(Q42856450)

8 November 2017

title

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase (English)

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8 November 2017

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8 November 2017

Paolo De los Rios

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8 November 2017

Philipp Christen

series ordinal

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8 November 2017

Ariel Lustig

series ordinal

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8 November 2017

Pierre Goloubinoff

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8 November 2017

language of work or name

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17 October 2010

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8 November 2017

published in

Nature Chemical Biology

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8 November 2017

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8 November 2017

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8 November 2017

page(s)

914-920

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

8 November 2017

cites work

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Crossref

https://api.crossref.org/works/10.1038%2FNCHEMBIO.455

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

21 January 2018

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12 December 2020

Structural dynamics of the DnaK-peptide complex

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12 December 2020

Protein folding and misfolding

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12 December 2020

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

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12 December 2020

Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14

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12 December 2020

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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12 December 2020

Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system

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12 December 2020

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

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12 December 2020

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

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12 December 2020

Protein disaggregation mediated by heat-shock protein Hsp104.

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12 December 2020

The mechanism of Hsp70 chaperones: (entropic) pulling the models together

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12 December 2020

Residues in chaperonin GroEL required for polypeptide binding and release

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Potassium ions and the molecular-chaperone activity of DnaK.

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12 December 2020

Increased efficiency of GroE-assisted protein folding by manganese ions

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Small heat shock proteins are molecular chaperones.

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12 December 2020

Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets.

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12 December 2020

Principles that govern the folding of protein chains

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12 December 2020

Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling

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12 December 2020

D-Peptides as inhibitors of the DnaK/DnaJ/GrpE chaperone system

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12 December 2020

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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12 December 2020

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

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12 December 2020

Structure of the Hsp110:Hsc70 nucleotide exchange machine

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12 December 2020

The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

1 reference

12 December 2020

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

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12 December 2020

Hsp90 chaperones protein folding in vitro.

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12 December 2020

Modulation of neurodegeneration by molecular chaperones

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12 December 2020

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

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12 December 2020

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

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12 December 2020

[Folding of the firefly luciferase polypeptide chain with immobilized C-terminus]

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

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12 December 2020

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

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12 December 2020

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

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12 December 2020

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

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12 December 2020

Disaggregating chaperones: an unfolding story.

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes

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12 December 2020

Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.

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12 December 2020

Modeling Hsp70-mediated protein folding

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12 December 2020

Influence of GrpE on DnaK-substrate interactions

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12 December 2020

Identifiers

DOI

10.1038/NCHEMBIO.455

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8 November 2017

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