HSP82/YPL240C Literature Guide Help

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

HSP82 - Protein/Nucleic Acid Structure (32)

Results: 1 - 30 of 32 records
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ReferenceOther Genes Addressed
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
Lee CT, et al.  (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO J 31(6):1518-28
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
Schmid AB, et al.  (2012) The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J 31(6):1506-17
Hagn F, et al.  (2011) Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.LID - 10.1038/nsmb.2114 [doi] Nat Struct Mol Biol ()
Hietpas RT, et al.  (2011) Experimental illumination of a fitness landscape. Proc Natl Acad Sci U S A 108(19):7896-901
Krukenberg KA, et al.  (2011) Conformational dynamics of the molecular chaperone Hsp90. Q Rev Biophys 44(2):229-55
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
Retzlaff M, et al.  (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54
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
Immormino RM, et al.  (2009) Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. J Mol Biol 388(5):1033-42
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
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
Zhang M, et al.  (2008) Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes. EMBO J 27(20):2789-98
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
Ali MM, et al.  (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440(7087):1013-7
Guo W, et al.  (2006) The bioreduction of a series of benzoquinone ansamycins by NAD(P)H:quinone oxidoreductase 1 to more potent heat shock protein 90 inhibitors, the hydroquinone ansamycins. Mol Pharmacol 70(4):1194-203
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
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
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
Siligardi G, et al.  (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem 279(50):51989-98
Meyer P, et al.  (2003) Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell 11(3):647-58
Wegele H, et al.  (2003) Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90. J Biol Chem 278(41):39303-10
Prodromou C, et al.  (2000) The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J 19(16):4383-92
Roe SM, et al.  (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42(2):260-6
Obermann WM, et al.  (1998) In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol 143(4):901-10
Results: 1 - 30 of 32 records
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