title: Strategies and tools to explore protein S-nitrosylation.
abstract: BACKGROUND
  A biochemical pathway by which nitric oxide accomplishes functional diversity is the specific modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, interactions and location. However, comprehensive studies exploring protein signaling pathways or interrelated protein clusters that are regulated by S-nitrosylation have not been performed on a global scale.
  
  
  METHODS
  To provide insights to these important biological questions, sensitive, validated and quantitative proteomic approaches are required. This review summarizes current approaches for the global identification of S-nitrosylated proteins.
  
  
  CONCLUSIONS
  The application of novel methods for identifying S-nitrosylated proteins, especially when combined with mass-spectrometry based proteomics to provide site-specific identification of the modified cysteine residues, promises to deliver critical clues for the regulatory role of this dynamic posttranslational modification in cellular processes.
  
  
  CONCLUSIONS
  Though several studies have established S-nitrosylation as a regulator of protein function in individual proteins, the biological chemistry and the structural elements that govern the specificity of this modification in vivo are vastly unknown. Additionally, a gap in knowledge exists concerning the potential global regulatory role(s) this modification may play in cellular physiology. By further studying S-nitrosylation at a global scale, a greater appreciation of nitric oxide and protein S-nitrosylation in cellular function can be achieved. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.
authors.affiliation: Department of Pediatrics, Children's Hospital of Philadelphia Research Institute, Philadelphia, PA 19104, USA.
authors.forename: Karthik
authors.initials: K
authors.lastname: Raju
authors.forename: Paschalis-Thomas
authors.initials: PT
authors.lastname: Doulias
authors.forename: Margarita
authors.initials: M
authors.lastname: Tenopoulou
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Greene
authors.forename: Harry
authors.initials: H
authors.lastname: Ischiropoulos
mesh_terms: D003545:Cysteine / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000378:metabolism*; D013058:Mass Spectrometry; D009569:Nitric Oxide / Q000378:metabolism; D015538:Nitrosation / Q000502:physiology; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics; D026403:S-Nitrosothiols; D015398:Signal Transduction
chemical_list: D011506:Proteins; D026403:S-Nitrosothiols; D009569:Nitric Oxide; C021315:S-nitrosocysteine; D003545:Cysteine