Review
Nature Reviews Molecular Cell Biology 6, 150-166 (February 2005) | doi:10.1038/nrm1569
Protein S-nitrosylation: purview and parameters
Douglas T. Hess1, Akio Matsumoto2, Sung-Oog Kim1, Harvey E. Marshall1 & Jonathan S. Stamler1,2 About the authors
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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Author affiliations
- Departments of Medicine and Biochemistry, Box 2612 Duke University Medical Center, Durham, North Carolina 27710 USA.
- Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA.
Correspondence to: Jonathan S. Stamler1,2 Email: staml001@mc.duke.edu
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