title: Development and application of site-specific proteomic approach for study protein S-nitrosylation.
abstract: Protein S-nitrosylation is the covalent redox-related modification of cysteine sulfhydryl groups with nitric oxide, creating a regulatory impact similar to phosphorylation. Recent studies have reported a growing number of proteins to be S-nitrosylated in vivo resulting in altered functions. These studies support S-nitrosylation as a critical regulatory mechanism, fine-tuning protein activities within diverse cellular processes and biochemical pathways. In addition, S-nitrosylation appears to have key roles in the etiology of a broad range of human diseases. In this review, we discuss recent advances in proteomic approaches for the enrichment, identification, and quantitation of cysteine S-nitrosylated proteins and peptides. These advances have provided analytical tools with the power to interpret the impact of S-nitrosylation at the system level, providing a new platform for drug discovery and the identification of diagnostic markers for human diseases.
authors.affiliation: Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198, USA. mli1@unmc.edu
authors.forename: Miao
authors.initials: M
authors.lastname: Liu
authors.forename: James E
authors.initials: JE
authors.lastname: Talmadge
authors.forename: Shi-Jian
authors.initials: SJ
authors.lastname: Ding
mesh_terms: D003545:Cysteine / Q000737:chemistry / Q000378:metabolism*; D055808:Drug Discovery; D006801:Humans; D009569:Nitric Oxide / Q000378:metabolism*; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics
chemical_list: D010455:Peptides; D011506:Proteins; D009569:Nitric Oxide; D003545:Cysteine