant dis2Δ
PMID:36108046	(****NEW TERM REQUESTED->ACTIVATION) but dnt1Δ cells stayed for extended length of time at ana- phase B (Fig 1D–1F)
PMID:36108046	Consistent with this assumption, we found that dnt1Δ cells lost minichromosomes (Ch16, ade6-M216) at an elevated rate that is almost 100 times higher than that of the wild-type (Fig 1B), and displayed increased frequency of lagging chromosomes and chromosome mis-segre- gation at mitotic anaphase (Fig 1C).
PMID:36108046	but dnt1Δ cells stayed for extended length of time at ana- phase B (Fig 1D–1F)
PMID:36108046	Consequently, sensitivity of dnt1Δ cells to TBZ was largely but not completely suppressed by excessive Slp1Cdc20 expression achieved by three copies of slp1+ (Fig 3E).
PMID:36112198	figure 2
PMID:36112198	figure 3
PMID:36112198	Fig. S2
PMID:36112198	Fig. S2
PMID:36112198	Fig. S2
PMID:36112198	Fig. S2
PMID:36112198	Fig. S2
PMID:36112198	Fig S2
PMID:36112198	Fig. S2
PMID:36112198	figure 2
PMID:36112198	figure 2
PMID:36112198	fig1 (double mutant with cyr1 is more sensitive)
PMID:36112198	figure 2
PMID:36112198	Fig. S2
PMID:36112198	figure S2
PMID:36112198	figure 2
PMID:36112198	figure 2
PMID:36112198	figure 2
PMID:36112198	observed Pka1-GFP
PMID:36112198	fig5
PMID:36112198	observed Pka1-GFP
PMID:36112198	observed Pka1-GFP
PMID:36112198	observed Pka1-GFP
PMID:36112198	low glucose MM
PMID:36112198	glucose MM
PMID:36112198	glucose MM
PMID:36112198	rst2∆ rescues pka1∆ plb1∆ on KCl
PMID:36112198	rst2∆ partially rescues pka1∆ plb1∆ on KCl
PMID:36112198	Fig 1b
PMID:36112198	Fig.1 Overexpression of Pka1 restores the KCl-sensitive pheno- type of the plb1∆ strain.
PMID:36112198	Fig.1 Overexpression of Pka1 restores the KCl-sensitive pheno- type of the plb1∆ strain.
PMID:36112198	cgs1∆ rescues cyr1∆ plb1∆ on sorbitol
PMID:36112198	cgs1∆ partially rescues cyr1∆ plb1∆ on KCl
PMID:36112198	rst2∆ rescues pka1∆ on KCl
PMID:36112198	rst2∆ rescues pka1∆ on KCl
PMID:36112198	Fig 4 rst2∆ partially rescues plb1∆ on KCl
PMID:36112198	Fig 4 rst2∆ partially rescues plb1∆ on KCl
PMID:36112198	cgs1∆ partially rescues plb1∆ on KCl
PMID:36112198	cgs1∆ partially rescues plb1∆ on KCl
PMID:36112198	figure 2b
PMID:36112198	figure 2b
PMID:36112198	fig4
PMID:36138017	though HU treatment caused equally efficient arrest at S phase in both wild-type and dma1Δ cells (Supplementary Fig. 4)
PMID:36138017	(Fig. 4)
PMID:36138017	(Fig. 4)
PMID:36138017	(Fig. 2d)
PMID:36138017	Strikingly, Tip1 ubiquitination was abolished in both dma1 mutants (Fig. 2d), demonstrating that both functional FHA and RF domains in Dma1 are required for Tip1 ubiquitination in vivo.
PMID:36138017	More interestingly, in the presence of HU, the binding between Tea4 and Tip1 was elevated in dma1Δ cells and in wild-type cells treated with deubiquitinating enzyme USP2 to remove Tip1 ubi- quitination (Fig. 4f), this is consistent with increased polar growth in dma1Δ cells (Fig. 4b).
PMID:36138017	Dma1 ubiquitinates Tip1
PMID:36138017	figure 1D.
PMID:36138017	We found that Tip1 was efficiently ubiquitinated in the absence of the calcineurin catalytic subunit Ppb1, with a similar degree of modification to that of wild-type cells (Fig. 6a).
PMID:36174923	Microscopic examination revealed that Δsty1Δppr10 cells were highly elongated compared to WT, Δppr10, and Δsty1 cells (Fig. 5B), suggesting that progression from G2 into mitosis was impaired in Δsty1Δppr10 cells.
PMID:36174923	Fig. 5.
PMID:36174923	Fig. 7b partial rescue - still loses viabiltiy at 48 hours
PMID:36174923	Fig. 5.
PMID:36174923	fig 4
PMID:36174923	Fig. S5.
PMID:36174923	fig S2
PMID:36174923	fig S2
PMID:36174923	fig S2
PMID:36174923	fig S2
PMID:36174923	Fig. 7b partial rescue - still loses viabiltiy at 48 hours
PMID:36174923	figure1
PMID:36174923	Fig 6
PMID:36174923	Fig. 5.
PMID:36174923	Fig. S5.
PMID:36174923	Fig. 5.
PMID:36174923	Fig. S5.
PMID:36174923	fig S2
PMID:36174923	Fig. 5.
PMID:36174923	Fig. 5.
PMID:36200823	However, deletion strains of two genes encod- ing SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supple- mentary Figure S2A).
PMID:36200823	In addition, a low concentra- tion of TBZ enhanced the chromosome segregation de- fects of the temperature-sensitive sfh1-13 mutant (Supple- mentary Figure S1A).
PMID:36200823	In addition, a low concentra- tion of TBZ enhanced the chromosome segregation de- fects of the temperature-sensitive sfh1-13 mutant (Supple- mentary Figure S1A).
PMID:36200823	sfh1-13 mutant strain exhibited a slow growth phenotype at 32◦C upon nmt41-cnp1 expression (sfh1-13 at 32◦C in the lower panel of Supplementary Figure S1B
PMID:36200823	sfh1-13 mutant strain exhibited a slow growth phenotype at 32◦C upon nmt41-cnp1 expression (sfh1-13 at 32◦C in the lower panel of Supplementary Figure S1B
PMID:36200823	However, deletion strains of two genes encod- ing SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supple- mentary Figure S2A).
PMID:36200823	at pericentromeric heterochromatin When CENP-ACnp1 was expressed at wild- type levels, specific accumulation at pericentromeric heterochromatin domains of all centromeres (Figure 1A), but not at non-centromeric locations
PMID:36200823	Importantly, no significant dif- ference in the level of Cnp1 protein or mRNA was seen in sfh1-13 cells (Figure 1E).
PMID:36200823	at pericentromeric heterochromatin When CENP-ACnp1 was expressed at wild- type levels, specific accumulation at pericentromeric heterochromatin domains of all centromeres (Figure 1A), but not at non-centromeric locations
PMID:36200823	Furthermore, we observed ectopic CENP-ACnp1 deposition at pericentromeric heterochromatin domains in snf21-36 but not in rsc1 and rsc4 deletion mutants (Figure 1F)
PMID:36200823	However, the sfh1-13 mutation had only a mild influence on H3K9me levels (Figure 1C), as we re- ported previously (12).
PMID:36200823	In sfh1-13 mutant cells, a small but signifi- cant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C);
PMID:36200823	In sfh1-13 mutant cells, a small but signifi- cant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C);
PMID:36200823	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	while loss of Clr3 eliminated CENP-ACnp1 accumulation at the pericentromere in a sfh1- 13 mutant background, indicating that Clr3 is required for ectopic deposition of CENP-ACnp1 (Figure 3D).
PMID:36200823	(Figure 3E). As reported previously, deletion of clr3 increased the loading of Snf21 at pericentromeric repeats; however, we did not observe greater Snf21 occupancy in our sfh1-13 clr3Δ double mutant relative to a sfh1-13 sin- gle mutant, suggesting that sfh1-13 prevents the acetylation- dependent recruitment of Snf21 at pericentromeres, and that the elimination of misloaded CENP-ACnp1 in sfh1-13Δ clr3Δ cells is not due to the increase in Snf21 level.
PMID:36200823	Importantly, MNase protection at sites i, iii, and v, which are located between CENP-ACnp1 and heterochro- matin domains, was elevated in sfh1-13 cells (site i: 1.5-fold, P-value = 0.027; site iii: 2.2-fold, P-value = 0.0001; site v: 1.2-fold, P-value = 0.02; left panel of Figure 5B), indicat- ing that Sfh1/RSC contributes to chromatin decompaction at the boundary.
PMID:36200871	Supplemental Figure S5A). We concluded that the calcium-permeable Pkd2 primarily localizes to the plasma membrane.
PMID:36200871	Figure 2, E and F). We concluded that Pkd2 is calcium-permeable under the mechanical stimulus of membrane stretching.
PMID:36200871	At 36°C, the average calcium level of pkd2-B42 cells was 34% lower than that of wild type cells (Figure 3, C and D).
PMID:36200871	********** move to new decreased immediate intracellular calcium spike following osmotic shock :: The peak amplitude of the cal- cium spikes in pkd2-B42 cells was similarly reduced by 62% (Figure 4D).
PMID:36200871	********* move to new decreased immediate intracellular calcium spike following osmotic shock
PMID:36259651	When cells were grown in media containing nitro- gen sources, some of the nc1669􏰄 cells underwent mating (followed by meiosis), whereas WT cells never initiated mat- ing (Figure 3B, C)
PMID:36259651	When cells were grown in media containing nitro- gen sources, some of the nc1669􏰄 cells underwent mating (followed by meiosis), whereas WT cells never initiated mat- ing (Figure 3B, C)
PMID:36302945	data not shown, related data in Figure 2A
PMID:36302945	Figure 3, this phenotype was observed for cat1_delta leu1-32 double mutant.
PMID:36302945	Figure 4 In 3.0% NH4Cl medium, the growth speed of both strains became slower after exposure to the high NH4Cl condition for 14 h.
PMID:36302945	Figure 1. Cells with leucine auxotrophy (leu1-32 strain) show weak growth on the synthetic medium EMM supplemented with 0.2 mM leucine (Fig. 1B). EMM contains 0.5% NH4Cl
PMID:36361590	Gpl1-Gih35-Wdr83 complex
PMID:36361590	Gpl1-Gih35-Wdr83 complex
PMID:36361590	Gpl1-Gih35-Wdr83 complex
PMID:36361590	figure3
PMID:36361590	figure3
PMID:36361590	figure3
PMID:36361590	figure3
PMID:36361590	We detected wdr83 (Figure S1) and performed the Western blot and RT-qPCR analyses. We detected no significant changes in the mRNA levels of gpl1, gih35 or wdr83 in the analyzed mu- no significant changes in the mRNA levels of gpl1, gih35 or wdr83 in the analyzed mutants tants (Figure 5a).
PMID:36361590	Figure 2& 4 These results indicated that the Gih35 helicase is part of the Gih35 and Wdr83 on one side, and as an anchoring protein that allows the binding of the Gpl1-Gih35-Wdr83 complex to the spliceosome on the other side. Gpl1- Gih35-Wdr83 complex, but to associate with the spliceosome, it requires the interaction with Gpl1. Altogether, these findings confirmed the above results of the Y2H assay and provided further support for the hypothesis that Gpl1 functions as a bridging protein for
PMID:36361590	Figure 2
PMID:36408846	Upon inhibition of Cdk1-as, Clr4S458 phosphorylation rapidly decreased and was undetectable 3 h postinhibition, whereas Clr4 phosphorylation levels remained unaffected in cdk1+ cells (Figs 6D and EV5D).
PMID:36408846	Furthermore, fewer clr4F449Y/clr4F449Y cells displayed lagging DNA upon expression of Swi6Chp1-like-CD (Fig 4C and D).
PMID:36408846	This revealed reduced H3K9me2, but increased H3K9me3 levels upon 1-NM-PP1 addition in cdk1-as cells specifi- cally (Fig 6F),
PMID:36408846	clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	figure 3F
PMID:36408846	spores formed colonies again (Fig 4G).
PMID:36408846	Indeed, CDK1/Cyclin B phosphorylated recombinant Clr4 specifically at S458 (Fig 6E).
PMID:36408846	(Check tomorrow should this be tri methylation)
PMID:36408846	clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	(Fig 3C and D). Indeed, the distribution of the GFP dots revealed aberrant segregation of sister chromatids in MI of clr4F449Y/clr4F449Y cells, with a high frequency of equational segregation that normally occurs during MII (Fig 3D
PMID:36408846	(Fig 3C and D). Indeed, the distribution of the GFP dots revealed aberrant segregation of sister chromatids in MI of clr4F449Y/clr4F449Y cells, with a high frequency of equational segregation that normally occurs during MII (Fig 3D
PMID:36408846	figure 4a
PMID:36408846	Consistent with earlier findings, we frequently observed spores with two GFP dots in a sin- gle nucleus of a tetrad derived from clr4D/clr4D cells (Fig 3E, green fraction). Such a pattern (i.e., normal segregation during MI but not MII) occurred in < 1% of clr4F449Y/clr4F449Y cells that we have ana- lyzed (Fig 3E)
PMID:36408846	figure 4a
PMID:36408846	Figure 4 A (This obser- vation indicates that highest binding affinity of Swi6 towards H3 is necessary for proper subnuclear localization in meiocytes, for which H3K9 needs to be tri-methylated.
