PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9746361-4	1998	The modulating effects of the lipid-phase state and effects on the function of the nucleotide-binding domains of P-glycoprotein have been studied in reconstituted vesicles of the synthetic phospholipids 1-palmitoyl-2-myristoylphosphatidylcholine (PamMyrGroPCho) and dimyristoylphosphatidylcholine (Myr2GroPCho).	Dimyristoylphosphatidylcholine	266-296	ATP binding cassette subfamily B member 1	Homo sapiens	113-127	
9245413-4	1997	In the present study, purified P-glycoprotein of high specific ATPase activity was reconstituted into defined bilayers of dimyristoylphosphatidylcholine (DMPC), and its effects on lipid thermodynamic properties were then investigated using differential scanning calorimetry.	Dimyristoylphosphatidylcholine	122-152	ATP binding cassette subfamily B member 1	Homo sapiens	31-45	
9245413-4	1997	In the present study, purified P-glycoprotein of high specific ATPase activity was reconstituted into defined bilayers of dimyristoylphosphatidylcholine (DMPC), and its effects on lipid thermodynamic properties were then investigated using differential scanning calorimetry.	Dimyristoylphosphatidylcholine	154-158	ATP binding cassette subfamily B member 1	Homo sapiens	31-45	
9245413-5	1997	P-Glycoprotein had a large perturbing effect on DMPC bilayers, even at relatively high lipid:protein ratios.	Dimyristoylphosphatidylcholine	48-52	ATP binding cassette subfamily B member 1	Homo sapiens	0-14	
9245413-10	1997	At lipid:protein ratios below 16:1 (w/w), transition enthalpy increased with higher P-glycoprotein content, until the DeltaH value reached that of pure DMPC.	Dimyristoylphosphatidylcholine	152-156	ATP binding cassette subfamily B member 1	Homo sapiens	84-98