The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? (Q34808336)

4 August 2017

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title

The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? (English)

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4 August 2017

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Sergey V Slepenkov

1

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PubMed ID

12207689

4 August 2017

Stephan N Witt

series ordinal

2

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PubMed ID

12207689

4 August 2017

language of work or name

English

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publication date

1 September 2002

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4 August 2017

Molecular Microbiology

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4 August 2017

45

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4 August 2017

5

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4 August 2017

1197-1206

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Roles of molecular chaperones in cytoplasmic protein folding

4 August 2017

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https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Principles that govern the folding of protein chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

The Hsp70 and Hsp60 chaperone machines

21 January 2018

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https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Principles of protein folding in the cellular environment

21 January 2018

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https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Catapult mechanism renders the chaperone action of Hsp70 unidirectional.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Specificity of DnaK-peptide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

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/10.1046%2FJ.1365-2958.2002.03093.X

The role of heat-shock and chaperone proteins in protein folding: possible molecular mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

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/10.1046%2FJ.1365-2958.2002.03093.X

The J-domain family and the recruitment of chaperone power

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

GrpE accelerates peptide binding and release from the high affinity state of DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

A GrpE mutant containing the NH(2)-terminal "tail" region is able to displace bound polypeptide substrate from DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Cell biology. An unfolding story of protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Chaperonin function: folding by forced unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

The second step of ATP binding to DnaK induces peptide release.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.03093.X

10.1046/J.1365-2958.2002.03093.X

21 January 2018

Identifiers

DOI

1 reference

4 August 2017

1 reference

PubMed ID

12207689