PMID:36435910	Dis1 uses its TOG domains to induce microtubule catastrophe, in which polymerisation turns into depolymerisation
PMID:36435910	Figure 2a
PMID:36435910	Figure 2a
PMID:36435910	Figure 2a
PMID:36435910	Evidence: in vitro biochemical assays using purified tubulin and recombinant Dis1 protein / New GO term requested: microtubule destabilization activity
PMID:36435910	Figure 2a
PMID:36481249	figure 1a
PMID:36481249	cells were unable to grow on the plates containing canavanine (Fig. 4C). Interestingly, wat1Δ, wat1-17, and tor2-287 mutant cells exhibited resistance to canavanine (Fig. 4C) suggesting that disruption of wat1 leads to inactivation of the TORC1 pathway resulting in the defect in amino acid uptake
PMID:36481249	The phosphorylation of Psk1 and Rps602 was completely abolished in wat1Δ, wat1-17, and tor2-287 mutants after shifting the cells at non-permissive temperature (Fig. 4A, upper and middle panel).
PMID:36481249	The tor2-287 mutant cells also showed a similar phenotype after shifting at 36 ◦C (Fig. 3C, upper panel), indicating the G1 arrest.
PMID:36481249	having 1C and 2C DNA peak (Fig. 3C, upper panel) with a majority of cells having 1C DNA peak indicating a G1 arrest while only 2C DNA peak was observed in wild type cells grown under similar conditions
PMID:36481249	Interestingly, the average cell size of tor-287 mutant cells also decreases from 18.2 μm at 25 ◦C to 7.0 μm at 36 ◦C (Fig. 3A and 3B
PMID:36481249	In contrast, under the same condition, the wat1Δ and wat1-17 mutant cells became shorter in size with a round morphology having an average cell length of 7.7 and 8.3 μm, respectively (Fig. 3A and 3B)
PMID:36481249	wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B).
PMID:36481249	wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B).
PMID:36481249	Real-time quantitative PCR analysis revealed the up-regulation of transcripts of per1 and isp5 genes and down regulation of cat1 gene in wat1Δ, wat1-17, and tor2-287 mutant background at the non-permissive temperature (Fig. 4B),
PMID:36481249	The phosphorylation of Psk1 and Rps602 was completely abolished in wat1Δ, wat1-17, and tor2-287 mutants after shifting the cells at non-permissive temperature (Fig. 4A, upper and middle panel).
PMID:36537249	abolished Mhf1 localization
PMID:36537249	Intriguingly, similar to the percentage of mitotic WT cells, the percentage of mitotic mhf2Δ cells increased over time upon cold treatment, but to a lesser degree (Fig. 1A,B).
PMID:36537249	As shown in Fig. 1A,B, the percentage of mitotic WT cells displaying Plo1–GFP signals increased over time upon incubation at 16°C and, 8 h after cold treatment, ∼90% of WT cells were arrested at preanaphase, presumably due to the activation of the SAC. As Bub1 is a core component of the SAC (Fischer et al., 2021), the absence of Bub1 was expected to abolish the SAC. Consistently, the percentage of mitotic bub1Δ cells remained low (<10%) throughout the period of cold treatment (Fig. 1A,B).
PMID:36537249	binds to Mhf1
PMID:36537249	binds to Mhf2
PMID:36537249	mitotic prophase
PMID:36617881	These results suggest that Epe1 promotes assembly of the RNAi machinery at constitutive heterochromatin by expressing dg/dh ncRNAs.
PMID:36626373	Thus we found that wildtype Cat1-GFP cells growing in nitrogen-starvation conditions is localised to the plasma membrane, particularly at the growing cell ends, as previously reported [12,26].
PMID:36633091	Fig. 1A, 1B, S1A
PMID:36633091	Fig. 1A, 1B, S1A
PMID:36633091	Fig. 2C
PMID:36633091	Fig. 5C
PMID:36633091	Fig. 1C, Fig. 1D and Fig. 1E
PMID:36633091	Fig. 1A, 1B, S1A
PMID:36633091	Fig. 5C
PMID:36633091	Fig. 5C
PMID:36633091	Supplementary Fig. S1D and S1E
PMID:36633091	Fig. 3B
PMID:36633091	Fig. 2C
PMID:36633091	Fig. S1D and S1E
PMID:36633091	Fig. 3B
PMID:36633091	Fig. 2A and 2B
PMID:36633091	Fig. 5C
PMID:36633091	Fig. 2A and 2C
PMID:36633091	Fig. 1C, ID and 1E
PMID:36633091	Fig. 2A and 2C
PMID:36633091	Fig. 3B
PMID:36633091	Fig. 1C, 1D and 1E
PMID:36633091	Fig. 2D
PMID:36650056	change to: twin horsetail nucleus
PMID:36650056	Change to: Nuclear congression without nuclear fusion
PMID:36650056	Lower levels in the akr1 mutant
PMID:36650056	Lower levels in the akr1 mutant
PMID:36650056	palmitoylation of tht1D is reduced by ark1D
PMID:36650056	Was annotated as normal meiosis
PMID:36650056	akr1Δ affecting tht1
PMID:36650056	Change to: Nuclear congression without nuclear fusion
PMID:36650056	change to: twin horsetail nucleus
PMID:36650056	change to: twin horsetail nucleus
PMID:36650056	Change to: Nuclear congression without nuclear fusion
PMID:36695178	LC-MS
PMID:36695178	Very high levels of diploidization in minimal medium
PMID:36695178	Very prominent in minimal medium due to the lack of the Kennedy pathway precursors
PMID:36695178	Very prominent in minimal medium due to the lack of the Kennedy pathway precursors
PMID:36695178	Sub-lethal phenotype, with only 10% of expected double mutants recovered.
PMID:36695178	LC-MS
PMID:36695178	LC-MS
PMID:36695178	LC-MS
PMID:36695178	LC-MS
PMID:36695178	LC-MS
PMID:36695178	Severe buckling of the mitotic spindle was observed in 31% of cells, resulting in bowshaped nuclear intermediates during anaphase (Fig. 4D). It took longer for these nuclei to divide, and they often formed daughter nuclei of unequal sizes (Fig. S4E)
PMID:36695178	Severe buckling of the mitotic spindle was observed in 31% of cells, resulting in bowshaped nuclear intermediates during anaphase (Fig. 4D). It took longer for these nuclei to divide, and they often formed daughter nuclei of unequal sizes (Fig. S4E)
PMID:36695178	Very prominent in minimal medium due to the lack of the Kennedy pathway precursors
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36705602	Figure 3 summarizes data
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 3
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5B
PMID:36749320	Figure 10 - Manu: transfer to FYPO:0008075
PMID:36749320	Figure 10 - Manu: Transfer to FYPO:0008075
PMID:36749320	Figure 5C
PMID:36749320	Figure 5C
PMID:36749320	Figure 10
PMID:36749320	Figure 10
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 5 S2
PMID:36749320	Fig. 3E
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 10
PMID:36749320	Figure 10
PMID:36749320	Figure 4
PMID:36749320	Figure 5
PMID:36749320	Figure 5C
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 5A
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36749320	Figure 3
PMID:36779416	phosphate replete. Zfs1 is involved in the repression of the ecl3+ transcript level in a nutrient-rich environment but is not required for the induction by phosphate starvation. Next,
PMID:36779416	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	Phosphate starvation did not induce ecl3+ expression in Δckb1 cells, indicating that the induction was dependent on Ckb1 (Fig. 2B)
PMID:36779416	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	figure 1A,B
PMID:36793083	Fig. 3
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 4D
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36793083	Fig. 3
PMID:36799444	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	We performed an IP–WB experiment on the bqt4 background (‘bqt4’ in Fig.2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36799444	Fig.3D
PMID:36799444	We performed an IP–WB experiment on the bqt4 background (‘bqt4’ in Fig.2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36799444	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	We performed an IP–WB experiment on the bqt4 background (‘bqt4’ in Fig.2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36820394	Fig.1
PMID:36820394	Fig.1
PMID:36820394	Fig.1
PMID:36820394	Fig.1
PMID:36820394	Fig.1
PMID:36820394	Fig.1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Fig.1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36820394	Fig.1
PMID:36820394	Fig.1
PMID:36820394	Table 1
PMID:36820394	Table 1
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. 6B
PMID:36882296	Fig. S4
PMID:36882296	Fig. S4
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S3
PMID:36882296	Fig. S5A
PMID:36882296	Fig. S5B
PMID:36882296	Fig. S6A
PMID:36882296	Fig. S6A
PMID:36882296	Fig. S6B
PMID:36882296	Fig. S6B
PMID:36882296	Fig. S7A
PMID:36882296	Fig. S7A
PMID:36882296	Fig. S7A
PMID:36882296	Fig. S7B
PMID:36882296	Fig. S7B
PMID:36882296	Fig. S7B
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. S8
PMID:36882296	Fig. 1A. Redundancy with rpb1-T4A
PMID:36882296	Fig. 3
PMID:36882296	Fig. 3
PMID:36882296	Fig. 4
PMID:36882296	Fig. 4
PMID:36882296	Fig. 4
PMID:36882296	Fig. 4
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 13
PMID:36882296	Fig. 13
PMID:36882296	Fig. 13
PMID:36882296	Fig. 13
PMID:36882296	Fig. 13
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6A
PMID:36882296	Fig. 6A
PMID:36882296	Fig. 6A, 10A
PMID:36882296	Fig. 6A
PMID:36882296	Fig. 6A
PMID:36882296	Fig. 6A
PMID:36882296	Fig. 6A
PMID:36882296	Fig. 5B
PMID:36882296	Fig. 5B
PMID:36882296	Fig. 5B
PMID:36882296	Fig. 5B
PMID:36882296	Fig. 5B
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 5A
PMID:36882296	Fig. 1B
PMID:36882296	Fig. 1B
PMID:36882296	Fig. 1B
PMID:36882296	Fig. 1A
PMID:36882296	Fig. 1B
PMID:36882296	Fig. 1B
PMID:36882296	Fig. 1B
PMID:36882296	Fig. 1A
PMID:36882296	Fig. 1A
PMID:36882296	Figs. 1B, 5B, 6B, 7B, 8B, 9B, 10B
PMID:36882296	Fig. 1A
PMID:36882296	Figs. 1A, 5A, 6A, 7A, 8A
PMID:36882296	Fig. 1A
PMID:36882296	Fig. 1A
PMID:36882296	Fig. S4
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 6B
PMID:36882296	Fig. 7B, 10B, 12B
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7A
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 8A
PMID:36882296	Fig. 8B
PMID:36882296	Fig. 8A
PMID:36882296	Fig. 8B
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9A
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 10A
PMID:36882296	Fig. 10A
PMID:36882296	Fig. 10A
PMID:36882296	Fig. 10A
PMID:36882296	Fig. 10B
PMID:36882296	Fig. 10B
PMID:36882296	Fig. 11A
PMID:36882296	Fig. 11B
PMID:36882296	Fig. 11B
PMID:36882296	Fig. 11B
PMID:36882296	Fig. 11B
PMID:36882296	Fig. 12A
PMID:36882296	Fig. 12B
PMID:36882296	Fig. 7B
PMID:36882296	Fig. 9B
PMID:36882296	Fig. 12A
PMID:36882296	Fig. 12B
PMID:36882296	Fig. 12A
PMID:37052630	Main text Table S1
PMID:37052630	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	Fig. 2b - control
PMID:37052630	Main text Table S1
PMID:37052630	Fig. S1
PMID:37052630	Fig. S1
PMID:37052630	Fig. S1
PMID:37052630	Main text Table S1
PMID:37052630	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	Main text Table S1
PMID:37052630	Main text Table S1
PMID:37076472	Figure 1.
PMID:37076472	Figure 1.
PMID:37076472	Figure 1.
PMID:37076472	Figure 1.
PMID:37076472	Figure 3.
PMID:37076472	Figure 1.
PMID:37076472	Figure 1.
PMID:37076472	Figure 3.
PMID:37076472	Figure 1.
PMID:37076472	Figure 3.
PMID:37076472	Figure 3.
PMID:37076472	Figure 3.
PMID:37076472	Figure 3.
PMID:37076472	Figure 1.
PMID:37076472	Figure 1.
PMID:37099380	Closer to tip
PMID:37099380	Closer to tip
PMID:37099380	Closer to ring
PMID:37120429	Sz. pombe cells expressing SpHsp90-EA had an osmolyte-remediated temperature sensitivity phenotype, which strongly suggested conservation of EA-specific phenotypes (Fig. 3b).
PMID:37120429	Sz. pombe cells expressing SpHsp90-EA had an osmolyte-remediated temperature sensitivity phenotype, which strongly suggested conservation of EA-specific phenotypes (Fig. 3b).
PMID:37120429	Using this system, we observed that SpHsp90-EA supported viability of Sz. pombe cells (Fig. 1b).
PMID:37120429	The suppressive effect of TA and EK on EA defects in non-essential functions were not specific to S. cerevisiae, as these mutations also rescued SpHsp90-EA mediated temperature sensitivity in Sz. pombe (Fig. 5d).
PMID:37120429	The suppressive effect of TA and EK on EA defects in non-essential functions were not specific to S. cerevisiae, as these mutations also rescued SpHsp90-EA mediated temperature sensitivity in Sz. pombe (Fig. 5d).
