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Title: Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Author: Jaffrey SR, Erdjument-Bromage H, Ferris CD, Tempst P, Snyder SH. Journal: Nat Cell Biol; 2001 Feb; 3(2):193-7. PubMed ID: 11175752. Abstract: Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.[Abstract] [Full Text] [Related] [New Search]