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National Institute of Environmental Health Sciences

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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: No MeSH terms associated with this publication

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