PMID:37128864	The phenotype can be seen at 32˚C. The phenotype can be seen at 32˚C. Furthermore, the log phase chromosomes more actively fluctuated in cdc2-L7 cells than in WT cells, and despite a repression in chromosome fluctuation, fluctuation was still elevated in the stationary phase, as demonstrated by an upward shift of the cdc2-L7 MSD plot of the ade6 locus and a complete lack of an overlap of their 95% confidence intervals with those of the WT plot (Fig. 5H).
PMID:37128864	The N/C ratio was also reduced but not significantly different from that of stationary phase cells (Fig. 1E; Fig. S1G), suggesting that the observed nuclear size differences from stationary phase originate from the cell size differences.
PMID:37128864	Localization depends on Cdc2 kinase activity but not on Clp1.
PMID:37128864	Cell length increases during log and stationary phases at 32 degree.
PMID:37128864	Loss of viability is evident only when cells are exposed to 32 degree before and upon entry into stationary phase.
PMID:37128864	The phenotype can be seen at 32 degree.
PMID:37156397	Figs. 2B, S1B
PMID:37156397	We first noticed that ∆coq11 and ∆coq12 strains did not grow well on minimal medium, as was observed for CoQ-deficient S. pombe (Fig. 2A, S1A)
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	low CoQ10 level
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	Interestingly, NAD+ reduction activity was clearly detected in purified Coq12-8xHis from S. pombe (Fig. 9A)
PMID:37156397	The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants
PMID:37156397	(Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains
PMID:37156397	Figs. 3, S1C. Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	********growth auxotrophic for para-hydroxy benzoic acid
PMID:37156397	(Fig. 2A) By contrast, the ∆coq12 strain showed almost no growth on PMLU medium containing cysteine.
PMID:37156397	LC-MS
PMID:37156397	Coq12-GFP fusion (Fig. 8A). The GFP fluorescence pattern was similar to that of Mitotracker Red, a mitochondria stain. Mitochondrial localization of Coq12 was therefore confirmed
PMID:37156397	low CoQ10 level
PMID:37156397	The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants
PMID:37156397	(Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains
PMID:37156397	Figs. 3, S1C. Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	(Figs. 2A, S1A) Like other mutants lacking CoQ, the ∆coq11 strain showed better growth on cysteine-containing medium.
PMID:37156397	LC-MS analysis
PMID:37156397	Figs. 3, S1C. Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	Figs. 3, S1C. Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37156397	Figs. 2B, S1B
PMID:37158439	Figure 4C
PMID:37158439	Figure 1B
PMID:37158439	Figure 1B. From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	Figure 1C
PMID:37158439	Figure 1C
PMID:37158439	Figure 1E and G
PMID:37158439	Figure 1 E and G
PMID:37158439	Figure 1E and G
PMID:37158439	Figure 1
PMID:37158439	Figure 1
PMID:37158439	Figure 1
PMID:37158439	Figure 2
PMID:37158439	Figure 2
PMID:37158439	Figure 2
PMID:37158439	Figure 2
PMID:37158439	Figure 2 Fig. 2. fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
PMID:37158439	Figure 2 Fig. 2. fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
PMID:37158439	Figure 3B
PMID:37158439	Figure 3B
PMID:37158439	Figure 3B
PMID:37158439	Figure 3C
PMID:37158439	Figure 3C
PMID:37158439	Figure 3C
PMID:37158439	Figure 3C
PMID:37158439	Figure 3C We next asked if S. pombe Cyk3 was required for fic1-2A’s suppression of myo2-E1. Indeed, cyk3Δ prevented fic1-2A from suppressing myo2-E1
PMID:37158439	Figure 4A
PMID:37158439	Figure 4A
PMID:37158439	Figure 4A
PMID:37158439	Figure 4A
PMID:37158439	Figure 4A
PMID:37158439	Figure 4A
PMID:37158439	Figure 4A
PMID:37158439	Figure 4C
PMID:37158439	Figure 4C
PMID:37158439	Figure 4C
PMID:37158439	Figure 4C
PMID:37158439	Figure 4C
PMID:37158439	Figure 4D
PMID:37158439	Figure 4D
PMID:37158439	Figure 4D
PMID:37158439	Figure S1
PMID:37158439	Figure S1
PMID:37158439	Figure S1
PMID:37158439	Figure S1
PMID:37158439	Figure S1
PMID:37158439	Figure S1
PMID:37158439	Figure S1
PMID:37158439	Figure S2
PMID:37158439	Figure S2
PMID:37158439	Figure S2
PMID:37158439	Figure S2
PMID:37158439	Figure S3
PMID:37158439	Figure S3
PMID:37158439	Figure S3
PMID:37158439	Figure S3
PMID:37158439	Figure S3
PMID:37158439	Figure S3
PMID:37158439	Figure S3
PMID:37158439	From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37162093	Figure 7
PMID:37162093	Figure 3CF, Figure 6ACE
PMID:37162093	Figure 7
PMID:37162093	Figure 7
PMID:37162093	Figure 7
PMID:37162093	Figure 4AC, Figure 6BDE
PMID:37162093	Figure 7
PMID:37162093	Figure 4AC
PMID:37162093	Figure 4AC
PMID:37162093	Figure 3BE, Figure 6ACE
PMID:37162093	Figure 7
PMID:37162093	Figure 3AD, Figure 6ACE
PMID:37162093	Figure 6BDE, Figure S2
PMID:37162093	Figure S2
PMID:37162093	Figure S2
PMID:37162093	Figure 4BD, Figure 6BDE
PMID:37162093	Figure 4BD
PMID:37162093	Figure 4BD
PMID:37162093	Figure 5AB, Figure S3
PMID:37162093	Figure 5AB
PMID:37162093	Figure 5AB
PMID:37164017	Growth rate improved by addition of either glutamate, glutamine, or arginine
PMID:37164017	Growth rate improved by addition of arginine
PMID:37191320	Fig. S4E revealed that the ER-shaping activities of the ΔC21–60 and ΔN29 mutants were partially and severely impaired, respectively (Fig. S4E)
PMID:37191320	(Fig. S4F), the ΔC21–60 and ΔN29 mutants exhibited partial and severe defects in reticulophagy, respectively, whereas the both mutant proteins were detectable on the ER (Fig. S4G)
PMID:37191320	In hva22Δ cells, reticulophagy was abolished, similar to cells lacking the core autophagy protein Atg1 (Figure 1B).
PMID:37191320	Consistently, Hva22 was observed on the ER under both nitrogen-rich and starvation conditions (Figure 3C).
PMID:37191320	We further found that the inner nuclear membrane protein Lem2 [26] was also degraded in a manner dependent on Hva22 (Figure 1H,I), indicating that the nuclear envelope undergoes Hva22- dependent reticulophagy. (vw I think this should be nucleophagy becasue IMN is not comnnected to ER)
PMID:37191320	Next, selective types of autophagy, such as mitophagy and pexophagy, were monitored by the processing of the mitochondrial protein Tuf1- RFP or Sdh2-GFP [21] and the peroxisomal protein Pex11- GFP, respectively. We observed that the hva22Δ mutant was partially defective in both mitophagy (Figure 2D and Fig. S2E) and pexophagy (Figure 2E).
PMID:37191320	The growth defect of the triple mutant strain defective in Spo7, Rtn1, and Yop1 is restored by the overexpression of the budding yeast reticulophagy receptor Atg40, a reticulon- and REEP-like protein that contains an ER-shaping activit
PMID:37191320	(Fig. S4F), the ΔC21–60 and ΔN29 mutants exhibited partial and severe defects in reticulophagy, respectively, whereas the both mutant proteins were detectable on the ER (Fig. S4G)
PMID:37191320	Fig. S4E revealed that the ER-shaping activities of the ΔC21–60 and ΔN29 mutants were partially and severely impaired, respectively (Fig. S4E)
PMID:37192628	Unexpectedly, wenoticed that addition of Sp-Atg44 caused fragmentation of lipid bilayers on the mica (compare Figures 7B and 7C), and the fragmented lipid bilayers abundant with Sp-Atg44 underwent division and fusion (Figure 7D; Video S6). These observations suggest that Sp-Atg44 has the ability to cause membrane fragility through physical interaction.
PMID:37192628	Atg44 binds to lipid membranes in vitro (Figures 5A and 5E), and the cryo-EM and HS-AFM analyses (Figures 5F–5I) suggest that Atg44 tends to bind to lipid membranes with high curvature.
PMID:37192628	Based on these results, we conclude that Atg44 localizes in the IMS and is not a transmembrane protein.
PMID:37192628	In atg44D cells, mitophagy was completely blocked similarly to cells lacking Atg1, a core autophagy protein (Figures 1A and S1B).
PMID:37192628	Similarly, loss of Atg44 in S. pombe affected mitochondrial morphology; some of the Sp-atg44D cells showed spherically enlarged mitochondria like Sp-dnm1D cells (Figure 3D)
PMID:37192628	Loss of Atg44 in either S. pombe or S. cerevisiae did not or only marginally affected non-selective macroautophagy, as measured by GFP/RFP processing (Figures S1C, S1D, and S1F) or the Pho8D60 assay (Figure 1E), or other types of selective autophagy including the Cvt pathway that delivers the precursor form of the hydrolase aminopeptidase I to the vacuole (Figure S1G), endoplasmic reticulum-phagy/reticulophagy (Figures S1E and S1H), and pexophagy (Figure S1I), suggesting that Atg44 is specifically required for mitophagy.
PMID:37192628	Overexpression of Atg44 in both species caused mitochondrial fragmentation not only in wild-type cells but also in Dnm1-deficient cells (Figures 3E and 3F).
PMID:37192628	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmentedand mitophagy was partially rescued (Figures 4A and S3F).
PMID:37192628	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmentedand mitophagy was partially rescued (Figures 4A and S3F).
PMID:37200372	Fig. 1
PMID:37200372	Fig. 1
PMID:37200372	Fig. 6
PMID:37200372	Fig. 6
PMID:37200372	Fig. 6
PMID:37200372	Fig. 6
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PMID:37200372	Fig. 6
PMID:37200372	Fig. 6
PMID:37200372	Fig. 6B
PMID:37200372	Fig. 6
PMID:37200372	Fig. 6B
PMID:37200372	Fig. 6
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PMID:37200372	Fig. 6
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PMID:37200372	Fig. S2 and text
PMID:37200372	Fig. S2 and text
PMID:37200372	Fig. S2 and text
PMID:37200372	Fig. S2 and text
PMID:37200372	Fig. 2
PMID:37200372	Fig. S12
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PMID:37237082	Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d).
PMID:37237082	figure 3a
PMID:37237082	figure 3a
PMID:37237082	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also addi- tively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37237082	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also addi- tively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37237082	figure 3a
PMID:37237082	(Fig. 6a) In wild-type and rad51 deletion backgrounds
PMID:37237082	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	(Fig. 3e).
PMID:37237082	Fig 1e Genome sequencing of one of them identified the srr1/ ber1-W157R and skb1-A377V mutations in their SRR1-like and arginine methyltransferase (RMTase) domains, respectively (Fig. 1b).
PMID:37237082	figure 5e
PMID:37237082	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	figure 3a
PMID:37237082	We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b),
PMID:37237082	We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b),
PMID:37237082	In the wild-type background, srr1Δ but not skb1Δ slightly reduced GCR rates, showing that Srr1 is required for GCRs even in the presence of Rad51
PMID:37237082	Unlike chk1Δ, in the srr1Δ strain, the septation index declined to the wild-type level by 6 h after MMS addition, suggesting that Srr1 is dispensable for cell cycle arrest.
PMID:37237082	(Fig. 3e). We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds)
PMID:37237082	(Fig. 3e). We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds)
PMID:37237082	The rad52-R45K, rad52Δ, and srr1Δ mutations eliminate ~90% of isochromosomes in rad51Δ cells (Fig. 2c and ref. 32), indicating that both Rad52 and Srr1 are essential for the major pathway of isochromosome formation.
PMID:37237082	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	figure 3a
PMID:37237082	figure 3a
PMID:37237082	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	figure 5e
PMID:37237082	figure 3a
PMID:37237082	figure 5e
PMID:37237082	figure 5e
PMID:37237082	Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d).
PMID:37237082	(Fig. 3e).
PMID:37237082	figure 5e
PMID:37237082	figure 5e
PMID:37237082	figure 3a
PMID:37237082	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	(Fig. 6a) In wild-type and rad51 deletion backgrounds
PMID:37237082	skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background.
PMID:37237082	skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background.
PMID:37237082	figure 3a
PMID:37279920	Strikingly, however, silencing at the mating type locus was completely abolished in the 22 absence of Caf1 and Mot2, similar to clr4∆ cells, as revealed by the lack of cell growth on 23 5FOA-containing medium and the marked accumulation of ura4+ transcripts (Fig. 1g-h).
PMID:37279920	We also detected intermediate phenotypes for the 8 ccr4∆ mutant, pointing to a partial contribution of this RNA deadenylase (Fig. 1g-h; 9 Supplementary Fig. 1b-d).
PMID:37279920	Figure 2
PMID:37279920	Strikingly, however, silencing at the mating type locus was completely abolished in the 22 absence of Caf1 and Mot2, similar to clr4∆ cells, as revealed by the lack of cell growth on 23 5FOA-containing medium and the marked accumulation of ura4+ transcripts (Fig. 1g-h).
PMID:37403782	we examined our Bmc1 RIP-Seq dataset (20), which revealed an interaction between Bmc1 and snoZ30, which guides 2′-O-methylation of U6 at position 41 (41) (Supplementary Figures S1A, S2A, B).
