PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	lipoprotein lipase	Homo sapiens	19-37	
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	lipoprotein lipase	Homo sapiens	39-42	
3964650-1	1986	The interaction of lipoprotein lipase (LpL) and a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), has been studied by several physical methods.	Dimyristoylphosphatidylcholine	87-132	lipoprotein lipase	Homo sapiens	19-37	
3964650-1	1986	The interaction of lipoprotein lipase (LpL) and a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), has been studied by several physical methods.	Dimyristoylphosphatidylcholine	87-132	lipoprotein lipase	Homo sapiens	39-42	
6733134-0	1984	Lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	43-73	lipoprotein lipase	Homo sapiens	0-18	
6733134-2	1984	The effect of phospholipid organization on the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine was examined with sonicated vesicles and Triton X-100 or lysomyristoylphosphatidylcholine solubilized lipid.	Dimyristoylphosphatidylcholine	90-120	lipoprotein lipase	Homo sapiens	47-65	
6733134-4	1984	Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested.	Dimyristoylphosphatidylcholine	135-165	lipoprotein lipase	Homo sapiens	47-65	
6733134-4	1984	Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested.	Dimyristoylphosphatidylcholine	135-165	lipoprotein lipase	Homo sapiens	92-110	
22008704-6	2012	RESULTS: Activity of APOA5 variants on LPL-mediated 1,2-dimyristoyl-sn-glycero-3-phosphocholine hydrolysis was reduced by 17 to 74% in comparison to wild type APOA5 (P<0.0001).	Dimyristoylphosphatidylcholine	52-95	lipoprotein lipase	Homo sapiens	39-42