PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
1600082-0	1992	Bilayer structure and physical dynamics of the cytochrome b5 dimyristoylphosphatidylcholine interaction.	Dimyristoylphosphatidylcholine	61-91	cytochrome b5 type A	Homo sapiens	47-60
1600082-2	1992	Low angle x-ray diffraction has been used to determine the structure of an asymmetrically reconstituted cytochrome b5:DMPC model membrane system.	Dimyristoylphosphatidylcholine	118-122	cytochrome b5 type A	Homo sapiens	104-117
1600082-7	1992	In these studies, we have obtained a reconstituted cytochrome b5:DMPC bilayer structure at approximately 6.3 A resolution and conclude that the nonpolar peptide does not penetrate beyond the bilayer midplane.	Dimyristoylphosphatidylcholine	65-69	cytochrome b5 type A	Homo sapiens	51-64
1810252-7	1991	Chem., 261, 16191) of apo A-I/DMPC complexes which predicted 68% alpha-helix and 7% beta-structure.	Dimyristoylphosphatidylcholine	30-34	apolipoprotein A1	Homo sapiens	22-29
1734956-1	1992	We have previously shown that the synthetic peptide apoE(129-169) forms lipid-peptide complexes with dimyristoylphosphatidylcholine (DMPC) with an L:P molar ratio of 125:1; the peptide in the isolated complex contains approximately 56% alpha-helicity.	Dimyristoylphosphatidylcholine	101-131	apolipoprotein E	Homo sapiens	52-56
1734956-1	1992	We have previously shown that the synthetic peptide apoE(129-169) forms lipid-peptide complexes with dimyristoylphosphatidylcholine (DMPC) with an L:P molar ratio of 125:1; the peptide in the isolated complex contains approximately 56% alpha-helicity.	Dimyristoylphosphatidylcholine	133-137	apolipoprotein E	Homo sapiens	52-56
1734956-4	1992	Although all four peptides formed alpha-helices in the helix-forming solvent 30% hexafluoropropanol, we found that only apoE(263-286) formed a stable complex with DMPC.	Dimyristoylphosphatidylcholine	163-167	apolipoprotein E	Homo sapiens	120-124
1613982-4	1992	ApoE-rich HDL, as well as, apoE.DMPC potently inhibited platelet aggregation in a dose-dependent manner.	Dimyristoylphosphatidylcholine	32-36	apolipoprotein E	Homo sapiens	0-4
1613982-4	1992	ApoE-rich HDL, as well as, apoE.DMPC potently inhibited platelet aggregation in a dose-dependent manner.	Dimyristoylphosphatidylcholine	32-36	apolipoprotein E	Homo sapiens	27-31
1613982-5	1992	ApoE.DMPC stimulated the release of cholesterol into the supernatant, suggesting that apoE plays a major role in the inhibitory effect of apoE-rich HDL in platelet function, presumably due to the release of cholesterol from the plasma membrane.	Dimyristoylphosphatidylcholine	5-9	apolipoprotein E	Homo sapiens	0-4
1613982-5	1992	ApoE.DMPC stimulated the release of cholesterol into the supernatant, suggesting that apoE plays a major role in the inhibitory effect of apoE-rich HDL in platelet function, presumably due to the release of cholesterol from the plasma membrane.	Dimyristoylphosphatidylcholine	5-9	apolipoprotein E	Homo sapiens	86-90
1613982-5	1992	ApoE.DMPC stimulated the release of cholesterol into the supernatant, suggesting that apoE plays a major role in the inhibitory effect of apoE-rich HDL in platelet function, presumably due to the release of cholesterol from the plasma membrane.	Dimyristoylphosphatidylcholine	5-9	apolipoprotein E	Homo sapiens	138-142
1731921-6	1992	The metarhodopsin I in equilibrium with meta II equilibrium constant, Keq has a linear relationship with fv for rhodopsin in PAPC vesicles with and without cholesterol as well as for rhodopsin in DMPC vesicles, and these two correlation lines have different slopes.	Dimyristoylphosphatidylcholine	196-200	rhodopsin	Homo sapiens	8-17
1655762-8	1991	Similarly, egg yolk phosphatidylcholine complexes containing CF4 (CF4.egg PC) showed higher affinity binding than CF1-egg yolk phosphatidylcholine complexes confirming the results obtained with DMPC complexes.	Dimyristoylphosphatidylcholine	194-198	Cardiac cell morphology QTL 1	Rattus norvegicus	114-117
1655762-9	1991	Furthermore, ligand blotting studies showed that only 125I-labeled CF4.DMPC associated specifically with HB1 and HB2, two HDL binding proteins recently identified in rat liver plasma membranes.	Dimyristoylphosphatidylcholine	71-75	activated leukocyte cell adhesion molecule	Rattus norvegicus	113-116
1798016-2	1991	Furthermore, while CsA associated with DMPG was embedded within the hydrophobic region of phospholipids, CsA associated with DMPC was excluded from the hydrophobic region and was entrapped in the hydrophilic region of these liposomes.	Dimyristoylphosphatidylcholine	125-129	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	105-108
1799438-0	1991	Dependence on neutral salt concentration of the latency phase in the time course of hydrolysis of dimyristoylphosphatidylcholine liposomes by phospholipase A2.	Dimyristoylphosphatidylcholine	98-128	phospholipase A2 group IB	Homo sapiens	142-158
1799438-1	1991	The time course of the hydrolytic action of porcine pancreatic phospholipase A2 on sonicated dimyristoylphosphatidylcholine liposomes in the presence of variable NaCl concentrations has been studied at temperatures between 17 and 36 degrees C; at these temperatures liposomes are in the gel phase.	Dimyristoylphosphatidylcholine	93-123	phospholipase A2 group IB	Homo sapiens	63-79
1799439-0	1991	The interfacial calcium ion concentration as modulator of the latency phase in the hydrolysis of dimyristoylphosphatidylcholine liposomes by phospholipase A2.	Dimyristoylphosphatidylcholine	97-127	phospholipase A2 group IB	Homo sapiens	141-157
1871138-7	1991	The lipid-poor apoB-17 present in p greater than 1.21 g/ml readily associates with exogenously added dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles to form discoidal particles.	Dimyristoylphosphatidylcholine	101-131	apolipoprotein B	Mus musculus	15-19
1871138-7	1991	The lipid-poor apoB-17 present in p greater than 1.21 g/ml readily associates with exogenously added dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles to form discoidal particles.	Dimyristoylphosphatidylcholine	133-137	apolipoprotein B	Mus musculus	15-19
1871138-9	1991	Based on volume calculations we conclude that apoB-17 forms an annulus about one bilayer high and 10 A thick surrounding the DMPC disc.	Dimyristoylphosphatidylcholine	125-129	apolipoprotein B	Mus musculus	46-50
1871138-10	1991	Circular dichroic spectra of apoB-17 on DMPC discs showed apoB-17 to contain 39% alpha-helix, 36% beta-sheet, 9% beta-turn, and 16% random coil.	Dimyristoylphosphatidylcholine	40-44	apolipoprotein B	Mus musculus	29-33
1871138-11	1991	To be consistent with this model greater than 70% of apoB-17 on DMPC discs must bind to lipid.	Dimyristoylphosphatidylcholine	64-68	apolipoprotein B	Mus musculus	53-57
2025633-1	1991	The effect of insulin on the bilayer properties of dimyristoylphosphatidylcholine liposomes at the gel and the liquid crystalline state was measured by differential scanning calorimetry and absorbance at 450 nm.	Dimyristoylphosphatidylcholine	51-81	insulin	Homo sapiens	14-21
1770308-1	1991	The structure, composition, and physico-chemical properties of lipid-protein complexes generated between dimyristoylphosphatidylcholine (DPMC) and the CNBr fragments of human apoA-I were studied.	Dimyristoylphosphatidylcholine	105-135	apolipoprotein A1	Homo sapiens	175-181
1770308-5	1991	The fragments 1 and 4 of apoA-I, containing, respectively, two and three amphipathic helices, recombined with the phospholipid to generate discoidal particles with sizes similar to that of apoA-I- and apoA-II-DMPC complexes.	Dimyristoylphosphatidylcholine	209-213	apolipoprotein A1	Homo sapiens	25-31
1770308-8	1991	In conclusion, we propose that apoA-I and its longest CNBr fragments are able to generate discoidal particles with DMPC, with apolipoprotein helical segments oriented parallel to the acyl chains of the phospholipids.	Dimyristoylphosphatidylcholine	115-119	apolipoprotein A1	Homo sapiens	31-37
2054375-3	1991	DMPC liposomes released entrapped solute on exposure to phospholipase A2, whereas mixed vesicles were resistant.	Dimyristoylphosphatidylcholine	0-4	phospholipase A2 group IB	Homo sapiens	56-72
1710494-7	1991	This number is in agreement with earlier results for reconstitutions of PLP in dimyristoylphosphatidylcholine (DMPC) [Brophy, P. J., Horvath, L. I., & Marsh, D. (1984) Biochemistry 23, 860-865] and is consistent with a hexameric arrangement of the PLP molecules in DMPG bilayers.	Dimyristoylphosphatidylcholine	79-109	proteolipid protein 1	Bos taurus	72-75
1710494-7	1991	This number is in agreement with earlier results for reconstitutions of PLP in dimyristoylphosphatidylcholine (DMPC) [Brophy, P. J., Horvath, L. I., & Marsh, D. (1984) Biochemistry 23, 860-865] and is consistent with a hexameric arrangement of the PLP molecules in DMPG bilayers.	Dimyristoylphosphatidylcholine	111-115	proteolipid protein 1	Bos taurus	72-75
1710494-7	1991	This number is in agreement with earlier results for reconstitutions of PLP in dimyristoylphosphatidylcholine (DMPC) [Brophy, P. J., Horvath, L. I., & Marsh, D. (1984) Biochemistry 23, 860-865] and is consistent with a hexameric arrangement of the PLP molecules in DMPG bilayers.	Dimyristoylphosphatidylcholine	111-115	proteolipid protein 1	Bos taurus	252-255
1651120-7	1991	For either the binary lipid or ternary lipid-protein systems reconstituted with DMPC-d54, linewidth parameters of the DMPC-d54 acyl chain CD2 symmetric stretching modes at 2,103 cm-1 provide a sensitive measure of the conformational and dynamic properties of the perdeuterated lipid component, while the 3,000 cm-1 C-H spectral region reflects the bilayer characteristics of the DMPA species in the complex.	Dimyristoylphosphatidylcholine	80-84	CD2 molecule	Homo sapiens	138-141
