Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90. - Wikidata - wikimedia - TriplyDB

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

http://www.wikidata.org/entity/Q44532388

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Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones Hsp90 is regulated by a switch point in the C-terminal domain Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase.Functional specificity of co-chaperone interactions with Hsp90 client proteins.Fungal heat-shock proteins in human disease.Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.Conformational dynamics of the molecular chaperone Hsp90 The Mechanism of Hsp90 ATPase Stimulation by Aha1 Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.The charged linker region is an important regulator of Hsp90 function.Synthesis and fluorescence characteristics of ATP-based FRET probes.Conserved conformational changes in the ATPase cycle of human Hsp90.Intrinsic inhibition of the Hsp90 ATPase activity.Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers.Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.Importance of cycle timing for the function of the molecular chaperone Hsp90.Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues.Artificial Accelerators of the Molecular Chaperone Hsp90 Facilitate Rate-Limiting Conformational Transitions

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P2860

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

http://www.wikidata.org/entity/Q44532388

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@en

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@nl

type

label

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@en

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@nl

prefLabel

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@en

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@nl

P1433

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P1476

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P698

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P356

P1433

Journal of Biological Chemistry

P1476

Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

@en

P2093

Harald Wegele

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

Jochen Reinstein

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

Johannes Buchner

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

Melanie Bunck

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

Paul Muschler

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

P2860

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

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

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

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.

Sti1 is a novel activator of the Ssa proteins.

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

P304

39303-39310

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P31

scholarly article

P356

10.1074/JBC.M305751200

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P407

P433

41

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P478

278

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P577

2003-07-30T00:00:00Z

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P698

12890674

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