Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system (Q43619818)

25 November 2017

Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system (English)

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25 November 2017

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Han W

1

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PubMed ID

11376662

25 November 2017

Christen P

series ordinal

2

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PubMed ID

11376662

25 November 2017

language of work or name

English

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publication date

1 May 2001

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25 November 2017

4

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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25 November 2017

497

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25 November 2017

1

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25 November 2017

55-58

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Molecular chaperones in cellular protein folding

25 November 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Potassium ions and the molecular-chaperone activity of DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Role of the J-domain in the cooperation of Hsp40 with Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Catapult mechanism renders the chaperone action of Hsp70 unidirectional.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Peptide binding and release by proteins implicated as catalysts of protein assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

The role of ATP in the functional cycle of the DnaK chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

D-peptide ligands for the co-chaperone DnaJ

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

Interaction of auxilin with the molecular chaperone, Hsc70

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902435-8

10.1016/S0014-5793(01)02435-8

7 January 2021

Identifiers

DOI

1 reference

25 November 2017

1 reference

PubMed ID

11376662