Influence of GrpE on DnaK-substrate interactions (Q44854763)

6 December 2017

Influence of GrpE on DnaK-substrate interactions (English)

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6 December 2017

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6 December 2017

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Bernd Bukau

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6 December 2017

1

Dirk Brehmer

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6 December 2017

Claudia Gässler

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PubMed ID

15102842

6 December 2017

language of work or name

English

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publication date

21 April 2004

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Journal of Biological Chemistry

6 December 2017

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6 December 2017

279

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6 December 2017

27957-27964

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6 December 2017

27

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The Hsp70 and Hsp60 chaperone machines

6 December 2017

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https://api.crossref.org/works/10.1074%2FJBC.M403558200

Molecular basis for interactions of the DnaK chaperone with substrates.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M403558200

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Molecular chaperones: How J domains turn on Hsp70s

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M403558200

GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M403558200

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.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Interdomain communication in the molecular chaperone DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Thermodynamic linkage in the GrpE nucleotide exchange factor, a molecular thermosensor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Different peptide binding specificities of hsp70 family members.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

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.M403558200

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.M403558200

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.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

The C terminus of sigma(32) is not essential for degradation by FtsH.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

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.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Deletion of DnaK's lid strengthens binding to the nucleotide exchange factor, GrpE: a kinetic and thermodynamic analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

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/10.1074%2FJBC.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

Structure and Energetics of an Allele-Specific Genetic Interaction between dnaJ and dnaK: Correlation of Nuclear Magnetic Resonance Chemical Shift Perturbations in the J-Domain of Hsp40/DnaJ with Binding Affinity for the ATPase Domain of Hsp70/DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M403558200

21 January 2018

Identifiers

DOI

10.1074/JBC.M403558200

1 reference

6 December 2017

1 reference

PubMed ID

15102842