PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10718121-0	2000	Metabolite-intermediate complexation and inhibition of microsomal CYP3A in rat liver by diltiazem.	Diltiazem	88-97	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	66-71	
15681897-9	2004	However, ketoconazole and cyclosporin A, which are specific CYP3A inhibitors, inhibited the metabolic extraction of diltiazem (0.05 mM) by only about 20% at the concentration (40 microM) at which they inhibited CYP3A almost completely, suggesting that the contribution of CYP3A to intestinal diltiazem metabolism is not marked.	Diltiazem	116-125	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	60-65	
10454523-2	1999	In this study, we examined whether treatment with the calcium channel antagonists, nicardipine, nifedipine or diltiazem, alters cytochrome P-450 2B or 3A (CYP2B or CYP3A, respectively) expression in rat liver.	Diltiazem	110-119	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	164-169	
28766866-0	2017	Enhanced Oral Bioavailability of Diltiazem by the Influence of Gallic Acid and Ellagic Acid in Male Wistar Rats: Involvement of CYP3A and P-gp Inhibition.	Diltiazem	33-42	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	128-133	
28766866-8	2017	Gallic acid and ellagic acid significantly increased the bioavailability of diltiazem due to the inhibition of both CYP3A-mediated metabolism and P-glycoprotein-mediated efflux in the intestine and/or liver.	Diltiazem	76-85	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	116-121	
15681897-9	2004	However, ketoconazole and cyclosporin A, which are specific CYP3A inhibitors, inhibited the metabolic extraction of diltiazem (0.05 mM) by only about 20% at the concentration (40 microM) at which they inhibited CYP3A almost completely, suggesting that the contribution of CYP3A to intestinal diltiazem metabolism is not marked.	Diltiazem	116-125	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	211-216	
15681897-9	2004	However, ketoconazole and cyclosporin A, which are specific CYP3A inhibitors, inhibited the metabolic extraction of diltiazem (0.05 mM) by only about 20% at the concentration (40 microM) at which they inhibited CYP3A almost completely, suggesting that the contribution of CYP3A to intestinal diltiazem metabolism is not marked.	Diltiazem	116-125	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	211-216	
12951478-4	2003	The simultaneous addition of GBE to small intestine and liver microsomes inhibited the formation of N-demethyl DTZ (MA), an active metabolite of DTZ produced by CYP3A, in a concentration-dependent manner, with an IC(50) of about 50 and 182 microg/ml, respectively.	Diltiazem	111-114	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	161-166	
12951478-9	2003	These results indicated that the concomitant use of GBE in rats increased the bioavailability of DTZ by inhibiting both intestinal and hepatic metabolism, at least in part, via a mechanism-based inhibition for CYP3A.	Diltiazem	97-100	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	210-215