Interaction of Hsp70 chaperones with substrates (Q41465900)

1 October 2017

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title

Interaction of Hsp70 chaperones with substrates (English)

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1 October 2017

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Rüdiger S

1

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1 October 2017

Buchberger A

series ordinal

2

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1 October 2017

Bukau B

series ordinal

3

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1 October 2017

language of work or name

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1 May 1997

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Nature structural biology

1 October 2017

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1 October 2017

4

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1 October 2017

342-349

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1 October 2017

5

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https://scigraph.springernature.com/pub.10.1038/nsb0597-342

1 October 2017

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cites work

Molecular chaperones in cellular protein folding

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https://api.crossref.org/works/10.1038%2FNSB0597-342

Protein folding in the cell

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

The emergence of the chaperone machines

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Functional specificity among Hsp70 molecular chaperones

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0597-342

Common principles of protein translocation across membranes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Uncoating ATPase is a member of the 70 kilodalton family of stress proteins.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Escherichia coli heat shock gene mutants are defective in proteolysis

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0597-342

DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Is hsp70 the cellular thermometer?

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0597-342

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Regulation of the Escherichia coli heat-shock response.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0597-342

Peptide-binding specificity of the molecular chaperone BiP

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Structural analysis of substrate binding by the molecular chaperone DnaK

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Mutations in the C-terminal fragment of DnaK affecting peptide binding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Specificity of DnaK-peptide binding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Different peptide binding specificities of hsp70 family members.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Kinetics of molecular chaperone action

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Heregulin-stimulated signaling in rat pheochromocytoma cells. Evidence for ErbB3 interactions with Neu/ErbB2 and p85

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Conformational characterization of DnaK and its complexes by small-angle X-ray scattering

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

A new ATP-binding fold in actin, hexokinase and Hsc70.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

Normal mode analysis of G-actin

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

inferred from DOI database lookup

7 January 2021

based on heuristic

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

inferred from DOI database lookup

7 January 2021

based on heuristic

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

1 reference

https://api.crossref.org/works/10.1038%2FNSB0597-342

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NSB0597-342

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Dimensions Publication ID

1 October 2017

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1 reference