Pub. Date : 2016 Jan 19
PMID : 26704937
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | 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 | mitochondrially encoded cytochrome c oxidase II | Homo sapiens |
| 2 | 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 | mitochondrially encoded cytochrome c oxidase II | Homo sapiens |
| 3 | 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 | mitochondrially encoded cytochrome c oxidase II | Homo sapiens |
| 4 | 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 | mitochondrially encoded cytochrome c oxidase II | Homo sapiens |
| 5 | 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 | mitochondrially encoded cytochrome c oxidase II | Homo sapiens |