James R. Burke
Drug Discovery Research
Bristol-Myers Squibb Pharmaceutical Research Institute
Princeton
New Jersey 08543
USA
Name/email consistency: high
- BMS-345541 is a highly selective inhibitor of I kappa B kinase that binds at an allosteric site of the enzyme and blocks NF-kappa B-dependent transcription in mice. Burke, J.R., Pattoli, M.A., Gregor, K.R., Brassil, P.J., MacMaster, J.F., McIntyre, K.W., Yang, X., Iotzova, V.S., Clarke, W., Strnad, J., Qiu, Y., Zusi, F.C. J. Biol. Chem. (2003)
- Targeting I kappa B kinase for the treatment of inflammatory and other disorders. Burke, J.R. Curr. Opin. Drug. Discov. Devel (2003)
- The catalytic subunits of IkappaB kinase, IKK-1 and IKK-2, contain non-equivalent active sites when expressed as homodimers. Burke, J.R., Strnad, J. Biochem. Biophys. Res. Commun. (2002)
- BMS-229724 is a tight-binding inhibitor of cytosolic phospholipase A2 that acts at the lipid/water interface and possesses anti-inflammatory activity in skin inflammation models. Burke, J.R., Davern, L.B., Stanley, P.L., Gregor, K.R., Banville, J., Remillard, R., Russell, J.W., Brassil, P.J., Witmer, M.R., Johnson, G., Tredup, J.A., Tramposch, K.M. J. Pharmacol. Exp. Ther. (2001)
- Targeting phospholipase A2 for the treatment of inflammatory skin diseases. Burke, J.R. Curr. Opin. Investig. Drugs (2001)
- Peptides corresponding to the N and C termini of IkappaB-alpha, -beta, and -epsilon as probes of the two catalytic subunits of IkappaB kinase, IKK-1 and IKK-2. Burke, J.R., Wood, M.K., Ryseck, R.P., Walther, S., Meyers, C.A. J. Biol. Chem. (1999)
