(Q73897313)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10854438%20AND%20SRC:MED&resulttype=core&format=json

7 November 2019

title

Disulfide bonds are generated by quinone reduction (English)

1 reference

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7 November 2019

author name string

M W Bader

1

1 reference

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7 November 2019

T Xie

2

1 reference

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7 November 2019

C A Yu

3

1 reference

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7 November 2019

J C Bardwell

4

1 reference

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7 November 2019

language of work or name

English

0 references

publication date

1 August 2000

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10854438%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

7 November 2019

number of pages

7

1 reference

based on heuristic

inferred from page(s)

published in

1 reference

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7 November 2019

volume

275

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10854438%20AND%20SRC:MED&resulttype=core&format=json

7 November 2019

issue

34

1 reference

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7 November 2019

page(s)

26082-26088

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10854438%20AND%20SRC:MED&resulttype=core&format=json

The genetics of disulfide bond metabolism

7 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

Electron avenue: pathways of disulfide bond formation and isomerization

21 January 2018

1 reference

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Where do the electrons go?

21 January 2018

1 reference

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

A pathway for disulfide bond formation in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

Oxidative protein folding is driven by the electron transport system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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.M003850200

Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

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Reconstitution of a protein disulfide catalytic system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

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Protein disulphide isomerase: building bridges in protein folding

21 January 2018

1 reference

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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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

An in vivo pathway for disulfide bond isomerization in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

Reassessment of Ellman's reagent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

Contributions of substrate binding to the catalytic activity of DsbC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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.M003850200

Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

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.M003850200

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

https://api.crossref.org/works/10.1074%2FJBC.M003850200

Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

DsbG, a protein disulfide isomerase with chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M003850200

21 January 2018

Identifiers

DOI

10.1074/JBC.M003850200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10854438%20AND%20SRC:MED&resulttype=core&format=json

7 November 2019

1 reference