PMID:37403782	Still, as mean intron retention values indeed showed an in- crease upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi- quantitative RT-PCR (one of which, intron 1 of pud1, dis- played a statistically significant increase upon Bmc1 dele- tion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	U6
PMID:37403782	U6
PMID:37403782	U6
PMID:37403782	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	We validated the interaction between Bmc1 and sno530 by RNP immunoprecipitation/qPCR and showed that much like snoZ30 and U6, this interaction is dependent on the presence of the assembled Bmc1-Pof8-Thc1 com- plex (Figure 1A).
PMID:37403782	we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B).
PMID:37403782	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	Still, as mean intron retention values indeed showed an in- crease upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi- quantitative RT-PCR (one of which, intron 1 of pud1, dis- played a statistically significant increase upon Bmc1 dele- tion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3).
PMID:37403782	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3).
PMID:37403782	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3).
PMID:37403782	we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B).
PMID:37403782	we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B).
PMID:37403782	Importantly, co-migration of Pof8 with U6 was lost upon deletion of Bmc1 (Figure 1B), as well as co-migration of Bmc1 with U6 upon deletion of Pof8 (Supplementary Fig- ure S1C).
PMID:37403782	Importantly, co-migration of Pof8 with U6 was lost upon deletion of Bmc1 (Figure 1B), as well as co-migration of Bmc1 with U6 upon deletion of Pof8 (Supplementary Fig- ure S1C).
PMID:37403782	Further support- ing the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	Further support- ing the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	Further support- ing the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	Still, as mean intron retention values indeed showed an in- crease upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi- quantitative RT-PCR (one of which, intron 1 of pud1, dis- played a statistically significant increase upon Bmc1 dele- tion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37531259	Figure 1C
PMID:37531259	Figure S1D
PMID:37531259	Figure S1D
PMID:37531259	Figure S1D
PMID:37531259	Figure 1F
PMID:37531259	Figure 1E
PMID:37531259	Figure 1E
PMID:37531259	Figure 3A
PMID:37531259	Fig. 1, Fig. 1B, Fig. 2D
PMID:37531259	Figure 1C &F
PMID:37531259	Figure 1C
PMID:37531259	Figure 1C
PMID:37531259	Figure 1D
PMID:37531259	Figure S1B
PMID:37531259	Figure S1D (vw: same pathway)
PMID:37531259	Figure S1D
PMID:37531259	Figure S1C
PMID:37531259	Figure 1C
PMID:37531259	Figure 3C
PMID:37531259	Figure 3E
PMID:37531259	Figure 3E
PMID:37531259	Figure 3C
PMID:37531259	Figure 3B Furthermore, in cells overproducing ank1+, ~10% of Fim1-mCherry patches internalized compared to ~95% of Fim1-mCherry patches internalized in the control cells (Fig. 3B)
PMID:37531259	Figure S1C
PMID:37531259	Figure 1C
PMID:37531259	Figure 3A in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A).
PMID:37531259	Figure 1C
PMID:37531259	Figure S1A
PMID:37531259	Figure 1C
PMID:37531259	vw, I think we can conclude this from the EXP, especially as we know that myo1 binds phopshilipids in other species :Addition of Ank1 resulted in a reduction in the amount of co-pelleting of the Myo1(1-964)-FLAG-Cam1-Cam2 complex with liposomes (Fig. 2F). We therefore conclude that Ank1 directly binds and inhibits Myo1 membrane binding, supporting our model.
PMID:37531259	Given the AF model and the above results, we hypothesized that Ank1 In contrast, in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A). These data support our model that Ank1 blocks Myo1 membrane association and normally sequesters the bulk of Myo1 in the cytoplasm.precludes Myo1 membrane binding and sequesters the myosin-1 complex in the cytoplasm (Fig. 2F).Addition of Ank1 resulted in a reduction in the amount of co-pelleting of the Myo1(1-964)-FLAG-Cam1-Cam2 complex with liposomes (Fig. 2F). We therefore conclude that Ank1 directly binds and inhibits Myo1 membrane binding, supporting our model.
PMID:37531259	Figure 1C
PMID:37531259	Figure 1C
PMID:37540145	Figure 4G
PMID:37540145	Figure 4F mitochondrial net-like morphology
PMID:37540145	loss of Mdi1 did not impact Dnm1 recruitment to mitochondria and Dnm1 foci appeared associated with the hyperfused net structures (Fig. 4 F, arrows).
PMID:37540145	Figure 4G
PMID:37540145	Thus, our data indicate that Mdi1 plays a conserved role as a profission factor that is not required for Dnm1 recruitment but is required to facilitate the completion of mitochondrial division. Fig 4
PMID:37540145	Figure 4F mitochondrial net-like morphology
PMID:3870979	at 33.5 degrees, which is restrictive for cdc10129 but allows sporulation
PMID:3870979	at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation
PMID:3870979	homozygous diploid
PMID:3870979	homozygous diploid
PMID:3870979	homozygous diploid
PMID:3870979	homozygous diploid
PMID:3870979	homozygous diploid
PMID:3870979	at 33.5 degrees, which is restrictive for cdc10-129 but allows sporulation
PMID:3870979	at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation
PMID:3870979	Saccharomyces LEU2 used for disruption
PMID:3870979	done in h- cells kinetics depend on medium composition (see fig 6B)
PMID:4154968	"well this is a slight fudge. The activity was assayed and present. We know this is glutamate dehydrogenase...so sone and will make ""published"""
PMID:4309177	activated by ATP
PMID:4698209	inhibited_by CHEBI:17191
PMID:4698210	inhibited_by CHEBI:27266
PMID:4708672	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4708672	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4708672	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4821071	activated_by FAD , inhibited_by L-valine
PMID:6094012	parent child relationship with term above requested
PMID:6094012	actually this only occurs in 30% of cells.. I don't know if it is viable or inviable
PMID:6526818	inhibited by methionine
PMID:6828164	cell size at septation is 9.6µm
PMID:6828164	cell size at septation is 8.4µm
PMID:6828164	cell size at septation is 8.9µm
PMID:6828164	fig1A Table 1 cdc13 transition point (0.78) is not advanced in a cdc13-117 wee1.6 mutant
PMID:6828164	fig1A Table 1 cdc13 transition point is 0.69 using a cdc13-117 mutant
PMID:6828164	The transition point for cdc1 is advanced in a cdc1.P13 wee1.6 mutant from 0.62 to 0.33. An asynchronous population of a cdc1-P13 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant
PMID:6828164	fig1A The transition point for cdc2 (0.68) is not advanced using a cdc2.M63 wee1.6 mutant
PMID:6828164	fig1A
PMID:6828164	The transition point for cdc2 is advanced from 0.65 to 0.53 using a cdc2.M26 wee1.6 mutant
PMID:6828164	The transition point for cdc2 is advanced from 0.68 to 0.47 using a cdc2.L7 wee1.6 mutant
PMID:6828164	fig1A The transition point for cdc2 is advanced from 0.69 to 0.48 using a cdc2.33 wee1 [more...]
PMID:6828164	fig1A The transition point for cdc2 is 0.65 using cdc2.M55
PMID:6828164	fig1A The transition point for cdc2 (0.74) is not advanced using a cdc2.M35 wee1.6 mutant
PMID:6828164	fig1A The transition point for cdc2 is 0.66 using cdc2.M35
PMID:6828164	fig1A The transition point for cdc2 is 0.65 using cdc2.M26
PMID:6828164	fig1A The transition point for cdc2 is 0.70 using cdc2.M63
PMID:6828164	fig1A The transition point for cdc2 is 0.68 using cdc2.L7
PMID:6828164	fig1A The transition point for cdc2 is 0.65 using cdc2.33
PMID:6828164	fig1A The transition point for cdc27 is advanced from 0.63 to 0.22 in a cdc27-K3 wee1.6 mutant. An asynchronous population of a cdc1-7 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc27 gene and the number of cells that went on to divide was increased compared to a cdc27-K3 mutant
PMID:6828164	fig1A TTable 1 cdc27 transition point is 0.62 using a cdc27.K3 mutant
PMID:6828164	"fig1A EXP The transition point for cdc1 is not advanced in a cdc1.7 cdc2-1w mutant (0.64). An asynchronous population of a cdc1-7cdc2-1w mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was similar to a cdc1-7 mutant. The transition point for cdc1 (0.58) is not advanced in a cdc1.7 cdc2-2w mutant (cdc2-2w is the same change as cdc2-1w, but also consider comment transferred from duplicate annotation: ""I think this allele cdc2-2w maybe a typo or a changed annotation since this paper was published and is actually cdc2-3w"")."
PMID:6828164	fig1A The transition point s advanced from 0.68 to 0.29 in a cdc1.7 wee1.6 mutant. An asynchronous population of a cdc1-7 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant
PMID:6828164	TP. 0.33
PMID:6828164	fig1A The cdc1 gene has a execution point of ~0.62 which means its function is completed just before entry into mitosis. An asynchronous population of the cdc1-7 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the gene and the number of cells that went on to divide was measured
PMID:6828164	???
PMID:6828164	fig1A The cdc1 gene has a execution point of ~0.65 which means its function is completed just before entry into mitosis. An asynchronous population of the cdc1-7 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the gene and the number of cells that went on to divide was measured
PMID:6828164	cell size at septation is 9.5µm in cdc2-1w (9.7µm in cdc2-2w)
PMID:6828164	cell size at septation is 8.7µm
PMID:6828164	cell size at septation is 8.9µm
PMID:6828164	cell size at separation is 16.7µm compared to 12.8µm for wild type
PMID:6828164	cell size at septation is 8.5µm
PMID:6828164	cell size at separation is 22.4µm compared to 12.8µm for wild type
PMID:6828164	cell size at septation is 10.3µm
PMID:689088	at division
PMID:6943408	abolished DNA replication
PMID:6943408	abolished
PMID:6961452	This was really IGI complemetnation of E-coli pyrB
PMID:7262540	cells divide at 11% longer than wild diploid cells at division
PMID:7262540	cells divide at 6% longer than wild diploid cells at division
PMID:7262540	cells divide at 10% longer than wild diploid cells at division
PMID:7262540	This mutation is probably allelic with cdc2-56. Cells divide at 10.0 µm. I think it is useful to have it annotated as it is in old literature and people may wonder what it is
PMID:7262540	cells divide at 10.2µm at 25°C
PMID:7262540	cells divide at 22.4µm at 25°C
PMID:7262540	cdc2-1w was previously called wee2-1
PMID:7262540	cells septate at 56% of wild type diploid length
PMID:7262540	cells septate at 58% of wild type diploid length
PMID:7262540	cells divide at 8% longer than wild diploid cells at division
PMID:7262540	cells divide at 75% of wild type diploid cell length at division at 25°C
PMID:7262540	cells divide at 9% longer than wild diploid cells at division
PMID:7262540	cells septate at 85% of wild type diploid length
PMID:7262540	small cell size at division is partially suppressed in the presence of sup3-5 an opal nonsense suppressor mutation in the sup3 tRNA gene. Cells divide at 89% of control cell length at division so are not really normal size
PMID:7262540	cells divide at 7% longer than wild diploid cells at division
PMID:7262540	cells divide at 12% longer than wild diploid cells at division
PMID:7262540	cells divide at 10% longer than wild diploid cells at division
PMID:7262540	cells divide at 51% of control cell length at division
PMID:7262540	cells divide at 16.7µm at 25°C
PMID:7262540	cells septate at 54% of wild type diploid length
PMID:7262540	cells septate at 58% of wild type diploid length
PMID:7262540	Cells divide at 65% of wild type diploid cell length
PMID:7262540	cells septate at 52% of wild type diploid length
PMID:7262540	cells divide at 56% of the size at division of wild type diploids
PMID:7262540	cells septate at 81% of wild type diploid length
PMID:7262540	cells divide at 82% of wild diploid size at division
PMID:7262540	cells septate at 77% of wild type diploid length
PMID:7262540	cells septate at 87% of wild type diploid length
PMID:7262540	cells divide at 11% longer than wild diploid cells at division
PMID:7262540	cells septate at 82% of wild type diploid length
PMID:7498507	activated_by(CHEBI:16356)
PMID:7501024	salt stress
PMID:7501024	salt stress
PMID:7501024	non-ionic osmotic stress
PMID:7501454	higher affinity during S phase than G2/M
PMID:7501454	hyperphosphorylated in late S phase; phosphorylated on different sites in S versus G2/M
PMID:7501454	constant throughout cell cycle
PMID:7559598	not shown
PMID:7559598	not shown
PMID:7588609	heterozygous diploid
PMID:7596817	polysome profile
PMID:7596817	polysome profile
PMID:7622618	evidence is essentially IC, as I inferred sterility from the lack of shmoo formation (h- cells)
PMID:7626804	Fig5 B wee1 is necessary for T14 phosphorylation no peptide 3 is observed when wee1 is deleted
PMID:7626804	Table 2 cdc2-T14A is present on multicopy plasmid cells are viable and have a normal cell size phenotype
PMID:7626804	Fig1D peptide 3
PMID:7626804	Fig1A
PMID:7626804	Fig 4A middle panel cells average size 11.6µm This strain is a gene replacement of cdc2+
PMID:7626804	Fig 4A right panel cells average size 16.6µm This strain is a gene replacement of cdc2+
PMID:7626804	Fig 4B absence of peptide 3 This strain is a gene replacement of cdc2+
PMID:7626804	Fig 4B middle right panel presence of peptide 3 This strain is a gene replacement of cdc2+
PMID:7626804	Fig 4B absence of peptide 3 Overexpression of wee1 does not phosphorylate T14A residue. This strain is a gene replacement of cdc2+
PMID:7626804	Fig 4B increased peptide 3 compared to when wee1 is not overexpressed . This strain is a gene replacement of cdc2+
PMID:7626804	Table 2 cdc2-T14A is present on multicopy plasmid cells are viable but have a semi wee phenotype
PMID:7626804	Fig7A,B At restrictive temperature T14 is not phosphorylated (no peptide when cells blocked at RT.)
