Oxidative protein folding in bacteria (Q34124799)

31 July 2017

title

Oxidative protein folding in bacteria (English)

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31 July 2017

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1

Jean-Francois Collet

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31 July 2017

James C A Bardwell

2

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31 July 2017

publication date

1 April 2002

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31 July 2017

language of work or name

English

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published in

Molecular Microbiology

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31 July 2017

volume

44

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31 July 2017

issue

1

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31 July 2017

page(s)

1-8

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publication type of scholarly work

31 July 2017

review article

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A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins

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

21 January 2018

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Identification of a protein required for disulfide bond formation in vivo

21 January 2018

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A pathway for disulfide bond formation in vivo

21 January 2018

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Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex.

21 January 2018

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The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain

21 January 2018

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Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli

21 January 2018

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Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes

21 January 2018

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Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12.

21 January 2018

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Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

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The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding

21 January 2018

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Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

21 January 2018

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Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA

21 January 2018

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PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA

21 January 2018

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Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

21 January 2018

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

21 January 2018

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Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli

21 January 2018

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Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway

21 January 2018

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Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells

21 January 2018

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Identification of a segment of DsbB essential for its respiration-coupled oxidation

21 January 2018

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

21 January 2018

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

21 January 2018

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https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.02851.X

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

21 January 2018

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https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.02851.X

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

21 January 2018

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Disulfide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion

21 January 2018

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Making and breaking disulfide bonds

21 January 2018

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An in vivo pathway for disulfide bond isomerization in Escherichia coli

21 January 2018

1 reference

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Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.

21 January 2018

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Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+.

21 January 2018

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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/10.1046%2FJ.1365-2958.2002.02851.X

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/10.1046%2FJ.1365-2958.2002.02851.X

Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.02851.X

Does DsbA have chaperone-like activity?

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.02851.X

An essential role for DsbA in cytochromec synthesis and formate-dependent nitrite reduction byEscherichia coli K-12

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-2958.2002.02851.X

10.1046/J.1365-2958.2002.02851.X

21 January 2018

Identifiers

DOI

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31 July 2017

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