Interdomain interaction through helices A and B of DnaK peptide binding domain (Q44264738)

1 December 2017

Interdomain interaction through helices A and B of DnaK peptide binding domain (English)

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1 December 2017

3

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1 December 2017

Fernando Moro

1

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PubMed ID

12505170

1 December 2017

Vanesa Fernández

series ordinal

2

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PubMed ID

12505170

1 December 2017

language of work or name

English

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publication date

1 January 2003

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1 December 2017

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1 December 2017

533

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1 December 2017

1-3

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1 December 2017

119-123

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The Hsp70 and Hsp60 chaperone machines

1 December 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

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/10.1016%2FS0014-5793%2802%2903752-3

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/10.1016%2FS0014-5793%2802%2903752-3

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/10.1016%2FS0014-5793%2802%2903752-3

Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

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%2802%2903752-3

Time-resolved fluorescence spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Coupled assay of Na+,K+-ATPase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903752-3

10.1016/S0014-5793(02)03752-3

7 January 2021

Identifiers

DOI

1 reference

1 December 2017

1 reference

PubMed ID

12505170