Skip Navigation
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Your Environment. Your Health.

Publication Detail

Title: Regulation of protein function and signaling by reversible cysteine S-nitrosylation.

Authors: Gould, Neal; Doulias, Paschalis-Thomas; Tenopoulou, Margarita; Raju, Karthik; Ischiropoulos, Harry

Published In J Biol Chem, (2013 Sep 13)

Abstract: NO is a versatile free radical that mediates numerous biological functions within every major organ system. A molecular pathway by which NO accomplishes functional diversity is the selective modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, stability, and location. Despite considerable advances with individual proteins, the in vivo biological chemistry, the structural elements that govern the selective S-nitrosylation of cysteine residues, and the potential overlap with other redox modifications are unknown. In this minireview, we explore the functional features of S-nitrosylation at the proteome level and the structural diversity of endogenously modified residues, and we discuss the potential overlap and complementation that may exist with other cysteine modifications.

PubMed ID: 23861393 Exiting the NIEHS site

MeSH Terms: Animals; Cysteine/analogs & derivatives*; Cysteine/chemistry; Gene Expression Regulation*; Humans; Mice; Myocardium/metabolism; Nitric Oxide Synthase/metabolism; Nitric Oxide/chemistry; Nitrogen/chemistry; Oxidation-Reduction; Protein Processing, Post-Translational; Proteins/chemistry*; Proteomics/methods; S-Nitrosothiols/chemistry*; Signal Transduction

Back
to Top