Ontology highlight
ABSTRACT:
SUBMITTER: Stebbins JL
PROVIDER: S-EPMC3174326 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Stebbins John L JL De Surya K SK Pavlickova Petra P Chen Vida V Machleidt Thomas T Chen Li-Hsing LH Kuntzen Christian C Kitada Shinichi S Karin Michael M Pellecchia Maurizio M
Journal of medicinal chemistry 20110823 18
c-Jun N-terminal kinases (JNKs) represent valuable targets in the development of new therapies. Present on the surface of JNK is a binding pocket for substrates and the scaffolding protein JIP1 in close proximity to the ATP binding pocket. We propose that bidentate compounds linking the binding energies of weakly interacting ATP and substrate mimetics could result in potent and selective JNK inhibitors. We describe here a bidentate molecule, 19, designed against JNK. 19 inhibits JNK kinase activ ...[more]