HSP82/YPL240C Literature Guide Help

Other names published for HSP82: HSP90, Hsp90 family chaperone HSP82, YPL240C

HSP82 - Function/Process (110)

Results: 1 - 30 of 110 records
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ReferenceOther Genes Addressed
Chen G, et al.  (2012) Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy.LID - 10.1038/nature10795 [doi] Nature ()
Cunningham CN, et al.  (2012) The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis. Protein Sci 21(8):1162-71
Pursell NW, et al.  (2012) Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth. Eukaryot Cell 11(8):1033-41
Tsutsumi S, et al.  (2012) Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity. Proc Natl Acad Sci U S A 109(8):2937-42
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Laskar S, et al.  (2011) HSP90 Controls SIR2 Mediated Gene Silencing. PLoS One 6(8):e23406
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
Morell M, et al.  (2011) Linking amyloid protein aggregation and yeast survival. Mol Biosyst 7(4):1121-8
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
Vallee F, et al.  (2011) Tricyclic series of heat shock protein 90 (Hsp90) inhibitors part I: discovery of tricyclic imidazo[4,5-c]pyridines as potent inhibitors of the Hsp90 molecular chaperone. J Med Chem 54(20):7206-19
Walter GM, et al.  (2011) Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. J Biol Chem 286(47):40486-93
Jarosz DF and Lindquist S  (2010) Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 330(6012):1820-4
Ma M and Liu LZ  (2010) Quantitative transcription dynamic analysis reveals candidate genes and key regulators for ethanol tolerance in Saccharomyces cerevisiae. BMC Microbiol 10():169
Mollapour M, et al.  (2010) Swe1(Wee1)-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function. Mol Cell 37(3):333-343
Rowlands M, et al.  (2010) Detection of the ATPase Activity of the Molecular Chaperones Hsp90 and Hsp72 Using the TranscreenerTM ADP Assay Kit. J Biomol Screen 15(3):279-86
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
DeZwaan DC, et al.  (2009) The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states. Nat Struct Mol Biol 16(7):711-6
Hainzl O, et al.  (2009) The charged linker region is an important regulator of Hsp90 function. J Biol Chem 284(34):22559-67
Mickler M, et al.  (2009) The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol 16(3):281-6
Retzlaff M, et al.  (2009) Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep 10(10):1147-53
Vaughan CK, et al.  (2009) A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J 276(1):199-209
Dudgeon DD, et al.  (2008) Nonapoptotic Death of Saccharomyces cerevisiae Cells That Is Stimulated by Hsp90 and Inhibited by Calcineurin and Cmk2 in Response to Endoplasmic Reticulum Stresses. Eukaryot Cell 7(12):2037-2051
Rancati G, et al.  (2008) Aneuploidy underlies rapid adaptive evolution of yeast cells deprived of a conserved cytokinesis motor. Cell 135(5):879-93
Toogun OA, et al.  (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28(1):457-67
Zhao R, et al.  (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 180(3):563-78
Fan Q, et al.  (2007) The Role of Sse1 in the de Novo Formation and Variant Determination of the [PSI+] Prion. Genetics 177(3):1583-93
Gray JV and Krause SA  (2007) Identifying in vivo pathways using genome-wide genetic networks. Biochem Soc Trans 35(Pt 6):1538-41
Hawle P, et al.  (2007) Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p). Eukaryot Cell 6(3):521-32
McClellan AJ, et al.  (2007) Diverse cellular functions of the hsp90 molecular chaperone uncovered using systems approaches. Cell 131(1):121-35
Pagant S, et al.  (2007) Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol Biol Cell 18(9):3398-413
Results: 1 - 30 of 110 records
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