(Q46425802)

English

Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities

scientific article published on 6 April 2005

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scholarly article

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities (English)

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

author name string

Ruoyu Xiao

1

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

Johanna Lundström-Ljung

2

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

Arne Holmgren

3

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

Hiram F Gilbert

4

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

language of work or name

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publication date

6 April 2005

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

Journal of Biological Chemistry

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

280

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

22

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

21099-21106

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

Thioredoxin--a fold for all reasons

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Identification of a protein required for disulfide bond formation in vivo.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

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/10.1074%2FJBC.M411476200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Calculation of protein extinction coefficients from amino acid sequence data

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

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

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M411476200

21 January 2018

Identifiers

10.1074/JBC.M411476200

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

1 reference

Europe PubMed Central

22 December 2017

http://europepmc.org/abstract/MED/15814611

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