PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15882068-6	2005	Subsequently, apo A-I forms small ( approximately 5-15 nm) complexes with lecithin and cholesterol that coexist with lipid-stabilized (400-800 nm) DAG oil droplets.	Lecithins	74-82	apolipoprotein A1	Homo sapiens	14-21	
23516040-1	2013	Existing kinetic data of cholesteryl ester formation by lecithin:cholesterol acyltransferase in discoidal high-density lipoproteins with 34 mutations of apoA-I that involved all putative helices were grouped by cluster analysis into four noncoincident regions with mutations both without any functional impairment and with profound isolated (V- and K-mutations) or common (VK-mutations) effect on V(max)(app) and K(m)(app).	Lecithins	56-64	apolipoprotein A1	Homo sapiens	153-159	
15882068-11	2005	A fluorescence assay involving dansylated lecithin shows that the suppression is an indirect effect of apo A-I rather than a direct inhibition of PLC enzyme activity.	Lecithins	42-50	apolipoprotein A1	Homo sapiens	103-110	
3082628-9	1986	These results indicated that apo A-II must be incorporated together with apo A-I into lecithin-cholesterol liposomes to exert its stimulatory effect on LCAT activity and that apo A-II in high-density lipoprotein may play an important role in the regulation of LCAT activity.	Lecithins	86-94	apolipoprotein A1	Homo sapiens	29-36	
14729075-6	2003	Apo A-I possibly induces the formation of small apo A-I/lecithin/cholesterol complexes of about 5-20 nm similar to the discoidal pre-HDL complexes found in blood when it can no longer effectively shield all the DAG molecules.	Lecithins	56-64	apolipoprotein A1	Homo sapiens	0-7	
14729075-6	2003	Apo A-I possibly induces the formation of small apo A-I/lecithin/cholesterol complexes of about 5-20 nm similar to the discoidal pre-HDL complexes found in blood when it can no longer effectively shield all the DAG molecules.	Lecithins	56-64	apolipoprotein A1	Homo sapiens	48-55	
9580110-4	1998	A possible mechanism of the pro-atherogenic action of human apoA-II could be the inhibition of reverse cholesterol transport and, in support of this, we observed an impairment of apoA-I-HDL particle interconversion in the plasma of 11.1 transgenic mice caused, at least in part, by a marked decrease in the endogenous lecithin:cholesterol acyltransferase activity.	Lecithins	318-326	apolipoprotein A1	Homo sapiens	60-66	
1644835-11	1992	Electron microscopy of the proteoliposome LCAT substrate generated by WT and mutant apoA-I forms showed that the carboxyl-terminal deletion mutants which displayed aberrant binding to HDL also displayed reduced ability to convert the spherical lecithin-cholesterol vesicles into discs compared with WT.	Lecithins	244-252	apolipoprotein A1	Homo sapiens	84-90	
3126801-0	1987	Formation of mixed micelles and vesicles of human apolipoproteins A-I and A-II with synthetic and natural lecithins and the bile salt sodium taurocholate: quasi-elastic light scattering studies.	Lecithins	106-115	apolipoprotein A1	Homo sapiens	50-78	
33861588-5	2021	In vitro, MPO-mediated damage of lipid-free apoA-I impaired its ability to promote cellular cholesterol efflux by the ABCA1 pathway, whereas oxidation to lipid-associated apoA-I inhibited lecithin:cholesterol acyltransferase activation, two key steps in reverse cholesterol transport.	Lecithins	188-196	apolipoprotein A1	Homo sapiens	44-50	
6423754-6	1984	The isoprotein-2 of normal apoA-I and the isoprotein-4 of Tangier apoA-I generate lipid-rich complexes with lecithin, while the isoprotein-2 of Tangier apoA-I shows only a limited association with lipids.	Lecithins	108-116	apolipoprotein A1	Homo sapiens	27-33	
6423754-6	1984	The isoprotein-2 of normal apoA-I and the isoprotein-4 of Tangier apoA-I generate lipid-rich complexes with lecithin, while the isoprotein-2 of Tangier apoA-I shows only a limited association with lipids.	Lecithins	108-116	apolipoprotein A1	Homo sapiens	66-72	
6423754-6	1984	The isoprotein-2 of normal apoA-I and the isoprotein-4 of Tangier apoA-I generate lipid-rich complexes with lecithin, while the isoprotein-2 of Tangier apoA-I shows only a limited association with lipids.	Lecithins	108-116	apolipoprotein A1	Homo sapiens	66-72	
6423754-9	1984	This transition was observed for the isoprotein-2 of apoA-I Tangier both in its lipid-free form and in the presence of lecithin.	Lecithins	119-127	apolipoprotein A1	Homo sapiens	53-59	
6801887-5	1981	These results suggest that apo A-II has a higher affinity than apo A-I for the lecithin-cholesterol vesicle and that 2 mol apo A-II are able to displace 1 mol apo A-I from the apo A-I lipid complexes.	Lecithins	79-87	apolipoprotein A1	Homo sapiens	27-34	
6801887-5	1981	These results suggest that apo A-II has a higher affinity than apo A-I for the lecithin-cholesterol vesicle and that 2 mol apo A-II are able to displace 1 mol apo A-I from the apo A-I lipid complexes.	Lecithins	79-87	apolipoprotein A1	Homo sapiens	63-70	
6801887-5	1981	These results suggest that apo A-II has a higher affinity than apo A-I for the lecithin-cholesterol vesicle and that 2 mol apo A-II are able to displace 1 mol apo A-I from the apo A-I lipid complexes.	Lecithins	79-87	apolipoprotein A1	Homo sapiens	63-70	
170277-12	1975	HDLs were also made by incubating dispersed lecithin or lecithin + cholesterol with Apo-HDL, ApoA-I, or ApoA-II.	Lecithins	44-52	apolipoprotein A1	Homo sapiens	93-99	
3918999-5	1985	Apo-A-I was a more potent activator than apo-A-IV with egg yolk lecithin, L-alpha-dioleoylphosphatidylcholine, and L-alpha-phosphatidylcholine substituted with one saturated and one unsaturated fatty acid regardless of the substitution position.	Lecithins	64-72	apolipoprotein A1	Homo sapiens	0-7	
193772-1	1977	Intermolecular cross-linkage between high-density apolipoprotein A-I and lecithins and sphingomyelins.	Lecithins	73-82	apolipoprotein A1	Homo sapiens	50-68	
33861588-5	2021	In vitro, MPO-mediated damage of lipid-free apoA-I impaired its ability to promote cellular cholesterol efflux by the ABCA1 pathway, whereas oxidation to lipid-associated apoA-I inhibited lecithin:cholesterol acyltransferase activation, two key steps in reverse cholesterol transport.	Lecithins	188-196	apolipoprotein A1	Homo sapiens	171-177