ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. - Wikidata - awgldk - TriplyDB

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.

http://www.wikidata.org/entity/Q33889333

about

Heterozygous yeast deletion collection screens reveal essential targets of Hsp90 Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein - The role of hsp90 Hsp90: a specialized but essential protein-folding tool Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone Dynamic regulation of p53 subnuclear localization and senescence by MORC3 Identification of a novel HSP70-binding cochaperone critical to HSP90-mediated activation of small serine/threonine kinase S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein Chronophin 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 receptor The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future Review: The HSP90 molecular chaperone-an enigmatic ATPase The 'active life' of Hsp90 complexes GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum Targeting Hsp90 in urothelial carcinoma Hsp90 selectively modulates phenotype in vertebrate development Identification of Cellular Proteome Modifications in Response to West Nile Virus Infection Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism Synthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90 Chaperone 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 domain The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90 Intra- 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 Function Mechanistic Asymmetry in Hsp90 Dimers The 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.

http://www.wikidata.org/entity/Q33889333

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

P1433

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P1433

The EMBO Journal

P1476

ATP binding and hydrolysis are ...... 0 molecular chaperone in vivo.

@en

P2093

B Panaretou

http://www.w3.org/2001/XMLSchema#string

J E Ladbury

http://www.w3.org/2001/XMLSchema#string

L H Pearl

http://www.w3.org/2001/XMLSchema#string

P W Piper

http://www.w3.org/2001/XMLSchema#string

R O'Brien

http://www.w3.org/2001/XMLSchema#string

S M Roe

http://www.w3.org/2001/XMLSchema#string

P2860

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock

Transformation of intact yeast cells treated with alkali cations

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Raster3D Version 2.0. A program for photorealistic molecular graphics

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

P304

4829-4836

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P31

scholarly article

P356

10.1093/EMBOJ/17.16.4829

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P407

P433

16

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P478

17

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P50

Chrisostomos Prodromou

P577

1998-08-01T00:00:00Z

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P5875

13578751

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P698

9707442

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P921

molecular chaperones

P932

1170812

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