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Protein S -nitrosylation, the covalent attachment of nitric oxide (NO) moiety to the reactive thiol group of a cysteine residue to form S -nitrosothiol is an important PTM for most classes of proteins ( S -nitrosylated proteins such as Bcl-2, p53, HIF-1α, PTEN, and Src are involved in cell survival, angiogenesis, tumorigenesis, and response to cancer treatment ( S -nitrosylation of Bcl-2, which inhibits its ubiquitination and subsequent proteasomal degradation ( S -nitrosylation on Cys498 residue of Src kinase induces autophosphorylation, which promotes nitric oxide-mediated cell invasion and resistance to anoikis in cancer cells ( S -nitrosoglutathione promote S -nitrosylation at the Cys183 residue of extracellular signal-regulated kinase 1/2 (ERK1/2), which leads to inducing apoptosis in U251 glioma cells ( S -nitrosylation affects a variety of proteins that play important roles in the cellular dysfunctions and contribute to cancer progression and response to chemotherapy
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Its distinct structure allows study of lipolytic pathways without directly triggering broader growth hormone-mediated endocrine responses, making it useful for investigating metabolic regulation mechanisms
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