A comparison of reversible versus irreversible protein glutathionylation.

@article{Townsend2014ACO,
  title={A comparison of reversible versus irreversible protein glutathionylation.},
  author={Danyelle M. Townsend and Volodymyr I. Lushchak and Arthur J. L. Cooper},
  journal={Advances in cancer research},
  year={2014},
  volume={122},
  pages={177-98}
}
Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical process can regulate various clusters of proteins, including those involved in critical cellular signaling functions. However, certain conditions can favor the formation of dehydroamino acids, such as 2,3-didehydroalanine (2,3-dehydroalanine, DHA) and 2,3-didehydrobutyrine (2,3-dehydrobutyrine), which can act as… CONTINUE READING