PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18202523-7	2007	In summary, Gd suppressed styrene-inducible expression of not only CYP2B1 but also several forms of P450 at both the mRNA and protein levels, along with attenuation of styrene-caused liver damage.	Styrene	26-33	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	67-73	
18202523-2	2007	Gd treatment significantly suppressed styrene-inducible cytochrome P4502B1 (CYP2B1), CYP2B2, CYP2E1, and CYP3A2 mRNA expressions to 48.6%, 69.8%, 61.1%, and 38.5%, accompanying with the reduction of proteins expression to 1.42%, 31.2%, 21.1% and 21.1%, respectively, compared with styrene alone treatment.	Styrene	38-45	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	76-82	
8996724-6	1996	CYP2B1 was induced by styrene to higher extent in the liver, where it was almost indetectable in controls.	Styrene	22-29	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	0-6	
16418063-0	2005	Styrene monomer primarily induces CYP2B1 mRNA in rat liver.	Styrene	0-7	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	34-40	
16418063-3	2005	The amount of CYP2B1 mRNA was significantly increased, 47-fold compared with controls, suggesting that this CYP is the primary cytochrome P450 in rats exposed to styrene.	Styrene	162-169	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	14-20	
16418063-5	2005	Western blot analysis also indicated that the protein levels of CYP2B1, CYP2B2, CYP2E1 and CYP1A2 showed clear increases after styrene treatment, corresponding to their mRNA expression.	Styrene	127-134	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	64-70	
16418063-11	2005	The results demonstrate that CYP2B1 is the primarily induced CYP form by styrene treatment to rats at acute toxic level.	Styrene	73-80	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	29-35	
8080435-0	1994	CYP2C11 and CYP2B1 are major cytochrome P450 forms involved in styrene oxidation in liver and lung microsomes from untreated rats, respectively.	Styrene	63-70	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	12-18	
8080435-5	1994	These results suggest that (1) at least four P450s, CYP2C11/6, CYP2E1, CYP2B1/2 and CYP1A1/2, contribute to the metabolism of styrene, (2) CYP2C11/6, which probably corresponds to CYP2C11, is the major form of P450 responsible for the metabolism in untreated rat liver microsomes, and also in those treated with ethanol.	Styrene	126-133	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	71-77	
8080435-8	1994	Only anti-CYP2B1/2, which probably corresponds to CYP2B1, inhibited styrene oxidation in lung microsomes from untreated and even styrene-treated rats.	Styrene	68-75	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	10-16	
8080435-8	1994	Only anti-CYP2B1/2, which probably corresponds to CYP2B1, inhibited styrene oxidation in lung microsomes from untreated and even styrene-treated rats.	Styrene	68-75	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	50-56	
8080435-8	1994	Only anti-CYP2B1/2, which probably corresponds to CYP2B1, inhibited styrene oxidation in lung microsomes from untreated and even styrene-treated rats.	Styrene	129-136	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	10-16	
8080435-8	1994	Only anti-CYP2B1/2, which probably corresponds to CYP2B1, inhibited styrene oxidation in lung microsomes from untreated and even styrene-treated rats.	Styrene	129-136	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	50-56