PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16327166-6	2005	The hexamers of insulin were dissociated to monomers only by chitosan, polyoxyethylene lauryl ether, and egg lecithin.	Lecithins	109-117	insulin	Homo sapiens	16-23	
3906680-1	1985	Microvesicles made of mixtures of lecithin and phosphatidic acid were precipitated by insulin in acid solution.	Lecithins	34-42	insulin	Homo sapiens	86-93	
6991910-0	1980	Insulin-lecithin interaction in non-aqueous solvents and its change after application of a static electric field.	Lecithins	8-16	insulin	Homo sapiens	0-7	
6991910-3	1980	The different strength of interaction of insulin with the two types of lecithins results also from experiments with a two-phase system.	Lecithins	71-80	insulin	Homo sapiens	41-48	
577607-3	1977	These results tend to support the hypothesis that insulin can inhibit lecithin synthesis.	Lecithins	70-78	insulin	Homo sapiens	50-57	
957026-0	1976	Letter: Effect of cortisol/insulin in lecithin synthesis.	Lecithins	38-46	insulin	Homo sapiens	27-34	
3548819-5	1987	With 1-fluoro-2,4-dinitrobenzene as the labeling reagent, the relative chemical reactivities of the functional groups of insulin were found to decrease markedly when insulin was incubated with liposomes consisting of egg lecithin and cholesterol (2:1 mol/mol) in 1.0 M KCl, pH 7.5 at 37 degrees C. The decrease for each functional group was found to directly correlate with its proximity to the dimer-forming surface of the monomer.	Lecithins	221-229	insulin	Homo sapiens	121-128	
24234896-1	1993	The interaction between zinc-stabilized insulin and lecithin liposomal membranes was studied using DPH fluorescence anisotropy and light-scattering techniques.	Lecithins	52-60	insulin	Homo sapiens	40-47	
24234896-3	1993	Measurements at pH 4.5 revealed significant changes in scattered light intensity induced by the addition of insulin to lecithin liposomes.	Lecithins	119-127	insulin	Homo sapiens	108-115	
3548819-5	1987	With 1-fluoro-2,4-dinitrobenzene as the labeling reagent, the relative chemical reactivities of the functional groups of insulin were found to decrease markedly when insulin was incubated with liposomes consisting of egg lecithin and cholesterol (2:1 mol/mol) in 1.0 M KCl, pH 7.5 at 37 degrees C. The decrease for each functional group was found to directly correlate with its proximity to the dimer-forming surface of the monomer.	Lecithins	221-229	insulin	Homo sapiens	166-173