HSC82/YMR186W Literature Guide Help

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

HSC82 - Strains/Constructs (92)

Results: 1 - 30 of 92 records
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ReferenceOther Genes Addressed
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
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
Dengjel J, et al.  (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035
Flom GA, et al.  (2012) Identification of an Hsp90 mutation that selectively disrupts cAMP/PKA signaling in Saccharomyces cerevisiae. Curr Genet 58(3):149-63
Kubota N, et al.  (2012) HSC90 is required for nascent hepatitis C virus core protein stability in yeast cells. FEBS Lett 586(16):2318-25
Lee CT, et al.  (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO J 31(6):1518-28
Pursell NW, et al.  (2012) Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth. Eukaryot Cell 11(8):1033-41
Robbins N, et al.  (2012) Lysine deacetylases Hda1 and Rpd3 regulate Hsp90 function thereby governing fungal drug resistance. Cell Rep 2(4):878-88
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
Francis BR and Thorsness PE  (2011) Hsp90 and mitochondrial proteases Yme1 and Yta10/12 participate in ATP synthase assembly in Saccharomyces cerevisiae. Mitochondrion 11(4):587-600
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Jung PP, et al.  (2011) Ploidy influences cellular responses to gross chromosomal rearrangements in Saccharomyces cerevisiae. BMC Genomics 12(1):331
Laskar S, et al.  (2011) HSP90 Controls SIR2 Mediated Gene Silencing. PLoS One 6(8):e23406
Sanada M, et al.  (2011) ROS production and apoptosis induction by formation of Gts1p-mediated protein aggregates. Biosci Biotechnol Biochem 75(8):1546-53
Suh MS, et al.  (2011) Aliphatic dipeptide tags for multi-2-plex protein quantification. Analyst 136(8):1614-9
Lopez-Garcia B, et al.  (2010) A genomic approach highlights common and diverse effects and determinants of susceptibility on the yeast Saccharomyces cerevisiae exposed to distinct antimicrobial peptides. BMC Microbiol 10():289
Millson SH, et al.  (2010) A simple yeast-based system for analyzing inhibitor resistance in the human cancer drug targets Hsp90alpha/beta. Biochem Pharmacol 79(11):1581-8
Mollapour M, et al.  (2010) Hsp90 phosphorylation, Wee1 and the cell cycle. Cell Cycle 9(12):2310-6
Reidy M and Masison DC  (2010) Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [PSI+] Prions by Hsp104. Mol Cell Biol 30(14):3542-52
Sekigawa M, et al.  (2010) Comprehensive screening of human genes with inhibitory effects on yeast growth and validation of a yeast cell-based system for screening chemicals. J Biomol Screen 15(4):368-78
Song H, et al.  (2010) Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals functional differences of AtHsp90s under abiotic stresses. J Plant Physiol 167(14):1172-1178
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
Wayne N, et al.  (2010) Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J Biol Chem 285(1):234-41
Anderson JB, et al.  (2009) Gene expression and evolution of antifungal drug resistance. Antimicrob Agents Chemother 53(5):1931-6
Gong Y, et al.  (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275
Hessling M, et al.  (2009) Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol 16(3):287-93
Narayanaswamy R, et al.  (2009) Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proc Natl Acad Sci U S A 106(25):10147-52
Nilapwar S, et al.  (2009) Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90. J Mol Biol 392(4):923-36
Retzlaff M, et al.  (2009) Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep 10(10):1147-53
Tsutsumi S, et al.  (2009) Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat Struct Mol Biol 16(11):1141-7
Results: 1 - 30 of 92 records
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