Regulation by S-nitrosylation of protein post-translational modification.


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


  • eng

Conference Location

  • United States