| Literature DB >> 15688001 |
Douglas T Hess1, Akio Matsumoto, Sung-Oog Kim, Harvey E Marshall, Jonathan S Stamler.
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.Entities:
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Year: 2005 PMID： 15688001 DOI： 10.1038/nrm1569
Source DB: PubMed Journal: Nat Rev Mol Cell Biol ISSN： 1471-0072 Impact factor: 94.444