PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
17980168-5	2007	In eosinophils, transcription of the CYP4F12 gene was started from two sites at 49 and 85 nucleotides upstream from the 3" end of exon I. Recombinant CYP4F12 expressed in yeast cell microsomes catalyzed the omega-hydroxylation of leukotriene B4 (LTB4) and 6-trans-LTB4.	Leukotriene B4	230-244	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	37-44
29976573-9	2018	For known CYP4 inhibitors, in contrast, HET0016 inhibited the activities of CYP4A11 and CYP4F2 (IC50 = 0.0137-0.0182 muM); 17-octadecynoic acid reduced activities of CYP4A11, CYP4F2, CYP4F3B, and CYP4F12 to a similar extent (IC50 = 5.70-17.7 muM).	17-octadecynoic acid	123-143	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	196-203
21778351-7	2011	When treated with saturated, monounsaturated, or polyunsaturated fatty acids, CYP4F3B and CYP4A11 expression remained unchanged whereas CYP4F2 and CYP4F12 expression was transiently up-regulated.	saturated,	18-28	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	147-154
21778351-7	2011	When treated with saturated, monounsaturated, or polyunsaturated fatty acids, CYP4F3B and CYP4A11 expression remained unchanged whereas CYP4F2 and CYP4F12 expression was transiently up-regulated.	monounsaturated,	29-45	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	147-154
30280198-7	2018	GSEA revealed high levels of CYP4F2, CYP4F12 and CYP4V2 mRNA expression to be negatively correlated with the expression of cell cycle-associated genes.	gsea	0-4	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	37-44
28620303-0	2017	Effect of Genetic Variability in the CYP4F2, CYP4F11, and CYP4F12 Genes on Liver mRNA Levels and Warfarin Response.	Warfarin	97-105	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	58-65
25074871-3	2014	By using astemizole as a probe substrate for CYP4F12 and CYP3A4, it was observed that although CYP4F12 favored astemizole O-demethylation as the primary route of metabolism, CYP3A4 was capable of metabolizing astemizole at multiple sites on the molecule.	Astemizole	9-19	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	45-52
25074871-3	2014	By using astemizole as a probe substrate for CYP4F12 and CYP3A4, it was observed that although CYP4F12 favored astemizole O-demethylation as the primary route of metabolism, CYP3A4 was capable of metabolizing astemizole at multiple sites on the molecule.	Astemizole	9-19	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	95-102
25074871-3	2014	By using astemizole as a probe substrate for CYP4F12 and CYP3A4, it was observed that although CYP4F12 favored astemizole O-demethylation as the primary route of metabolism, CYP3A4 was capable of metabolizing astemizole at multiple sites on the molecule.	Astemizole	111-121	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	45-52
25074871-3	2014	By using astemizole as a probe substrate for CYP4F12 and CYP3A4, it was observed that although CYP4F12 favored astemizole O-demethylation as the primary route of metabolism, CYP3A4 was capable of metabolizing astemizole at multiple sites on the molecule.	Astemizole	111-121	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	95-102
25074871-3	2014	By using astemizole as a probe substrate for CYP4F12 and CYP3A4, it was observed that although CYP4F12 favored astemizole O-demethylation as the primary route of metabolism, CYP3A4 was capable of metabolizing astemizole at multiple sites on the molecule.	Astemizole	111-121	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	45-52
25074871-3	2014	By using astemizole as a probe substrate for CYP4F12 and CYP3A4, it was observed that although CYP4F12 favored astemizole O-demethylation as the primary route of metabolism, CYP3A4 was capable of metabolizing astemizole at multiple sites on the molecule.	Astemizole	111-121	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	95-102
