DsbD-catalyzed transport of electrons across the membrane of Escherichia coli (Q31583197)

3 July 2017

title

DsbD-catalyzed transport of electrons across the membrane of Escherichia coli (English)

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3 July 2017

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Krupp R

1

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3 July 2017

Chan C

series ordinal

2

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3 July 2017

Missiakas D

series ordinal

3

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3 July 2017

language of work or name

English

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publication date

20 November 2000

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Journal of Biological Chemistry

3 July 2017

published in

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3 July 2017

volume

276

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3 July 2017

issue

5

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3 July 2017

page(s)

3696-3701

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Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins

3 July 2017

cites work

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Pathways for protein disulphide bond formation

21 January 2018

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Making and breaking disulfide bonds

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009500200

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

21 January 2018

1 reference

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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

1 reference

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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/10.1074%2FJBC.M009500200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009500200

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

21 January 2018

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Thioredoxin genetics.

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Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide

21 January 2018

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An in vivo pathway for disulfide bond isomerization in Escherichia coli

21 January 2018

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Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase

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

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Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha-subunit.

21 January 2018

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Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon

21 January 2018

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

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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Electron avenue: pathways of disulfide bond formation and isomerization

21 January 2018

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Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis

21 January 2018

1 reference

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High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol- or kanamycin-resistance selection

21 January 2018

1 reference

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M009500200

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3 July 2017

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