Modification of tubulin cysteines by nitric oxide and nitroxyl donors alters tubulin polymerization activity.

@article{Landino2007ModificationOT,
  title={Modification of tubulin cysteines by nitric oxide and nitroxyl donors alters tubulin polymerization activity.},
  author={Lisa M. Landino and Maria T Koumas and Courtney E Mason and Jane A Alston},
  journal={Chemical research in toxicology},
  year={2007},
  volume={20 11},
  pages={
          1693-700
        }
}
  • Lisa M. Landino, Maria T Koumas, +1 author Jane A Alston
  • Published in
    Chemical research in…
    2007
  • Chemistry, Medicine
  • The modification of reduced cysteines of proteins by nitric oxide alters protein function, structure, and potentially, interactions with downstream signaling targets. We assessed the effect of the S-nitroso compounds S-nitrosoglutathione and S-nitroso-N-acetyl-penicillamine, the NO donor 2-(N,N-diethylamino)-diazenolate 2-oxide, and the nitroxyl donor Angeli's salt on the cysteines of the abundant cytoskeletal protein, tubulin. Total cysteine modification by each compound was quantitated and… CONTINUE READING

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