Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways (Q35970728)

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scholarly article

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

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

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

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

Laura Segatori

1

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

Paul J Paukstelis

2

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

Hiram F Gilbert

3

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

George Georgiou

4

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

language of work or name

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publication date

25 June 2004

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Europe PubMed Central

PMC publication ID

11 August 2017

Proceedings of the National Academy of Sciences of the United States of America

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Europe PubMed Central

PMC publication ID

11 August 2017

101

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

27

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

10018-10023

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

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

1 reference

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2 October 2017

Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities

1 reference

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2 October 2017

Protein disulfide bond formation in prokaryotes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

2 October 2017

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

1 reference

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2 October 2017

Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori

1 reference

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2 October 2017

Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.

1 reference

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2 October 2017

Oxidative protein folding in bacteria

1 reference

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2 October 2017

DsbC activation by the N-terminal domain of DsbD.

1 reference

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2 October 2017

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

1 reference

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2 October 2017

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

1 reference

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2 October 2017

Biochemical basis of oxidative protein folding in the endoplasmic reticulum

1 reference

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2 October 2017

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

1 reference

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2 October 2017

Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm

1 reference

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XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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2 October 2017

Expression of active human tissue-type plasminogen activator in Escherichia coli.

1 reference

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2 October 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

2 October 2017

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

1 reference

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2 October 2017

Leaderless polypeptides efficiently extracted from whole cells by osmotic shock

1 reference

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2 October 2017

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

1 reference

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2 October 2017

Thioredoxin--a fold for all reasons

1 reference

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

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A simple method for displaying the hydropathic character of a protein

1 reference

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Internal promoter in the ilvGEDA transcription unit of Escherichia coli K-12

1 reference

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2 October 2017

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

1 reference

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2 October 2017

Stimulation of glucose catabolism in Escherichia coli by a potential futile cycle

1 reference

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2 October 2017

Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide

1 reference

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2 October 2017

A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

11 July 2018

An engineered pathway for the formation of protein disulfide bonds

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

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Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli

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24 September 2018

Dimerization by domain hybridization bestows chaperone and isomerase activities

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

24 September 2018

Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase

1 reference

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24 September 2018

Reconstitution of a disulfide isomerization system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

24 September 2018

Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli

1 reference

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24 September 2018

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

1 reference

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24 September 2018

The CXXC motif: a rheostat in the active site.

1 reference

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24 September 2018

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

1 reference

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24 September 2018

Redox states of DsbA in the periplasm of Escherichia coli.

1 reference

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24 September 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=454158

24 September 2018

Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

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Characterization of mammalian thioredoxin reductase, thioredoxin and glutaredoxin by immunochemical methods

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Contributions of substrate binding to the catalytic activity of DsbC.

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analysis of chaperone function using citrate synthase as nonnative substrate protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Disulfide bonds are generated by quinone reduction

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and φ80 transducing phages

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/15220477

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.0403003101

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

2004PNAS..10110018S

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

ResearchGate publication ID

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