A novel strategy for global analysis of the dynamic thiol redox proteome.

@article{MartnezAcedo2012ANS,
  title={A novel strategy for global analysis of the dynamic thiol redox proteome.},
  author={Pablo Mart{\'i}nez-Acedo and Estefan{\'i}a Robayo N{\'u}{\~n}ez and Francisco Javier S{\'a}nchez G{\'o}mez and Margoth Moreno and Elena de Armas Ramos and Alicia Izquierdo-{\'A}lvarez and Elisabet Mir{\'o}-Casas and Raquel Esquiliche Mesa and Patricia Mar{\'i}a Llovet Rodr{\'i}guez and Antonio Mart{\'i}nez-Ruiz and David Garc{\'i}a Dorado and Santiago Lamas and Jes{\'u}s V{\'a}zquez},
  journal={Molecular & cellular proteomics : MCP},
  year={2012},
  volume={11 9},
  pages={
          800-13
        }
}
Nitroxidative stress in cells occurs mainly through the action of reactive nitrogen and oxygen species (RNOS) on protein thiol groups. Reactive nitrogen and oxygen species-mediated protein modifications are associated with pathophysiological states, but can also convey physiological signals. Identification of Cys residues that are modified by oxidative stimuli still poses technical challenges and these changes have never been statistically analyzed from a proteome-wide perspective. Here we show… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 29 CITATIONS

Thioredoxin and glutaredoxin regulate metabolism through di ff erent multiplex thiol switches

MJ López-Gruesoa, R González-Ojedab, +5 authors CA Padillaa
  • 2019
VIEW 1 EXCERPT
CITES BACKGROUND

Similar Papers

Loading similar papers…