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Review
. 2005 Feb;6(2):150-66.
doi: 10.1038/nrm1569.

Protein S-nitrosylation: purview and parameters

Douglas T Hess  1 , Akio Matsumoto, Sung-Oog Kim, Harvey E Marshall, Jonathan S Stamler
Affiliations
Review

Protein S-nitrosylation: purview and parameters

Douglas T Hess et al. Nat Rev Mol Cell Biol. 2005 Feb.

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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