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Nature Chemical Biology 5, 448 - 449 (2009)
Published online: 24 May 2009 | doi:10.1038/nchembio.f.11
Inhibitors paradoxically prime kinases
Stephen V Frye1 & Gary L Johnson2
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Stephen V. Frye is in the Division of Medicinal Chemistry and Natural Products of the Eshelman School of Pharmacy and directs the Center for Integrative Chemical Biology and Drug Discovery, Chapel Hill, North Carolina, USA.
e-mail: svfrye@email.unc.edu -
Gary L. Johnson is in the Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina, USA.
e-mail: gary_johnson@med.unc.edu
Abstract
Small-molecule inhibitors can induce phosphorylation priming of AGC kinases. Priming by ATP binding pocket conformation, rather than intrinsic kinase activity, has significant implications for drug discovery and therapeutic efficacy.
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