1651120-7	1991	For either the binary lipid or ternary lipid-protein systems reconstituted with DMPC-d54, linewidth parameters of the DMPC-d54 acyl chain CD2 symmetric stretching modes at 2,103 cm-1 provide a sensitive measure of the conformational and dynamic properties of the perdeuterated lipid component, while the 3,000 cm-1 C-H spectral region reflects the bilayer characteristics of the DMPA species in the complex.	Dimyristoylphosphatidylcholine	118-122	CD2 molecule	Homo sapiens	138-141
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	0-31	apolipoprotein E	Homo sapiens	46-50
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	0-31	apolipoprotein E	Homo sapiens	52-56
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	0-31	apolipoprotein E	Homo sapiens	52-56
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	57-61	apolipoprotein E	Homo sapiens	46-50
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	57-61	apolipoprotein E	Homo sapiens	52-56
1648354-1	1991	Interaction of micellar complexes apolipoprotein A1--phosphatidyl choline (apoA1--DMPC and apoA1--EPC) with complex components: apoA1 (dansyl-A1) and phosphatydil cholines (DMPC, EPC and spin labelled PC) was studied in the absence of lipoproteins and plasma components.	Dimyristoylphosphatidylcholine	82-86	apolipoprotein A1	Homo sapiens	34-51
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	57-61	apolipoprotein E	Homo sapiens	52-56
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein E	Homo sapiens	46-50
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein E	Homo sapiens	52-56
2026270-2	1991	Dimyristoyl phosphatidylcholine liposome with apoE (apoE.DMPC) also inhibited platelet aggregation, and incubation of washed platelets with apoE.DMPC resulted in the release of cholesterol into the supernatant in a time- and dose-dependent manner.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein E	Homo sapiens	52-56
1899020-0	1991	Rhodopsin in dimyristoylphosphatidylcholine-reconstituted bilayers forms metarhodopsin II and activates Gt.	Dimyristoylphosphatidylcholine	13-43	rhodopsin	Bos taurus	0-9
1899020-4	1991	Purified bovine rhodopsin was incorporated into vesicles consisting of dimyristoylphosphatidylcholine (DMPC), and the rapid formation of a photochemical intermediate absorbing maximally at 380 nm was quantified via both flash photolysis and equilibrium spectral measurements.	Dimyristoylphosphatidylcholine	71-101	rhodopsin	Bos taurus	16-25
1899020-4	1991	Purified bovine rhodopsin was incorporated into vesicles consisting of dimyristoylphosphatidylcholine (DMPC), and the rapid formation of a photochemical intermediate absorbing maximally at 380 nm was quantified via both flash photolysis and equilibrium spectral measurements.	Dimyristoylphosphatidylcholine	103-107	rhodopsin	Bos taurus	16-25
2029546-3	1991	By incubating the complexes with either purified human LCAT or the d greater than 1.21 g/ml fraction of rat serum as a source of LCAT activity, it was found that a high degree of cholesterol esterification could be achieved with either complex; however, the DLPE-containing complex possessed a much smaller Stokes" diameter than the DMPC-only particle despite compositional similarities between these complexes.	Dimyristoylphosphatidylcholine	333-337	lecithin-cholesterol acyltransferase	Homo sapiens	129-133
1997324-8	1991	At neutral pH, in the presence of dimyristoylglycerophosphocholine (Myr2GroPCho), GALA is known to form discoidal structures similar to those formed under the same conditions by apolipoproteins AI and AII.	Dimyristoylphosphatidylcholine	34-66	galactosidase alpha	Homo sapiens	82-86
1648354-1	1991	Interaction of micellar complexes apolipoprotein A1--phosphatidyl choline (apoA1--DMPC and apoA1--EPC) with complex components: apoA1 (dansyl-A1) and phosphatydil cholines (DMPC, EPC and spin labelled PC) was studied in the absence of lipoproteins and plasma components.	Dimyristoylphosphatidylcholine	82-86	apolipoprotein A1	Homo sapiens	75-80
1648355-0	1991	[Features of the structure of apolipoprotein A1 as an HDL and complexes with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	77-107	apolipoprotein A1	Homo sapiens	30-47
2117038-4	1990	Extremely prolonged serum titers are caused by IFN-gamma liposomes with a phospholipid composition of dimyristoylphosphatidylcholine/cholesterol/dicetylphosphate and an average particle size of 333 nm.	Dimyristoylphosphatidylcholine	102-132	interferon gamma	Mus musculus	47-56
2268337-1	1990	Apolipoprotein A-I (apo A-I)*/DMPC complexes have been previously shown to promote cholesterol efflux from cholesterol-preloaded adipose cells whereas apo A-II/DMPC complexes, which bind to the same cell surface binding sites, were ineffective.	Dimyristoylphosphatidylcholine	30-34	apolipoprotein A1	Homo sapiens	0-18
2268337-1	1990	Apolipoprotein A-I (apo A-I)*/DMPC complexes have been previously shown to promote cholesterol efflux from cholesterol-preloaded adipose cells whereas apo A-II/DMPC complexes, which bind to the same cell surface binding sites, were ineffective.	Dimyristoylphosphatidylcholine	30-34	apolipoprotein A1	Homo sapiens	20-29
2268337-2	1990	Addition of apo A-I/DMPC complexes led to a rapid and transient formation of diacylglycerol.	Dimyristoylphosphatidylcholine	20-24	apolipoprotein A1	Homo sapiens	12-19
2268337-9	1990	Stimulation by apo A-I/DMPC complexes or native HDL3 of cells prelabelled with (2-palmitoyl 9,10[3H])phosphatidylcholine induced also the formation of labelled diacylglycerol whereas apo A-II/DMPC complexes and HDL3 treated with tetranitromethane showed no effect.	Dimyristoylphosphatidylcholine	23-27	apolipoprotein A1	Homo sapiens	15-22
2171644-1	1990	Beef-heart cytochrome c oxidase lacking endogenous lipids can be prepared by cholate-mediated exchange with dimyristoylphosphatidylcholine (Powell, G. L., Knowles, P. F. and Marsh, D. (1985) Biochim.	Dimyristoylphosphatidylcholine	108-138	cytochrome c, somatic	Homo sapiens	11-23
2252889-2	1990	We studied the interaction of transferrin receptors (of cell line Molt-4) with mixed model membranes as a function of lipid chain length (phospholipids with C14:0 and C18:1 hydrocarbon chains) and of the surface charge of the membrane using mixtures of C14:0 lecithin (DMPC) with C14:0 phosphatidylglycerol (DMPG) and C14:0 phosphatidylserine (DMPS).	Dimyristoylphosphatidylcholine	269-273	transferrin	Homo sapiens	30-41
2168737-2	1990	Circular dichroic (CD) spectra of apoE bound to large (LME) and small (SME) microemulsion particles, composed of dimyristoylphosphatidylcholine (DMPC) and cholesteryl oleate (CO), and to DMPC disks revealed that at 4 degrees C, where all of the lipid constituents were in an ordered state, apoE bound to LME displayed approximately 60% alpha-helicity, while apoE bound to SME and DMPC disks displayed 73% and 95% helicity, respectively.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein E	Homo sapiens	34-38
2168737-2	1990	Circular dichroic (CD) spectra of apoE bound to large (LME) and small (SME) microemulsion particles, composed of dimyristoylphosphatidylcholine (DMPC) and cholesteryl oleate (CO), and to DMPC disks revealed that at 4 degrees C, where all of the lipid constituents were in an ordered state, apoE bound to LME displayed approximately 60% alpha-helicity, while apoE bound to SME and DMPC disks displayed 73% and 95% helicity, respectively.	Dimyristoylphosphatidylcholine	187-191	apolipoprotein E	Homo sapiens	34-38
2168737-2	1990	Circular dichroic (CD) spectra of apoE bound to large (LME) and small (SME) microemulsion particles, composed of dimyristoylphosphatidylcholine (DMPC) and cholesteryl oleate (CO), and to DMPC disks revealed that at 4 degrees C, where all of the lipid constituents were in an ordered state, apoE bound to LME displayed approximately 60% alpha-helicity, while apoE bound to SME and DMPC disks displayed 73% and 95% helicity, respectively.	Dimyristoylphosphatidylcholine	187-191	apolipoprotein E	Homo sapiens	34-38
2268337-9	1990	Stimulation by apo A-I/DMPC complexes or native HDL3 of cells prelabelled with (2-palmitoyl 9,10[3H])phosphatidylcholine induced also the formation of labelled diacylglycerol whereas apo A-II/DMPC complexes and HDL3 treated with tetranitromethane showed no effect.	Dimyristoylphosphatidylcholine	23-27	NLR family pyrin domain containing 3	Homo sapiens	187-191
2268337-9	1990	Stimulation by apo A-I/DMPC complexes or native HDL3 of cells prelabelled with (2-palmitoyl 9,10[3H])phosphatidylcholine induced also the formation of labelled diacylglycerol whereas apo A-II/DMPC complexes and HDL3 treated with tetranitromethane showed no effect.	Dimyristoylphosphatidylcholine	23-27	HDL3	Homo sapiens	211-215
2268337-9	1990	Stimulation by apo A-I/DMPC complexes or native HDL3 of cells prelabelled with (2-palmitoyl 9,10[3H])phosphatidylcholine induced also the formation of labelled diacylglycerol whereas apo A-II/DMPC complexes and HDL3 treated with tetranitromethane showed no effect.	Dimyristoylphosphatidylcholine	192-196	apolipoprotein A1	Homo sapiens	15-22
2268337-9	1990	Stimulation by apo A-I/DMPC complexes or native HDL3 of cells prelabelled with (2-palmitoyl 9,10[3H])phosphatidylcholine induced also the formation of labelled diacylglycerol whereas apo A-II/DMPC complexes and HDL3 treated with tetranitromethane showed no effect.	Dimyristoylphosphatidylcholine	192-196	HDL3	Homo sapiens	48-52
2383558-0	1990	Interaction between perdeuterated dimyristoylphosphatidylcholine and low molecular weight pulmonary surfactant protein SP-C.	Dimyristoylphosphatidylcholine	34-64	surfactant protein C	Homo sapiens	119-123
2116166-4	1990	Although incubation of dimyristoylphosphatidylcholine (DMPC) with apolipoprotein A-I at the gel-liquid crystalline phase transition temperature results in the spontaneous formation of lipid-protein complexes, the presence of proportionately small amounts of PE prevents the formation of such complexes, suggesting that PE profoundly alters the phase properties of the phospholipid bilayers.	Dimyristoylphosphatidylcholine	23-53	apolipoprotein A1	Homo sapiens	66-84
