Literature Help
SBA1 / YKL117W Literature
All manually curated literature for the specified gene, organized by relevance to the gene and by
association with specific annotations to the gene in SGD. SGD gathers references via a PubMed search for
papers whose titles or abstracts contain “yeast” or “cerevisiae;” these papers are reviewed manually and
linked to relevant genes and literature topics by SGD curators.
- Unique References
- 140
- Aliases
-
CST18
6
Primary Literature
Literature that either focuses on the gene or contains information about function, biological role,
cellular location, phenotype, regulation, structure, or disease homologs in other species for the gene
or gene product.
No primary literature curated.
Download References (.nbib)
- Fangaria N, et al. (2022) DNA damage-induced nuclear import of HSP90α is promoted by Aha1. Mol Biol Cell 33(14):ar140 PMID:36260391
- Biebl MM, et al. (2021) Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle. Nat Commun 12(1):828 PMID:33547294
- Hohrman K, et al. (2021) Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics 217(3) PMID:33789348
- Reidy M and Masison DC (2020) Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast. J Mol Biol 432(16):4673-4689 PMID:32565117
- Wang A, et al. (2020) Mechanism of Long-Range Chromosome Motion Triggered by Gene Activation. Dev Cell 52(3):309-320.e5 PMID:31902656
- Reidy M, et al. (2018) Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle. Genetics 209(4):1139-1154 PMID:29930177
- Daturpalli S, et al. (2017) Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins. J Mol Biol 429(9):1406-1423 PMID:28363677
- Valério E, et al. (2016) Proteomic and Real-Time PCR analyses of Saccharomyces cerevisiae VL3 exposed to microcystin-LR reveals a set of protein alterations transversal to several eukaryotic models. Toxicon 112:22-8 PMID:26806210
- Horvat NK, et al. (2014) A mutation in the catalytic loop of Hsp90 specifically impairs ATPase stimulation by Aha1p, but not Hch1p. J Mol Biol 426(12):2379-92 PMID:24726918
- Lancaster DL, et al. (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76 PMID:23148221
- Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 PMID:22842922
- Zelin E, et al. (2012) The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status. Mol Cell 48(3):459-70 PMID:23022381
- Echtenkamp FJ, et al. (2011) Global functional map of the p23 molecular chaperone reveals an extensive cellular network. Mol Cell 43(2):229-41 PMID:21777812
- Pullen L and Bolon DN (2011) Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo. J Biol Chem 286(13):11091-8 PMID:21278257
- Tapia H and Morano KA (2010) Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast. Mol Biol Cell 21(1):63-72 PMID:19889838
- Cha JY, et al. (2009) Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein. Cell Stress Chaperones 14(3):233-43 PMID:18800239
- Godin KS, et al. (2009) The box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme. J Mol Biol 390(2):231-44 PMID:19426738
- Forafonov F, et al. (2008) p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol Cell Biol 28(10):3446-56 PMID:18362168
- Toogun OA, et al. (2007) The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc Natl Acad Sci U S A 104(14):5765-70 PMID:17389357
- Ali MM, et al. (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440(7087):1013-7 PMID:16625188
- Cox MB and Miller CA (2004) Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling. Cell Stress Chaperones 9(1):4-20 PMID:15270073
- Richter K, et al. (2004) The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol 342(5):1403-13 PMID:15364569
- Cox MB and Miller CA (2002) The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system. Toxicol Lett 129(1-2):13-21 PMID:11879970
- Donzé O, et al. (2001) The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J 20(14):3771-80 PMID:11447118
- Freeman BC, et al. (2000) The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev 14(4):422-34 PMID:10691735
- Young JC and Hartl FU (2000) Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J 19(21):5930-40 PMID:11060043
- Donzé O and Picard D (1999) Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]. Mol Cell Biol 19(12):8422-32 PMID:10567567
- Knoblauch R and Garabedian MJ (1999) Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol Cell Biol 19(5):3748-59 PMID:10207098
- Ouspenski II, et al. (1999) New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res 27(15):3001-8 PMID:10454593
- Bohen SP (1998) Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins. Mol Cell Biol 18(6):3330-9 PMID:9584173
- Fang Y, et al. (1998) SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol 18(7):3727-34 PMID:9632755
- Dujon B, et al. (1994) Complete DNA sequence of yeast chromosome XI. Nature 369(6479):371-8 PMID:8196765
Related Literature
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Additional Literature
Papers that show experimental evidence for the gene or describe homologs in other species, but
for which the gene is not the paper’s principal focus.