25074871-4	2014	Deuteration of astemizole at the site of O-demethylation resulted in an isotope effect of 7.1 as well as an 8.3-fold decrease in the rate of clearance for astemizole by CYP4F12.	Astemizole	15-25	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	169-176
25074871-4	2014	Deuteration of astemizole at the site of O-demethylation resulted in an isotope effect of 7.1 as well as an 8.3-fold decrease in the rate of clearance for astemizole by CYP4F12.	Astemizole	155-165	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	169-176
25074871-7	2014	As predicted, multiple favorable binding orientations were available for astemizole docked into the active site of CYP3A4, but only a single binding orientation with the site of O-demethylation oriented toward the heme was identified for CYP4F12.	Heme	214-218	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	238-245
19129222-4	2009	Of these, only CYP4F12 demonstrated increased binding in the presence of rifampicin.	Rifampin	73-83	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	15-22
17980168-5	2007	In eosinophils, transcription of the CYP4F12 gene was started from two sites at 49 and 85 nucleotides upstream from the 3" end of exon I. Recombinant CYP4F12 expressed in yeast cell microsomes catalyzed the omega-hydroxylation of leukotriene B4 (LTB4) and 6-trans-LTB4.	Leukotriene B4	230-244	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	150-157
15238214-4	2004	The HL60 cells, which were differentiated into PMN-like shapes by treatment with all-trans-retinoic acid (RA), also expressed CYP4F3, CYP4F3B and CYP4F12.	Tretinoin	81-104	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	146-153
16112640-0	2005	Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8.	Tyrosine	116-119	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	80-87
16112640-0	2005	Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8.	Glycine	128-131	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	80-87
16112640-1	2005	Recombinant CYP4F8 and CYP4F12 metabolize prostaglandin H2 (PGH2) analogs by omega2- and omega3-hydroxylation and arachidonic acid (20:4n-6) by omega3-hydroxylation.	Prostaglandin H2	42-58	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	23-30
16112640-1	2005	Recombinant CYP4F8 and CYP4F12 metabolize prostaglandin H2 (PGH2) analogs by omega2- and omega3-hydroxylation and arachidonic acid (20:4n-6) by omega3-hydroxylation.	Prostaglandin H2	60-64	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	23-30
16112640-1	2005	Recombinant CYP4F8 and CYP4F12 metabolize prostaglandin H2 (PGH2) analogs by omega2- and omega3-hydroxylation and arachidonic acid (20:4n-6) by omega3-hydroxylation.	Arachidonic Acid	114-130	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	23-30
16112640-7	2005	CYP4F enzymes with omega-hydroxylase activity contain a heme-binding Glu residue, whereas CYP4F8 (and CYP4F12) with omega2- and omega 3-hydroxylase activities has a Gly residue in this position of SRS-4.	Glycine	165-168	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	102-109
16112640-0	2005	Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8.	polyunsaturated long chain fatty acids	15-53	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	80-87
15238214-4	2004	The HL60 cells, which were differentiated into PMN-like shapes by treatment with all-trans-retinoic acid (RA), also expressed CYP4F3, CYP4F3B and CYP4F12.	Tretinoin	106-108	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	146-153
15078342-2	2004	CYP4F12 can oxidize arachidonic acid, two stable prostaglandin H2 analogues, and an antihistamine, ebastine, but the tissue distribution and catalytic properties of CYP4F12 have not been fully investigated.	Arachidonic Acid	20-36	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
15078342-2	2004	CYP4F12 can oxidize arachidonic acid, two stable prostaglandin H2 analogues, and an antihistamine, ebastine, but the tissue distribution and catalytic properties of CYP4F12 have not been fully investigated.	Prostaglandin H2	49-65	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
