Title : Isoform-selective interaction of cyclooxygenase-2 with indomethacin amides studied by real-time fluorescence, inhibition kinetics, and site-directed mutagenesis.

Pub. Date : 2002 Jul 30

PMID : 12135387






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Conversion of carboxylate-containing nonsteroidal antiinflammatory drugs, such as indomethacin, to esters or amides provides potent and selective inhibitors of cyclooxygenase-2 (COX-2) [Kalgutkar et al. Indomethacin prostaglandin-endoperoxide synthase 2 Homo sapiens
2 Conversion of carboxylate-containing nonsteroidal antiinflammatory drugs, such as indomethacin, to esters or amides provides potent and selective inhibitors of cyclooxygenase-2 (COX-2) [Kalgutkar et al. Indomethacin prostaglandin-endoperoxide synthase 2 Homo sapiens
3 Synthesis of cinnamyl- or coumarinyl-substituted ethanolamide derivatives of indomethacin produced fluorescent probes of inhibitor interaction with COX-2 and COX-1. Indomethacin prostaglandin-endoperoxide synthase 2 Homo sapiens
4 Site-directed mutagenesis indicated that residues in the carboxylate-binding region of the COX-2 active site (Arg-120, Tyr-355, and Glu-524) are critical for the binding of the indomethacin conjugates that leads to slow fluorescence enhancement and cyclooxygenase inhibition. Indomethacin prostaglandin-endoperoxide synthase 2 Homo sapiens
5 The indomethacin conjugates described herein represent powerful tools for the investigation of a novel class of selective inhibitors of COX-2. Indomethacin prostaglandin-endoperoxide synthase 2 Homo sapiens