PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21178301-7	2011	The k(inact)/K(I) ratios of these lignans were higher than those reported for some therapeutic drugs that act as mechanism-based inhibitors of CYP3A4.	Lignans	34-41	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	143-149	
24462213-7	2014	Metabolism study in the human recombinant CYP 3A showed that these lignans had higher affinity to CYP3A than that of FK506, and thus had a stronger CYP3A-mediated metabolism.	Lignans	67-74	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	42-48	
24462213-7	2014	Metabolism study in the human recombinant CYP 3A showed that these lignans had higher affinity to CYP3A than that of FK506, and thus had a stronger CYP3A-mediated metabolism.	Lignans	67-74	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	98-103	
24462213-7	2014	Metabolism study in the human recombinant CYP 3A showed that these lignans had higher affinity to CYP3A than that of FK506, and thus had a stronger CYP3A-mediated metabolism.	Lignans	67-74	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	148-153	
24462213-8	2014	It was concluded that the blood concentrations of these lignans were decreased and their CYP3A-mediated metabolisms were increased in the presence of FK506 since these lignans had higher affinity to CYP3A.	Lignans	56-63	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	199-204	
24462213-8	2014	It was concluded that the blood concentrations of these lignans were decreased and their CYP3A-mediated metabolisms were increased in the presence of FK506 since these lignans had higher affinity to CYP3A.	Lignans	168-175	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	89-94	
24462213-8	2014	It was concluded that the blood concentrations of these lignans were decreased and their CYP3A-mediated metabolisms were increased in the presence of FK506 since these lignans had higher affinity to CYP3A.	Lignans	168-175	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	199-204	
33802239-6	2021	We found that lignans with one or two methylenedioxyphenyl groups inhibited CYP2B6, CYP2C8, CYP2C9, CYP2C19, and CYP2E1 activities in a time- and concentration-dependent like their CYP3A inhibition.	Lignans	14-21	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	181-186	
18563665-0	2008	Mechanism-based inactivation of cytochrome P450 3A4 by methylenedioxyphenyl lignans from Acanthopanax chiisanensis.	Lignans	76-83	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	32-51	
18563665-1	2008	The purpose of this investigation is to characterize the inhibition of CYP3A4 by methylenedioxyphenyl lignans isolated from ACANTHOPANAX CHIISANENSIS.	Lignans	102-109	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	71-77	
18563665-3	2008	The inhibition of CYP3A4 activity by these lignans was suppressed in the presence of a competitive CYP3A4 substrate, ketoconazole.	Lignans	43-50	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	18-24	
18563665-3	2008	The inhibition of CYP3A4 activity by these lignans was suppressed in the presence of a competitive CYP3A4 substrate, ketoconazole.	Lignans	43-50	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	99-105	
28344076-2	2017	However, the potential herb-drug interactions (HDI) between these lignans and other drugs through inhibiting human cytochrome P450 3A4 (CYP3A4) and CYP3A5 remains unclear.	Lignans	66-73	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	115-134	
28344076-2	2017	However, the potential herb-drug interactions (HDI) between these lignans and other drugs through inhibiting human cytochrome P450 3A4 (CYP3A4) and CYP3A5 remains unclear.	Lignans	66-73	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	136-142	
28344076-0	2017	Inhibition of human CYP3A4 and CYP3A5 enzymes by gomisin C and gomisin G, two lignan analogs derived from Schisandra chinensis.	Lignans	78-84	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	20-26