PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12135387-1	2002	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	82-94	prostaglandin-endoperoxide synthase 2	Homo sapiens	160-176	
12135387-1	2002	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	82-94	prostaglandin-endoperoxide synthase 2	Homo sapiens	178-183	
12135387-7	2002	Synthesis of cinnamyl- or coumarinyl-substituted ethanolamide derivatives of indomethacin produced fluorescent probes of inhibitor interaction with COX-2 and COX-1.	Indomethacin	77-89	prostaglandin-endoperoxide synthase 2	Homo sapiens	148-153	
12135387-14	2002	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	177-189	prostaglandin-endoperoxide synthase 2	Homo sapiens	91-96	
12135387-15	2002	The indomethacin conjugates described herein represent powerful tools for the investigation of a novel class of selective inhibitors of COX-2.	Indomethacin	4-16	prostaglandin-endoperoxide synthase 2	Homo sapiens	136-141