NOS2 regulation of NF-kappaB by S-nitrosylation of p65.

@article{Kelleher2007NOS2RO,
  title={NOS2 regulation of NF-kappaB by S-nitrosylation of p65.},
  author={Zachary T. Kelleher and Akio Matsumoto and Jonathan S. Stamler and Harvey E. Marshall},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 42},
  pages={30667-72}
}
Signal transduction in the NF-kappaB transcription factor pathway is inhibited by inducible nitric oxide synthase (NOS2) activity, although the molecular mechanism(s) are incompletely understood. We have previously shown that nitric oxide (NO), derived from NOS2 consequent upon cytokine stimulation, attenuates NF-kappaB p50-p65 heterodimer DNA binding and have identified the p50 monomer as a locus for inhibitory S-nitrosylation. We now show that the binding partner of p50, NF-kappaB p65, is… CONTINUE READING