PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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