PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7956732-0	1994	Evidence that the biotransformation of dapsone and monoacetyldapsone to their respective hydroxylamine metabolites in rat liver microsomes is mediated by cytochrome P450 2C6/2C11 and 3A1.	Dapsone	39-46	cytochrome P450, family 2, subfamily C, polypeptide 6, variant 1	Rattus norvegicus	154-173	
7956732-0	1994	Evidence that the biotransformation of dapsone and monoacetyldapsone to their respective hydroxylamine metabolites in rat liver microsomes is mediated by cytochrome P450 2C6/2C11 and 3A1.	monoacetyldapsone	51-68	cytochrome P450, family 2, subfamily C, polypeptide 6, variant 1	Rattus norvegicus	154-173	
7956732-0	1994	Evidence that the biotransformation of dapsone and monoacetyldapsone to their respective hydroxylamine metabolites in rat liver microsomes is mediated by cytochrome P450 2C6/2C11 and 3A1.	Hydroxylamine	89-102	cytochrome P450, family 2, subfamily C, polypeptide 6, variant 1	Rattus norvegicus	154-173	
7956732-2	1994	Preincubation with cimetidine (selective for inhibition of CYP2C11), but not troleandomycin (selective for inhibition of CYP3A1/2), inhibited metabolite formation.	Cimetidine	19-29	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	59-66	
7956732-4	1994	Together, these data indicate that N-hydroxylation of DDS and MADDS in rat liver microsomes from untreated male rats is catalyzed by CYP2C6/2C11.	Nitrogen	35-36	cytochrome P450, family 2, subfamily C, polypeptide 6, variant 1	Rattus norvegicus	133-139