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Academic Journal

CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation.

  • Authors : Goemans CV; WELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.

Subjects: Tetratricopeptide Repeat*; Escherichia coli/Escherichia coli/Escherichia coli/*metabolism ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*metabolism

  • Source: Molecular cell [Mol Cell] 2018 May 17; Vol. 70 (4), pp. 614-627.e7. Date of Electronic Publication: 2018 May 10.Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Quiescin sulfhydryl oxidase from Trypanosoma brucei: catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain.

  • Authors : Kodali VK; Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA.; Thorpe C

Subjects: Cysteine/Cysteine/Cysteine/*chemistry ; Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/*chemistry ; Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/*metabolism

  • Source: Biochemistry [Biochemistry] 2010 Mar 09; Vol. 49 (9), pp. 2075-85.Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Internet ISSN:

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Academic Journal

Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase.

  • Authors : Chung JS; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, USA.; Noguera-Mazon V

Subjects: Escherichia coli/Escherichia coli/Escherichia coli/*metabolism ; Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/*metabolism ; Pseudomonas aeruginosa/Pseudomonas aeruginosa/Pseudomonas aeruginosa/*enzymology

  • Source: The Journal of biological chemistry [J Biol Chem] 2009 Nov 06; Vol. 284 (45), pp. 31181-9. Date of Electronic Publication: 2009 Sep 10.Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication

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Academic Journal

DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN.

  • Authors : Le HT; Institut Jacques Monod, Université Paris 7, Paris, France.; Gautier V

Subjects: DNA Replication/DNA Replication/DNA Replication/*genetics ; Escherichia coli/Escherichia coli/Escherichia coli/*genetics ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*genetics

  • Source: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2011 Feb 04; Vol. 405 (1), pp. 52-7. Date of Electronic Publication: 2010 Dec 31.Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase.

  • Authors : Kthiri F; Stress molecules, Institut Jacques Monod, Université Paris 7, 2 place Jussieu, 75005 Paris, France.; Le HT

Subjects: Hot Temperature*; Escherichia coli/Escherichia coli/Escherichia coli/*metabolism ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*metabolism

  • Source: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2008 Oct 03; Vol. 374 (4), pp. 668-72. Date of Electronic Publication: 2008 Jul 25.Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Catalytic mechanism of Sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin.

  • Authors : Roussel X; Unité Mixte de Recherche CNRS-UHP 7214 AREMS, ARN-RNP Structure-Fonction-Maturation, Enzymologie Moléculaire et Structurale, Faculté des Sciences et Techniques, Nancy Université, Blvd. des Aiguillettes, BP 70239, 54506 Vandoeuvre-lès-Nancy Cedex, France.; Kriznik A

Subjects: Disulfides/Disulfides/Disulfides/*metabolism ; Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/*metabolism ; Saccharomyces cerevisiae/Saccharomyces cerevisiae/Saccharomyces cerevisiae/*metabolism

  • Source: The Journal of biological chemistry [J Biol Chem] 2009 Nov 27; Vol. 284 (48), pp. 33048-55. Date of Electronic Publication: 2009 Sep 30.Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication

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Academic Journal

Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine.

  • Authors : Kim HY; Department of Biochemistry and Molecular Biology, Aging-associated Vascular Disease Research Center, Yeungnam University College of Medicine, 317-1 Daemyung-dong, Namgu, Daegu 705-717, Republic of Korea. ; Kim JR

Subjects: Cysteine/Cysteine/Cysteine/*chemistry ; Oxidoreductases/Oxidoreductases/Oxidoreductases/*chemistry ; Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/*chemistry

  • Source: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2008 Jul 04; Vol. 371 (3), pp. 490-4. Date of Electronic Publication: 2008 Apr 29.Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

The interaction of 5'-adenylylsulfate reductase from Pseudomonas aeruginosa with its substrates.

  • Authors : Kim SK; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, USA. ; Rahman A

Subjects: Cysteine/Cysteine/Cysteine/*chemistry ; Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/Oxidoreductases Acting on Sulfur Group Donors/*chemistry ; Pseudomonas aeruginosa/Pseudomonas aeruginosa/Pseudomonas aeruginosa/*enzymology

  • Source: Biochimica et biophysica acta [Biochim Biophys Acta] 2005 Dec 20; Vol. 1710 (2-3), pp. 103-12. Date of Electronic Publication: 2005 Oct 07.Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print-Electronic Cited Medium: Print ISSN:

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Academic Journal

Redefining reductive sulfate assimilation in higher plants: a role for APS reductase, a new member of the thioredoxin superfamily?

  • Authors : Wray JL; Research Division of Environmental and Evolutionary Biology, School of Biological and Medical Sciences, University of St. Andrews, Fife, UK.; Campbell EI

Subjects: Oxidoreductases Acting on Sulfur Group Donors*; Oxidoreductases/Oxidoreductases/Oxidoreductases/*metabolism ; Plants/Plants/Plants/*enzymology

  • Source: Chemico-biological interactions [Chem Biol Interact] 1998 Feb 20; Vol. 109 (1-3), pp. 153-67.Publisher: Elsevier Country of Publication: Ireland NLM ID: 0227276 Publication Model: Print Cited Medium: Print ISSN: 0009-2797 (Print)

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Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and "APS reductase" activity.

  • Authors : Gutierrez-Marcos JF; Plant Sciences Laboratory, School of Biological and Medical Sciences, University of St. Andrews, Fife, United Kingdom.; Roberts MA

Subjects: Multigene Family* ; Oxidoreductases Acting on Sulfur Group Donors*; Arabidopsis/Arabidopsis/Arabidopsis/*enzymology

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1996 Nov 12; Vol. 93 (23), pp. 13377-82.Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Print ISSN:

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  • 1-10 of  28 results for ""Oxidoreductases Acting on Sulfur Group Donors""