Conserved conformational changes in the ATPase cycle of human Hsp90.
about
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognitionContribution of chaperones to STAT pathway signaling.Hsp90 is regulated by a switch point in the C-terminal domainElucidation of the Hsp90 C-terminal inhibitor binding siteExploring the Functional Complementation between Grp94 and Hsp90The Hsp90 machinery facilitates the transport of diphtheria toxin into human cellsA novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxinA review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesBiological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.Production and purification of human Hsp90β in Escherichia coli.Downregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegansIdentification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIPSTAT3 interacts directly with Hsp90.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen.Resolving hot spots in the C-terminal dimerization domain that determine the stability of the molecular chaperone Hsp90A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityConformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment.Crowding Activates Heat Shock Protein 90.A stress protein interface of innate immunity.New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.Conformational dynamics of the molecular chaperone Hsp90HSP90: chaperone-me-not.Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90.Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.Destabilizing RET in targeted treatment of thyroid cancers.ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.The Mechanism of Hsp90 ATPase Stimulation by Aha1Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.Hop/Sti1 phosphorylation inhibits its co-chaperone function.The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein.
P2860
Q24297748-C7C3C4F7-E26B-4738-9EED-38B62B7F96DDQ27687561-9E25C3D8-93BD-4624-8C56-86B8C9354377Q27933174-182789A9-19FC-4891-BE5E-C3FF4FDFB9D9Q28236934-5DB623C5-2BA0-44C7-9643-189F51A1DBB6Q28553251-0EE368E8-6F3F-4A2C-B098-E2C85688E0D5Q30313276-BCB5957A-486B-4686-9D78-B17387812AEBQ30315590-C87D25EA-A69C-4A27-910E-0A31108E05E8Q30402024-BE822446-62B7-4953-A7C2-FC35D90553B3Q33581226-39137880-469A-45DA-BFEE-409FCF6291F4Q33692255-720ADE73-F812-4452-B2B8-FCF8292C575CQ33721206-216AA7D7-DCC3-40D5-8C76-C1C0CDBB6E5FQ33834707-3DA2C8CA-35A4-49E3-9F13-A7CD62BB3A50Q34043288-CD25C452-34BA-41EC-A4F8-308BF044BC02Q34048681-0205A41B-CF3B-4C4E-9A32-CB929FF93BC3Q34136959-325168EE-3C37-4170-B626-FCB6FD864F25Q34280087-A805A05B-9BB5-4FFE-A07A-EC20120F7990Q34544082-4D410B69-13B5-4056-AF16-A777AED55F2FQ35156305-21F345B4-2529-4BC3-9084-6FAEC7425C2DQ35384807-4BB71935-4722-45D1-B917-2C853D36E7C5Q35764464-2EB13F8D-5D3B-47D7-8A2A-1694E58D8717Q35796269-7587BA44-F683-4B8F-B1CF-291C38565364Q35800838-69FDB4CE-D5B0-4641-9E1E-AEC5285E078BQ36744829-23128635-83BE-4227-99D5-F577E218D259Q37016452-5319BCDA-5B8A-4BE3-964E-B4DD6CE1F669Q37215989-9EE882D1-9C78-4965-95B0-B88C2CC4EE07Q37661766-E72BF8D8-AE4B-4E36-B778-F70E0EC5E7DCQ37854116-76132EB7-D0A0-4BF4-A793-0E41BDDB6DC3Q38125419-B76D41DE-4CCF-447D-B59C-6457FAEBA3F0Q38629563-6908119D-3D32-4803-ACEE-BFC3F778688AQ38735183-C663A42C-C44B-45F2-A9A0-EF83BE80FCB0Q38819099-E4B77B53-EC5F-4363-A4D2-606DD3FDCFCFQ39670676-3E23BC39-93D1-49F7-AE9B-55D79A37C3BAQ41063812-03FC95D9-99F3-46F7-8A66-40EE5CFFCD68Q41198216-E335F38F-86B8-4F75-A91E-4FCCF19342F2Q41281023-F6027AAC-50F8-47D9-856E-70DE890F652DQ41329945-12CC52F2-876B-41CF-A286-5AC9B13C5314Q41792117-5861DE0C-4FD7-44E2-885D-1253CBBD706CQ41792131-66394C72-EB90-406C-BC6D-7037DFB86C0CQ41854369-BD8F02C1-A7ED-4588-8214-320DA7BAD2ECQ41987647-7493DDE4-CC3A-432A-BCB8-AB5D44718A0A
P2860
Conserved conformational changes in the ATPase cycle of human Hsp90.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
Conserved conformational changes in the ATPase cycle of human Hsp90.
@en
Conserved conformational changes in the ATPase cycle of human Hsp90.
@nl
type
label
Conserved conformational changes in the ATPase cycle of human Hsp90.
@en
Conserved conformational changes in the ATPase cycle of human Hsp90.
@nl
prefLabel
Conserved conformational changes in the ATPase cycle of human Hsp90.
@en
Conserved conformational changes in the ATPase cycle of human Hsp90.
@nl
P2093
P2860
P356
P1476
Conserved conformational changes in the ATPase cycle of human Hsp90.
@en
P2093
Adriane Leskovar
Joanna Soroka
Jochen Reinstein
Johannes Buchner
Martin Hessling
P2860
P304
17757-17765
P356
10.1074/JBC.M800540200
P407
P577
2008-04-09T00:00:00Z