The activation state of p38 mitogen-activated protein kinase determines the efficiency of ATP competition for pyridinylimidazole inhibitor binding.

@article{Frantz1998TheAS,
  title={The activation state of p38 mitogen-activated protein kinase determines the efficiency of ATP competition for pyridinylimidazole inhibitor binding.},
  author={Bill Frantz and Tatjana Klatt and Margaret Pang and Janey N Parsons and Antonio Rolando and Huw Williams and Michael J. Tocci and Stephen J O'keefe and Edward A O'neill},
  journal={Biochemistry},
  year={1998},
  volume={37 39},
  pages={13846-53}
}
The serine/threonine kinase p38 is a ubiquitous, highly conserved, stress responsive, signal-transducing enzyme. It regulates the production of proinflammatory mediators and is the target of the cytokine synthesis inhibitory pyridinylimidazoles. We have expressed human p38 in Drosophila S2 cells and characterized preparations of mixed unphosphorylated/monophosphorylated (inactive) and homogeneously diphosphorylated (active) forms of the enzyme. We observed that only the active preparation of… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 66 extracted citations

Deoxynivalenol induces p38 interaction with the ribosome in monocytes and macrophages.

Toxicological sciences : an official journal of the Society of Toxicology • 2008
View 2 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…