Regulatory Control of Human Cytosolic Branched-Chain Aminotransferase by Oxidation and S-Glutathionylation and Its Interactions with Redox Sensitive Neuronal Proteins
- 18 April 2008
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 47 (19), 5465-5479
- https://doi.org/10.1021/bi800303h
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significanceKidney International, 2007
- Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular systemAmerican Journal of Physiology-Heart and Circulatory Physiology, 2007
- Redox modifications of protein–thiols: Emerging roles in cell signalingBiochemical Pharmacology, 2006
- Thiol redox control via thioredoxin and glutaredoxin systemsBiochemical Society Transactions, 2005
- Widespread sulfenic acid formation in tissues in response to hydrogen peroxideProceedings of the National Academy of Sciences of the United States of America, 2004
- Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction pathNature Structural & Molecular Biology, 2004
- Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductasesArchives of Biochemistry and Biophysics, 2004
- Protein Sulfenic Acids in Redox SignalingAnnual Review of Pharmacology and Toxicology, 2004
- Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulationPublished by Elsevier BV ,2001
- Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox RegulationBiochemistry, 1998