PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16896065-11	2006	In conclusion, our data for the first time, to our knowledge, suggest that both CYP2J2 and CYP3A play important roles in ebastine sequential metabolism: dealkylation of ebastine and its metabolites is mainly catalyzed by CYP3A4, whereas the hydroxylation reactions are preferentially catalyzed by CYP2J2.	ebastine	169-177	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	91-96	
16896065-3	2006	Although CYP3A4 and CYP2J2 have been implicated in ebastine N-dealkylation and hydroxylation, the enzyme catalyzing the subsequent metabolic steps (conversion of hydroxyebastine to desalkylebastine and carebastine) have not been identified.	ebastine	51-59	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	9-15	
16896065-11	2006	In conclusion, our data for the first time, to our knowledge, suggest that both CYP2J2 and CYP3A play important roles in ebastine sequential metabolism: dealkylation of ebastine and its metabolites is mainly catalyzed by CYP3A4, whereas the hydroxylation reactions are preferentially catalyzed by CYP2J2.	ebastine	169-177	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	221-227	
16896065-6	2006	Of the 11 cDNA-expressed P450s, CYP3A4 was the main enzyme catalyzing the N-dealkylation of ebastine, hydroxyebastine, and carebastine to desalkylebastine [intrinsic clearance (CL(int)) = 0.44, 1.05, and 0.16 microl/min/pmol P450, respectively].	ebastine	92-100	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	32-38	
16896065-8	2006	Ebastine hydroxylation to hydroxyebastine is mainly mediated by CYP2J2 (0.45 microl/min/pmol P450; 22.5- and 7.5-fold higher than that for CYP3A4 and CYP3A5, respectively), whereas CYP2J2 and CYP3A4 contributed to the formation of carebastine from hydroxyebastine.	ebastine	0-8	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	139-145	
11396753-1	2001	OBJECTIVES: Ebastine is a potent and selective H1-receptor antagonist indicated for allergic rhinitis which undergoes extensive first pass metabolism by CYP3A4 to form an active metabolite, carebastine.	ebastine	12-20	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	153-159	
16896065-8	2006	Ebastine hydroxylation to hydroxyebastine is mainly mediated by CYP2J2 (0.45 microl/min/pmol P450; 22.5- and 7.5-fold higher than that for CYP3A4 and CYP3A5, respectively), whereas CYP2J2 and CYP3A4 contributed to the formation of carebastine from hydroxyebastine.	ebastine	0-8	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	192-198	
16896065-11	2006	In conclusion, our data for the first time, to our knowledge, suggest that both CYP2J2 and CYP3A play important roles in ebastine sequential metabolism: dealkylation of ebastine and its metabolites is mainly catalyzed by CYP3A4, whereas the hydroxylation reactions are preferentially catalyzed by CYP2J2.	ebastine	121-129	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	91-96	
16896065-11	2006	In conclusion, our data for the first time, to our knowledge, suggest that both CYP2J2 and CYP3A play important roles in ebastine sequential metabolism: dealkylation of ebastine and its metabolites is mainly catalyzed by CYP3A4, whereas the hydroxylation reactions are preferentially catalyzed by CYP2J2.	ebastine	121-129	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	221-227	
9616193-9	1998	Among 12 cDNA-expressed human CYP isoforms, which account for up to 70% of the total CYP enzyme content in human liver, CYP3A4 alone metabolized ebastine; the ratio of des-BP to M-OH formation was 12:1.	ebastine	145-153	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	120-126	
9616193-11	1998	This change in ratio, which is attributed to a decrease in M-OH formation, indicates that, although ebastine is metabolized to two major metabolites, N-dealkylation to des-BP is mediated by CYP3A, whereas hydroxylation to M-OH appears to be mediated mainly by unidentified enzymes other than CYP3A.	ebastine	100-108	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	292-297