Identification of a redox-regulated chaperone network (Q34107320)

31 July 2017

title

Identification of a redox-regulated chaperone network (English)

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31 July 2017

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Jörg H Hoffmann

1

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31 July 2017

Katrin Linke

2

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31 July 2017

Paul C F Graf

3

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31 July 2017

Hauke Lilie

4

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31 July 2017

Ursula Jakob

5

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31 July 2017

language of work or name

English

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publication date

11 December 2003

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31 July 2017

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31 July 2017

volume

23

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31 July 2017

issue

1

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31 July 2017

page(s)

160-168

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Trigger Factor and DnaK possess overlapping substrate pools and binding specificities

31 July 2017

cites work

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Chaperone activity with a redox switch

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

How chaperones fold proteins.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Activation of the OxyR transcription factor by reversible disulfide bond formation

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1271656

Redox switch of hsp33 has a novel zinc-binding motif

28 October 2018

1 reference

12 December 2020

Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

1 reference

12 December 2020

Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism

1 reference

12 December 2020

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

1 reference

12 December 2020

Interaction of DnaK with native proteins and membrane proteins correlates with their accessible hydrophobicity

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12 December 2020

The molecular chaperone concept

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12 December 2020

GroE facilitates refolding of citrate synthase by suppressing aggregation

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12 December 2020

Identifiers

DOI

10.1038/SJ.EMBOJ.7600016

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31 July 2017

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31 July 2017

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