No additional literature curated.
Download References (.nbib)
- Kaduhr L, et al. (2025) Diphthamide synthesis is linked to the eEF2-client chaperone machinery. FEBS Lett 599(9):1260-1268 PMID:39825589
- Giannoulis A, et al. (2021) Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance. J Phys Chem Lett 12(51):12235-12241 PMID:34928609
- Lanz MC, et al. (2021) In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Rep 22(2):e51121 PMID:33491328
- Seike T, et al. (2021) Random Transfer of Ogataea polymorpha Genes into Saccharomyces cerevisiae Reveals a Complex Background of Heat Tolerance. J Fungi (Basel) 7(4) PMID:33921057
- Keinan E, et al. (2018) High-Reynolds Microfluidic Sorting of Large Yeast Populations. Sci Rep 8(1):13739 PMID:30214051
- Sahasrabudhe P, et al. (2017) The Plasticity of the Hsp90 Co-chaperone System. Mol Cell 67(6):947-961.e5 PMID:28890336
- Gu X, et al. (2016) The Hsp90 Co-chaperones Sti1, Aha1, and P23 Regulate Adaptive Responses to Antifungal Azoles. Front Microbiol 7:1571 PMID:27761133
- Buck TM, et al. (2015) Expression of three topologically distinct membrane proteins elicits unique stress response pathways in the yeast Saccharomyces cerevisiae. Physiol Genomics 47(6):198-214 PMID:25759377
- Johnson JL, et al. (2014) Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones. Curr Genet 60(4):265-76 PMID:24923785
- Sung MK, et al. (2013) Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast. Genome Res 23(4):736-46 PMID:23403034
- Armstrong H, et al. (2012) The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. PLoS One 7(11):e49322 PMID:23166640
- Zuehlke AD and Johnson JL (2012) Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics 191(3):805-14 PMID:22505624
- Echeverría PC, et al. (2011) Detection of changes in gene regulatory patterns, elicited by perturbations of the Hsp90 molecular chaperone complex, by visualizing multiple experiments with an animation. BioData Min 4(1):15 PMID:21672238
- Franzosa EA, et al. (2011) Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. PLoS One 6(11):e28211 PMID:22140548
- Laskar S, et al. (2011) HSP90 controls SIR2 mediated gene silencing. PLoS One 6(8):e23406 PMID:21829731
- Li J, et al. (2011) Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol 18(1):61-6 PMID:21170051
- Esposito AM and Kinzy TG (2010) The eukaryotic translation elongation Factor 1Bgamma has a non-guanine nucleotide exchange factor role in protein metabolism. J Biol Chem 285(49):37995-8004 PMID:20926387
- Mandal AK, et al. (2010) Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell 21(9):1439-48 PMID:20237159
- Mollapour M, et al. (2010) Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol Cell 37(3):333-43 PMID:20159553
- Retzlaff M, et al. (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54 PMID:20159554
- Ghazal G, et al. (2009) Yeast RNase III triggers polyadenylation-independent transcription termination. Mol Cell 36(1):99-109 PMID:19818713
- Hainzl O, et al. (2009) The charged linker region is an important regulator of Hsp90 function. J Biol Chem 284(34):22559-67 PMID:19553666
- Hontz RD, et al. (2009) Genetic identification of factors that modulate ribosomal DNA transcription in Saccharomyces cerevisiae. Genetics 182(1):105-19 PMID:19270272
- Millson SH, et al. (2009) The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae. Yeast 26(6):339-47 PMID:19399909
- Wilcox AJ and Laney JD (2009) A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex. Nat Cell Biol 11(12):1481-6 PMID:19915556
- Trott A, et al. (2008) Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thiol-targeted molecule. Mol Biol Cell 19(3):1104-12 PMID:18199679
- Weeks SA and Miller DJ (2008) The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae. J Virol 82(4):2004-12 PMID:18057252
- Johnson JL, et al. (2007) Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol Cell Biol 27(2):768-76 PMID:17101799
