PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19482014-5	2009	Formation of reactive intermediates of chlorpromazine and thioridazine was primarily mediated by heterologously expressed recombinant CYP2D6, and to a less extent, CYP1A2.	Thioridazine	58-70	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	164-170	
16272405-3	2006	The results indicate that CYP1A2 and CYP3A4 are the main enzymes responsible for 5-sulfoxidation and N-demethylation (34-52%), whereas CYP2D6 is the basic enzyme that catalyzes mono-2- and di-2-sulfoxidation of thioridazine in human liver (49 and 64%, respectively).	Thioridazine	211-223	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	26-32	
20615392-7	2010	The obtained results indicate that the catalysis of chlorpromazine N-demethylation and 5-sulfoxidation in humans exhibits a stricter CYP1A2 preference compared to the previously tested phenothiazines (promazine, perazine, and thioridazine).	Thioridazine	226-238	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	133-139	
10587283-6	1999	In conclusion, fluvoxamine markedly interferes with the metabolism of THD, probably at the CYP2C19 and/or CYP1A2 enzyme level.	Thioridazine	70-73	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	106-112