Identification of the critical features of a small peptide inhibitor of JNK activity.

@article{Barr2002IdentificationOT,
  title={Identification of the critical features of a small peptide inhibitor of JNK activity.},
  author={Renae K. Barr and Tulene S. Kendrick and Marie A. Bogoyevitch},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 13},
  pages={
          10987-97
        }
}
The c-Jun N-terminal kinases (JNKs) are a subfamily of the mitogen-activated protein kinases (MAPKs). Although progress in evaluating the functions of other MAPKs has been facilitated by the characterization of specific inhibitors, no JNK-directed inhibitor is commercially available. We have identified a 21-amino acid peptide inhibitor of activated JNKs, based on amino acids 143-163 of the JNK-binding domain (JBD) of the JNK scaffolding protein, JNK-interacting protein-1 (JIP-1). This peptide… CONTINUE READING
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