Catalysis of disulfide bond formation and isomerization in Escherichia coli (Q34545621)

2 August 2017

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title

Catalysis of disulfide bond formation and isomerization in Escherichia coli (English)

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2 August 2017

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Bader MW

1

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2 August 2017

Bardwell JC

series ordinal

2

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2 August 2017

publication date

1 January 2001

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Advances in Protein Chemistry

2 August 2017

published in

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2 August 2017

volume

59

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2 August 2017

page(s)

283-301

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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

2 August 2017

cites work

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7 January 2021

Principles that govern the folding of protein chains

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7 January 2021

Oxidative protein folding is driven by the electron transport system

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7 January 2021

Reconstitution of a protein disulfide catalytic system

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7 January 2021

Disulfide bonds are generated by quinone reduction

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7 January 2021

Building bridges: disulphide bond formation in the cell

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7 January 2021

Identification of a protein required for disulfide bond formation in vivo

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7 January 2021

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

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7 January 2021

Chaperone activity of DsbC

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase

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7 January 2021

Contributions of substrate binding to the catalytic activity of DsbC.

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7 January 2021

On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily

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7 January 2021

Biogenesis of the bundle-forming pilus of enteropathogenic Escherichia coli: reconstitution of fimbriae in recombinant E. coli and role of DsbA in pilin stability--a review.

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7 January 2021

Principles of protein folding in the cellular environment

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7 January 2021

Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation

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7 January 2021

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

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7 January 2021

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum

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7 January 2021

Why is DsbA such an oxidizing disulfide catalyst?

1 reference

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7 January 2021

Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959009-9

7 January 2021

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

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7 January 2021

Thioredoxin--a fold for all reasons

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959009-9

7 January 2021

Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli

1 reference

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7 January 2021

Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo

1 reference

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7 January 2021

Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

1 reference

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7 January 2021

Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B

1 reference

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7 January 2021

The CcmE protein from Escherichia coli is a haem-binding protein

1 reference

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7 January 2021

Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coli

1 reference

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7 January 2021

The genetics of disulfide bond metabolism

1 reference

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7 January 2021

The reductive cleavage of disulfide bonds and its application to problems of protein structure.

1 reference

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7 January 2021

DsbG, a protein disulfide isomerase with chaperone activity

1 reference

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7 January 2021

Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959009-9

7 January 2021

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

1 reference

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7 January 2021

Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA− menA− double quinone mutant

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7 January 2021

Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli

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7 January 2021

Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959009-9

7 January 2021

The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo

1 reference

https://api.crossref.org/works/10.1016%2FS0065-3233%2801%2959009-9

7 January 2021

10.1016/S0065-3233(01)59009-9

Identifiers

DOI

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2 August 2017

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