Abstract
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.
MeSH terms
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Amino Acid Sequence
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Animals
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Cell Membrane / metabolism
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Cysteine / chemistry
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GTP Phosphohydrolases / metabolism
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Humans
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Models, Biological
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Models, Chemical
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Models, Molecular
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Molecular Sequence Data
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Nitric Oxide / metabolism
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Nitrogen / chemistry*
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Oxidation-Reduction
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Protein Processing, Post-Translational
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Proteins / chemistry*
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Signal Transduction
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Sulfhydryl Compounds / chemistry
Substances
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Proteins
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Sulfhydryl Compounds
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Nitric Oxide
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GTP Phosphohydrolases
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Cysteine
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Nitrogen