PMID:7626804	Fig7A, B At shift to permissive temperature T14 becomes phosphorylated. Peptide 3 is only present at low stoichiometry
PMID:7626804	Fig8
PMID:7626804	Fig8
PMID:7626804	Fig1B, C and D x = a small phospho peptide of T14Y15. T14 phosphorylation only occurs when wee1 is overexpressed
PMID:7626804	data not shown
PMID:7626804	Fig3 chk1 1 is not required for T14 phosphorylation by wee1
PMID:7626804	Fig1D peptide 2
PMID:7626804	Fig1D peptide 3 and peptide1
PMID:7651412	switches specificity from direct repeats to inverted repeats
PMID:7651414	matmi and matpi
PMID:7651414	matmi and matpi
PMID:7651414	matmi and matpi
PMID:7651414	matmi and matpi
PMID:7651414	matmi and matpi
PMID:7657164	residue not determined, but probably Y173
PMID:7687541	fig4
PMID:7706287	assayed for bulk poly(A)+ RNA
PMID:7706287	arrest point determined by H1 kinase activity peak
PMID:7706287	assayed for bulk poly(A)+ RNA
PMID:7739540	(Figure 3b)
PMID:7739540	(Figure 3b)
PMID:7739540	(Figure 3b)
PMID:7773104	NADP-GDH-defective
PMID:7774573	child term of abnormal regulation of mitotic metaphase/anaphase transition. pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	About 75% of cells do not enter mitosis in presence of HU Figure 6A, showing that this mutant does not disrupt normal controls regulating entry into mitosis. pRIP45cdc2-DL45 is integrated cdc2-DL41 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	pRIP45DL45 is integrated. cdc2-DL41 has same phenotype but it is not clear if it is under the same conditions. Figure 6B the 20% of cells that are in mitosis are probably cells that were in mitosis when the culture was shifted to the restrictive temperature
PMID:7774573	pREP41cdc2-DL41 is a multi copy plasmid . No data shown
PMID:7774573	pREP41cdc2-DL41 is a multi copy plasmid . No data shown
PMID:7774573	pREP41cdc2-DL45 is a multi copy plasmid. No data shown
PMID:7774573	pREP41cdc2-DL45 is a multi copy plasmid . No data shown
PMID:7774573	pRIP45cdc2+ is integrated
PMID:7774573	pRIP45cdc2-DL45 is integrated
PMID:7774573	pRIP45cdc2-DL41 is integrated
PMID:7774573	pIRT2suc1 multi copy plasmid partially rescues the pREP5cdc2-DL41 integrant mitotic arrest phenotype and allows formation of micro colonies. cdc2-DL45 is also partially rescued but it is not clear whether this is under the same conditions
PMID:7774573	pREP41cdc2-DL50 is integrated
PMID:7774573	pREP41cdc2-DL50 is integrated
PMID:7774573	pREP41cdc2-DL50 is integrated
PMID:7774573	pREP5cdc2+ is integrated. 24% cells enter mitosis compared to 2% when cdc2+ is not over expressed but they did not say that it was a cut phenotype
PMID:7774573	pREP41cdc2-DL50 is integrated
PMID:7774573	pREP5-DL41 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid
PMID:7774573	pREP5-DL45 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid
PMID:7774573	pREP41-DL50 is integrated
PMID:7774573	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	pREP5cdc2-DL41 is integrated.cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions. Abnormal septum phenotype include misplace septum, multi septa and partially formed septa
PMID:7774573	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	abnormal mitotic arrest with 4C DNA content Cells undergo an extra round of DNA replication without undergoing cytokinesis pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7796804	Fig 6, Fig7B panel 8,
PMID:7796804	Fig 5C cyclin cdc13 cdc2 complex are not detected when cells are blocked in G1 with cdc10-129 mutant complex precipitated with p13 beads
PMID:7796804	Fig 5B cdc22-M45 blocked in G1/S
PMID:7796804	Fig 5B cdc22-M45 blocks in G1/S
PMID:7796804	Fig7A 8,
PMID:7796804	Fig 6 top panels , Fig7B panel 2 cells examined 7 hour after refeeding with nitrogen After 7 hour the cdc10-V50 cells start to leak through and this allows the mik1D wee1-50 cells to start entering mitosis
PMID:7796804	Fig 6 top panels, Fig7B panel 1 cells examined 7 hour after refeeding with nitrogen
PMID:7796804	Fig 6 middle panels Fig7B panel 3 cells examined 7 hour after refeeding with nitrogen
PMID:7796804	Fig 6 middle panels Fig7B panel 4 cells examined 7 hour after refeeding with nitrogen
PMID:7796804	Fig 6 bottom panels Fig7B panel 5 cells nitrogen starved and examined 7 hour after refeeding with nitrogen
PMID:7796804	Figure 1, 4,5
PMID:7796804	Fig7C
PMID:7796804	Fig 6 bottom panels Fig7B panel 6 cells examined 7 hour after refeeding with nitrogen
PMID:7796804	fypo/issues/3164 Fig 5C the cyclin cdc13 cdc2 complex are detected when cells are blocked at G1/S with cdc20-M10 mutant, complex precipitated with p13 beads
PMID:7796804	fypo/issues/3164 Fig 5C the cyclin cdc13 cdc2 complex are detected when cells are blocked at G1/S with cdc20-M45 mutant, complex precipitated with p13 beads
PMID:7796804	Fig7B. It is the soluble form (upper panel) that disappears not the insoluble form (lower panel) which has implications for which form is allowing replication. I don't know whether to leave this annotation out
PMID:7796804	Fig 7C
PMID:7796804	Fig 7C
PMID:7796804	Fig7A panel 5
PMID:7796804	Fig5B cdc10-129 cells blocked in G1
PMID:7796804	Fig7A panel 2
PMID:7796804	Fig7A panel 1
PMID:7796804	Fig7A panel 4
PMID:7796804	Fig7A panel 6
PMID:7796804	Figure 1, 4,5
PMID:7796804	Figure 1, 4,5
PMID:7796804	Fig7A panel 3
PMID:7796804	Figure 1, 4,5
PMID:7796804	Fig5A
PMID:7796804	Fig 5A
PMID:7796804	Fig 5A
PMID:7813446	higher than wee1 not overexp, but lower than wee1-50 overexp in wt bkg
PMID:7813446	not arrested like wee1-50 overexp alone
PMID:7813446	not arrested like wee1+ overexp alone
PMID:7813446	not arrested like wee1-50 overexp alone
PMID:7859738	Figure 4
PMID:7859738	Figure 4
PMID:7859738	Figure 4
PMID:7859738	Figure 4
PMID:7859738	Figure 4
PMID:7859738	Figure 4
PMID:7859738	Figure 4
PMID:7876257	endoglycosidase-H cleaves N-linked glycosylation
PMID:7883794	Figure 1A
PMID:7883794	Figure 2C
PMID:7883794	Figure 2B
PMID:7883794	Table 1, Figure 2C
PMID:7883794	Figure 3A
PMID:7883794	Figure 3B
PMID:7883794	Table 1, Figure 1B appearance of IC peak at early timepoint
PMID:7883794	Data not shown
PMID:7883794	Fig1 B
PMID:7889932	crystal structure
PMID:7903653	ABOLISHED
PMID:7903653	ABOLISHED
PMID:7903653	ABOLISHED
PMID:7909513	the basal level of the 3.2 kb transcript was lower than that in h90 wild type cells, but the 3 kb transcript was properly induced upon nitrogen starvation
PMID:7909513	3 kb transcript
PMID:7916653	deletion with expressed plasmid, after plasmid loss
PMID:7916658	constitutive cdc18+ expression
PMID:7916658	constitutive cdc18+ expression
PMID:7916658	inferred from combination of phenotype shown in this paper with background knowledge
PMID:7916658	constitutive cdc18+ expression
PMID:7923372	they interacted in the Y2H experiment, so inferring this relationship
PMID:7957097	no mitotic spindle
PMID:7957097	inhibits
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as cdc25-22 alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7957098	same as cdc13-117 alone
PMID:7957098	same as cdc2-33 alone
PMID:7957098	same as cdc10-129 alone
PMID:7957098	same as rad4 cut5 allele alone
PMID:7975894	increased transcriptional response to nitrogen starvation
PMID:7975894	increased transcription from TR box SO:0001858
PMID:7975894	increased transcriptional response to nitrogen starvation
PMID:7983142	33 degrees (may be standard for them)
PMID:7983142	33 degrees (may be standard for them); morphology same as ppe1delta alone
PMID:7983142	33 degrees (may be standard for them)
PMID:7983142	33 degrees (may be standard for them)
PMID:7983142	33 degrees (may be standard for them)
PMID:7983142	33 degrees (may be standard for them)
PMID:7983142	33 degrees (may be standard for them)
PMID:8006074	fig8
PMID:8006074	fig8
PMID:8006074	fig8
PMID:8006074	fig8
PMID:8026462	assayed using casein
PMID:8039497	also some genetic interactions that cannot be described with biogrid
PMID:8039497	unstable plasmid loss experiment
PMID:8039497	also some genetic interactions that cannot be described with biogrid
PMID:8087848	cdc10-129 cells blocked in G1 over expressing cdc2 from integrated pREP5cdc2 and cdc13 from episomal pREP41-cdc13. The nmt1 promoter is derepressed Figure 4
PMID:8087848	cdc13delete cells were kept alive by episomal pSM2 cdc13. Cell phenotype was observed after plasmid loss. Figure 2C
PMID:8087848	cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment
PMID:8087848	cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment
PMID:8087848	FACS analysis of germinating haploid cdc13delta spores. Up to 32C DNA content was observed by 19 hour after referring spores to allow germination Figure 2
PMID:8087848	germinating haploid cdc13delta spores, observed by 14 hour after spores allowed to germination (Figure 2b). cdc13delete cells kept alive by a multicopy plasmid, pSM2-cdc13. Cell phenotype was observed after plasmid loss same phenotype as in Figure 2b
PMID:8087848	p34cdc2 cdc13-9 complex was pulled down using p13suc1 beads and then western blotted using anti cdc13 antibody SP4 to show reduced levels of Cdc13 complexed with cdc2 compared to the wild type control
PMID:8087848	cdc10-129 cells blocked in G1 over expressing cdc2 from integrated pREP5cdc2 and cdc13 from episomal pREP41-cdc13. The nmt1 promoter is derepressed Figure 4
PMID:8087848	cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment
PMID:8187760	same as cdc2-33 alone
PMID:8187760	assayed in vitro using casein
PMID:8187760	grows in three dimensions instead of just at cell ends
PMID:8187760	same as cdc25-22 alone
PMID:8196631	NEG REG OF PHEROMONE RESPONSE MAPK
PMID:8223442	fig 1
PMID:8223442	fig 1
PMID:8227198	response curve differs from wt and other git mutants
PMID:8264625	casein substrate (vw changed from GO:0004674 with contributes to)
PMID:8264625	casein substrate
PMID:8292390	same as cps8-185 alone
PMID:8299169	C868T (nt)
PMID:8319772	present throughout cell cycle
PMID:8334988	binucleate fypo/issues/#2400 fypo/issues/#2401
PMID:8346915	inhibiyted by CHEBI:43040
PMID:8413241	tyrosine; residue not determined
PMID:8413241	tyrosine; residue not determined
PMID:8437586	Table 1 Fig 4 nmt1 promoter ON
PMID:8437586	Table1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 Fig 2 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 surpresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	Table 1 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	Table 1 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 give partial suppression
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Fig 4 nmt1 promoter ON
PMID:8437586	Fig 4 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Fig 4 Table 1 nmt1 promoter ON
PMID:8437586	Fig 4 Table 1 nmt1 promoter ON
PMID:8437586	Table 1 Fig 4 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Table 1 nmt1 promoter ON
PMID:8437586	Fig 5 nmt1 promoter ON
PMID:8437586	Fig 5 nmt1 promoter ON
PMID:8437586	Fig 5 nmt1 promoter ON
PMID:8437586	Table 1 Fig 4 nmt1 ON
PMID:8437586	Cdc2 is only mildly over expressed as it is expressed from a multi copy plasmid pIRT2. This is much lower over expression than from the nmt1 promoter and for all the other annotations were the cdc2 mutant is expressed from pIRT2 I have said 'unknown' for expression level
PMID:8437586	Cdc2 is only mildly over expressed as it is expressed from a multi copy plasmid pIRT2. This is much lower over expression than from the nmt1 promoter and for all the other annotations were the cdc2 mutant is expressed from pIRT2 I have said 'unknown' for expression level
PMID:8437586	Fig 5 increased duration of G1 phase
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 Fig 2 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	Table 1, Fig2 mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant expressed from multi copy plasmid pIRT2
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8443406	NEG REG PHEROMONE RESPONSIVE MAPK CASC
PMID:8463273	kinase assay, and hybridization with S. cerevisiae PKC
PMID:8485317	like dis1-288 alone
PMID:8485317	like dis1-288 alone
PMID:8496185	inhibited by P(1),P(5)-bis(5'-adenosyl) pentaphosphate(5-)?
