
doi: 10.1038/nrm1569
pmid: 15688001
S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mechanism for dynamic, post-translational regulation of most or all main classes of protein. S-nitrosylation thereby conveys a large part of the ubiquitous influence of nitric oxide (NO) on cellular signal transduction, and provides a mechanism for redox-based physiological regulation.
Models, Molecular, Nitrogen, Cell Membrane, Molecular Sequence Data, Proteins, Nitric Oxide, Models, Biological, GTP Phosphohydrolases, Models, Chemical, Animals, Humans, Amino Acid Sequence, Cysteine, Sulfhydryl Compounds, Oxidation-Reduction, Protein Processing, Post-Translational, Signal Transduction
Models, Molecular, Nitrogen, Cell Membrane, Molecular Sequence Data, Proteins, Nitric Oxide, Models, Biological, GTP Phosphohydrolases, Models, Chemical, Animals, Humans, Amino Acid Sequence, Cysteine, Sulfhydryl Compounds, Oxidation-Reduction, Protein Processing, Post-Translational, Signal Transduction
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