2116166-4	1990	Although incubation of dimyristoylphosphatidylcholine (DMPC) with apolipoprotein A-I at the gel-liquid crystalline phase transition temperature results in the spontaneous formation of lipid-protein complexes, the presence of proportionately small amounts of PE prevents the formation of such complexes, suggesting that PE profoundly alters the phase properties of the phospholipid bilayers.	Dimyristoylphosphatidylcholine	55-59	apolipoprotein A1	Homo sapiens	66-84
2159800-1	1990	The interactions of neuropeptide Y with dimyristoylphosphatidylcholine and cell membranes were examined by several physical techniques to probe the potential role of its putative C-terminal amphipathic alpha-helix.	Dimyristoylphosphatidylcholine	40-70	neuropeptide Y	Homo sapiens	20-34
2159800-2	1990	Neuropeptide Y binding was demonstrated by a rapid release of entrapped 6-carboxyfluorescein and a rapid decrease in the turbidity of dimyristoylphosphatidylcholine liposomes.	Dimyristoylphosphatidylcholine	134-164	neuropeptide Y	Homo sapiens	0-14
2159462-3	1990	The half-maximal concentration was found to be 0.3 X 10(-6) M for apolipoprotein A-IV.DMPC complexes.	Dimyristoylphosphatidylcholine	86-90	apolipoprotein A4	Homo sapiens	66-85
2159807-0	1990	Spin label ESR and 31P-NMR studies of the cubic and inverted hexagonal phases of dimyristoylphosphatidylcholine/myristic acid (1:2, mol/mol) mixtures.	Dimyristoylphosphatidylcholine	81-111	spindlin 1	Homo sapiens	0-4
2159462-4	1990	Binding experiments performed in intact cells at 4 degrees C with labeled apolipoprotein A-IV.DMPC complexes showed the existence of specific binding sites, with a Kd value of 0.32 x 10(-6) M and a maximal binding capacity of 223,000 sites/cell.	Dimyristoylphosphatidylcholine	94-98	apolipoprotein A4	Homo sapiens	74-93
34231557-6	2021	Similar to ApoE NTD-MHC alpha3, in the mice model ApoE NTD-scFv bound to the liver cells" surfaces in vitro and accumulated mainly in the liver, when complexed with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC).	Dimyristoylphosphatidylcholine	165-208	apolipoprotein E	Mus musculus	50-54
2158344-0	1990	Examination of the role of the amphipathic alpha-helix in the interaction of neuropeptide Y and active cyclic analogues with cell membrane receptors and dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	153-183	neuropeptide Y	Mus musculus	77-91
8844260-3	1996	The lipid binding properties of apoA-II(18-30)+ were assessed using optical spectroscopy in the presence of sodium dodecyl sulfate (SDS), dodecylphosphocholine (DPC), tetradecyltrimethyl ammonium chloride (TMA) and dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	215-245	apolipoprotein A2	Homo sapiens	32-39
8844260-3	1996	The lipid binding properties of apoA-II(18-30)+ were assessed using optical spectroscopy in the presence of sodium dodecyl sulfate (SDS), dodecylphosphocholine (DPC), tetradecyltrimethyl ammonium chloride (TMA) and dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	247-251	apolipoprotein A2	Homo sapiens	32-39
8844260-4	1996	The fluorescence emission spectra and the circular dichroism data suggested that apoA-II(18-30)+ interacted most strongly with SDS and most weakly with DMPC.	Dimyristoylphosphatidylcholine	152-156	apolipoprotein A2	Homo sapiens	81-88
34329823-2	2021	Here, we report for the first time, the early-stage interaction of hIAPP oligomers on the DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) lipid membrane using electrochemical parameters.	Dimyristoylphosphatidylcholine	90-94	islet amyloid polypeptide	Homo sapiens	67-72
34329823-2	2021	Here, we report for the first time, the early-stage interaction of hIAPP oligomers on the DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) lipid membrane using electrochemical parameters.	Dimyristoylphosphatidylcholine	96-139	islet amyloid polypeptide	Homo sapiens	67-72
34329823-4	2021	The surface level interactions between the peptide (hIAPP) and lipid membrane (DMPC) were investigated using atomic force microscopy (AFM), confocal microscopy (CM) and electrochemical techniques such as Tafel polarization, cyclic voltammetry (CV), differential pulse voltammetry (DPV), linear sweep voltammetry (LSV) and electrochemical impedance spectroscopy (EIS).	Dimyristoylphosphatidylcholine	79-83	islet amyloid polypeptide	Homo sapiens	52-57
2340306-5	1990	Transblotted to nitrocellulose sheet could be identified as recognizing 125I-apo A-IV-DMPC by autoradiography.	Dimyristoylphosphatidylcholine	86-90	apolipoprotein A4	Rattus norvegicus	77-85
2306737-2	1990	IL-2 liposomes made by hydration of powdered dimyristoyl-phosphatidylcholine with aqueous recombinant IL-2 had 95% of the IL-2 associated with the lipid fraction.	Dimyristoylphosphatidylcholine	45-76	interleukin 2	Mus musculus	0-4
2155032-2	1990	The lateral diffusion, D of CSL in DMPC/POPC/cholesterol ternary mixtures, is measured utilizing an improved dynamic imaging electron spin resonance method.	Dimyristoylphosphatidylcholine	35-39	chorionic somatomammotropin hormone like 1	Homo sapiens	28-31
34298139-9	2021	The purified ApoA-I formed discoidal objects in the presence of zwitterionic phospholipid DMPC, showing its retained function of interacting with lipids.	Dimyristoylphosphatidylcholine	90-94	apolipoprotein A1	Homo sapiens	13-19
34231557-6	2021	Similar to ApoE NTD-MHC alpha3, in the mice model ApoE NTD-scFv bound to the liver cells" surfaces in vitro and accumulated mainly in the liver, when complexed with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC).	Dimyristoylphosphatidylcholine	210-214	apolipoprotein E	Mus musculus	50-54
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	27-31	apolipoprotein E	Mus musculus	5-9
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	27-31	alpha-2-macroglobulin	Mus musculus	84-91
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein E	Mus musculus	36-40
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	52-56	alpha-2-macroglobulin	Mus musculus	84-91
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	173-177	apolipoprotein E	Mus musculus	36-40
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	173-177	apolipoprotein E	Mus musculus	157-161
34231557-7	2021	Both ApoE NTD-MHC alpha3 + DMPC and ApoE NTD-scFv + DMPC significantly switched the beta2-m accumulation in mice from the kidneys to the liver, but only the ApoE NTD-scFv + DMPC group showed a significantly higher ratio of beta2-m accumulation in the liver versus the kidneys, compared with the control group.	Dimyristoylphosphatidylcholine	173-177	alpha-2-macroglobulin	Mus musculus	223-230
35629795-6	2022	In this study, we have utilized all-atom molecular dynamics simulations to characterize the molecular motions and the interactions of KCNE3 in a bilayer composed of: a mixture of POPC and POPG lipids (3:1), POPC alone, and DMPC alone.	Dimyristoylphosphatidylcholine	223-227	potassium voltage-gated channel subfamily E regulatory subunit 3	Homo sapiens	134-139
35311662-11	2022	DMPC and PMPC markedly inhibited wild type and D614G mutant SARS-CoV-2 infection in HEK293T-ACE2 and Vero-E6 cells.	Dimyristoylphosphatidylcholine	0-4	angiotensin converting enzyme 2	Homo sapiens	92-96
2512989-7	1989	Similar measurements also revealed that the microenvironments around tyrosines of apo A-II bound to DMPC in the gel phase are different from those observed in the liquid crystalline phase.	Dimyristoylphosphatidylcholine	100-104	apolipoprotein A2	Homo sapiens	82-90
2624682-2	1989	Some of these regions have been identified by reassembly of the total tryptic peptides of apo B-100 with bovine brain sphingomyelin, 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC) and dimyristoylphosphatidylcholine (DPMC).	Dimyristoylphosphatidylcholine	185-215	apolipoprotein B	Bos taurus	90-99
2512989-1	1989	Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods.	Dimyristoylphosphatidylcholine	69-112	apolipoprotein A2	Homo sapiens	6-25
2512989-1	1989	Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods.	Dimyristoylphosphatidylcholine	69-112	apolipoprotein A2	Homo sapiens	27-35
2512989-1	1989	Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods.	Dimyristoylphosphatidylcholine	114-118	apolipoprotein A2	Homo sapiens	6-25
2512989-1	1989	Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods.	Dimyristoylphosphatidylcholine	114-118	apolipoprotein A2	Homo sapiens	27-35
2512990-4	1989	The kinetics of hydrolysis of apo A-II associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine showed several differences.	Dimyristoylphosphatidylcholine	55-98	apolipoprotein A2	Homo sapiens	30-38
2804107-1	1989	The changes in steady-state fluorescence lifetimes and anisotropy decay parameters, as well as enzyme activities, of dansyl-labeled cytochrome b5 (DNS-cytochrome b5), on interaction with NADH-cytochrome-b5 reductase in DMPC vesicles, have been measured as a function of temperature.	Dimyristoylphosphatidylcholine	219-223	cytochrome b5 type A	Homo sapiens	132-145
2804107-1	1989	The changes in steady-state fluorescence lifetimes and anisotropy decay parameters, as well as enzyme activities, of dansyl-labeled cytochrome b5 (DNS-cytochrome b5), on interaction with NADH-cytochrome-b5 reductase in DMPC vesicles, have been measured as a function of temperature.	Dimyristoylphosphatidylcholine	219-223	cytochrome b5 type A	Homo sapiens	151-164
2804107-2	1989	Steady-state fluorescence of DNS-cytochrome b5 in DMPC vesicles with and without cholesterol was increased on interaction with reductase at temperatures both above and below the DMPC phase transition.	Dimyristoylphosphatidylcholine	50-54	cytochrome b5 type A	Homo sapiens	33-46