PMID:8497322	fig 2 c
PMID:8497322	fig 3 cells fail to separate and are clupmed together, multiple rounds of nuclear division
PMID:8497322	fig 2 c
PMID:8497322	fig 4
PMID:8497322	fig 3
PMID:8497322	fig 2a
PMID:8497322	fig 2 c
PMID:8497322	fig 3 a
PMID:8497322	data not shown
PMID:8497322	fig 3 fypo/issues/2818
PMID:8497322	fig 3 fypo/issues/2818
PMID:8497322	fig 2 c
PMID:8497322	fig 2a DROPS TO ZERO
PMID:8497322	partial rescue of chk1, fig 2 b
PMID:8515818	Fig 2b
PMID:8515818	Fig2a lane1
PMID:8515818	Fig1b bottom R panel , bottom R K41A is predicted to be catalytically inactive. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig1b bottom R panel , bottom R K41A is predicted to be catalytically inactive. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig1b bottom R panel, top
PMID:8515818	Fig1b top R panel, top cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig1b top R panel bottom L cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig1b bottom R panel, top
PMID:8515818	Fig1b top R panel bottom R. K41A is predicted to be catalytically inactive ref 18. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig1b top R panel bottom R K41A is predicted to be catalytically inactive. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig2a lane 3
PMID:8515818	Fig2b,
PMID:8515818	Fig1b bottom R panel, bottom L
PMID:8515818	Fig1b bottom R panel, bottom L
PMID:8515818	Fig1b top R panel, top cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	Fig1b top R panel bottom L cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	data not shown ref16
PMID:8515818	(directly inhibits) Fig4a,b together with data from fig 2,3
PMID:8515818	Fig2b
PMID:8515818	Fig2b 2x serine phos to T phos
PMID:8521469	same as cdc18+ oe alone
PMID:8521469	same as cdc18+ oe alone
PMID:8521500	Fig3A
PMID:8521500	Fig3B
PMID:8521500	Fig3B
PMID:8521500	Fig4 rum1HA pulldown brings down both cdc13 and cdc2 to form rum1-cdc13-cdc2 complex. so I really need to add 3 proteins not two in the annotation extensions
PMID:8521500	Fig 3C
PMID:8521500	Fig 3C
PMID:8521500	Fig5A
PMID:8521500	Fig5A
PMID:8521500	FigB over expression reduces cdc2 kinase activity even in absence of added rum1 protein
PMID:8521500	Fig5B over expression abolishes cdc13 associated kinase activity even in absence of added rum1 protein
PMID:8521500	Fig3A
PMID:8521500	Fig3A
PMID:8521500	[ move to specific cyclin] Fig6 2.6nM rum1 inhibits cig2 associated cdc2 kinase activity by ~50%
PMID:8521500	Fig 6 cdc2-cig1 complex is insensitive to inhibition by rum1. There is ~100% activity in the presence of 26nM rum
PMID:8521500	Fig3A
PMID:8521500	Fig3A
PMID:8521500	Fig2C rum1+ driven by nmt1 promoter in pREP6X is integrated
PMID:8521500	[MOVE 'occurs at' TO M-PHASE CYCLIN] Fig1 and 2B 0.26nM pRum1 inhibits in vitro cdc2-cdc13 kinase activity by ~80%, Fig3C ig5B,C, D addition of 2.6nM rum1 reduces cdc2 associated kinase activity
PMID:8521500	Fig 1 Histone H1 used as substrate
PMID:8521500	Fig1 Histone H1 used as substrate
PMID:8522609	same as cdc2-33 alone
PMID:8522609	same as orb2-34 alone
PMID:8522609	same as orb2-34 alone
PMID:8522609	same as orb3-167 alone
PMID:8522609	same as orb3-167 alone
PMID:8522609	same as orb3-167 alone
PMID:8552670	, activated_by(CHEBI:18420)
PMID:8557036	assayed in S. cerevisiae cell extracts, with S.c. CDK2 substrate
PMID:8557036	assayed in S. cerevisiae cell extracts, with S.c. CTD substrate
PMID:8557037	activated_by(CHEBI:63041)
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8569679	fig2
PMID:8590464	inhibited_by L-lysine
PMID:8590474	partial rescuie
PMID:8618924	also inferred from orthology to all other Orc1s in the world
PMID:8621436	transient phenotype, they then attempt to divide without segregation
PMID:8621436	transient phenotype, they then attempt to divide without segregation
PMID:8621436	transient phenotype, they then attempt to divide without segregation
PMID:8621436	they show it is not abnormal regulation of rereplication in cdc25 double mutant expts
PMID:8621436	transient phenotype, they then attempt to divide without segregation
PMID:8621436	they show it is not abnormal regulation of rereplication in cdc25 double mutant expts
PMID:8649397	Can't say if they are viable vegetative because it is in a pyp2+ background
PMID:8654750	PHEROMONE
PMID:8668131	func comps S cer ABC1
PMID:8688826	Val: changed from nuclear lumen to nuclear periphery
PMID:872890	Fig 2 This suggests that wee1-50 only has an indirect effect on the G1-S transition because when wee1-50 is shifted to the permissive temperature cells are still small, this is not affected by the presence of active wee1 and cells enter S-phase at the same size as they did at the restrictive temperature
PMID:872890	Table 1, Fig1
PMID:872890	Fig6, Table 2 cell size measure by protein content per cell, cells need to reach ~7pg/cell. This measurement is also the same for wild type cells which are small after nitrogen starvation (Fig5)
PMID:872890	Table 1
PMID:872890	Table 1, DNA replication initiated at low protein content
PMID:872890	Table 1, Fig1
PMID:872890	Fig1, data not shown cdc2-1w is called wee 2-1 in this paper. Wee cells enter mitosis at a small cell size compared to wild type cells and thus daughter cells are born smaller than wild type cells. Wee cells have similar cell cycle timing (doubling time) to wild type cells
PMID:872890	Fig4, Table 2 cell size measure by protein content per cell, cells need to reach ~7pg/cell. This measurement is also the same for wild type cells which are small after spore germination (Fig3)
PMID:872890	Fig 2 This shows that wee1-50 has a direct effect on the G2-M transition because cells now at the permissive temperature (active wee1) detect that they are too small to enter mitosis and the G2/M transition is inhibited
PMID:8799335	present with ammonium, allantoin, or proline nitrogen source
PMID:8799851	Fig10
PMID:8799851	Data not shown cdc13 protein level in asynchronous culture of wee1-50 cells at restrictive temperature is reduced by 40% compared to asynchronous culture of WT cells
PMID:8799851	Uses elutriation synchrony. Fig5 cdc13 protein level in synchronous culture of wee1-50 cells at restrictive temperature is absent during longer G1 phase
PMID:8799851	Fig 9
PMID:8811082	thymine glycols, urea
PMID:8811082	The capacity of Nth-Spo to generate strand breaks in a variety of damaged plasmid DNA substrates was investigated. Figure 4shows the activity of Nth-Spo and Nth-Eco in incising super- coiled damaged DNA. None of the proteins caused breaks in undamaged DNA.
PMID:8824588	also has AP1 binding site
PMID:8834798	abnormal septum forms on the surface from one side of the cell and then extends in a disor- ganized manner into the interior
PMID:8876193	Fig 1 77% asymmetric distribution by 5 hours, aggregation observed after 1 hour
PMID:8876193	73% asymmetric distribution at old end by 5 hours asymmetric mitochondrial aggregation at old cell end
PMID:8876193	data not shown
PMID:8876193	Fig4
PMID:8876193	Fig3
PMID:8876193	Fig3
PMID:8876193	Fig2 1% of cells still have a short mitotic spindle after 5h at restrictive temperature
PMID:8876193	Fig2
PMID:8876193	data not shown, cells blocked in absence of septation, cells need to complete cell cycle to observe asymmetry
PMID:8876193	data not shown, cells blocked at G2/M, cells need to complete cell cycle to observe asymmetry
PMID:8876193	data not shown, cells blocked in S phase, cells need to complete cell cycle to observe asymmetry
PMID:8876193	data not shown, cells blocked at G1/S, cells need to complete cell cycle to observe asymmetry
PMID:8879048	NEG REG PHEROMONE MAPK
PMID:8918598	ubiquitin conjugate
PMID:8918598	ubiquitin conjugate
PMID:8918880	fig 1
PMID:8918880	fig 1
PMID:8918880	fig 1
PMID:8918880	fig 5
PMID:8918880	fig 1
PMID:8943330	tyrosine; position(s) not determined
PMID:8943330	not sure this annotation is 100% supported, can revise later if needed.
PMID:8946912	fig 2a
PMID:8946912	fig 2a
PMID:8946912	fig 2a
PMID:8946912	fig 3
PMID:8978670	figure 1
PMID:8978670	figure 1
PMID:8978670	figure 1
PMID:8978670	figure 1
PMID:8978687	figure 2
PMID:8978687	fig 7
PMID:8978687	fig 7
PMID:8978687	fig 6 a
PMID:8978687	figure 5
PMID:8978687	figure 5
PMID:8978687	fig 4 b
PMID:8978687	figure 1a
PMID:8978687	fig 6 a
PMID:8978687	fig 6 a
PMID:8978687	fig 6 c
PMID:8978687	figure 6
PMID:8978687	figure 5
PMID:8978687	figure 5
PMID:9024682	severe when both cells are cpb1delta
PMID:9024682	sporulation of homozygous diploid
PMID:9024682	sporulation of homozygous diploid
PMID:9034337	Fig 3B
PMID:9034337	Fig 3B
PMID:9034337	Data not shown chk1+ over expression phenotype is suppressed by over expressing cdc25+ independently of cdr1
PMID:9034337	Fig 4,
PMID:9034337	Fig 2C
PMID:9034337	Fig 2B Histone H1 used as cdc2 substrate Chk2 expressed from nmt1 promoter
PMID:9034337	Fig1
PMID:9034337	Fig 5, Fig6
PMID:9034337	Fig 2 D
PMID:9034337	Fig 2 D
PMID:9034337	Fig 2 A
PMID:9034337	Fig 6 GST wee1 has been phosphorylated in vitro by chk1. This assay shows that phosphorylation of wee1 by chk1 does not affect wee1 kinase activity
PMID:9034337	Fig 3C cell elongation as a result of chk1 over expression is dependent on wee1+
PMID:9034337	Fig 3C wee cell phenotype cell cycle distribution FACS profile of vegetatively growing wee cells show a cell cycle distribution with increased number of cells with a 1C DNA content compared to wild type cells. Note the increase in the G1 peak depends on the size of the cell and semi-wee cells do not always shown an increased G1 peak
PMID:9034337	Fig 3A
PMID:9042863	temperature permissive for wee1-50; unirradiated
PMID:9042863	temperature restrictive for wee1-50
PMID:9042863	dephosphorylation of Cdc2 Y15 by Cdc25 delayed in response to ionising radiation
PMID:9042863	Activity inhibited in response to mitotic G2 DNA damage checkpoint
PMID:9062192	mei2 promotes g1 arrest, premeiotic dna replication and meiosis I
PMID:9078365	homozygous diploid
PMID:9078390	fig 3a
PMID:9078390	fig 2 C
PMID:9078390	fig 3a
PMID:9078390	fig 3a
PMID:9078390	fig 3a
PMID:9078390	fig 3a
PMID:9078390	fig 2 C
PMID:9078390	fig 2 C
PMID:9078390	fig 2 C
PMID:9078390	fig 2 C
PMID:9078390	fig 2 C
PMID:9090050	inhibition by CCCP and DCCD
PMID:9105045	cdc12 froms a cortical spot
PMID:9111307	not sure if this is the right term, sent a question
PMID:9125114	also increased (WT overexppression) normal (WT)
PMID:9135147	tyrosine; residue not determined
PMID:9135148	inferring that residue is Y15, though not shown experimentally
PMID:9136929	not annotated to other stresses as subsequent papers show it is critical for assembly of signaling MAPKKK-MAPKKmodule
PMID:9153313	same as rad3delta alone
PMID:9153313	same as crb2delta alone
PMID:9153313	same as rad26delta alone
PMID:9154834	residue not determined, but probably Y173
PMID:9154834	doesn't resume normally
PMID:9154834	residue not determined, but probably Y173
PMID:9154838	has condensed chromosomes
PMID:9177184	as cyclin-CDK complex with Cdc13 or Cig2
PMID:9182664	swollen
PMID:9182664	swollen
PMID:9182664	this might be dumbbell ask Jacky
PMID:9191273	PHEROMONE MAPK
PMID:9200612	Fig3A
PMID:9200612	Fig1C iii
PMID:9200612	Fig1C ii
PMID:9200612	Fig6D
PMID:9200612	Fig1C ii
PMID:9200612	Fig1C iii
PMID:9200612	Fig1C iii
PMID:9200612	data not shown
PMID:9200612	data not shown. 95% of cells re bent or T shaped but don't say the different percentages so I've left it as bent
PMID:9200612	data not shown. tea1 on multi copy plasmid -R2 suppresses the cell shape defect of tea1 delta
PMID:9200612	Fig 6D
PMID:9200612	Fig5C cells blocked in mitosis so have no interphase MTs
PMID:9200612	Fig2B C
PMID:9200612	Fig 2B,C
PMID:9200612	Fig5C
PMID:9200612	Fig5C
PMID:9200612	Fig5C
PMID:9200612	Fig5 shown using TBZ treatment and wash out and by cold shock and relocalization
PMID:9200612	Fig4 A
PMID:9200612	Fig4 A
PMID:9200612	Fig4 A
PMID:9200612	Fig4 A
PMID:9200612	Fig 2C protein localised to both cell tips
PMID:9200612	Fig 2C Protein localised to both cell tips during monopolar growth
PMID:9200612	Fig 2D Protein localised to both cell tips during monopolar growth
PMID:9200612	Fig3A
PMID:9201720	physically interacts with and IMP evidence
PMID:9201720	physically interacts with and IMP evidence
PMID:9201720	not shown that it is ser/thr kinase activity, just that it is kinase activity
PMID:9211982	truncated Gar2 accumulates in this dense body
PMID:9252327	Cell growth rate is reduced in later generation due to telomere shortening. In early generation, cells growth rate is not distingushiable from trt1+ cells.
