(Q34743720)

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

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scholarly article

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Europe PubMed Central

4 August 2017

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

1 reference

Europe PubMed Central

4 August 2017

author name string

Aslund F

1

1 reference

Europe PubMed Central

4 August 2017

Berndt KD

2

1 reference

Europe PubMed Central

4 August 2017

Holmgren A

3

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Europe PubMed Central

4 August 2017

language of work or name

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publication date

1 December 1997

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Europe PubMed Central

4 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

4 August 2017

272

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Europe PubMed Central

4 August 2017

30780-30786

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Europe PubMed Central

4 August 2017

49

1 reference

Europe PubMed Central

4 August 2017

Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione

1 reference

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21 January 2018

Construction and characterization of glutaredoxin-negative mutants of Escherichia coli

1 reference

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21 January 2018

Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.

1 reference

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21 January 2018

A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme.

1 reference

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21 January 2018

Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

1 reference

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21 January 2018

Why is DsbA such an oxidizing disulfide catalyst?

1 reference

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21 January 2018

Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione

1 reference

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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/10.1074%2FJBC.272.49.30780

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

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21 January 2018

Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase.

1 reference

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21 January 2018

Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase

1 reference

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21 January 2018

Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.

1 reference

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21 January 2018

Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold

1 reference

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21 January 2018

3 The preparation of guanidine hydrochloride

1 reference

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21 January 2018

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein

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21 January 2018

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

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21 January 2018

Escherichia coli glutaredoxin: cloning and overexpression, thermodynamic stability of the oxidized and reduced forms, and report of an N-terminal extended species.

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21 January 2018

Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.

1 reference

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21 January 2018

Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide

1 reference

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21 January 2018

Thioredoxin--a fold for all reasons

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.49.30780

21 January 2018

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.49.30780

21 January 2018

Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Identifiers

10.1074/JBC.272.49.30780

1 reference

Europe PubMed Central

4 August 2017

1 reference

Europe PubMed Central

4 August 2017

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