- Catlett MG and Kaplan KB (2006) Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J Biol Chem 281(44):33739-48 PMID:16945921
- Millson SH, et al. (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4(5):849-60 PMID:15879519
- Siligardi G, et al. (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem 279(50):51989-98 PMID:15466438
- Kanelakis KC and Pratt WB (2003) Regulation of glucocorticoid receptor ligand-binding activity by the hsp90/hsp70-based chaperone machinery. Methods Enzymol 364:159-73 PMID:14631845
- Grandin N and Charbonneau M (2001) Hsp90 levels affect telomere length in yeast. Mol Genet Genomics 265(1):126-34 PMID:11370858
- Prodromou C, et al. (2000) The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J 19(16):4383-92 PMID:10944121
- Muñoz MJ, et al. (1999) The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts. Genetics 153(4):1561-72 PMID:10581266
- Maillet I, et al. (1996) Rapid identification of yeast proteins on two-dimensional gels. J Biol Chem 271(17):10263-70 PMID:8626593
- Fairhead C and Dujon B (1994) Transcript map of two regions from chromosome XI of Saccharomyces cerevisiae for interpretation of systematic sequencing results. Yeast 10(11):1403-13 PMID:7871880
Reviews
No reviews curated.
Download References (.nbib)
- Engler S and Buchner J (2025) The evolution and diversification of the Hsp90 co-chaperone system. Biol Chem PMID:40261701
- Rios EI, et al. (2024) Insights into Hsp90 mechanism and in vivo functions learned from studies in the yeast, Saccharomyces cerevisiae. Front Mol Biosci 11:1325590 PMID:38389899
- Backe SJ, et al. (2023) Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function. Essays Biochem 67(5):781-795 PMID:36912239
- Bhattacharya K and Picard D (2021) The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration. Cell Mol Life Sci 78(23):7257-7273 PMID:34677645
- Wickner RB, et al. (2019) Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems. Viruses 11(3) PMID:30857327
- Morano KA, et al. (2012) The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics 190(4):1157-95 PMID:22209905
- Verghese J, et al. (2012) Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol Mol Biol Rev 76(2):115-58 PMID:22688810
- Cox MB and Johnson JL (2011) The role of p23, Hop, immunophilins, and other co-chaperones in regulating Hsp90 function. Methods Mol Biol 787:45-66 PMID:21898226
- Wandinger SK, et al. (2008) The Hsp90 chaperone machinery. J Biol Chem 283(27):18473-7 PMID:18442971
Gene Ontology Literature
Paper(s) associated with one or more GO (Gene Ontology) terms in SGD for the specified gene.
No gene ontology literature curated.
Download References (.nbib)
- Zelin E, et al. (2012) The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status. Mol Cell 48(3):459-70 PMID:23022381
- Toogun OA, et al. (2007) The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc Natl Acad Sci U S A 104(14):5765-70 PMID:17389357
- Knoblauch R and Garabedian MJ (1999) Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol Cell Biol 19(5):3748-59 PMID:10207098
- Fang Y, et al. (1998) SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol 18(7):3727-34 PMID:9632755
Phenotype Literature
Paper(s) associated with one or more pieces of classical phenotype evidence in SGD for the specified gene.
No phenotype literature curated.
Download References (.nbib)
- Fangaria N, et al. (2022) DNA damage-induced nuclear import of HSP90α is promoted by Aha1. Mol Biol Cell 33(14):ar140 PMID:36260391
- Toogun OA, et al. (2007) The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc Natl Acad Sci U S A 104(14):5765-70 PMID:17389357
- Ouspenski II, et al. (1999) New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res 27(15):3001-8 PMID:10454593
Interaction Literature
Paper(s) associated with evidence supporting a physical or genetic interaction between the
specified gene and another gene in SGD. Currently, all interaction evidence is obtained from
BioGRID.
