Access

Review

Nature Reviews Molecular Cell Biology 6, 150–166 (1 February 2005) | doi:10.1038/nrm1569

Protein S-nitrosylation: purview and parameters

Douglas T. Hess , Akio Matsumoto , Sung-Oog Kim , Harvey E. Marshall & Jonathan S. Stamler

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.