2804107-2	1989	Steady-state fluorescence of DNS-cytochrome b5 in DMPC vesicles with and without cholesterol was increased on interaction with reductase at temperatures both above and below the DMPC phase transition.	Dimyristoylphosphatidylcholine	178-182	cytochrome b5 type A	Homo sapiens	33-46
2846071-2	1988	The binding of human high-density lipoprotein (HDL3), apolipoprotein A-I (apoA-I) and recombinants of apoA-I with cholesterol and/or dimyristoylphosphatidylcholine (DMPC) to the HDL receptor on isolated human small intestine epithelial cells was studied.	Dimyristoylphosphatidylcholine	133-163	apolipoprotein A1	Homo sapiens	102-108
2506867-0	1989	[Detergent properties of apolipoprotein A1 in micellar complexes with dimyristoyl phosphatidylcholine].	Dimyristoylphosphatidylcholine	70-101	apolipoprotein A1	Homo sapiens	25-42
2506867-1	1989	Bilayer micellar complexes of the human plasma apolipoprotein A1 with dimyristoyl phosphatidylcholine were prepared under kinetically controlled conditions.	Dimyristoylphosphatidylcholine	70-101	apolipoprotein A1	Homo sapiens	47-64
2547451-2	1989	Using the lipid-soluble spin trap 2-methyl-nitrosopropane (MNP), we have detected both the lipid and hydrogen-atom spin adducts in liposomes composed of a fully saturated phospholipid (dimyristoylphosphatidylcholine, DMPC) with various mol fractions of unsaturated phospholipid (1-palmitoyl-2-arachidonoylphosphatidylcholine, PAPC) or fatty acid (arachidonic acid, AA).	Dimyristoylphosphatidylcholine	185-215	spindlin 1	Homo sapiens	24-28
2547451-2	1989	Using the lipid-soluble spin trap 2-methyl-nitrosopropane (MNP), we have detected both the lipid and hydrogen-atom spin adducts in liposomes composed of a fully saturated phospholipid (dimyristoylphosphatidylcholine, DMPC) with various mol fractions of unsaturated phospholipid (1-palmitoyl-2-arachidonoylphosphatidylcholine, PAPC) or fatty acid (arachidonic acid, AA).	Dimyristoylphosphatidylcholine	185-215	spindlin 1	Homo sapiens	115-119
2547451-2	1989	Using the lipid-soluble spin trap 2-methyl-nitrosopropane (MNP), we have detected both the lipid and hydrogen-atom spin adducts in liposomes composed of a fully saturated phospholipid (dimyristoylphosphatidylcholine, DMPC) with various mol fractions of unsaturated phospholipid (1-palmitoyl-2-arachidonoylphosphatidylcholine, PAPC) or fatty acid (arachidonic acid, AA).	Dimyristoylphosphatidylcholine	217-221	spindlin 1	Homo sapiens	24-28
2547925-6	1989	The results of this study have established that acetylcholinesterase associated with unilamellar DMPC liposomes was primarily entrapped within the aqueous compartment of the vesicles and was not present in the phospholipid bilayer.	Dimyristoylphosphatidylcholine	97-101	acetylcholinesterase (Cartwright blood group)	Homo sapiens	48-68
2543978-3	1989	Profiles of the local oxygen transport parameter across the membrane were obtained as a function of cholesterol mol fraction and temperature in L-alpha-dimyristoylphosphatidylcholine ([ Myr2]PtdCho) and L-alpha-dioleoylphosphatidylcholine ([ Ole2]PtdCho) membranes.	Dimyristoylphosphatidylcholine	144-182	myosin IC	Homo sapiens	186-190
2705988-1	1989	The kinetics of the dithionite reduction of calf liver microsomal cytochrome b5, both free in solution and bound to dimyristoyl phosphatidylcholine vesicles, are consistent with electron transfer between SO2- and the exposed haem edge of the protein.	Dimyristoylphosphatidylcholine	116-147	cytochrome b5 type A	Bos taurus	66-79
2705988-6	1989	In systems comprising cytochrome b5 and negatively charged vesicles, the effect of increasing the charge density of mixed dimyristoyl phosphatidylcholine/dicetyl phosphate vesicles and of increasing the concentration of dicetyl phosphate vesicles is to lower the rate of electron transfer from dithionite to the haem moiety of the cytochrome.	Dimyristoylphosphatidylcholine	122-153	cytochrome b5 type A	Bos taurus	22-35
2537098-2	1989	Exposure of HepG2 cells to cholesterol and oleic acid, which elevated intracellular cholesterol levels, stimulated apoB secretion and reduced receptor-mediated uptake of LDL, whereas recombinant complexes of apolipoprotein A-I with dimyristoylphosphatidylcholine, which depleted the cellular cholesterol pool, inhibited apoB secretion and up-regulated LDL receptors.	Dimyristoylphosphatidylcholine	232-262	apolipoprotein A1	Homo sapiens	208-226
2612438-1	1989	Ultrasonic and calorimetric studies of small homogeneously-sized DMPC unilamellar vesicles showed two thermal transitions at temperatures Tc1 and Tc2 (Tc2 greater than or equal to Tc1); Tc2 is close to the phase transition temperature, Tc, of large vesicles.	Dimyristoylphosphatidylcholine	65-69	transcobalamin 1	Homo sapiens	138-141
2612438-1	1989	Ultrasonic and calorimetric studies of small homogeneously-sized DMPC unilamellar vesicles showed two thermal transitions at temperatures Tc1 and Tc2 (Tc2 greater than or equal to Tc1); Tc2 is close to the phase transition temperature, Tc, of large vesicles.	Dimyristoylphosphatidylcholine	65-69	transcobalamin 2	Homo sapiens	146-149
2612438-1	1989	Ultrasonic and calorimetric studies of small homogeneously-sized DMPC unilamellar vesicles showed two thermal transitions at temperatures Tc1 and Tc2 (Tc2 greater than or equal to Tc1); Tc2 is close to the phase transition temperature, Tc, of large vesicles.	Dimyristoylphosphatidylcholine	65-69	transcobalamin 2	Homo sapiens	151-154
2612438-1	1989	Ultrasonic and calorimetric studies of small homogeneously-sized DMPC unilamellar vesicles showed two thermal transitions at temperatures Tc1 and Tc2 (Tc2 greater than or equal to Tc1); Tc2 is close to the phase transition temperature, Tc, of large vesicles.	Dimyristoylphosphatidylcholine	65-69	transcobalamin 1	Homo sapiens	180-183
2612438-1	1989	Ultrasonic and calorimetric studies of small homogeneously-sized DMPC unilamellar vesicles showed two thermal transitions at temperatures Tc1 and Tc2 (Tc2 greater than or equal to Tc1); Tc2 is close to the phase transition temperature, Tc, of large vesicles.	Dimyristoylphosphatidylcholine	65-69	transcobalamin 2	Homo sapiens	151-154
2612438-3	1989	The temperatures Tc1 and Tc2 become increasingly similar as the cholesterol content is increased, while the clusters at Tc2 (congruent to 85 lipid molecules in pure DMPC) increase in size up to approximately 180 lipid molecules at 12 mol% cholesterol.	Dimyristoylphosphatidylcholine	165-169	transcobalamin 2	Homo sapiens	120-123
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	11-15	apolipoprotein A1	Homo sapiens	4-10
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	11-15	HDL3	Homo sapiens	46-50
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	11-15	HDL3	Homo sapiens	83-87
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	11-15	apolipoprotein A1	Homo sapiens	98-104
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	11-15	HDL3	Homo sapiens	83-87
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	105-109	apolipoprotein A1	Homo sapiens	4-10
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	105-109	HDL3	Homo sapiens	46-50
2846071-4	1988	The apoA-I/DMPC recombinant competed for 125I-HDL3 binding sites nearly as well as HDL3, and 125I-apoA-I/DMPC recombinant bound to cells with at least the same efficiency as 125I-HDL3.	Dimyristoylphosphatidylcholine	105-109	apolipoprotein A1	Homo sapiens	98-104
2846071-5	1988	The apoA-I/DMPC/cholesterol recombinant failed to compete for 125I-HDL3 binding sites, and the 125I-apoA-I/DMPC/cholesterol complex binding to cells was several-fold lower than that of other particles.	Dimyristoylphosphatidylcholine	107-111	apolipoprotein A1	Homo sapiens	100-106
2853635-0	1988	[Formation of micellar complexes of apolipoprotein A-I with dimyristoylphosphatidylcholine].	Dimyristoylphosphatidylcholine	60-90	apolipoprotein A1	Homo sapiens	36-54
2853635-4	1988	It thus follows that formation of complexes of apolipoprotein AI with dimyristoylphosphatidylcholine is caused by lipid micella aggregation.	Dimyristoylphosphatidylcholine	70-100	apolipoprotein A1	Homo sapiens	47-64
3233207-1	1988	Fourier transform infrared spectroscopy has been used to characterize the carbonyl stretching vibration of DMPC, DMPE, DMPG, and DMPA, all labeled with 13C at the carbonyl group of the sn-2 chain.	Dimyristoylphosphatidylcholine	107-111	solute carrier family 38 member 5	Homo sapiens	185-189
3233207-17	1988	In the gel and liquid-crystalline phase of DMPC the sn-2 C = O group is more hydrated than the sn-1 C = O.	Dimyristoylphosphatidylcholine	43-47	solute carrier family 38 member 5	Homo sapiens	52-56
3233207-17	1988	In the gel and liquid-crystalline phase of DMPC the sn-2 C = O group is more hydrated than the sn-1 C = O.	Dimyristoylphosphatidylcholine	43-47	solute carrier family 38 member 3	Homo sapiens	95-99
3139042-0	1988	Incorporation of cholesterol into apolipoprotein A-I-dimyristoylphosphatidylcholine recombinants.	Dimyristoylphosphatidylcholine	53-83	apolipoprotein A1	Homo sapiens	34-52
3139042-1	1988	Apolipoprotein A-I (apoA-I) spontaneously associates with dimyristoylphosphatidylcholine (DMPC) liposomes to form discoidal high-density lipoprotein (HDL) recombinants.	Dimyristoylphosphatidylcholine	58-88	apolipoprotein A1	Homo sapiens	0-18
3061458-1	1988	In the first part, we study the interaction of the insulin receptor with model membranes of dimyristoylphosphatidylcholine (DMPC) by various techniques, including calorimetry, densitometry, static light scattering, and electron microscopy.	Dimyristoylphosphatidylcholine	92-122	insulin	Homo sapiens	51-58
3139042-1	1988	Apolipoprotein A-I (apoA-I) spontaneously associates with dimyristoylphosphatidylcholine (DMPC) liposomes to form discoidal high-density lipoprotein (HDL) recombinants.	Dimyristoylphosphatidylcholine	58-88	apolipoprotein A1	Homo sapiens	20-26
