PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26704937-2	2016	Neutralization of the carboxylic acid moiety of the NSAID indomethacin to an ester or amide functionality confers COX-2 selectivity, but the molecular basis for this selectivity has not been completely revealed through mutagenesis studies and/or X-ray crystallographic attempts.	Esters	77-82	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	114-119	
26704937-3	2016	We expressed and assayed a number of divergent secondary shell COX-2 active site mutants and found that a COX-2 to COX-1 change at position 472 (Leu in COX-2, Met in COX-1) reduced the potency of enzyme inhibition by a series of COX-2-selective indomethacin amides and esters.	Esters	269-275	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	63-68	
26704937-3	2016	We expressed and assayed a number of divergent secondary shell COX-2 active site mutants and found that a COX-2 to COX-1 change at position 472 (Leu in COX-2, Met in COX-1) reduced the potency of enzyme inhibition by a series of COX-2-selective indomethacin amides and esters.	Esters	269-275	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	106-111	
26704937-3	2016	We expressed and assayed a number of divergent secondary shell COX-2 active site mutants and found that a COX-2 to COX-1 change at position 472 (Leu in COX-2, Met in COX-1) reduced the potency of enzyme inhibition by a series of COX-2-selective indomethacin amides and esters.	Esters	269-275	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	106-111	
26704937-3	2016	We expressed and assayed a number of divergent secondary shell COX-2 active site mutants and found that a COX-2 to COX-1 change at position 472 (Leu in COX-2, Met in COX-1) reduced the potency of enzyme inhibition by a series of COX-2-selective indomethacin amides and esters.	Esters	269-275	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	106-111