DsbC activation by the N-terminal domain of DsbD. (Q33932871)

30 July 2017

DsbC activation by the N-terminal domain of DsbD. (English)

1 reference

30 July 2017

D Goldstone

1

1 reference

30 July 2017

P W Haebel

2

1 reference

30 July 2017

F Katzen

3

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30 July 2017

M W Bader

4

1 reference

30 July 2017

J C Bardwell

5

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30 July 2017

J Beckwith

6

1 reference

30 July 2017

P Metcalf

7

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30 July 2017

language of work or name

English

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publication date

7 August 2001

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Proceedings of the National Academy of Sciences of the United States of America

30 July 2017

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30 July 2017

98

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30 July 2017

17

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30 July 2017

9551-9556

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

30 July 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

DsbD-catalyzed transport of electrons across the membrane of 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=55490

Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm 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=55490

Crystal structure of the protein disulfide bond isomerase, DsbC, from 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=55490

Efficient folding of proteins with multiple 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=55490

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of 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=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Expression of active human tissue-type plasminogen activator 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=55490

Low ubiquinone content in Escherichia coli causes thiol hypersensitivity

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox 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=55490

Protein disulfide isomerase and assisted protein folding

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

An in vivo pathway for disulfide bond isomerization 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=55490

Mutants in disulfide bond formation that disrupt flagellar assembly 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=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

A pathway for disulfide bond formation in vivo

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in 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=55490

Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein 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=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Identification and characterization of a new disulfide isomerase-like protein (DsbD) 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=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Reassessment of Ellman's reagent

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Calculation of protein extinction coefficients from amino acid sequence data

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Use of T7 RNA polymerase to direct expression of cloned genes

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55490

Redox states of DsbA in the periplasm of Escherichia coli.

5 July 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.171315498

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

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.171315498

In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.171315498

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

12 December 2020

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

1 reference

12 December 2020

Disulfide bonds are generated by quinone reduction

1 reference

12 December 2020

Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase

1 reference

12 December 2020

DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA

1 reference

12 December 2020

Contributions of substrate binding to the catalytic activity of DsbC.

1 reference

12 December 2020

Reconstitution of a protein disulfide catalytic system

1 reference

12 December 2020

Improved folding of apo-retinol-binding protein in the periplasm of Escherichia coli: positive influences of dsbC coexpression and of an amino acid exchange in the vitamin A binding site

1 reference

12 December 2020

In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG

1 reference

12 December 2020

Chaperone activity of DsbC

1 reference

12 December 2020

Oxidative protein folding is driven by the electron transport system

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.171315498

1 reference

30 July 2017

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1 reference

30 July 2017

1 reference