3139042-1	1988	Apolipoprotein A-I (apoA-I) spontaneously associates with dimyristoylphosphatidylcholine (DMPC) liposomes to form discoidal high-density lipoprotein (HDL) recombinants.	Dimyristoylphosphatidylcholine	90-94	apolipoprotein A1	Homo sapiens	0-18
3061458-1	1988	In the first part, we study the interaction of the insulin receptor with model membranes of dimyristoylphosphatidylcholine (DMPC) by various techniques, including calorimetry, densitometry, static light scattering, and electron microscopy.	Dimyristoylphosphatidylcholine	124-128	insulin	Homo sapiens	51-58
3061458-10	1988	Insulin exhibits a weak but remarkable nonspecific binding to bilayers of pure DMPC and DMPC containing 20% positively charged lipid and a strong binding to DMPC containing negatively charged lipids such as phosphatidylserine or ganglioside (GT1b).	Dimyristoylphosphatidylcholine	79-83	insulin	Homo sapiens	0-7
3139042-1	1988	Apolipoprotein A-I (apoA-I) spontaneously associates with dimyristoylphosphatidylcholine (DMPC) liposomes to form discoidal high-density lipoprotein (HDL) recombinants.	Dimyristoylphosphatidylcholine	90-94	apolipoprotein A1	Homo sapiens	20-26
3061458-10	1988	Insulin exhibits a weak but remarkable nonspecific binding to bilayers of pure DMPC and DMPC containing 20% positively charged lipid and a strong binding to DMPC containing negatively charged lipids such as phosphatidylserine or ganglioside (GT1b).	Dimyristoylphosphatidylcholine	88-92	insulin	Homo sapiens	0-7
3061458-10	1988	Insulin exhibits a weak but remarkable nonspecific binding to bilayers of pure DMPC and DMPC containing 20% positively charged lipid and a strong binding to DMPC containing negatively charged lipids such as phosphatidylserine or ganglioside (GT1b).	Dimyristoylphosphatidylcholine	88-92	insulin	Homo sapiens	0-7
3139042-5	1988	In another set of experiments, the association of apoA-I with DMPC-cholesterol liposomes was shown to result in complexes with characteristics similar to those obtained by the cholesterol-uptake experiments.	Dimyristoylphosphatidylcholine	62-66	apolipoprotein A1	Homo sapiens	50-56
3167047-1	1988	Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE.	Dimyristoylphosphatidylcholine	114-144	phospholipase A2 group IB	Homo sapiens	37-42
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
3401474-1	1988	The effects of bovine alpha-lactalbumin on the thermotropic properties of dimyristoylphosphatidylcholine liposomes are studied by Raman spectroscopy, fluorescence polarization and differential scanning calorimetry.	Dimyristoylphosphatidylcholine	74-104	lactalbumin alpha	Bos taurus	22-39
3167047-1	1988	Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE.	Dimyristoylphosphatidylcholine	114-144	phospholipase A2 group IB	Homo sapiens	19-35
3167047-1	1988	Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE.	Dimyristoylphosphatidylcholine	146-150	phospholipase A2 group IB	Homo sapiens	37-42
3167047-1	1988	Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE.	Dimyristoylphosphatidylcholine	307-311	phospholipase A2 group IB	Homo sapiens	37-42
3167047-5	1988	DMPC/CO vesicles were resistant to hydrolysis at every temperature tested; however, discoidal structures formed by interaction of apoE with these vesicles were hydrolyzed maximally above their thermal transition.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein E	Homo sapiens	130-134
3355846-0	1988	Probucol reduces the rate of association of apolipoprotein C-III with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	70-100	apolipoprotein C3	Homo sapiens	44-64
3360782-10	1988	Assessment by circular dichroism demonstrated that both model domains and apoE had over 54% alpha-helical content, which changed little in a detergent (octyl-beta-D-glucopyranoside) or lipid (dimyristoylphosphatidylcholine) environment.	Dimyristoylphosphatidylcholine	192-222	apolipoprotein E	Homo sapiens	74-78
3355846-1	1988	The effect of low concentrations of probucol and cholesterol on the association of dimyristoylphosphatidylcholine with human plasma apolipoprotein C-III was studied.	Dimyristoylphosphatidylcholine	83-113	apolipoprotein C3	Homo sapiens	132-152
3355846-2	1988	Liposomes of dimyristoylphosphatidylcholine with or without probucol or cholesterol were prepared by swelling the lipids in buffer at 37 degrees C. The association of apolipoprotein C-III with the liposomes was determined at 24 degrees C by measuring the rate of clearing of turbidity at 400 nm following addition of protein.	Dimyristoylphosphatidylcholine	13-43	apolipoprotein C3	Homo sapiens	167-187
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	334-338	galactosidase alpha	Homo sapiens	154-158
2838099-7	1988	From Kx, lateral diffusion constants of CSL in dimyristoylphosphatidylcholine (DMPC) were calculated (D = 1.7 x 10(-8) at 27 degrees C and 2.7 x 10(-8) cm2/s at 37 degrees C).	Dimyristoylphosphatidylcholine	47-77	chorionic somatomammotropin hormone like 1	Homo sapiens	40-43
2838099-7	1988	From Kx, lateral diffusion constants of CSL in dimyristoylphosphatidylcholine (DMPC) were calculated (D = 1.7 x 10(-8) at 27 degrees C and 2.7 x 10(-8) cm2/s at 37 degrees C).	Dimyristoylphosphatidylcholine	79-83	chorionic somatomammotropin hormone like 1	Homo sapiens	40-43
2450589-2	1988	They were studied by competitive inhibition of 125I-labeled HDL3 with HDL subfractions, delipidated apo A-I, and complexes of dimyristoylphosphatidylcholine (DMPC) containing apo A-I and apo A-II.	Dimyristoylphosphatidylcholine	158-162	apolipoprotein A1	Homo sapiens	175-182
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	68-98	galactosidase alpha	Homo sapiens	0-4
3389515-9	1988	The hydrolysis of DMPC-PPHTE vesicles was measured by following the increase in pyrene monomer fluorescence emission due to phospholipase A2 action on PPHTE.	Dimyristoylphosphatidylcholine	18-22	phospholipase A2 group IB	Homo sapiens	124-140
3410874-5	1988	When the fluidity of the membrane was changed by utilizing a synthetic dimyristoylphosphatidylcholine, which shows a well-defined gel to liquid crystalline phase transition, the activation energy of the monooxygenase reaction was changed at around the phase transition temperature, suggesting a conformational change of cytochrome P-450 caused by the fluidity change of the membrane.	Dimyristoylphosphatidylcholine	71-101	cytochrome P-450	Oryctolagus cuniculus	320-336
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	334-338	galactosidase alpha	Homo sapiens	154-158
3255105-8	1988	A DMPC-GALA:19/1 (molar ratio) complex can be isolated by gel-permeation chromatography.	Dimyristoylphosphatidylcholine	2-6	galactosidase alpha	Homo sapiens	7-11
3255105-10	1988	GALA activates LCAT with DMPC but not with unsaturated phospholipids as the substrate.	Dimyristoylphosphatidylcholine	25-29	galactosidase alpha	Homo sapiens	0-4
3255105-10	1988	GALA activates LCAT with DMPC but not with unsaturated phospholipids as the substrate.	Dimyristoylphosphatidylcholine	25-29	lecithin-cholesterol acyltransferase	Homo sapiens	15-19
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	68-98	galactosidase alpha	Homo sapiens	154-158
3255105-11	1988	The apparent partition coefficient of GALA into DMPC vesicles is 100-fold larger than into egg phosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	48-52	galactosidase alpha	Homo sapiens	38-42
3680211-0	1987	Topography of the C terminus of cytochrome b5 tightly bound to dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	63-93	cytochrome b5 type A	Homo sapiens	32-45
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	68-98	galactosidase alpha	Homo sapiens	154-158
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	100-104	galactosidase alpha	Homo sapiens	0-4
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	100-104	galactosidase alpha	Homo sapiens	154-158
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	100-104	galactosidase alpha	Homo sapiens	154-158
3255105-7	1988	GALA behaves like the serum apolipoproteins in its interaction with dimyristoylphosphatidylcholine (DMPC) at neutral pH; the amino terminal tryptophan of GALA undergoes a blue shift in its fluorescence emission spectrum, and the circular dichroism (CD) spectrum indicates that GALA acquires alpha helical structure in the presence of DMPC.	Dimyristoylphosphatidylcholine	334-338	galactosidase alpha	Homo sapiens	0-4
3126801-6	1987	Although apo A-I interacted spontaneously with DMPC at 25 degrees C, it was necessary to dilute mixed micellar solutions of sodium taurocholate (TC) and egg yolk phosphatidylcholine (EYPC) with apo A-I solutions to form apo A-I/EYPC mixed micelles.	Dimyristoylphosphatidylcholine	47-51	apolipoprotein A1	Homo sapiens	9-16
3680211-1	1987	Cytochrome b5 holoenzyme was bound asymmetrically in the tightly bound form to small unilamellar dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	97-127	cytochrome b5 type A	Homo sapiens	0-13
3670075-5	1987	This conclusion is supported by the finding that dimyristoyl phosphatidylcholine (DMPC)- apo E complexes were effective in competing for the hepatic uptake of 125I-VLDL remnants.	Dimyristoylphosphatidylcholine	49-80	apolipoprotein E	Rattus norvegicus	89-94
3122827-1	1987	NADPH-cytochrome P-450 reductase and cytochrome P-450, both purified from liver microsomes of phenobarbital-treated rabbits, were incorporated into dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	148-178	NADPH--cytochrome P450 reductase	Oryctolagus cuniculus	0-32
3122827-1	1987	NADPH-cytochrome P-450 reductase and cytochrome P-450, both purified from liver microsomes of phenobarbital-treated rabbits, were incorporated into dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	148-178	cytochrome P-450	Oryctolagus cuniculus	6-22
3670075-5	1987	This conclusion is supported by the finding that dimyristoyl phosphatidylcholine (DMPC)- apo E complexes were effective in competing for the hepatic uptake of 125I-VLDL remnants.	Dimyristoylphosphatidylcholine	82-86	apolipoprotein E	Rattus norvegicus	89-94