PMID:9252327	Cells look normal in early generation, but show many elongated cells in later generation due to telomere shortening.
PMID:9252327	Cells show progressive telomere shortening.
PMID:9252327	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar extent of delayed cell elongation phenotype as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9252327	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar delayed grow defect phenotype as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9252327	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar rate of telomere shortening as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9278510	fig 2 b
PMID:9278510	fig 2 b
PMID:9278510	fig 1
PMID:9285594	in vitro
PMID:9285594	Fig 1
PMID:9285594	Fig 1
PMID:9287302	vw: I deleted accidintally , then readded
PMID:9287302	vw: I deleted accidintally , then readded
PMID:9301023	(Figure 2a)
PMID:9301023	(Figure 2b)
PMID:9301025	just getting the allele in the database (they used it in the exp)
PMID:9303310	Fig2
PMID:9303310	Fig2
PMID:9303310	Fig 1 cells blocked in G1 at the restrictive temp
PMID:9303310	Fig 1 exponentially growing cells mainly in G2
PMID:9303310	Fig7A
PMID:9303310	Fig7B
PMID:9303310	Fig 8 added by cig1 associated CDK1
PMID:9303310	Fig5 (vw, I edited the extensions)
PMID:9303310	Fig2, Fig3
PMID:9303310	Fig2, Fig3
PMID:9303312	Fig3A cdc18 transcript accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	Fig3A cdc18 transcript accumulates in absence of cdc13
PMID:9303312	Fig3B cdc18 protein accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	Fig3C no DNA replication in absence of all 3 cyclins
PMID:9303312	Fig3C DNA replication in presence of cig1 and cig2
PMID:9303312	Fig3C Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. NOT sure the data warrants an annotation
PMID:9303312	Fig3C, D Absence of cdc2 kinase activity in absence cig1, cig2 and cdc13
PMID:9303312	Fig3C, D cdc13 promoter ON cdc2 kinase activity acts after the accumulation of cdc18 protein to bring about the G1/S transition
PMID:9303312	Fig4B decreased cdc18 transcript level as cells proceed through S phase and G2 and increases as cell go though G1
PMID:9303312	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	Fig 5, 6, 7,
PMID:9303312	Fig 5, 6, 7,
PMID:9303312	Fig8B DSC1 is now called MBF
PMID:9303312	Fig 4C Cdc2 not required for active cdc10 dependent transcription during S phase
PMID:9303312	Fig 4C Cdc18 transcript is low during G2
PMID:9303312	Fig 4C Cdc18 transcript is low during G2
PMID:9303312	Cdc2 kinase activity is low during G2 data not shown
PMID:9303312	Fig 4D
PMID:9303312	Fig 4D
PMID:9303312	Fig8 DSC1 is now called MBF
PMID:9303312	Fig8B DSC1 is now called MBF
PMID:9303312	Fig8 DSC1 is now called MBF
PMID:9303312	Fig7 res2 on multi copy pREP3X ON
PMID:9303312	Fig7 res2 on multi copy pREP3X ON
PMID:9303312	Fig5A, B decreased cdc18 transcript in HU block and on release
PMID:9303312	Fig5A decreased cdc18 transcript in HU block and on release
PMID:9303312	Fig5A, B decreased cdc18 transcript in HU block and on release
PMID:9303312	Fig5A, B level of cdc18 transcript does not decreased after release from HU block
PMID:9303312	Fig 5C
PMID:9303312	Fig5C rep2delta has no effect on cdc18 transcript levels in the absence of res2
PMID:9303312	Fig6A cdc18 transcript maximal around peak of septation
PMID:9303312	Fig6C
PMID:9303312	Fig6D
PMID:9303312	Fig6D
PMID:9303312	Fig6C
PMID:9303312	Fig7
PMID:9303312	Fig2 B
PMID:9303312	Fig8 C
PMID:9303312	Fig8 C
PMID:9303312	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	Fig7 res1 on multi copy pREP3X ON
PMID:9303312	Fig3C Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. NOT sure the data warrants an annotation
PMID:9303312	Fig7 res1 on multi copy pREP3X ON
PMID:9303312	Data not shown
PMID:9303312	Fig6B
PMID:9303312	Fig6B
PMID:9303312	Fig 1A and C cdc18 transcription is not dependent on cdc2 function
PMID:9303312	Fig 1 B cdc2-M26 has no detectable kinase activity in G1 at restrictive temperature
PMID:9303312	Fig 1D cdc2-M26 does not enter S phase even though cdc18 transcription is presence
PMID:9303312	Fig2 B
PMID:9303312	Fig2 B
PMID:9303312	Fig2 B cells do not undergo re replication at restrictive temperature
PMID:9303312	Fig2A cells do not undergo re replication at restrictive temperature but cdc18 transcript increases
PMID:9303312	Fig7 res1 on multi copy pREP3X ON
PMID:9303312	Fig2 B
PMID:9312055	fig 1c
PMID:9312055	fig 1b
PMID:9312055	fig 1b
PMID:9312055	fig 1b
PMID:9312055	fig 1b
PMID:9312055	fig 1b
PMID:9312055	fig 1c
PMID:9312055	fig 1c
PMID:9312055	fig 1c
PMID:9312055	fig 1c
PMID:9312055	fig 1c
PMID:9312055	fig 2
PMID:9312055	fig 2 (synthetic rescue)
PMID:9312055	fig 2 (synthetic rescue)
PMID:9312055	fig 3b
PMID:9312055	fig 3b
PMID:9312055	fig 3b
PMID:9312055	fig 3b (rescue)
PMID:9312055	fig 3b (rescue)
PMID:9312055	fig 4
PMID:9312055	fig 4
PMID:9312055	fig 4a
PMID:9312055	fig 4 b-d
PMID:9312055	fig 6
PMID:9312055	fig 6
PMID:9312055	fig7
PMID:9312055	poly...
PMID:9312055	fig9
PMID:9312055	fig9
PMID:9315645	fig7, sort of indirect - kinase dead mutant doesn't activate
PMID:9315645	"This one comes in ""from the side"", see Ladds, Bond post 2010 publication summary"
PMID:9321395	(Figure 4)
PMID:9321395	(Figure 4)
PMID:9321395	(Figure 4)
PMID:9321395	data not shown
PMID:9321395	An increased level of phosphotyrosine was detected on Spc1 in wis1􏰁 cells overexpressing Wis4∆N, but not in wis1∆ cells, indicating that the action of Wis4 is Wis1- dependent.
PMID:9321395	not shown
PMID:9321395	(Figure 4)
PMID:9321395	(Figure 5)
PMID:9321395	(Figure 5)
PMID:9321395	(Figure 5)
PMID:9321395	(Figure 5)
PMID:9325108	activated_by(CHEBI:18420)| activated_by(CHEBI:29035)
PMID:9325304	3B
PMID:9325304	3B
PMID:9325304	via purification assay
PMID:9325304	via purification assay
PMID:9325316	author intent
PMID:9325316	binds DNA in complex (2,3,11)
PMID:9325316	binds DNA in complex (2,3,11)
PMID:9325316	binds DNA in complex (2,3,11)
PMID:9325316	author intent
PMID:9325316	author intent
PMID:9325316	author intent
PMID:9325316	binds DNA on its own
PMID:9325316	author intent
PMID:9325316	author intent
PMID:9325316	author intent
PMID:9325316	author intent
PMID:9371883	two-hybrid assay
PMID:9371883	two-hybrid assay
PMID:9371883	two-hybrid assay
PMID:9371883	two-hybrid assay
PMID:9372936	assayed using SV40 NLS-GFP-LacZ reporter protein
PMID:9372936	same as rae1-167 single mutant
PMID:9372936	same as rae1-167 single mutant
PMID:9372936	assayed using SV40 NLS-GFP-LacZ reporter protein
PMID:9398669	nitrogen induced arrest
PMID:9398669	because slp1 can bypass wee1 it must independently inhibit cd2
PMID:9398669	add penetrance?
PMID:9398669	fig 5c switched from conjugtion freqeuncy to sterility as can only capture penetance on cell phenotypes
PMID:9398669	fig 5a
PMID:9398669	G1 phase nitrogen induced arrest
PMID:9398669	because slp1 can bypass wee1 it must independently inhibit cd2
PMID:9420333	(GTP bound)
PMID:9420333	Fig5B
PMID:9420333	Fig2A loss of cdc16 function does not affect cdc7 kinase activity
PMID:9420333	Fig3A,C spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	"Fig 1 vw interpretation for ""active form"""
PMID:9420333	Fig2A loss of spg1 function does not affect cdc7 kinase activity
PMID:9420333	Fig 6A in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	Fig3A,C spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	Fig5A
PMID:9420333	Fig5A
PMID:9420333	Fig 6C in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	cdc7 is associated with both SPBs when a short spindle is present
PMID:9420333	(IN gthis paper we don't actually know that it's the new one, that comes later, but ...)cdc7 is associated with both SPBs when a short spindle is present
PMID:9428701	MBP substrate, activated_by(CHEBI:29035)
PMID:9430640	Fig7B rum1 A58A62 mutant protein is unable to be phosphorylated by cdc2/cig1
PMID:9430640	Fig5
PMID:9430640	Fig1B
PMID:9430640	Fig1C Peaks at the end of G2 40 min before peak of rum1 protein
PMID:9430640	Fig1B
PMID:9430640	Fig2
PMID:9430640	Fig2
PMID:9430640	this isn't quite the right way to capture this target, still thinking
PMID:9430640	this isn't quite the right way to capture this target, still thinking
PMID:9430640	Fig 4B inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity
PMID:9430640	Fig1B
PMID:9430640	Fig 10
PMID:9430640	Fig7, Fig8 cdc2-cig1 complex efficiently phosphorylates rum1 T58T62 residues in vivo . Phosphorylation by cdc2-cig2 or cdc2-cdc13 only observed after a very long exposure
PMID:9430640	Fig6
PMID:9430640	Fig5B
PMID:9430640	Fig3C
PMID:9430640	Fig 4B inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity
PMID:9430640	Fig3C integrated copy
PMID:9430640	Fig3B, similar to rum1+OP more severe than either single mutant. expressed from muliticopy plasmid. Colonies were integrants
PMID:9430640	Fig3, data not shown phenotype similar to rum+OP
PMID:9450991	figure 1A
PMID:9450991	30x figure 4B
PMID:9450991	figure 4B
PMID:9450991	fig 4A
PMID:9450991	figure 1A
PMID:9450991	figure 2A/B
PMID:9450991	figure 1A
PMID:9450991	figure 1A
PMID:9450991	figure 1A
PMID:9459302	is this OK? its aseptate?
PMID:9468529	inhibited_by CHEBI:29035
PMID:9488736	looks very likely it is a ser/thr kinase, but if anything comes up that contradicts it this annotation can be made less specific
PMID:9491802	expressed Clostridium botulinum C3 protein to ADP-ribosylate Rho proteins including Rho1
PMID:9524127	(Fig. 3)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9524127	(Fig. 3a)
PMID:9531532	over 25
PMID:9531532	over 25
PMID:9531532	over 25
PMID:9531532	over 25
PMID:9531532	over 35
PMID:9535817	inferred from FYPO:0000825, FYPO:0001117, FYPO:0005743, FYPO:0007674 phenotypes (including conditions)
PMID:9552380	cig2-cdc2
PMID:9560390	osmotic stress
PMID:9560390	osmotic stress
PMID:9571240	4e
PMID:9571240	4e
PMID:9571240	Ste9 was indispensable for the growth of the wee1 cells, which had to lengthen the pre-Start G1 period to restrain DNA synthesis until the critical size to override Start control was attained....Ste9 might be required for main- tenance of the Cdc2 kinase in a pre-Start form, suggested by the fact that overexpression of Ste9 in- duced rereplication of the genome due to reduction of the mitotic kinase activity of the Cdc13/Cdc2 com- plex, and rereplication in the cdc2ts strain was pre- vented by the ste9 mutation.