No interaction literature curated.
Download References (.nbib)
- Filali-Mouncef Y, et al. (2024) An APEX2-based proximity-dependent biotinylation assay with temporal specificity to study protein interactions during autophagy in the yeast Saccharomyces cerevisiae. Autophagy 20(10):2323-2337 PMID:38958087
- O'Brien MJ and Ansari A (2024) Protein interaction network revealed by quantitative proteomic analysis links TFIIB to multiple aspects of the transcription cycle. Biochim Biophys Acta Proteins Proteom 1872(1):140968 PMID:37863410
- Rani K, et al. (2024) Identification of a chaperone-code responsible for Rad51-mediated genome repair. J Biol Chem 300(6):107342 PMID:38705392
- Backe SJ, et al. (2023) Activation of autophagy depends on Atg1/Ulk1-mediated phosphorylation and inhibition of the Hsp90 chaperone machinery. Cell Rep 42(7):112807 PMID:37453059
- Cohen N, et al. (2023) A systematic proximity ligation approach to studying protein-substrate specificity identifies the substrate spectrum of the Ssh1 translocon. EMBO J 42(11):e113385 PMID:37073826
- Kolhe JA, et al. (2023) The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions. Mol Cell 83(12):2035-2044.e7 PMID:37295430
- Mercier R, et al. (2023) Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle. PLoS Genet 19(5):e1010772 PMID:37228112
- Michaelis AC, et al. (2023) The social and structural architecture of the yeast protein interactome. Nature 624(7990):192-200 PMID:37968396
- Biebl MM, et al. (2021) Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle. Nat Commun 12(1):828 PMID:33547294
- Hohrman K, et al. (2021) Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics 217(3) PMID:33789348
- Bartolec TK, et al. (2020) Cross-linking Mass Spectrometry Analysis of the Yeast Nucleus Reveals Extensive Protein-Protein Interactions Not Detected by Systematic Two-Hybrid or Affinity Purification-Mass Spectrometry. Anal Chem 92(2): 1874-1882. PMID:31851481
- Biebl MM, et al. (2020) Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation. Cell Rep 32(8):108063 PMID:32846121
- Reidy M and Masison DC (2020) Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast. J Mol Biol 432(16):4673-4689 PMID:32565117
- Bryant EE, et al. (2019) Rad5 dysregulation drives hyperactive recombination at replication forks resulting in cisplatin sensitivity and genome instability. Nucleic Acids Res 47(17):9144-9159 PMID:31350889
- Girstmair H, et al. (2019) The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range. Nat Commun 10(1):3626 PMID:31399574
- Reidy M, et al. (2018) Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle. Genetics 209(4):1139-1154 PMID:29930177
- Daturpalli S, et al. (2017) Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins. J Mol Biol 429(9):1406-1423 PMID:28363677
- Jungfleisch J, et al. (2017) A novel translational control mechanism involving RNA structures within coding sequences. Genome Res 27(1):95-106 PMID:27821408
- Lapointe CP, et al. (2017) Architecture and dynamics of overlapped RNA regulatory networks. RNA 23(11):1636-1647 PMID:28768715
- Zuehlke AD, et al. (2017) An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans. Nat Commun 8:15328 PMID:28537252
- Costanzo M, et al. (2016) A global genetic interaction network maps a wiring diagram of cellular function. Science 353(6306) PMID:27708008
- Echtenkamp FJ, et al. (2016) Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler. Mol Cell 64(5):888-899 PMID:27818141
- Woodford MR, et al. (2016) Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors. Cell Rep 14(4):872-884 PMID:26804907
- Zierer BK, et al. (2016) Importance of cycle timing for the function of the molecular chaperone Hsp90. Nat Struct Mol Biol 23(11):1020-1028 PMID:27723736
- Ho KL, et al. (2015) A role for the budding yeast separase, Esp1, in Ty1 element retrotransposition. PLoS Genet 11(3):e1005109 PMID:25822502
- Lapointe CP, et al. (2015) Protein-RNA networks revealed through covalent RNA marks. Nat Methods 12(12):1163-70 PMID:26524240
- Johnson JL, et al. (2014) Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones. Curr Genet 60(4):265-76 PMID:24923785
- Mollapour M, et al. (2014) Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors. Mol Cell 53(2):317-29 PMID:24462205
- Ratzke C, et al. (2014) Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery. Nat Commun 5:4192 PMID:24947016
