PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8070855-0	1993	Characterization of the human cytochrome P450 isozymes responsible for styrene metabolism.	Styrene	71-78	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	30-45	
8070855-3	1993	The forms of cytochrome P450 that are responsible for transforming styrene to styrene glycol were determined by vaccinia virus-mediated cDNA expression of individual P450 forms in cultured cells.	Styrene	67-74	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	13-28	
8070855-3	1993	The forms of cytochrome P450 that are responsible for transforming styrene to styrene glycol were determined by vaccinia virus-mediated cDNA expression of individual P450 forms in cultured cells.	styrene glycol	78-92	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	13-28	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	36-42	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	108-114	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	116-122	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	159-165	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 3 subfamily A member 5	Homo sapiens	170-176	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 2 subfamily A member 6	Homo sapiens	235-241	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	243-249	
8070855-4	1993	Of the 10 human P450 forms studied, CYP2B6 was the most effective in forming of styrene glycol, followed by CYP1A2, CYP2E1 and CYP2C8; the human P450s CYP3A3, CYP3A4 and CYP3A5 also catalysed metabolism, but were much less active; and CYP2A6, CYP2C9 and CYP2D6 had little detectable activity.	styrene glycol	80-94	cytochrome P450 family 2 subfamily D member 6	Homo sapiens	254-260	
8070855-5	1993	CYP1A1 from mouse liver was more active in forming styrene glycol than mouse CYP1A2; the latter was less active than human CYP1A2.	styrene glycol	51-65	cytochrome P450, family 1, subfamily a, polypeptide 1	Mus musculus	0-6