(Q43885153)

English

Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm

scientific article published in December 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Escherichia coli

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Escherichia coli

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based on heuristic

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author name string

Li Q

1

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Hu HY

2

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Wang WQ

3

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Xu GJ

4

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

publication date

1 December 2001

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Europe PubMed Central

PubMed publication ID

27 November 2017

Biological Chemistry

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Europe PubMed Central

PubMed publication ID

27 November 2017

382

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

1679-1686

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Building bridges: disulphide bond formation in the cell

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Identification of a protein required for disulfide bond formation in vivo

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Cytochromes c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like protein

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Tissue sulfhydryl groups

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

The formation of protein disulphide bonds

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Why is DsbA such an oxidizing disulfide catalyst?

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Protein disulphide oxidoreductases in bacteria

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Paracoccus denitrificans CcmG is a periplasmic protein-disulphide oxidoreductase required for c- and aa3-type cytochrome biogenesis; evidence for a reductase role in vivo

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Escherichia coli ccm in-frame deletion mutants can produce periplasmic cytochrome b but not cytochrome c.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

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/10.1515%2FBC.2001.203

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Replacement of Trp inEscherichia coliThioredoxin by Site-directed Mutagenesis Affects Thermodynamic Stability but Not Function

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.203

21 January 2018

Identifiers

10.1515/BC.2001.203

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

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