PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10587458-3	1999	We have studied the interaction of a spin-labeled biotinyl diacyl phospholipid, with and without specifically bound avidin, with the myelin proteolipid protein (or the DM-20 isoform) reconstituted in dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	200-230	proteolipid protein 1	Homo sapiens	133-159	
12512771-4	2002	In addition, the interactions between the myelin proteolipid protein and avidin that was membrane-anchored by binding to N-biotinyl phosphatidylethanolamine were studied in dimyristoyl phosphatidylcholine membranes.	Dimyristoylphosphatidylcholine	173-204	proteolipid protein 1	Homo sapiens	42-68	
7150594-1	1982	The hydrophobic myelin protein, lipophilin, has been incorporated into bilayers of dimyristoylphosphatidylcholine by dialysis from 2-chloroethanol.	Dimyristoylphosphatidylcholine	83-113	proteolipid protein 1	Homo sapiens	32-42	
7682453-1	1993	The microwave saturation properties of various spin-labeled lipids in reconstituted complexes of the myelin proteolipid protein with dimyristoyl phosphatidylcholine have been studied both by conventional and saturation transfer electron spin resonance (ESR) spectroscopy.	Dimyristoylphosphatidylcholine	133-164	proteolipid protein 1	Homo sapiens	101-127	
3597388-1	1987	The secondary structure of a hydrophobic myelin protein (lipophilin), reconstituted with dimyristoylphosphatidylcholine or dimyristoylphosphatidylglycerol, was investigated by Fourier-transform infrared spectroscopy.	Dimyristoylphosphatidylcholine	89-119	proteolipid protein 1	Homo sapiens	57-67	
8386549-1	1993	Lipid-protein interactions with the myelin proteolipid protein incorporated in the gel phase of dimyristoylphosphatidylcholine bilayers have been studied by saturation transfer EPR spectroscopy of spin-labelled phospholipids.	Dimyristoylphosphatidylcholine	96-126	proteolipid protein 1	Homo sapiens	36-62	
2844256-2	1988	The pH and salt dependences of the interaction of phosphatidic acid, phosphatidylserine, and stearic acid with myelin proteolipid apoprotein (PLP) in dimyristoylphosphatidylcholine (DMPC) recombinants have been studied by electron spin resonance spectroscopy, using spin-labeled lipids.	Dimyristoylphosphatidylcholine	150-180	proteolipid protein 1	Homo sapiens	142-145	
2844256-2	1988	The pH and salt dependences of the interaction of phosphatidic acid, phosphatidylserine, and stearic acid with myelin proteolipid apoprotein (PLP) in dimyristoylphosphatidylcholine (DMPC) recombinants have been studied by electron spin resonance spectroscopy, using spin-labeled lipids.	Dimyristoylphosphatidylcholine	182-186	proteolipid protein 1	Homo sapiens	142-145