Glutaredoxins in Thiol/Disulfide Exchange
Author:
Affiliation:
1. Institut für Biochemie und Molekularbiologie, Universitätsmedizin Greifswald, Ernst Moritz Arndt-Universität Greifswald, Greifswald, Germany.
2. Department of Neurology, Medical Faculty, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Publisher
Mary Ann Liebert Inc
Subject
Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry
Link
http://www.liebertpub.com/doi/pdf/10.1089/ars.2012.5007
Reference108 articles.
1. S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
2. Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria
3. Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215
4. Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
5. Glutaredoxin 2 Catalyzes the Reversible Oxidation and Glutathionylation of Mitochondrial Membrane Thiol Proteins
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