(Q41456212)

30 September 2017

title

Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. (English)

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30 September 2017

Laura Segatori

1

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30 September 2017

Lori Murphy

2

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30 September 2017

Silvia Arredondo

3

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30 September 2017

Hiroshi Kadokura

4

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30 September 2017

Hiram Gilbert

5

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30 September 2017

Jon Beckwith

6

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30 September 2017

George Georgiou

7

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30 September 2017

language of work or name

English

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publication date

9 November 2005

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Journal of Biological Chemistry

30 September 2017

published in

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30 September 2017

volume

281

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30 September 2017

issue

8

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30 September 2017

page(s)

4911-4919

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Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm

30 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Protein disulfide bond formation in prokaryotes

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M505453200

Oxidative protein folding in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

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.M505453200

Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Structure of DsbC from Haemophilus influenzae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Snapshots of DsbA in action: detection of proteins in the process of oxidative folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

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.M505453200

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.M505453200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

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.M505453200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

An engineered pathway for the formation of protein disulfide bonds

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505453200

21 January 2018

Identifiers

DOI

10.1074/JBC.M505453200

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30 September 2017

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