ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.
about
Heterozygous yeast deletion collection screens reveal essential targets of Hsp90Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein - The role of hsp90Hsp90: a specialized but essential protein-folding toolHsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cellsAha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperoneDynamic regulation of p53 subnuclear localization and senescence by MORC3Identification of a novel HSP70-binding cochaperone critical to HSP90-mediated activation of small serine/threonine kinaseS-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activitiesA proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinChronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation.Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptorThe ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domainsThe molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasomeParalog Specific Hsp90 Inhibitors - A Brief History and a Bright FutureReview: The HSP90 molecular chaperone-an enigmatic ATPaseThe 'active life' of Hsp90 complexesGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumTargeting Hsp90 in urothelial carcinomaHsp90 selectively modulates phenotype in vertebrate developmentIdentification of Cellular Proteome Modifications in Response to West Nile Virus InfectionStructural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity ReceptorsStructural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismSynthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90Chaperone ligand-discrimination by the TPR-domain protein Tah1.Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha.Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.Sti1 is a novel activator of the Ssa proteins.A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).Hsp90 is regulated by a switch point in the C-terminal domainThe phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 FunctionMechanistic Asymmetry in Hsp90 DimersThe FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
P2860
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P2860
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@ast
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@en
type
label
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@ast
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@en
prefLabel
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@ast
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@en
P2093
P2860
P356
P1433
P1476
ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/17.16.4829
P407
P577
1998-08-01T00:00:00Z