(Q43988793)

28 November 2017

title

Reconstitution of a disulfide isomerization system (English)

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28 November 2017

1

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28 November 2017

Jan Riemer

2

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28 November 2017

Martin W Bader

series ordinal

3

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28 November 2017

James C A Bardwell

series ordinal

4

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28 November 2017

language of work or name

English

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publication date

9 May 2002

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Journal of Biological Chemistry

28 November 2017

published in

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28 November 2017

volume

277

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28 November 2017

issue

30

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28 November 2017

page(s)

26886-26892

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Oxidative protein folding in bacteria

28 November 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M203028200

Identification of a protein required for disulfide bond formation in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

An in vivo pathway for disulfide bond isomerization in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

DsbD-catalyzed transport of electrons across the membrane of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

DsbC activation by the N-terminal domain of DsbD.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

21 January 2018

Tissue sulfhydryl groups

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

DsbG, a protein disulfide isomerase with chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M203028200

21 January 2018

Identifiers

DOI

10.1074/JBC.M203028200

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28 November 2017

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