HSP82/YPL240C Literature Guide Help

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

HSP82 - Protein Processing/Modification/Regulation (28)

ReferenceOther Genes Addressed
Robbins N, et al.  (2012) Lysine deacetylases Hda1 and Rpd3 regulate Hsp90 function thereby governing fungal drug resistance. Cell Rep 2(4):878-88
Soroka J, et al.  (2012) Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation. Mol Cell 45(4):517-28
Stewart-Ornstein J, et al.  (2012) Cellular Noise Regulons Underlie Fluctuations in Saccharomyces cerevisiae. Mol Cell 45(4):483-93
Geiler-Samerotte KA, et al.  (2011) Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast. Proc Natl Acad Sci U S A 108(2):680-5
Helbig AO, et al.  (2011) The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae. Mol Biosyst 7(12):3316-26
Kim IS, et al.  (2011) Adaptive stress response to menadione-induced oxidative stress in Saccharomyces cerevisiae KNU5377. J Microbiol 49(5):816-23
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
Mollapour M, et al.  (2011) Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity. Oncotarget 2(5):407-17
Mollapour M, et al.  (2011) Threonine 22 phosphorylation attenuates hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell 41(6):672-81
Deluna A, et al.  (2010) Need-based up-regulation of protein levels in response to deletion of their duplicate genes. PLoS Biol 8(3):e1000347
Mollapour M, et al.  (2010) Hsp90 phosphorylation, Wee1 and the cell cycle. Cell Cycle 9(12):2310-6
Mollapour M, et al.  (2010) Swe1(Wee1)-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function. Mol Cell 37(3):333-343
Almeida B, et al.  (2009) Yeast protein expression profile during acetic acid-induced apoptosis indicates causal involvement of the TOR pathway. Proteomics 9(3):720-32
Park H, et al.  (2007) A novel class of Hsp90 inhibitors isolated by structure-based virtual screening. Bioorg Med Chem Lett 17(22):6345-9
Scroggins BT, et al.  (2007) An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol Cell 25(1):151-9
Wayne N and Bolon DN  (2007) Dimerization of Hsp90 Is Required for in Vivo Function: DESIGN AND ANALYSIS OF MONOMERS AND DIMERS. J Biol Chem 282(48):35386-95
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
Wandinger SK, et al.  (2006) The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J 25(2):367-76
Guo W, et al.  (2005) Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res 65(21):10006-15
Cox MB and Miller CA 3rd  (2004) Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling. Cell Stress Chaperones 9(1):4-20
Reverter-Branchat G, et al.  (2004) Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. J Biol Chem 279(30):31983-9
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
Rowlands MG, et al.  (2004) High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 327(2):176-83
Zhou W, et al.  (2004) Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J Biol Chem 279(31):32262-8
Cox MB and Miller CA 3rd  (2003) Pharmacological and genetic analysis of 90-kDa heat shock isoprotein-aryl hydrocarbon receptor complexes. Mol Pharmacol 64(6):1549-56
Lotz GP, et al.  (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35
Piper PW, et al.  (2003) Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast. Eur J Biochem 270(23):4689-95
Nadeau K, et al.  (1993) Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J Biol Chem 268(2):1479-87