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Sci. STKE, 12 June 2001
Vol. 2001, Issue 86, p. re1
[DOI: 10.1126/stke.2001.86.re1]


S-Nitrosylation Is Emerging as a Specific and Fundamental Posttranslational Protein Modification: Head-to-Head Comparison with O-Phosphorylation

Paul Lane, Gang Hao, and Steven S. Gross

The authors are in the Department of Pharmacology, Weill Medical College of Cornell University, 1300 York Avenue, Room LC-218, New York, NY 10021, USA. E-mail: ssgross{at}

Gloss: Nitric oxide (NO) is a mammalian cell product that has been implicated in the control of essentially all cellular functions. Key to NO's bioactivity is its chemical reactivity. Recent studies suggest that a biologically important reaction of NO is with SH-groups on cysteine residues of proteins--this modification has been termed S-nitrosylation. Until recently, our appreciation of the importance of S-nitrosylation as a mechanism for posttranslational regulation of protein activity has been hindered by an inadequate understanding of how S-nitrosylation may be targeted to specific protein thiols and the lack of a simple method for identification of proteins that are S-nitrosylated in vivo. This review highlights emerging concepts and a new technique that may help to overcome these obstacles. A head-to-head comparison suggests that S-nitrosylation, like O-phosphorylation, may similarly play a fundamental role in the post-translational control of protein activity and cellular function.

Citation: P. Lane, G. Hao, S. S. Gross, S-Nitrosylation Is Emerging as a Specific and Fundamental Posttranslational Protein Modification: Head-to-Head Comparison with O-Phosphorylation. Sci. STKE 2001, re1 (2001).

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