3097001-4	1986	The complex of apo A-I with DMPC denatures at elevated temperatures giving rise to a calorimetrically detectable transition.	Dimyristoylphosphatidylcholine	28-32	apolipoprotein A1	Homo sapiens	15-22
3676290-2	1987	The action of residual phospholipase A2 in melittin samples resulted in mixtures of DMPC and its hydrolytic products that underwent reversible transitions at temperatures between 30 and 35 degrees C from extended bilayers to micellar particles which gave narrow single-line deuterium and phosphorus-31 NMR spectra.	Dimyristoylphosphatidylcholine	84-88	phospholipase A2 group IB	Homo sapiens	23-39
3607051-1	1987	Release of acetylcholinesterase-containing vesicles from human erythrocyte membranes induced by dimyristoylphosphatidylcholine (DMPC) was inhibited by exposure of red cells to cationic amphiphilic drugs like tetracaine, chlorpromazine and primaquine which all are known to induce stomatocyte formation.	Dimyristoylphosphatidylcholine	96-126	acetylcholinesterase (Cartwright blood group)	Homo sapiens	11-31
3607051-1	1987	Release of acetylcholinesterase-containing vesicles from human erythrocyte membranes induced by dimyristoylphosphatidylcholine (DMPC) was inhibited by exposure of red cells to cationic amphiphilic drugs like tetracaine, chlorpromazine and primaquine which all are known to induce stomatocyte formation.	Dimyristoylphosphatidylcholine	128-132	acetylcholinesterase (Cartwright blood group)	Homo sapiens	11-31
2442277-15	1987	This was confirmed by testing of apoC-I-DMPC complexes, which yielded curves that paralleled those produced by apoC-I-Intralipid.	Dimyristoylphosphatidylcholine	40-44	apolipoprotein C1	Homo sapiens	33-39
2442277-15	1987	This was confirmed by testing of apoC-I-DMPC complexes, which yielded curves that paralleled those produced by apoC-I-Intralipid.	Dimyristoylphosphatidylcholine	40-44	apolipoprotein C1	Homo sapiens	111-117
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
3038180-1	1987	The photoreceptor protein rhodopsin has been reconstituted with a single phospholipid species, dimyristoylphosphatidylcholine, at a range of different lipid/protein ratios, and the exchange rate at the lipid-protein interface has been determined from the electron spin resonance spectra of spin-labeled phosphatidylcholine.	Dimyristoylphosphatidylcholine	95-125	rhodopsin	Homo sapiens	26-35
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	18-22	HDL3	Homo sapiens	34-38
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	18-22	HDL3	Homo sapiens	47-51
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	18-22	HDL3	Homo sapiens	47-51
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	18-22	HDL3	Homo sapiens	47-51
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	40-44	HDL3	Homo sapiens	34-38
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	40-44	HDL3	Homo sapiens	47-51
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	40-44	HDL3	Homo sapiens	47-51
3572257-5	1987	The reconstituted DMPC-containing HDL3 (DMPC-r-HDL3) was similar to native HDL3 and to C-r-HDL3 in its agarose gel electrophoretic mobility, in its chemical composition, and in its binding to rat liver plasma membranes.	Dimyristoylphosphatidylcholine	40-44	HDL3	Homo sapiens	47-51
3572257-6	1987	When treated with TNM, DMPC-r-HDL3, like the native HDL3 and C-r-HDL3, lost its ability to bind to the HDL binding sites of rat liver plasma membranes, as determined by competitive binding assays with 125I-labeled human HDL3 as the tracer.	Dimyristoylphosphatidylcholine	23-27	HDL3	Homo sapiens	30-34
3663692-1	1987	The kinetics of the bovine cholesterol esterase-catalyzed hydrolysis of three stereoisomers of alpha-tocopheryl acetate (alpha T-Ac) have been examined in vitro at 37 degrees C in the presence of dimyristoylphosphatidylcholine and sodium cholate.	Dimyristoylphosphatidylcholine	196-226	carboxyl ester lipase	Bos taurus	27-47
3681145-3	1987	Of all the examined liposomes prepared from cholesterol and various synthetic phosphatidylcholines, liposomes with dimyristoylphosphatidylcholine (DMPC) were found to be the most reactive in the LCAT reaction.	Dimyristoylphosphatidylcholine	115-145	lecithin-cholesterol acyltransferase	Homo sapiens	195-199
3681145-3	1987	Of all the examined liposomes prepared from cholesterol and various synthetic phosphatidylcholines, liposomes with dimyristoylphosphatidylcholine (DMPC) were found to be the most reactive in the LCAT reaction.	Dimyristoylphosphatidylcholine	147-151	lecithin-cholesterol acyltransferase	Homo sapiens	195-199
3681145-5	1987	Using DMPC-cholesterol liposomes as the substrate, the LCAT activities in 120 human sera showed a mean value of 485.4 +/- 64.6 nmol/hr per ml (mean +/- SD), which is 4.4- to 5.4-fold higher than the values obtained by self-substrate methods.	Dimyristoylphosphatidylcholine	6-10	lecithin-cholesterol acyltransferase	Homo sapiens	55-59
3038192-4	1987	We tested the ability of lipid-poor apolipoprotein A-I from Hep G2 to form complexes with dimyristoylphosphatidylcholine (DMPC) vesicles at DMPC/apolipoprotein A-I molar ratios of 100:1 and 300:1.	Dimyristoylphosphatidylcholine	90-120	apolipoprotein A1	Homo sapiens	36-54
3038192-4	1987	We tested the ability of lipid-poor apolipoprotein A-I from Hep G2 to form complexes with dimyristoylphosphatidylcholine (DMPC) vesicles at DMPC/apolipoprotein A-I molar ratios of 100:1 and 300:1.	Dimyristoylphosphatidylcholine	122-126	apolipoprotein A1	Homo sapiens	36-54
3038192-4	1987	We tested the ability of lipid-poor apolipoprotein A-I from Hep G2 to form complexes with dimyristoylphosphatidylcholine (DMPC) vesicles at DMPC/apolipoprotein A-I molar ratios of 100:1 and 300:1.	Dimyristoylphosphatidylcholine	122-126	apolipoprotein A1	Homo sapiens	145-163
3038192-4	1987	We tested the ability of lipid-poor apolipoprotein A-I from Hep G2 to form complexes with dimyristoylphosphatidylcholine (DMPC) vesicles at DMPC/apolipoprotein A-I molar ratios of 100:1 and 300:1.	Dimyristoylphosphatidylcholine	140-144	apolipoprotein A1	Homo sapiens	36-54
3024721-4	1986	The less cytotoxic congener of VM-26, VP-16, was only one-third as active as VM-26 in its ordering effects on DMPC.	Dimyristoylphosphatidylcholine	110-114	host cell factor C1	Homo sapiens	38-43
3097001-7	1986	It is concluded that the complexes of apo A-I with DMPC are thermodynamically stable only at temperatures near Tc, whereas above and below this temperature range the stability of these recombinants is determined by kinetic factors.	Dimyristoylphosphatidylcholine	51-55	apolipoprotein A1	Homo sapiens	38-45
3097001-10	1986	Both apo A-I X DMPC and apo A-I X DMPG complexes form lipoprotein particles having a discoidal shape.	Dimyristoylphosphatidylcholine	15-19	apolipoprotein A1	Homo sapiens	5-12
3099838-1	1986	Fluorescence lifetime and intensity quenching studies of human plasma apolipoprotein A-I (apo A-I) in aqueous solution and in recombinant lipoprotein complexes with dimyristoylphosphatidylcholine (DMPC) indicate differences in conformational dynamics.	Dimyristoylphosphatidylcholine	165-195	apolipoprotein A1	Homo sapiens	70-88
3099838-1	1986	Fluorescence lifetime and intensity quenching studies of human plasma apolipoprotein A-I (apo A-I) in aqueous solution and in recombinant lipoprotein complexes with dimyristoylphosphatidylcholine (DMPC) indicate differences in conformational dynamics.	Dimyristoylphosphatidylcholine	165-195	apolipoprotein A1	Homo sapiens	90-97
3099838-1	1986	Fluorescence lifetime and intensity quenching studies of human plasma apolipoprotein A-I (apo A-I) in aqueous solution and in recombinant lipoprotein complexes with dimyristoylphosphatidylcholine (DMPC) indicate differences in conformational dynamics.	Dimyristoylphosphatidylcholine	197-201	apolipoprotein A1	Homo sapiens	70-88
3099838-5	1986	In recombinant DMPC/apo A-I complexes (100:1 molar ratio) the protein increases in amphiphilic alpha-helical structure as it blankets the lipid matrix.	Dimyristoylphosphatidylcholine	15-19	apolipoprotein A1	Homo sapiens	20-27
3099838-7	1986	We have introduced a two-compartment model, which discriminates the source of quencher molecules as aqueous or lipid, to describe oxygen quenching of DMPC/apo A-I fluorescence.	Dimyristoylphosphatidylcholine	150-154	apolipoprotein A1	Homo sapiens	155-162
3026456-5	1986	Binding of apoE to spin-labeled DMPC vesicles increased the order of the 5"-position of the sn-2 acyl chain over the range 15-33 degrees C; the thermal transition was broadened and its midpoint elevated.	Dimyristoylphosphatidylcholine	32-36	apolipoprotein E	Homo sapiens	11-15
3767949-1	1986	Rat apoA-IV complexes with dimyristoyl phosphatidylcholine (apoA-IV-DMPC) have been prepared and their ability to bind to purified rat liver plasma membranes investigated.	Dimyristoylphosphatidylcholine	68-72	apolipoprotein A4	Rattus norvegicus	60-67
3767949-1	1986	Rat apoA-IV complexes with dimyristoyl phosphatidylcholine (apoA-IV-DMPC) have been prepared and their ability to bind to purified rat liver plasma membranes investigated.	Dimyristoylphosphatidylcholine	27-58	apolipoprotein A4	Rattus norvegicus	4-11
3767949-1	1986	Rat apoA-IV complexes with dimyristoyl phosphatidylcholine (apoA-IV-DMPC) have been prepared and their ability to bind to purified rat liver plasma membranes investigated.	Dimyristoylphosphatidylcholine	27-58	apolipoprotein A4	Rattus norvegicus	60-67
3827833-5	1986	ApoE complexed with dimyristoyl phosphatidylcholine (DMPC) was able to complete with VLDL for binding to the cells.	Dimyristoylphosphatidylcholine	20-51	apolipoprotein E	Homo sapiens	0-4
3827833-5	1986	ApoE complexed with dimyristoyl phosphatidylcholine (DMPC) was able to complete with VLDL for binding to the cells.	Dimyristoylphosphatidylcholine	53-57	apolipoprotein E	Homo sapiens	0-4
