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Article
Nature 372, 739 - 746 (29 December 1994); doi:10.1038/372739a0

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

John C. Lee*, Jeffrey T. Laydon*, Peter C. McDonnell, Timothy F. Gallagher, Sanjay Kumar, David Green§, Dean McNulty§, Mary Jane Blumenthal*, J. Richard Keys, Scott W. Land vatter, James E. Strickler§, Megan M. McLaughlin£, Ivo R. Siemens§, Seth M. Fisher§, George P. Livi, John R. White, Jerry L. Adams & Peter R. Young

Departments of * Cellular Biochemistry, Molecular Immunology, t Medicinal Chemistry, Radiochemistry, § Protein Biochemistry and £Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406, USA
Present addresses: Bristol-Myers-Squibb Pharmaceutical Research Institute, Princeton, New Jersey 08543, USA (D.G.); Ares Advanced Technology, Randolph, Massachusetts 02368, USA (J.E.S.).

Production of interleukin-1 and tumour necrosis factor from stimulated human monocytes is inhibited by a new series of pyridinyl-imidazole compounds. Using radiolabelled and radio-photoaffinity-labelled chemical probes, the target of these compounds was identified as a pair of closely related mitogen-activated protein kinase homologues, termed CSBPs. Binding of the pyridinyl-imidazole compounds inhibited CSBP kinase activity and could be directly correlated with their ability to inhibit cytokine production, suggesting that the CSBPs are critical for cytokine production.

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