PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12167563-1	2002	The principal enzyme involved in the oxidation of mifepristone is cytochrome P450 3A4 (CYP3A4), which undergoes mechanism-based inactivation by the drug.	Mifepristone	50-62	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	66-85	
12167563-1	2002	The principal enzyme involved in the oxidation of mifepristone is cytochrome P450 3A4 (CYP3A4), which undergoes mechanism-based inactivation by the drug.	Mifepristone	50-62	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	87-93	
12167563-3	2002	Oxidation of mifepristone by recombinant CYP3A4 produced mono- and didemethylated products and one C-hydroxylated metabolite, as reported previously.	Mifepristone	13-25	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	41-47	
12167563-10	2002	Together these results indicate that mifepristone fails to orient itself in the CYP3A5 active site in such a way that its propylenic group is accessible for oxidation, thus rendering CYP3A5 unable to produce the C-hydroxylated product or putative ketene that leads to enzyme inactivation.	Mifepristone	37-49	cytochrome P450 family 3 subfamily A member 5	Homo sapiens	80-86	
12167563-10	2002	Together these results indicate that mifepristone fails to orient itself in the CYP3A5 active site in such a way that its propylenic group is accessible for oxidation, thus rendering CYP3A5 unable to produce the C-hydroxylated product or putative ketene that leads to enzyme inactivation.	Mifepristone	37-49	cytochrome P450 family 3 subfamily A member 5	Homo sapiens	183-189	
12167563-10	2002	Together these results indicate that mifepristone fails to orient itself in the CYP3A5 active site in such a way that its propylenic group is accessible for oxidation, thus rendering CYP3A5 unable to produce the C-hydroxylated product or putative ketene that leads to enzyme inactivation.	ketene	247-253	cytochrome P450 family 3 subfamily A member 5	Homo sapiens	80-86	
12167563-11	2002	Identification of mifepristone as a selective mechanism-based inactivation of CYP3A4 may be very useful in distinguishing between the two major CYP3A enzymes collectively responsible for the oxidative metabolism of over half of the drugs currently in use.	Mifepristone	18-30	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	78-84	
12167563-11	2002	Identification of mifepristone as a selective mechanism-based inactivation of CYP3A4 may be very useful in distinguishing between the two major CYP3A enzymes collectively responsible for the oxidative metabolism of over half of the drugs currently in use.	Mifepristone	18-30	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	78-83