Nitrosylation is any chemical reaction that adds a nitrosyl group (NO). S-nitrosylation is a post-translational modification of proteins by which thiol groups (SH groups) of cysteine residues are modified by nitric oxide to generate S-nitrosothiols (protein S-nitrosocysteine), impacting protein function stability, and localization.

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News and Comment

  • News and Views |

    New findings demonstrate that endothelial nitric oxide synthase regulates major metabolic pathways in the kidney proximal tubule, which confers protection against oxidative stress during acute kidney injury (AKI). These findings give new insights into AKI pathophysiology and nitric oxide biology, and identify new targets for the treatment of AKI.

    • Pierre-Yves Martin
    •  & Sophie de Seigneux
  • News |

    A University of Texas–led team has identified the nitrosylation of C. difficile toxins as a host defense mechanism that decreases cellular damage caused by the pathogen. The researchers are developing pharmacological strategies to augment this response to prevent recurrence after antibiotic treatment.

    • Chris Cain
  • News and Views |

    Protein S-nitrosylation is thought to be mediated primarily by nitric oxide synthases. S-nitrosylated GAPDH is now shown to function within signal transduction cascades as a nuclear nitrosylase. Along with other recent demonstrations of regulated protein–protein transnitrosylation, these findings point to a new mechanism of signal transduction with transformative implications for nitric oxide biology and redox signalling.

    • Jonathan S. Stamler
    •  & Douglas T. Hess
    Nature Cell Biology 12, 1024-1026