PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12110367-7	2002	In reconstituted systems containing CYP2C9, CYP2C19, and CYP3A4, the formation of 3",4"-diHPPH was also enhanced by catalase to different extents.	3",4"-dihpph	82-94	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	57-63	
11038165-9	2000	These results suggest that CYP2C9, CYP2C19, and CYP3A4 all have catalytic activities in 3",4"-diHPPH formation from primary hydroxylated metabolites in human liver and that the hepatic contents of these three P450 forms determine which P450 enzymes play major roles of DPH oxidation in individual humans.	3",4"-dihpph	88-100	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	48-54	
11038165-5	2000	In the presence of liver cytosol, 3",4"-diHPPH formation activity from 100 microM 4"-HPPH was correlated with testosterone 6beta-hydroxylation activity and CYP3A4 content.	3",4"-dihpph	34-46	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	156-162	
11038165-7	2000	Of 10 cDNA-expressed human P450 enzymes examined, CYP2C19, CYP2C9, and CYP3A4 catalyzed 3",4"-diHPPH formation from the primary hydroxylated metabolites (3"-hydroxy-DPH and 4"-HPPH).	3",4"-dihpph	88-100	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	71-77