Bleach activates a redox-regulated chaperone by oxidative protein unfolding (Q24643056)

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17 January 2020

title

Bleach activates a redox-regulated chaperone by oxidative protein unfolding (English)

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17 January 2020

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2

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17 January 2020

Paul Graf

3

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17 January 2020

Dennis Özcelik

4

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17 January 2020

author name string

J Winter

1

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17 January 2020

U Jakob

5

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17 January 2020

language of work or name

English

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publication date

1 November 2008

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17 January 2020

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17 January 2020

volume

135

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17 January 2020

issue

4

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17 January 2020

page(s)

691-701

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Protein thiol modifications visualized in vivo

17 January 2020

cites work

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Role of oxidants in microbial pathophysiology

7 April 2017

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Thiol chemistry and specificity in redox signaling

7 April 2017

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Pathways of Oxidative Damage

7 April 2017

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Thioredoxins and glutaredoxins as facilitators of protein folding.

7 April 2017

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The methionine sulfoxide reductases: Catalysis and substrate specificities

27 September 2017

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Effects of protein oxidation on the structure and stability of model discoidal high-density lipoproteins

27 September 2017

1 reference

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Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.

27 September 2017

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The redox-switch domain of Hsp33 functions as dual stress sensor

27 September 2017

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Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines

27 September 2017

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Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases

27 September 2017

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Identification of a redox-regulated chaperone network

27 September 2017

1 reference

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Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: specific structural motifs control protein oxidation

27 September 2017

1 reference

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Hypochlorite-induced oxidation of amino acids, peptides and proteins.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2606091

Chaperone-assisted protein folding in the cell cytoplasm

27 September 2017

1 reference

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Hsp70 chaperone machines.

27 September 2017

1 reference

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The role of oxidative stress in the pathophysiology of cerebrovascular lesions in Alzheimer's disease

27 September 2017

1 reference

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Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds

27 September 2017

1 reference

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Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders

27 September 2017

1 reference

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Hypochlorous acid activates the heat shock and soxRS systems of Escherichia coli.

27 September 2017

1 reference

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Hypochlorous acid stress in Escherichia coli: resistance, DNA damage, and comparison with hydrogen peroxide stress

27 September 2017

1 reference

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

27 September 2017

1 reference

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

30 May 2018

1 reference

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Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2606091

Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2606091

Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2606091

Activation of the redox-regulated chaperone Hsp33 by domain unfolding.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2606091

Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO-).

28 November 2018

1 reference

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

28 November 2018

1 reference

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Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase

28 November 2018

1 reference

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Oxidative autoactivation of latent collagenase by human neutrophils

28 November 2018

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12 December 2020

Binding of myeloperoxidase to bacteria: effect on hydroxyl radical formation and susceptibility to oxidant-mediated killing

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12 December 2020

Analysis of chaperone function using citrate synthase as nonnative substrate protein

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12 December 2020

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

1 reference

12 December 2020

The Acid Ionization Constant of HOCl from 5 to 35°

1 reference

Crossref

https://api.crossref.org/works/10.1016/J.CELL.2008.09.024

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1016/J.CELL.2008.09.024

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19013278 AND SRC:MED&resulttype=core&format=json

17 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19013278 AND SRC:MED&resulttype=core&format=json

17 January 2020

PubMed publication ID

19013278

1 reference