PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9193873-0	1997	Cytochrome P450 responsible for the stereoselective S-oxidation of flosequinan in hepatic microsomes from rats and humans.	flosequinan	67-78	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	0-15	
9193873-1	1997	The forms of cytochrome P450 involved in the stereoselective S-oxidation of flosequinan [(+/-)-7-fluoro-1-methyl-3-methylsulfinyl-4-quinolone] were investigated in vitro using liver microsomes from rats and humans.	flosequinan	76-87	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	13-28	
9193873-1	1997	The forms of cytochrome P450 involved in the stereoselective S-oxidation of flosequinan [(+/-)-7-fluoro-1-methyl-3-methylsulfinyl-4-quinolone] were investigated in vitro using liver microsomes from rats and humans.	flosequinan	89-141	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	13-28	
9193873-8	1997	Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations.	phenylalanylserine	94-96	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-8	1997	Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations.	r-fso	100-105	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-8	1997	Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations.	s-fso	119-124	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-8	1997	Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations.	r-fso	246-251	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-8	1997	Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations.	s-fso	256-261	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-8	1997	Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations.	fso2	265-269	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-9	1997	These results suggest that CYP3A is the major enzyme involved in all S-oxidation pathways in flosequinan metabolism in rats.	flosequinan	93-104	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	27-32	
9193873-11	1997	Anti-CYP3A2 antisera inhibited the activities of all the S-oxidases in human liver microsomes ranging from 40 to 80%, suggesting that CYP3A is also involved in all of the S-oxidations of flosequinan in humans.	flosequinan	187-198	cytochrome P450, family 3, subfamily a, polypeptide 2	Rattus norvegicus	5-11	
9193873-11	1997	Anti-CYP3A2 antisera inhibited the activities of all the S-oxidases in human liver microsomes ranging from 40 to 80%, suggesting that CYP3A is also involved in all of the S-oxidations of flosequinan in humans.	flosequinan	187-198	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	5-10