Protein S-nitrosylation: purview and parameters
Nature reviews Molecular cell biology, 2005•nature.com
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.
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.
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.
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