PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12124303-0	2002	Metabolism of tamoxifen by recombinant human cytochrome P450 enzymes: formation of the 4-hydroxy, 4"-hydroxy and N-desmethyl metabolites and isomerization of trans-4-hydroxytamoxifen.	hydroxytamoxifen	158-182	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	45-60	
12124303-1	2002	The cytochrome P450 (P450)-mediated biotransformation of tamoxifen is important in determining both the clearance of the drug and its conversion to the active metabolite, trans-4-hydroxytamoxifen.	hydroxytamoxifen	171-195	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	4-19	
27198207-1	2016	Tamoxifen is metabolically activated to 4-hydroxytamoxifen and endoxifen by cytochrome P450 (CYP).	hydroxytamoxifen	40-58	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	93-96	
19574470-2	2009	CONTENT: Tamoxifen requires enzymatic activation by cytochrome P450 (CYP) enzymes for the formation of active metabolites 4-hydroxytamoxifen and endoxifen.	hydroxytamoxifen	122-140	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	52-67	
22041137-2	2012	Tamoxifen requires metabolic activation by cytochrome P450 (CYP) enzymes for formation of active metabolites, 4-hydroxytamoxifen and endoxifen, which have 30- to 100-fold greater affinity to the estrogen receptor and the potency to suppress estrogen-dependent breast cancer cell proliferation.	hydroxytamoxifen	110-128	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	43-58	
22041137-2	2012	Tamoxifen requires metabolic activation by cytochrome P450 (CYP) enzymes for formation of active metabolites, 4-hydroxytamoxifen and endoxifen, which have 30- to 100-fold greater affinity to the estrogen receptor and the potency to suppress estrogen-dependent breast cancer cell proliferation.	hydroxytamoxifen	110-128	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	60-63	
21870861-0	2011	A mechanistic hypothesis for the cytochrome P450-catalyzed cis-trans isomerization of 4-hydroxytamoxifen: an unusual redox reaction.	hydroxytamoxifen	86-104	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	33-48	
21870861-1	2011	We provide a detailed description of the cis-trans isomerization of 4-hydroxytamoxifen/endoxifen catalyzed by several isoforms from the cytochrome P450 (CYP) superfamily, including CYP1B1, CYP2B6, and CYP2C19.	hydroxytamoxifen	68-86	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	136-151	
21870861-1	2011	We provide a detailed description of the cis-trans isomerization of 4-hydroxytamoxifen/endoxifen catalyzed by several isoforms from the cytochrome P450 (CYP) superfamily, including CYP1B1, CYP2B6, and CYP2C19.	hydroxytamoxifen	68-86	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	153-156	
26896706-2	2016	TAM is metabolized to the more active 4-hydroxytamoxifen (4-OH-TAM) and endoxifen by cytochrome P450 (CYP) mainly CYP2D6 and CYP3A4 enzymes.	hydroxytamoxifen	38-56	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	85-100	
26896706-2	2016	TAM is metabolized to the more active 4-hydroxytamoxifen (4-OH-TAM) and endoxifen by cytochrome P450 (CYP) mainly CYP2D6 and CYP3A4 enzymes.	hydroxytamoxifen	38-56	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	102-105	
19574470-2	2009	CONTENT: Tamoxifen requires enzymatic activation by cytochrome P450 (CYP) enzymes for the formation of active metabolites 4-hydroxytamoxifen and endoxifen.	hydroxytamoxifen	122-140	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	69-72