| Literature DB >> 22147701 |
Douglas T Hess1, Jonathan S Stamler.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2011 PMID: 22147701 PMCID: PMC3281651 DOI: 10.1074/jbc.R111.285742
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157