HSP82/YPL240C Literature Guide Help

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

HSP82 - Substrates/Ligands/Cofactors (50)

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ReferenceOther Genes Addressed
Armstrong H, et al.  (2012) The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922. PLoS One 7(11):e49322
Morra G, et al.  (2012) Corresponding Functional Dynamics across the Hsp90 Chaperone Family: Insights from a Multiscale Analysis of MD Simulations. PLoS Comput Biol 8(3):e1002433
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Mollapour M, et al.  (2011) Threonine 22 phosphorylation attenuates hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell 41(6):672-81
Vallee F, et al.  (2011) Tricyclic series of heat shock protein 90 (Hsp90) inhibitors part I: discovery of tricyclic imidazo[4,5-c]pyridines as potent inhibitors of the Hsp90 molecular chaperone. J Med Chem 54(20):7206-19
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
Retzlaff M, et al.  (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54
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
DeZwaan DC, et al.  (2009) The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states. Nat Struct Mol Biol 16(7):711-6
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
Mickler M, et al.  (2009) The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol 16(3):281-6
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
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
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
Ali MM, et al.  (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440(7087):1013-7
Avila C, et al.  (2006) High-throughput screening for Hsp90 ATPase inhibitors. Bioorg Med Chem Lett 16(11):3005-8
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
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
Richter K, et al.  (2006) Intrinsic inhibition of the Hsp90 ATPase activity. J Biol Chem 281(16):11301-11
Wegele H, et al.  (2006) Substrate transfer from the chaperone Hsp70 to Hsp90. J Mol Biol 356(3):802-11
Zhao R, et al.  (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27
Hainzl O, et al.  (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73
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
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
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