(Q52524766)

2 May 2018

title

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

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2 May 2018

author name string

Sone M

series ordinal

1

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2 May 2018

Akiyama Y

series ordinal

2

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2 May 2018

Ito K

series ordinal

3

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2 May 2018

language of work or name

English

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publication date

1 April 1997

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2 May 2018

Journal of Biological Chemistry

published in

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2 May 2018

volume

272

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2 May 2018

issue

16

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2 May 2018

page(s)

10349-10352

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2 May 2018

Principles that govern the folding of protein chains

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Building bridges: disulphide bond formation in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Identification of a protein required for disulfide bond formation in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

A pathway for disulfide bond formation in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

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

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

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.272.16.10349

Amino acid sequence of Escherichia coli alkaline phosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Product of a new gene, syd, functionally interacts with SecY when overproduced in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Redox states of DsbA in the periplasm of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

An in vivo pathway for disulfide bond isomerization in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

Roles of disulfide bonds in bacterial alkaline phosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10349

21 January 2018

Identifiers

DOI

10.1074/JBC.272.16.10349

1 reference

2 May 2018

1 reference

2 May 2018