15078342-2	2004	CYP4F12 can oxidize arachidonic acid, two stable prostaglandin H2 analogues, and an antihistamine, ebastine, but the tissue distribution and catalytic properties of CYP4F12 have not been fully investigated.	ebastine	99-107	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
15078342-2	2004	CYP4F12 can oxidize arachidonic acid, two stable prostaglandin H2 analogues, and an antihistamine, ebastine, but the tissue distribution and catalytic properties of CYP4F12 have not been fully investigated.	ebastine	99-107	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	165-172
11162607-5	2001	CYP4F12, expressed in yeast, oxidized arachidonic acid to 18-hydroxyarachidonic acid, and the omega-side chain of two stable prostaglandin (PG) H(2) analogs (11,9-epoxymethano-PGH(2) and 9,11-diazo-15-deoxy-PGH(2)).	Arachidonic Acid	38-54	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162645-6	2001	Interestingly, CYP4F12 catalyzes the hydroxylation of the antihistamine ebastine with significantly higher catalytic activity relative to CYP4F2 (385 vs 5 pmol/min/nmol P450).	antihistamine ebastine	58-80	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	15-22
14709627-5	2004	The reference inhibitor ketoconazole was less selective and exhibited potent inhibition (IC(50) values <10 microM) for CYP1A1, CYP1B1, CYP2B6, CYP2C8, CYP2C9, CYP2C19, CYP4F2, and CYP4F12.	Ketoconazole	24-36	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	183-190
11752129-0	2002	Involvement of CYP2J2 and CYP4F12 in the metabolism of ebastine in human intestinal microsomes.	ebastine	55-63	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	26-33
11162607-5	2001	CYP4F12, expressed in yeast, oxidized arachidonic acid to 18-hydroxyarachidonic acid, and the omega-side chain of two stable prostaglandin (PG) H(2) analogs (11,9-epoxymethano-PGH(2) and 9,11-diazo-15-deoxy-PGH(2)).	18-Hydroxyarachidonic acid	58-84	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-5	2001	CYP4F12, expressed in yeast, oxidized arachidonic acid to 18-hydroxyarachidonic acid, and the omega-side chain of two stable prostaglandin (PG) H(2) analogs (11,9-epoxymethano-PGH(2) and 9,11-diazo-15-deoxy-PGH(2)).	Prostaglandins H	125-145	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-5	2001	CYP4F12, expressed in yeast, oxidized arachidonic acid to 18-hydroxyarachidonic acid, and the omega-side chain of two stable prostaglandin (PG) H(2) analogs (11,9-epoxymethano-PGH(2) and 9,11-diazo-15-deoxy-PGH(2)).	11,9-epoxymethano-pgh	158-179	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-5	2001	CYP4F12, expressed in yeast, oxidized arachidonic acid to 18-hydroxyarachidonic acid, and the omega-side chain of two stable prostaglandin (PG) H(2) analogs (11,9-epoxymethano-PGH(2) and 9,11-diazo-15-deoxy-PGH(2)).	9,11-diazo-15-deoxy-pgh	187-210	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-6	2001	CYP4F12 oxidized the omega-side chain of leukotriene B(4), PGE(2), PGF(2 alpha), PGH(2), and 9,11-epoxymethano-PGH(2) poorly.	Leukotriene B4	41-54	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-6	2001	CYP4F12 oxidized the omega-side chain of leukotriene B(4), PGE(2), PGF(2 alpha), PGH(2), and 9,11-epoxymethano-PGH(2) poorly.	Prostaglandins E	59-62	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-6	2001	CYP4F12 oxidized the omega-side chain of leukotriene B(4), PGE(2), PGF(2 alpha), PGH(2), and 9,11-epoxymethano-PGH(2) poorly.	Prostaglandins F	67-70	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-6	2001	CYP4F12 oxidized the omega-side chain of leukotriene B(4), PGE(2), PGF(2 alpha), PGH(2), and 9,11-epoxymethano-PGH(2) poorly.	GH2 protein, human	81-84	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7
11162607-6	2001	CYP4F12 oxidized the omega-side chain of leukotriene B(4), PGE(2), PGF(2 alpha), PGH(2), and 9,11-epoxymethano-PGH(2) poorly.	9,11-epoxymethano-pgh	93-114	cytochrome P450 family 4 subfamily F member 12	Homo sapiens	0-7