HSC82/YMR186W Literature Guide Help

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

HSC82 - Primary Literature (89)

Results: 1 - 30 of 89 records
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ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Hsieh YY, et al.  (2013) Hsp90 regulates nongenetic variation in response to environmental stress. Mol Cell 50(1):82-92
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
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
Naicker MC, et al.  (2012) Identification of chaperones in freeze tolerance in Saccharomyces cerevisiae. J Microbiol 50(5):882-7
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
Schmid AB, et al.  (2012) The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J 31(6):1506-17
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
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
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
Sakurai H and Ota A  (2011) Regulation of chaperone gene expression by heat shock transcription factor in Saccharomyces cerevisiae: importance in normal cell growth, stress resistance, and longevity. FEBS Lett 585(17):2744-8
Street TO, et al.  (2011) Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol Cell 42(1):96-105
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
Ohlmeier S, et al.  (2010) Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae. Electrophoresis 31(17):2869-81
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
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
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
Wayne N, et al.  (2010) Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J Biol Chem 285(1):234-41
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
Krukenberg KA, et al.  (2009) Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Sci 18(9):1815-27
Millson SH, et al.  (2009) The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae. Yeast 26(6):339-47
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 89 records
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