Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of I kappa B alpha in NF-kappa B activation by an oxidative stress.

@article{Schoonbroodt2000CrucialRO,
  title={Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of I kappa B alpha in NF-kappa B activation by an oxidative stress.},
  author={Sonia Schoonbroodt and Val{\'e}rie Ferreira and M. Best-Belpomme and Johan R. Boelaert and Sylvie Legrand-Poels and M. M. Korner and Jacques Piette},
  journal={Journal of immunology},
  year={2000},
  volume={164 8},
  pages={4292-300}
}
Activation of transcription factor NF-kappa B involves the signal-dependent degradation of basally phosphorylated inhibitors such as I kappa B alpha. In response to proinflammatory cytokines or mitogens, the transduction machinery has recently been characterized, but the activation mechanism upon oxidative stress remains unknown. In the present work, we provide several lines of evidence that NF-kappa B activation in a T lymphocytic cell line (EL4) by hydrogen peroxide (H2O2) did not involve… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 73 extracted citations

Subcellular Redox Signaling.

Advances in experimental medicine and biology • 2017
View 8 Excerpts
Highly Influenced

The effect of reactive oxygen species on the synthesis of prostanoids from arachidonic acid.

Journal of physiology and pharmacology : an official journal of the Polish Physiological Society • 2013
View 8 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…