Regulation by S-nitrosylation of protein post-translational modification.
Published
Journal Article (Review)
Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the principal protein post-translational modifications that play a role in cell signaling, including phosphorylation, acetylation, ubiquitylation and related modifications, palmitoylation, and alternative Cys-based redox modifications. In this minireview, we discuss the mechanisms through which S-nitrosylation exerts its broad pleiotropic influence on protein post-translational modification.
Full Text
Duke Authors
Cited Authors
- Hess, DT; Stamler, JS
Published Date
- February 10, 2012
Published In
Volume / Issue
- 287 / 7
Start / End Page
- 4411 - 4418
PubMed ID
- 22147701
Pubmed Central ID
- 22147701
Electronic International Standard Serial Number (EISSN)
- 1083-351X
Digital Object Identifier (DOI)
- 10.1074/jbc.R111.285742
Language
- eng
Conference Location
- United States