PMID:9571240	fig3
PMID:9585506	western but we know this happens and I wanted to capture the extension
PMID:9585506	western but we know this happens and I wanted to capture the extension
PMID:9585506	salt stress
PMID:9585506	salt stress
PMID:9585506	salt stress
PMID:9585506	salt stress
PMID:9599405	PEHROMONE
PMID:9601094	fig 4B
PMID:9601094	fig 4B
PMID:9601094	(Fig. 4D
PMID:9601094	Fig 3C at metaphase/anaphase transiton
PMID:9601094	Fig 3C at metaphase/anaphase transiton
PMID:9601094	dph1∆ cells were not hypersensitive to TBZ, compared to wild-type cells (Fig. 6C)
PMID:9601094	figure 6
PMID:9601094	figure 6
PMID:9601094	figure 6
PMID:9601094	fig 2D
PMID:9601094	medium level of mph1 OEX (high is lethal)
PMID:9601094	fig 4B
PMID:9601094	Figure 4A
PMID:9606213	(slightly increased- In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes)
PMID:9606213	polarization, in shmoo DNS
PMID:9606213	DNS actin distributed in cytoplasm
PMID:9606213	fig1
PMID:9606213	fig1
PMID:9606213	fig1
PMID:9606213	polarization, during conjugation, in shmoo fig1. We interpret the data as indicating that F-actin is first cor- rectly localized to the tip in all fus1 mutants, but is then re- distributed after a defective attempt to fuse. Thus, it is likely that Fus1 is required for the correct organization and stabilization of polarized F-actin at the tip, but is no
PMID:9606213	By immunofluorescence, these antibod- ies stained a single dot at the very tip of each cell in wild- type pre-zygotes (Fig. 2, C and D).
PMID:9606213	fig7
PMID:9606213	Therefore, in a h90 mam2 strain, the P cells will attempt mating, but the M cells will be unable to respond due to the lack of the P-factor receptor, and so the cells will fail to initiate fusion
PMID:9606213	(slightly increased- In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes)
PMID:9606213	In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes
PMID:9614176	Fig5C
PMID:9614176	Fig5B
PMID:9614176	Fig5A
PMID:9614176	Fig4 - sows proteasome involvment as well
PMID:9614176	Fig2B after addition of P factor to nitrogen starved G1 arrested cells P factor does not further increase rum1 protein level. It is inferred that rum1 is required to maintain G1 arrest rather than bring it about.
PMID:9614176	Fig1 A
PMID:9614176	Fig3 A In absence of rum1 cdc2-cdc13 kinase activity remains high in presence of P factor
PMID:9614176	Fig3D loss of cig2 does not restore P factor induced G1 arrest
PMID:9614176	Fig4
PMID:9614176	Fig6A transcript assayed was Mat1-Mm
PMID:9614176	Fig5C
PMID:9614176	Fig5C
PMID:9614176	Fig5C
PMID:9614178	residue not determined experimentally, but probably Y173
PMID:9614178	residue not determined experimentally, but probably Y173
PMID:9614178	residue not determined experimentally, but probably Y173
PMID:9614178	residue not determined experimentally, but probably Y173
PMID:9614178	residue not determined experimentally, but probably Y173
PMID:9614178	residue not determined experimentally, but probably Y173
PMID:9622480	very mild as shown in xp
PMID:9635188	24 degrees
PMID:9635188	independent of F-actin (assayed using Latrunculin A)
PMID:9635188	29 degrees; permissive for either single mutant
PMID:9635188	independent of F-actin (assayed using Latrunculin A)
PMID:9635188	dependent on F-actin (assayed using Latrunculin A)
PMID:9635188	independent of F-actin (assayed using Latrunculin A)
PMID:9635190	(Fig 1i)
PMID:9635190	(Fig 1i)
PMID:9635190	Figure 2b
PMID:9635190	Figure 2c
PMID:9635190	cytoplasm during interphase (with nuclear localization)
PMID:9635190	fig 5 during mitotic M-phase
PMID:9635190	fig 5 during mitotic M-phase
PMID:9635190	cytoplasm in interphase (Figure 4a, I)
PMID:9635190	Figure 4b
PMID:9635190	fig 5 during mitotic M-phase
PMID:9635190	fig 5 during mitotic M-phase
PMID:9635190	fig 5 during mitotic M-phase
PMID:9635190	fig 5 during interphase
PMID:9635190	fig 5 during mitotic M-phase
PMID:9635190	Figure 2a
PMID:9635190	fig 5 during mitosis
PMID:9636183	same severity as wee1-50 alone
PMID:9658208	just to get the allele details of -P in the database
PMID:9660817	data not shown
PMID:9660817	data not shown
PMID:9660817	data not shown
PMID:9660818	including plasma membrane (GO:0005886)
PMID:9660818	assayed using myelin basic protein
PMID:9660818	when crossed with shk1delta overexpressing shk2+ or wild type
PMID:9660818	when crossed with partner overexpressing shk1-deltaN; normal in cross with wild type
PMID:9660818	same severity when crossed with wild type or shk1delta
PMID:9660818	assayed using myelin basic protein; interaction shown in separate experiment
PMID:9671458	h90 background
PMID:9671458	assayed in both h- and h90 backgrounds
PMID:9671458	h- background
PMID:9679144	Fig 3C cell length does not affect branching showing its not because cells are longer at high temp
PMID:9679144	Fig 3A-C pre NETO blocked cells do not branch if TBZ is added at shift down
PMID:9679144	Fig2C arrest released cells have NETO defect and do not branch.
PMID:9679144	Fig2C arrest released cells are pre NETO but only branch at low level.
PMID:9679144	Fig2C cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	Fig2C cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	Fig2B cells were pre NETO after temperature block
PMID:9679144	Fig2B cells were pre NETO after temperature block
PMID:9679144	Fig 6 F-actin localised to branch site in presence of TBZ
PMID:9679144	Fig5 C,D Fig 12 Normal protein localisation in presence of TBZ
PMID:9679144	Fig 11 in the absence of microtubules and actin
PMID:9679144	Fig 11 absence of microtubules
PMID:9679144	Fig 9 tea1 can relocalise to cell ends in absence of microtubules
PMID:9679144	Fig 8A-D Actin relocalisation to old or new cell end after microtubule disruption
PMID:9679144	Fig 6 abnormal septum in branched cell
PMID:9679144	Fig5 C,D
PMID:9679144	Fig 4 Short interphase microtubules located in the cell centre
PMID:9679144	Fig2 B cells were pre NETO after temperature block
PMID:9679144	Fig1 F, H cells were pre NETO after temperature block
PMID:9679144	Fig2A cdc25-22 arrest released cells ie post NETO do not branch
PMID:9693363	increased 25S/18S ration
PMID:9693384	probably Y173, but not determined experimentally
PMID:9693384	probably Y173, but not determined experimentally
PMID:9693384	probably Y173, but not determined experimentally
PMID:9718372	probably Y173, but not determined experimentally
PMID:9718372	probably Y173, but not determined experimentally
PMID:9718372	probably Y173, but not determined experimentally
PMID:9722643	fig5
PMID:9722643	fig3
PMID:9722643	table2
PMID:9722643	fig2
PMID:9722643	fig1
PMID:9722643	fig4
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	cdc18-1-141 when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	cdc18-150-577 when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	cdc18-150-577(T374A) when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	cdc1-577 (NTP) when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 2B cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig2B cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 3 the kinase assay substrate used is Histone H1
PMID:9739083	Fig 3 the kinase assay substrate used is Histone H1
PMID:9739083	data not shown the kinase assay substrate used is Histone H1
PMID:9739083	Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 3 not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot
PMID:9739083	Fig 3 not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	Data not shown Cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Data not shown Cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 5 cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations
PMID:9739083	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6 and cell phenotype data not shown. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9740803	can't use IPI because we don't have identifiers for human importin alpha or the GST-NLS construct
PMID:9740803	also assayed with GFP-NLS construct
PMID:9740803	actually combination of in vitro assay, interactions, and sequence similarity
PMID:9745017	inferred from decreased nda3 mRNA level
PMID:9745017	inferred from decreased nda3 mRNA level
PMID:9755169	Fig3A cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	Fig3B cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	Fig3B
PMID:9755169	Fig4C cd18 N term deletion can accumulate in a metaphase arrest
PMID:9755169	Fig4E cdc18 lacking cdc2 phosphorylation sites accumulates immediately as cells progress into mitosis
PMID:9755169	Fig5A nmt1 promoter OFF cdc18 is more stable when 5/6 P sites are mutated
PMID:9755169	Fig5B
PMID:9755169	Fig5B
PMID:9755169	Fig5C
PMID:9755169	Fig5D
PMID:9755169	Fig5C
PMID:9755169	Fig4C cd18 N term deletion can accumulate in a metaphase arrest
PMID:9755169	Fig 2C, cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	Fig 2C, cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	Fig 2C, cdc10 dependent transcription occurs during mitotic exit
PMID:9755190	requested chromatin silencing term but advised to use this one
PMID:9755190	requested chromatin silencing term but advised to use this one
PMID:9755190	vw: from chromatin organization to heterochromatin assembly : inconclusion this study implicates histone deacetylases in heterochromnatin assembly
PMID:9755190	vw: from chromatin organization to heterochromatin assembly : inconclusion this study implicates histone deacetylases in heterochromnatin assembly
PMID:9755190	requested chromatin silencing term but advised to use this one
PMID:9755190	vw: from chromatin organization to heterochromatin assembly : inconclusion this study implicates histone deacetylases in heterochromnatin assembly
PMID:9755190	requested chromatin silencing term but advised to use this one
PMID:9755190	requested chromatin silencing term but advised to use this one
PMID:9771717	not shown
PMID:9774107	fig 4a
PMID:9774107	fig 2 e
PMID:9774107	fig2
PMID:9774107	fig2
PMID:9774107	fig2e
PMID:9774107	fig2e
PMID:9774107	fig2
PMID:9774107	fig 4a
PMID:9774107	data not shown
PMID:9774107	fig2
PMID:9778252	Precise observation revealed that Mei2p dots could be visible in conjugating cells that completed cell fusion but did not undergo karyogamy yet.
PMID:9786952	fig 2b
PMID:9786952	4de
PMID:9786952	fig 2b
PMID:9786952	4ab
PMID:9786952	4a
PMID:9786952	4a
PMID:9786952	fig 2e
PMID:9786952	fig6
PMID:9786952	fig 2a
PMID:9790887	activated_by(CHEBI:18420), activated_by(CHEBI:29103)
PMID:9794798	mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+
PMID:9794798	mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+
PMID:9802907	ADVANCED I hope I got this right?A striking feature in dis1 mutant cells was that the back-and-forth cen1 DNA movements seen in phase 2 of wild-type cells were entirely absent. After spindle elongation (the SPB distance, 􏰆8 􏰈m), the cen1 signals were fused again and moved to one of the SPBs. Such prolonged centromere splitting while the spindle was elongating was never seen in wild-type or any of the other mutant cells examined so far.
PMID:9802907	(included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1–GFP) was expressed and found to be bound to the SPB throughout the cell cycle (Figure 1A), identical to immunolocalization data (Ha- gan and Yanagida, 1995)
PMID:9802907	(included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1–GFP) was expressed and found to be bound to the SPB throughout the cell cycle (Figure 1A), identical to immunolocalization data (Ha- gan and Yanagida, 1995)
PMID:9808627	(Fig. 2D)
PMID:9808627	G2 block
PMID:9808627	G1 block
PMID:9832516	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9832516	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9832516	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9832516	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9839953	low activity
PMID:9839953	at the second po- sition (Gal-Man-O)
PMID:9839953	at the second po- sition (Gal-Man-O)
PMID:9843572	figure 3 A&B
PMID:9843572	Figure 6B
PMID:9843572	Figure 7A
PMID:9843572	figure 3 B (additive)
PMID:9843572	Figure 8
PMID:9843572	Figure 8
PMID:9843572	Figure 9A
PMID:9843572	(Figure 3B)
PMID:9843572	(Figure 3B)
PMID:9843572	(Figure 3B)
PMID:9843572	(Figure 3B)
PMID:9843572	(Figure 1
PMID:9843572	figure 3 A&B
PMID:9843572	Figure 6A
PMID:9843577	single micrograph, so can't tell if they're viable
PMID:9843577	single micrograph, so can't tell if they're viable
PMID:9843966	neutral wrt viability because data not shown, so don't know if aseptate mononucleate cells are the same ones that manage to survive and eventually divide
PMID:9857040	biologically relevant? it can also cut these
PMID:9857040	biologically relevant? it can also cut these
PMID:9862966	Fig3 CD
PMID:9862966	https://github.com/pombase/fypo/issues/3931
PMID:9864354	Fig. 2 D
PMID:9864354	Fig. 2 E
PMID:9864354	Fig. 2 E
PMID:9864354	indicated by high level of H1 kinase activity
PMID:9872416	figure 2.
PMID:9872416	figure 2.
PMID:9872416	figure 2.
PMID:9872416	figure 2.
PMID:9872416	figure 2.
PMID:9872416	figure 2.
PMID:9872416	figure 2.
PMID:9891039	worse than cdc24-M38 alone (wt not shown)
PMID:9891039	worse than cdc24-M38 alone (wt not shown)
PMID:9891039	worse than cdc24-M38 alone (wt not shown)
PMID:9891039	worse than cdc24-M38 alone (wt not shown)
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without rad26delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without rad2delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9891047	temperature permissive for single mutant without cds1delta
PMID:9950674	fig 9
PMID:9950674	fig 9
PMID:9973368	galactose specific flocculation should have cell-cell ahdesion parentage
PMID:9973368	non-flocculating cells