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disulfide oxidoreductase activity

Known as: disulphide oxidoreductase activity 
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds. [MetaCyc:DISULFOXRED-RXN]
National Institutes of Health

Papers overview

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2014
2014
Background: Thioredoxins ("TRX") are ubiquitous 12-kDa oxidoreductase enzyme containing a dithiol-disulfide active site… Expand
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2007
2007
PrrC is a Sco homologue in Rhodobacter sphaeroides that is associated with PrrBA, a two-component signal transduction system that… Expand
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2005
2005
DsbA proteins, the primary catalysts of protein disulfide bond formation, are known to affect virulence and penicillin resistance… Expand
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2003
2003
Disulfide oxidoreductases are viewed as foldases that help to maintain proteins on productive folding pathways by enhancing the… Expand
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Highly Cited
1998
Highly Cited
1998
The application of an automated method for the screening of protein activity based on the sequence-to-structure-to-function… Expand
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1993
1993
Proteins of the internal nuclear matrix from chicken liver were fractionated, by chromatographic procedures, in non denaturing… Expand
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Highly Cited
1992
Highly Cited
1992
Glutaredoxin is essential for the glutathione (GSH)-dependent synthesis of deoxyribonucleotides by ribonucleotide reductase, and… Expand
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1991
1991
Thiol:protein-disulfide oxidoreductase catalyzes the GSH reduction of protein disulfides to sulfhydryls. Chromatography of… Expand
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Highly Cited
1988
Highly Cited
1988
Thioredoxin is the best representative enzyme of a group of proteins, widely distributed and possessing dithiol-disulfide… Expand
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Highly Cited
1979
Highly Cited
1979
  • Arne Holmgren
  • The Journal of biological chemistry
  • 1979
  • Corpus ID: 11371465
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative… Expand
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