3767949-1	1986	Rat apoA-IV complexes with dimyristoyl phosphatidylcholine (apoA-IV-DMPC) have been prepared and their ability to bind to purified rat liver plasma membranes investigated.	Dimyristoylphosphatidylcholine	68-72	apolipoprotein A4	Rattus norvegicus	4-11
3767949-5	1986	ApoE-poor HDL effectively competed with apoA-IV-DMPC.	Dimyristoylphosphatidylcholine	48-52	apolipoprotein E	Rattus norvegicus	0-4
3767949-5	1986	ApoE-poor HDL effectively competed with apoA-IV-DMPC.	Dimyristoylphosphatidylcholine	48-52	apolipoprotein A4	Rattus norvegicus	40-47
3964650-1	1986	The interaction of lipoprotein lipase (LpL) and a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), has been studied by several physical methods.	Dimyristoylphosphatidylcholine	87-132	lipoprotein lipase	Homo sapiens	19-37
3730406-0	1986	Interaction of tryptic peptides of apolipoprotein B-100 with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	61-91	apolipoprotein B	Homo sapiens	35-55
3730406-1	1986	Apolipoprotein B-100, the major protein constituent of human plasma low-density lipoproteins (LDL), was carboxyamidomethylated, digested with trypsin and the water-soluble tryptic peptides were coincubated with liposomes of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	224-254	apolipoprotein B	Homo sapiens	0-20
3730406-1	1986	Apolipoprotein B-100, the major protein constituent of human plasma low-density lipoproteins (LDL), was carboxyamidomethylated, digested with trypsin and the water-soluble tryptic peptides were coincubated with liposomes of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	256-260	apolipoprotein B	Homo sapiens	0-20
3017405-0	1986	Interaction of cytochrome c with mixed dimyristoylphosphatidylcholine-dimyristoylphosphatidylserine bilayers: a deuterium nuclear magnetic resonance study.	Dimyristoylphosphatidylcholine	39-69	cytochrome c, somatic	Equus caballus	15-27
3017405-1	1986	Deuterium nuclear magnetic resonance (2H NMR) was used to study the interaction of cytochrome c (from horse heart) with bilayers of mixed dimyristoylphosphatidylcholine (DMPC) and dimyristoylphosphatidylserine (DMPS).	Dimyristoylphosphatidylcholine	170-174	cytochrome c, somatic	Equus caballus	83-95
3017405-3	1986	Liposomes containing equimolar mixtures of DMPC and DMPS were found to bind cytochrome c with a maximum ratio of about 1 mg of cytochrome c per 1 mg of DMPS.	Dimyristoylphosphatidylcholine	43-47	cytochrome c, somatic	Equus caballus	76-88
3017405-3	1986	Liposomes containing equimolar mixtures of DMPC and DMPS were found to bind cytochrome c with a maximum ratio of about 1 mg of cytochrome c per 1 mg of DMPS.	Dimyristoylphosphatidylcholine	43-47	cytochrome c, somatic	Equus caballus	127-139
3699165-3	1986	Here we report their binding to Pr3+ and demonstrate, by 1H NMR, the peptide-mediated transport of Pr3+ across dimyristoylphosphatidylcholine unilamellar vesicles via a 2:1 ion-sandwich complex.	Dimyristoylphosphatidylcholine	111-141	proteinase 3	Homo sapiens	99-102
3768315-0	1986	Protein-lipid interactions at membrane surfaces: a deuterium and phosphorus nuclear magnetic resonance study of the interaction between bovine rhodopsin and the bilayer head groups of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	184-214	rhodopsin	Bos taurus	143-152
3768315-1	1986	Rhodopsin, isolated from bovine retinal rod outer segment disk membranes, has been reconstituted into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine which was deuterated in the terminal methyl groups of the choline polar head group.	Dimyristoylphosphatidylcholine	114-157	rhodopsin	Bos taurus	0-9
3734628-2	1986	The protein was recombined with the phospholipid dimyristoyl phosphatidylcholine (DMPC) to produce a complex of DMPC-apoB (4:1 w/w).	Dimyristoylphosphatidylcholine	49-80	apolipoprotein B	Homo sapiens	117-121
3734628-2	1986	The protein was recombined with the phospholipid dimyristoyl phosphatidylcholine (DMPC) to produce a complex of DMPC-apoB (4:1 w/w).	Dimyristoylphosphatidylcholine	82-86	apolipoprotein B	Homo sapiens	117-121
3734628-2	1986	The protein was recombined with the phospholipid dimyristoyl phosphatidylcholine (DMPC) to produce a complex of DMPC-apoB (4:1 w/w).	Dimyristoylphosphatidylcholine	112-116	apolipoprotein B	Homo sapiens	117-121
3734628-6	1986	Carboxyfluorescein and [3H]dextran entrapment studies show the DMPC-apoB 4:1 (w/w) complex to encapsulate an aqueous volume of 0.17 microliter/mumol of DMPC.	Dimyristoylphosphatidylcholine	63-67	apolipoprotein B	Homo sapiens	68-72
3734628-8	1986	Differential scanning calorimetry (DSC) and circular dichroic spectroscopy (CD) were used to investigate the physical properties of apoB in the mixed micellar complex with NaDC and in the vesicular DMPC-apoB complex.	Dimyristoylphosphatidylcholine	198-202	apolipoprotein B	Homo sapiens	132-136
3734628-8	1986	Differential scanning calorimetry (DSC) and circular dichroic spectroscopy (CD) were used to investigate the physical properties of apoB in the mixed micellar complex with NaDC and in the vesicular DMPC-apoB complex.	Dimyristoylphosphatidylcholine	198-202	apolipoprotein B	Homo sapiens	203-207
3734628-10	1986	The DMPC-apoB complex exhibits a reversible thermal transition centered at 24 degrees C (delta H = 3.34 Kcal/mol DMPC) which is associated with the order-disorder transition of the hydrocarbon chains of DMPC.	Dimyristoylphosphatidylcholine	4-8	apolipoprotein B	Homo sapiens	9-13
3734628-10	1986	The DMPC-apoB complex exhibits a reversible thermal transition centered at 24 degrees C (delta H = 3.34 Kcal/mol DMPC) which is associated with the order-disorder transition of the hydrocarbon chains of DMPC.	Dimyristoylphosphatidylcholine	113-117	apolipoprotein B	Homo sapiens	9-13
3734628-10	1986	The DMPC-apoB complex exhibits a reversible thermal transition centered at 24 degrees C (delta H = 3.34 Kcal/mol DMPC) which is associated with the order-disorder transition of the hydrocarbon chains of DMPC.	Dimyristoylphosphatidylcholine	113-117	apolipoprotein B	Homo sapiens	9-13
3964650-1	1986	The interaction of lipoprotein lipase (LpL) and a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), has been studied by several physical methods.	Dimyristoylphosphatidylcholine	87-132	lipoprotein lipase	Homo sapiens	39-42
2985608-2	1985	Both 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC were shown to bind to ovarian membranes with Kd = 2.87 and 5.70 micrograms of protein/ml, respectively.	Dimyristoylphosphatidylcholine	18-22	apolipoprotein A1	Rattus norvegicus	10-17
4054131-7	1985	Apo-E-stimulated cholesteryl ester formation by the enzyme was enhanced when 1-oleoyl-2-palmitoyl-glycerophosphocholine was used as a substrate phospholipid (45% of apo A-I/phosphatidylcholine control) and most pronounced with dimyristoylglycerophosphocholine (75% of apo A-I/phosphatidylcholine control).	Dimyristoylphosphatidylcholine	227-259	apolipoprotein E	Homo sapiens	0-5
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	lipoprotein lipase	Homo sapiens	19-37
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	lipoprotein lipase	Homo sapiens	39-42
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	apolipoprotein C2	Homo sapiens	71-90
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	apolipoprotein C2	Homo sapiens	92-99
4027218-3	1985	When rhodopsin is incorporated into the saturated short-chain phospholipid dimyristoylphosphatidylcholine, photolysis of the protein results in an abnormal sequence of spectral transitions, and the dominant product of metarhodopsin I decay is free retinal plus opsin [Baldwin, P. A., & Hubbell, W. L. (1985) Biochemistry (preceding paper in this issue)].	Dimyristoylphosphatidylcholine	75-105	rhodopsin	Homo sapiens	5-14
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	34-38	apolipoprotein A1	Rattus norvegicus	26-33
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein A1	Rattus norvegicus	26-33
4074836-5	1985	The orientation of the most-ordered axis of the DMPC molecule is found to be tilted at an angle of 27 +/- 2 degrees with respect to the long axis of the sn-1 chain in its extended all trans conformation.	Dimyristoylphosphatidylcholine	48-52	solute carrier family 38 member 3	Homo sapiens	153-157
4005253-0	1985	Influence of the protein conformation on the interaction between alpha-lactalbumin and dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	87-117	lactalbumin alpha	Bos taurus	65-82
4005253-2	1985	In this work, the interaction between bovine alpha-lactalbumin and sonicated dimyristoylphosphatidylcholine vesicles has been compared in different circumstances which influence the protein conformation i.e., pH, ionic strength, decalcification, guanidine hydrochloride denaturation.	Dimyristoylphosphatidylcholine	77-107	lactalbumin alpha	Bos taurus	45-62
3158653-2	1985	Sharp increases in the quenching constants were found in samples of ATPase reconstituted with dimyristoyl-phosphatidylcholine and dipalmitoylphosphatidylcholine at temperatures slightly below the Tc transition temperature of the pure phospholipid.	Dimyristoylphosphatidylcholine	94-125	dynein axonemal heavy chain 8	Homo sapiens	68-74
2988613-0	1985	Association of spin-labelled cardiolipin with dimyristoylphosphatidylcholine-substituted bovine heart cytochrome c oxidase.	Dimyristoylphosphatidylcholine	46-76	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	102-122
3995074-10	1985	At a 1:2 ratio, incorporation of DMPC into fraction I-HDL results in the loss of one molecule of apolipoprotein A-I; the resultant particle is a stable phospholipid-rich and protein-poor HDL which has a square-packing geometry.	Dimyristoylphosphatidylcholine	33-37	apolipoprotein A1	Homo sapiens	97-115
2985608-2	1985	Both 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC were shown to bind to ovarian membranes with Kd = 2.87 and 5.70 micrograms of protein/ml, respectively.	Dimyristoylphosphatidylcholine	41-45	apolipoprotein A1	Rattus norvegicus	10-17
