Nitric oxide-mediated protein modification

Nitric oxide-mediated protein modification comprises a family of chemical changes to proteins induced by nitric oxide, a small gaseous signaling molecule. Key modifications include S-nitrosylation (covalent addition of NO to cysteine thiols), metal nitrosylation (binding of NO to transition metal centers such as heme iron), and the nitration of tyrosine residues. These modifications regulate a wide spectrum of physiological processes including signal transduction, neural communication, vascular relaxation, immune response, and apoptosis. Dysregulation of these modifications is involved in various pathologies such as cardiovascular disease, neurodegeneration, cancer, and inflammation. S-nitrosylation is reversible and can affect protein conformation, activity, location, and interactions. The broad impact and context-dependent specificity of NO-mediated protein modification make it both a fundamental cellular regulatory mechanism and a challenging area for therapeutic intervention. In summary, “Nitric oxide-mediated protein modification” is not a singular drug target, but an umbrella for various biochemical events induced by NO. Structured drug or receptor-target information is better applied to individual modified proteins (e.g., “S-nitrosylated NMDA receptor”) rather than this general process.

Other names

Nitric oxide-dependent protein post-translational modificationNO-mediated PTMNO-dependent protein modificationS-nitrosylationNO-induced protein modification

For drugs affecting NO-mediated protein modification: Modulation of NO levels (e.g., NO donors, NOS inhibitors); Enhanced or inhibited S-nitrosylation; Effects on downstream NO signaling (e.g., sGC activation by NO for vasodilation).