title: Regulation by S-nitrosylation of protein post-translational modification.
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.
authors.affiliation: Institute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, USA.
authors.forename: Douglas T
authors.initials: DT
authors.lastname: Hess
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Stamler
mesh_terms: D000107:Acetylation; D000818:Animals; D006801:Humans; D009569:Nitric Oxide / Q000378:metabolism*; D010766:Phosphorylation / Q000502:physiology; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D009569:Nitric Oxide