title: Modulating noncatalytic function with kinase inhibitors.
abstract: In this issue of Chemistry & Biology, Hari and colleagues show that conformation-selective ATP-competitive kinase inhibitors have distinct noncatalytic effects on Erk2, including the ability to modulate protein-protein interactions outside the ATP-binding site. These findings enhance our knowledge about the diverse array of activities in which kinase inhibitors can target signaling pathways.
authors.affiliation: Departments of Medicinal Chemistry & Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109, USA.
authors.forename: Michael P
authors.initials: MP
authors.lastname: Agius
authors.affiliation: Departments of Medicinal Chemistry & Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109, USA. Electronic address: soellner@med.umich.edu.
authors.forename: Matthew B
authors.initials: MB
authors.lastname: Soellner
mesh_terms: D000255:Adenosine Triphosphate / Q000037:antagonists & inhibitors*; D006801:Humans; D020928:Mitogen-Activated Protein Kinases / Q000037:antagonists & inhibitors*; D047428:Protein Kinase Inhibitors / Q000494:pharmacology*
chemical_list: D047428:Protein Kinase Inhibitors; D000255:Adenosine Triphosphate; D020928:Mitogen-Activated Protein Kinases