R G Kurumbail
Affiliation: Monsanto Company
- Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agentsR G Kurumbail
G D Searle, St Louis, Missouri 63198, USA
Nature 384:644-8. 1996..0 to 2.5 A resolution. These structures explain the structural basis for the selective inhibition of COX-2, and demonstrate some of the conformational changes associated with time-dependent inhibition...
- A three-step kinetic mechanism for selective inhibition of cyclo-oxygenase-2 by diarylheterocyclic inhibitorsM C Walker
Searle Discovery Research, Pharmacia Corp, 700 Chesterfield Parkway N, St Louis, MO 63198, USA
Biochem J 357:709-18. 2001..A generalized mechanism for inhibition, consisting of three sequential reversible steps, can account for the various types of kinetic behaviour observed with these inhibitors...
- Three-dimensional structure of human cytomegalovirus proteaseH S Shieh
Department of Medicinal and Structural Chemistry, Monsanto Searle, Searle Discovery Research, St Louis, Missouri 63198, USA
Nature 383:279-82. 1996..Correlations of the structure with the sequences of herpesvirus proteases suggest that dimerization may confer specificity and recognition in substrate binding...
- Structural insights into the stereochemistry of the cyclooxygenase reactionJ R Kiefer
Searle Discovery Research, Monsanto Company, St Louis, Missouri 63198, USA
Nature 405:97-101. 2000..Here we report the co-crystal structures of murine apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin. These structures suggest the molecular basis for the stereospecificity of prostaglandin G2 synthesis...
- Cyclooxygenase enzymes: catalysis and inhibitionR G Kurumbail
Pharmacia Discovery Research, Pharmacia, Mailstop BB4K, 700 Chesterfield Parkway North, St Louis, Missouri 63198, USA
Curr Opin Struct Biol 11:752-60. 2001..Detailed kinetics, spectroscopic and crystallographic studies have shed new light on the complex mechanism of inhibition of these fascinating enzymes. Finally, novel substrates of cyclooxygenase-2 have been identified...