title: The SNO-proteome: causation and classifications.
abstract: Cell signaling is a complex and highly regulated process. Post-translational modifications of proteins serve to sense and transduce cellular signals in a precisely coordinated manner. It is increasingly recognized that protein S-nitrosylation, the addition of a nitric oxide group to cysteine thiols, serves an important role in a wide range of signaling pathways. In spite of the large number of SNO-proteins now identified (∼1000), the observed specificity of S-nitrosylation in terms of target proteins and specific cysteines within modified proteins is incompletely understood. Here we review the progress made in S-nitrosylation detection methods that have facilitated the study of the SNO-proteome under physiological and pathophysiological conditions, and some factors important in determining the SNO-proteome. Classification schemes for emergent denitrosylases and prospective 'protein S-nitrosylases' are provided.
authors.affiliation: Institute for Transformative Molecular Medicine, Case Western Reserve University School of Medicine and University Hospitals, Cleveland, OH 44106, USA.
authors.forename: Divya
authors.initials: D
authors.lastname: Seth
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Stamler
mesh_terms: D000818:Animals; D006801:Humans; D009569:Nitric Oxide / Q000032:analysis*; D015538:Nitrosation; D020543:Proteome / Q000737:chemistry*; D040901:Proteomics; D013379:Substrate Specificity
chemical_list: D020543:Proteome; D009569:Nitric Oxide