- Freeberg MA, et al. (2013) Pervasive and dynamic protein binding sites of the mRNA transcriptome in Saccharomyces cerevisiae. Genome Biol 14(2):R13 PMID:23409723
- Lancaster DL, et al. (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76 PMID:23148221
- Mitchell SF, et al. (2013) Global analysis of yeast mRNPs. Nat Struct Mol Biol 20(1):127-33 PMID:23222640
- Qiu J, et al. (2013) Coupling of mitochondrial import and export translocases by receptor-mediated supercomplex formation. Cell 154(3):596-608 PMID:23911324
- Snider J, et al. (2013) Mapping the functional yeast ABC transporter interactome. Nat Chem Biol 9(9):565-72 PMID:23831759
- Armstrong H, et al. (2012) The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. PLoS One 7(11):e49322 PMID:23166640
- Zuehlke AD and Johnson JL (2012) Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics 191(3):805-14 PMID:22505624
- Echtenkamp FJ, et al. (2011) Global functional map of the p23 molecular chaperone reveals an extensive cellular network. Mol Cell 43(2):229-41 PMID:21777812
- Mollapour M, et al. (2011) Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell 41(6):672-81 PMID:21419342
- Scherrer T, et al. (2011) Defining potentially conserved RNA regulons of homologous zinc-finger RNA-binding proteins. Genome Biol 12(1):R3 PMID:21232131
- Stirling PC, et al. (2011) The complete spectrum of yeast chromosome instability genes identifies candidate CIN cancer genes and functional roles for ASTRA complex components. PLoS Genet 7(4):e1002057 PMID:21552543
- Costanzo M, et al. (2010) The genetic landscape of a cell. Science 327(5964):425-31 PMID:20093466
- Kaake RM, et al. (2010) Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy. J Proteome Res 9(4):2016-29 PMID:20170199
- Mandal AK, et al. (2010) Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell 21(9):1439-48 PMID:20237159
- Mollapour M, et al. (2010) Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol Cell 37(3):333-43 PMID:20159553
- Retzlaff M, et al. (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54 PMID:20159554
- Batisse J, et al. (2009) Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure. J Biol Chem 284(50):34911-7 PMID:19840948
- Forafonov F, et al. (2008) p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol Cell Biol 28(10):3446-56 PMID:18362168
- Yu H, et al. (2008) High-quality binary protein interaction map of the yeast interactome network. Science 322(5898):104-10 PMID:18719252
- Collins SR, et al. (2007) Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446(7137):806-10 PMID:17314980
- Haarer B, et al. (2007) Modeling complex genetic interactions in a simple eukaryotic genome: actin displays a rich spectrum of complex haploinsufficiencies. Genes Dev 21(2):148-59 PMID:17167106
- Johnson JL, et al. (2007) Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol Cell Biol 27(2):768-76 PMID:17101799
- McClellan AJ, et al. (2007) Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131(1):121-35 PMID:17923092
- Ali MM, et al. (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440(7087):1013-7 PMID:16625188
- Krogan NJ, et al. (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440(7084):637-43 PMID:16554755
- Flom G, et al. (2005) Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae. Curr Genet 47(6):368-80 PMID:15871019
- Menon BB, et al. (2005) Reverse recruitment: the Nup84 nuclear pore subcomplex mediates Rap1/Gcr1/Gcr2 transcriptional activation. Proc Natl Acad Sci U S A 102(16):5749-54 PMID:15817685
- Millson SH, et al. (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4(5):849-60 PMID:15879519
- Lee P, et al. (2004) Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol Biol Cell 15(4):1785-92 PMID:14742721
- Millson SH, et al. (2004) Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach. Cell Stress Chaperones 9(4):359-68 PMID:15633294
- Richter K, et al. (2004) The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol 342(5):1403-13 PMID:15364569
- Siligardi G, et al. (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem 279(50):51989-98 PMID:15466438
- Fang Y, et al. (1998) SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol 18(7):3727-34 PMID:9632755
- Obermann WM, et al. (1998) In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol 143(4):901-10 PMID:9817749
Regulation Literature
Paper(s) associated with one or more pieces of regulation evidence in SGD, as found on the
Regulation page.
