PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12502361-6	2003	MD studies on the binding mode of sparteine, quinidine, and quinine in CYP2D2 and CYP2D6 furthermore concurred well with experimentally determined IC(50) values and metabolic profiles.	Quinine	60-67	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	82-88	
1763518-11	1991	As quinidine is a more potent inhibitor than quinine of debrisoquine 4-hydroxylase in man, the rat should be used only with full realization of its limitations when investigating substrates metabolized by this isoenzyme.	Quinine	45-52	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	56-82	
1763518-0	1991	Quinine is a more potent inhibitor than quinidine in rat of the oxidative metabolic routes of methoxyphenamine which involve debrisoquine 4-hydroxylase.	Quinine	0-7	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	125-151	
28347660-4	2017	Quinidine exhibited stronger inhibition than quinine; however, these two compounds inhibited the CYP2D6.10-mediated reaction more weakly than the CYP2D6.1 and CYP2D6.2 reactions.	Quinine	45-52	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	97-103	
28347660-4	2017	Quinidine exhibited stronger inhibition than quinine; however, these two compounds inhibited the CYP2D6.10-mediated reaction more weakly than the CYP2D6.1 and CYP2D6.2 reactions.	Quinine	45-52	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	146-152	
28347660-4	2017	Quinidine exhibited stronger inhibition than quinine; however, these two compounds inhibited the CYP2D6.10-mediated reaction more weakly than the CYP2D6.1 and CYP2D6.2 reactions.	Quinine	45-52	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	146-152