HSC82/YMR186W Literature Guide Help

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

HSC82 - Substrates/Ligands/Cofactors (23)

ReferenceOther Genes Addressed
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Day JE, et al.  (2010) Inhibition of hsp90 with resorcylic Acid macrolactones: synthesis and binding studies. Chemistry 16(34):10366-72
Jarosz DF and Lindquist S  (2010) Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 330(6012):1820-4
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
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
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
Vaughan CK, et al.  (2009) A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J 276(1):199-209
Cunningham CN, et al.  (2008) Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J Biol Chem 283(30):21170-8
Southworth DR and Agard DA  (2008) Species-dependent ensembles of conserved conformational States define the Hsp90 chaperone ATPase cycle. Mol Cell 32(5):631-40
McClellan AJ, et al.  (2007) Diverse cellular functions of the hsp90 molecular chaperone uncovered using systems approaches. Cell 131(1):121-35
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
Papamichael K, et al.  (2006) Effect of the Hsp90 modulators on the heat-shock response in eukaryotic cells. Folia Microbiol (Praha) 51(1):33-7
Proisy N, et al.  (2006) Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol. Chem Biol 13(11):1203-15
Wegele H, et al.  (2006) Substrate transfer from the chaperone Hsp70 to Hsp90. J Mol Biol 356(3):802-11
Cheung KM, et al.  (2005) The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg Med Chem Lett 15(14):3338-43
Cowen LE and Lindquist S  (2005) Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 309(5744):2185-9
Hainzl O, et al.  (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73
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
Abbas-Terki T, et al.  (2001) Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol 21(22):7569-75
Liu XD, et al.  (1999) The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J Biol Chem 274(38):26654-60
Scheibel T, et al.  (1998) Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc Natl Acad Sci U S A 95(4):1495-9