No regulation literature curated.
Post-translational Modifications Literature
Paper(s) associated with one or more pieces of post-translational modifications evidence in SGD.
No post-translational modifications literature curated.
Download References (.nbib)
- Leutert M, et al. (2023) The regulatory landscape of the yeast phosphoproteome. Nat Struct Mol Biol 30(11):1761-1773 PMID:37845410
- Bhagwat NR, et al. (2021) SUMO is a pervasive regulator of meiosis. Elife 10 PMID:33502312
- Lanz MC, et al. (2021) In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Rep 22(2):e51121 PMID:33491328
- Zhou X, et al. (2021) Cross-compartment signal propagation in the mitotic exit network. Elife 10 PMID:33481703
- Weinert BT, et al. (2013) Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep 4(4):842-51 PMID:23954790
- Henriksen P, et al. (2012) Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol Cell Proteomics 11(11):1510-22 PMID:22865919
Functional Complementation Annotations Literature
Paper(s) associated with one or more pieces of functional complementation annotations evidence in SGD.
No functional complementation annotations literature curated.
High-Throughput Literature
Paper(s) associated with one or more pieces of high-throughput evidence in SGD.
No high-throughput literature curated.
Download References (.nbib)
- Mondeel TDGA, et al. (2019) ChIP-exo analysis highlights Fkh1 and Fkh2 transcription factors as hubs that integrate multi-scale networks in budding yeast. Nucleic Acids Res 47(15):7825-7841 PMID:31299083
- Hoepfner D, et al. (2014) High-resolution chemical dissection of a model eukaryote reveals targets, pathways and gene functions. Microbiol Res 169(2-3):107-20 PMID:24360837
- Ostrow AZ, et al. (2014) Fkh1 and Fkh2 bind multiple chromosomal elements in the S. cerevisiae genome with distinct specificities and cell cycle dynamics. PLoS One 9(2):e87647 PMID:24504085
- Davey HM, et al. (2012) Genome-wide analysis of longevity in nutrient-deprived Saccharomyces cerevisiae reveals importance of recycling in maintaining cell viability. Environ Microbiol 14(5):1249-60 PMID:22356628
- Pir P, et al. (2012) The genetic control of growth rate: a systems biology study in yeast. BMC Syst Biol 6:4 PMID:22244311
- Qian W, et al. (2012) The genomic landscape and evolutionary resolution of antagonistic pleiotropy in yeast. Cell Rep 2(5):1399-410 PMID:23103169
- Venters BJ, et al. (2011) A comprehensive genomic binding map of gene and chromatin regulatory proteins in Saccharomyces. Mol Cell 41(4):480-92 PMID:21329885
- Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8 PMID:18622397
- Jin R, et al. (2008) Large-scale analysis of yeast filamentous growth by systematic gene disruption and overexpression. Mol Biol Cell 19(1):284-96 PMID:17989363
- Hu Z, et al. (2007) Genetic reconstruction of a functional transcriptional regulatory network. Nat Genet 39(5):683-7 PMID:17417638
- Proszynski TJ, et al. (2005) A genome-wide visual screen reveals a role for sphingolipids and ergosterol in cell surface delivery in yeast. Proc Natl Acad Sci U S A 102(50):17981-6 PMID:16330752
- Lum PY, et al. (2004) Discovering modes of action for therapeutic compounds using a genome-wide screen of yeast heterozygotes. Cell 116(1):121-37 PMID:14718172
- Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 PMID:12140549
- Hanway D, et al. (2002) Previously uncharacterized genes in the UV- and MMS-induced DNA damage response in yeast. Proc Natl Acad Sci U S A 99(16):10605-10 PMID:12149442
- Ouspenski II, et al. (1999) New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res 27(15):3001-8 PMID:10454593