Strategies and tools to explore protein S-nitrosylation

Richard Reece, Karthik Raju, Paschalis Thomas Doulias, Margarita Tenopoulou, Jennifer L. Greene, Harry Ischiropoulos

    Research output: Contribution to journalArticlepeer-review


    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. Scope of review: 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. Major 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. General significance: 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. © 2011 Elsevier B.V. All rights reserved.
    Original languageEnglish
    Pages (from-to)684-688
    Number of pages4
    JournalBiochimica et Biophysica Acta - General Subjects
    Issue number6
    Publication statusPublished - Jun 2012


    • Cysteine post translational modification
    • Mass spectrometry
    • Nitric oxide
    • Proteomics
    • S-nitrosylation


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