HSC82/YMR186W Literature Guide Help

Other names published for HSC82: HSP90, Hsp90 family chaperone HSC82, YMR186W

HSC82 - Protein Processing/Modification/Regulation (21)

ReferenceOther Genes Addressed
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
Kim KH, et al.  (2011) Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome. Mol Cells 31(2):151-8
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
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
Esposito AM and Kinzy TG  (2010) The Eukaryotic Translation Elongation Factor 1B{gamma} Has a Non-guanine Nucleotide Exchange Factor Role in Protein Metabolism. J Biol Chem 285(49):37995-8004
Kim IS, et al.  (2010) A cyclophilin A CPR1 overexpression enhances stress acquisition in Saccharomyces cerevisiae. Mol Cells 29(6):567-74
Mollapour M, et al.  (2010) Hsp90 phosphorylation, Wee1 and the cell cycle. Cell Cycle 9(12):2310-6
Ohlmeier S, et al.  (2010) Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae. Electrophoresis 31(17):2869-81
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
Lin FM, et al.  (2009) Temporal quantitative proteomics of Saccharomyces cerevisiae in response to a nonlethal concentration of furfural. Proteomics 9(24):5471-83
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
Tagwerker C, et al.  (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48
Wandinger SK, et al.  (2006) The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J 25(2):367-76
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
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