Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system (Q31578047)

3 July 2017

Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system (English)

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3 July 2017

Grimshaw JP

1

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3 July 2017

Jelesarov I

series ordinal

2

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3 July 2017

Schönfeld HJ

series ordinal

3

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3 July 2017

Christen P

series ordinal

4

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3 July 2017

language of work or name

English

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publication date

17 November 2000

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Journal of Biological Chemistry

3 July 2017

7

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based on heuristic

inferred from page(s)

published in

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3 July 2017

276

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3 July 2017

9

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3 July 2017

6098-6104

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The Hsp70 and Hsp60 chaperone machines

3 July 2017

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https://api.crossref.org/works/10.1074%2FJBC.M009290200

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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/10.1074%2FJBC.M009290200

Interaction between heat shock protein DnaK and recombinant staphylococcal protein A.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Potassium ions and the molecular-chaperone activity of DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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/10.1074%2FJBC.M009290200

A new ultrasensitive scanning calorimeter.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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/10.1074%2FJBC.M009290200

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/10.1074%2FJBC.M009290200

Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Physical interactions between members of the DnaK chaperone machinery: characterization of the DnaK.GrpE complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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/10.1074%2FJBC.M009290200

Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

Folding and refolding of thermolabile and thermostable bacterial luciferases: the role of DnaKJ heat-shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009290200

21 January 2018

Identifiers

DOI

10.1074/JBC.M009290200

1 reference

3 July 2017

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