HSP82/YPL240C Literature Guide Help

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

HSP82 - Protein Physical Properties (34)

Results: 1 - 30 of 34 records
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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
Lee CT, et al.  (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO J 31(6):1518-28
Mendonca YA and Ramos CH  (2012) Cloning, purification and characterization of a 90kDa heat shock protein from Citrus sinensis (sweet orange). Plant Physiol Biochem 50(1):87-94
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
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
Mollapour M, et al.  (2011) Threonine 22 phosphorylation attenuates hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell 41(6):672-81
Pullen L and Bolon DN  (2011) Enforced N-domain Proximity Stimulates Hsp90 ATPase Activity and Is Compatible with Function in Vivo. J Biol Chem 286(13):11091-8
Street TO, et al.  (2011) Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol Cell 42(1):96-105
Day JE, et al.  (2010) Inhibition of hsp90 with resorcylic Acid macrolactones: synthesis and binding studies. Chemistry 16(34):10366-72
Retzlaff M, et al.  (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54
Wayne N, et al.  (2010) Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J Biol Chem 285(1):234-41
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
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
Hainzl O, et al.  (2009) The charged linker region is an important regulator of Hsp90 function. J Biol Chem 284(34):22559-67
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
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
Li J, et al.  (2009) Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading. J Biol Chem 284(35):23852-9
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
Prodromou C, et al.  (2009) Structural basis of the radicicol resistance displayed by a fungal hsp90. ACS Chem Biol 4(4):289-97
Spichty M, et al.  (2009) The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts. Biophys Chem 143(3):111-23
Vaughan CK, et al.  (2009) A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J 276(1):199-209
Richter K, et al.  (2006) Intrinsic inhibition of the Hsp90 ATPase activity. J Biol Chem 281(16):11301-11
Guo W, et al.  (2005) Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res 65(21):10006-15
Hainzl O, et al.  (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73
Meyer P, et al.  (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23(3):511-9
Meyer P, et al.  (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23(6):1402-10
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
Rowlands MG, et al.  (2004) High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 327(2):176-83
Salek RM, et al.  (2002) Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone. J Biomol NMR 23(4):327-8
Results: 1 - 30 of 34 records
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