Redox modifications of the C-terminal cysteine residue cause structural changes in S100A1 and S100B proteins.

@article{Zhukova2004RedoxMO,
  title={Redox modifications of the C-terminal cysteine residue cause structural changes in S100A1 and S100B proteins.},
  author={Liliya Zhukova and Igor Zhukov and Wojciech Bal and Aleksandra Wyslouch-Cieszynska},
  journal={Biochimica et biophysica acta},
  year={2004},
  volume={1742 1-3},
  pages={191-201}
}
S100 is a family of small, acidic, calcium binding proteins involved in the control of a multitude of intra- and extracellular processes, including many pathologies. The application of the analytical methodology based on the combination of RP HPLC and ESI-MS allowed for the characterization of S-nitrosylation and S-glutathionylation in two representative S100 proteins: S100A1 and S100B. The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 22 extracted citations

Similar Papers

Loading similar papers…