2985608-2	1985	Both 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC were shown to bind to ovarian membranes with Kd = 2.87 and 5.70 micrograms of protein/ml, respectively.	Dimyristoylphosphatidylcholine	41-45	NLR family pyrin domain containing 3	Homo sapiens	36-40
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein A2	Rattus norvegicus	43-51
2985608-3	1985	The binding of both 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC was inhibited by unlabeled HDL3, apo-A-I.DMPC, apo-A-II.DMPC, apo-C-I.DMPC, apo-C-II.DMPC, apo-C-III1.DMPC, and apo-C-III2.DMPC, but not by DMPC vesicles, bovine serum albumin.DMPC or low density lipoprotein.	Dimyristoylphosphatidylcholine	33-37	apolipoprotein A1	Rattus norvegicus	25-32
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein A1	Rattus norvegicus	26-33
4016089-1	1985	Resonance energy transfer was used to study the structure of cytochrome b5 and its nonpolar segment reconstituted into sonicated vesicles of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	141-171	cytochrome b5 type A	Homo sapiens	61-74
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein A2	Rattus norvegicus	43-51
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein A1	Rattus norvegicus	26-33
2985608-4	1985	Since the binding labeled apo-A-I.DMPC and apo-A-II.DMPC was inhibited by the DMPC complexes of apo-C groups, the direct binding of 125I-apo-C-III1.DMPC was also demonstrated with Kd = 9.6 micrograms of protein/ml.	Dimyristoylphosphatidylcholine	52-56	apolipoprotein A2	Rattus norvegicus	43-51
2985608-5	1985	In addition, unlabeled apo-A-I.DMPC, and apo-A-II.DMPC, as well as apo-C.DMPC, inhibited 125I-HDL3 binding.	Dimyristoylphosphatidylcholine	31-35	apolipoprotein A1	Rattus norvegicus	23-30
2985608-8	1985	In vivo pretreatment of rats with human chorionic gonadotropin resulted in an increase of 125I-apo-A-I.DMPC, 125I-apo-A-II.DMPC, and 125I-apo-C-III1.DMPC binding activities.	Dimyristoylphosphatidylcholine	103-107	apolipoprotein A1	Homo sapiens	95-102
2985608-10	1985	An examination of the equilibrium dissociation constant and binding capacity for 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC after human chorionic gonadotropin treatment revealed that the increase in binding activity was due to an increase in the number of binding sites rather than a change in the binding affinity.	Dimyristoylphosphatidylcholine	94-98	apolipoprotein A1	Homo sapiens	86-93
2985608-10	1985	An examination of the equilibrium dissociation constant and binding capacity for 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC after human chorionic gonadotropin treatment revealed that the increase in binding activity was due to an increase in the number of binding sites rather than a change in the binding affinity.	Dimyristoylphosphatidylcholine	117-121	apolipoprotein A1	Homo sapiens	86-93
2985608-10	1985	An examination of the equilibrium dissociation constant and binding capacity for 125I-apo-A-I.DMPC and 125I-apo-A-II.DMPC after human chorionic gonadotropin treatment revealed that the increase in binding activity was due to an increase in the number of binding sites rather than a change in the binding affinity.	Dimyristoylphosphatidylcholine	117-121	NLR family pyrin domain containing 3	Homo sapiens	112-116
3922419-4	1985	Apolipoprotein A-IV associated with dimyristoylphosphatidylcholine (DMPC) to form recombinants which contained two molecules of apolipoprotein A-IV and had a lipid/protein molar ratio of 110.	Dimyristoylphosphatidylcholine	36-66	apolipoprotein A4	Rattus norvegicus	0-19
3922419-4	1985	Apolipoprotein A-IV associated with dimyristoylphosphatidylcholine (DMPC) to form recombinants which contained two molecules of apolipoprotein A-IV and had a lipid/protein molar ratio of 110.	Dimyristoylphosphatidylcholine	68-72	apolipoprotein A4	Rattus norvegicus	0-19
3922419-7	1985	However, by competition studies it was found that apolipoprotein A-I competed for the binding to DMPC more effectively than did apolipoprotein A-IV.	Dimyristoylphosphatidylcholine	97-101	apolipoprotein A1	Rattus norvegicus	50-68
3966801-3	1985	The tryptophan residue in both apo C-I and C-II and their sodium dodecyl sulfate (SDS) or dimyristoylphosphatidylcholine (DMPC) complexes displayed significant motional freedom on the nanosecond time scale.	Dimyristoylphosphatidylcholine	90-120	apolipoprotein C1	Homo sapiens	31-47
3966801-3	1985	The tryptophan residue in both apo C-I and C-II and their sodium dodecyl sulfate (SDS) or dimyristoylphosphatidylcholine (DMPC) complexes displayed significant motional freedom on the nanosecond time scale.	Dimyristoylphosphatidylcholine	122-126	apolipoprotein C1	Homo sapiens	31-47
6428456-1	1984	Enthalphy of association of apolipoprotein A-II with dimyristoylphosphatidylcholine-cholesterol mixtures.	Dimyristoylphosphatidylcholine	53-83	lipoprotein(a)	Homo sapiens	28-44
6093698-3	1984	First, ESR experiments involving spin-labeled phosphatidylserine, phosphatidic acid, and phosphatidylcholine demonstrated that, in the fluid-isotropic phase of dimyristoylphosphatidylcholine (DMPC)-rhodopsin membranes, the relative order of rhodopsin-induced immobilization was phosphatidic acid greater than phosphatidylcholine greater than phosphatidylserine.	Dimyristoylphosphatidylcholine	160-190	rhodopsin	Homo sapiens	198-207
6093698-3	1984	First, ESR experiments involving spin-labeled phosphatidylserine, phosphatidic acid, and phosphatidylcholine demonstrated that, in the fluid-isotropic phase of dimyristoylphosphatidylcholine (DMPC)-rhodopsin membranes, the relative order of rhodopsin-induced immobilization was phosphatidic acid greater than phosphatidylcholine greater than phosphatidylserine.	Dimyristoylphosphatidylcholine	160-190	rhodopsin	Homo sapiens	241-250
6093698-6	1984	A main result of this analysis was the finding that rhodopsin broadens and reduces the amplitude of the DMPS phase transition to a much smaller extent than it does the DMPC phase transition.	Dimyristoylphosphatidylcholine	168-172	rhodopsin	Homo sapiens	52-61
6432780-1	1984	Apolipoprotein A-I-dimyristoylphosphatidylcholine complex.	Dimyristoylphosphatidylcholine	19-49	apolipoprotein A1	Homo sapiens	0-18
6089844-2	1984	Complexes of [125I]apo E-3/3, 2/2, 3/2 and 4/3 with dimyristoyl phosphatidylcholine (DMPC) were prepared by a detergent-dialysis method: discoidal, bilayer complexes with a stoichiometry of 125 +/- 15 mol DMPC/mol apo E resulted.	Dimyristoylphosphatidylcholine	52-83	apolipoprotein E	Homo sapiens	19-44
6089844-2	1984	Complexes of [125I]apo E-3/3, 2/2, 3/2 and 4/3 with dimyristoyl phosphatidylcholine (DMPC) were prepared by a detergent-dialysis method: discoidal, bilayer complexes with a stoichiometry of 125 +/- 15 mol DMPC/mol apo E resulted.	Dimyristoylphosphatidylcholine	52-83	apolipoprotein E	Homo sapiens	19-24
6089844-2	1984	Complexes of [125I]apo E-3/3, 2/2, 3/2 and 4/3 with dimyristoyl phosphatidylcholine (DMPC) were prepared by a detergent-dialysis method: discoidal, bilayer complexes with a stoichiometry of 125 +/- 15 mol DMPC/mol apo E resulted.	Dimyristoylphosphatidylcholine	85-89	apolipoprotein E	Homo sapiens	19-44
6089844-2	1984	Complexes of [125I]apo E-3/3, 2/2, 3/2 and 4/3 with dimyristoyl phosphatidylcholine (DMPC) were prepared by a detergent-dialysis method: discoidal, bilayer complexes with a stoichiometry of 125 +/- 15 mol DMPC/mol apo E resulted.	Dimyristoylphosphatidylcholine	85-89	apolipoprotein E	Homo sapiens	19-24
6089844-3	1984	The predominant phenotype apo E-3/3, and the phenotype apo E-2/2 characteristic of patients with Type III hyperlipoproteinemia, interact similarly with DMPC and adopt the same conformation with 60-70% alpha-helix, as monitored by circular dichroism spectroscopy.	Dimyristoylphosphatidylcholine	152-156	apolipoprotein E	Homo sapiens	26-35
6089844-3	1984	The predominant phenotype apo E-3/3, and the phenotype apo E-2/2 characteristic of patients with Type III hyperlipoproteinemia, interact similarly with DMPC and adopt the same conformation with 60-70% alpha-helix, as monitored by circular dichroism spectroscopy.	Dimyristoylphosphatidylcholine	152-156	apolipoprotein E	Homo sapiens	55-64
6733134-0	1984	Lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	43-73	lipoprotein lipase	Homo sapiens	0-18
6733134-2	1984	The effect of phospholipid organization on the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine was examined with sonicated vesicles and Triton X-100 or lysomyristoylphosphatidylcholine solubilized lipid.	Dimyristoylphosphatidylcholine	90-120	lipoprotein lipase	Homo sapiens	47-65
6733134-4	1984	Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested.	Dimyristoylphosphatidylcholine	135-165	apolipoprotein C2	Homo sapiens	0-19
6733134-4	1984	Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested.	Dimyristoylphosphatidylcholine	135-165	lipoprotein lipase	Homo sapiens	47-65
6733134-4	1984	Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested.	Dimyristoylphosphatidylcholine	135-165	lipoprotein lipase	Homo sapiens	92-110
2983785-0	1985	[Effect of phosphatidylglycerol on the incorporation process of cytochrome P-450 in liposomes from dimyristoylphosphatidylcholine].	Dimyristoylphosphatidylcholine	99-129	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	64-80
2983785-1	1985	Using the electron paramagnetic resonance (EPR) method with spin-labeled fatty acids and gel-penetrating chromatography, the effect of phosphatidylglycerol on cytochrome P-450 incorporation into liposomes from dimyristoylphosphatidylcholine was investigated.	Dimyristoylphosphatidylcholine	210-240	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	159-175
6094531-5	1984	HDL and dimyristoyl phosphatidylcholine (DMPC) X apo-A-I complexes decreased binding by 80 and 65%, respectively.	Dimyristoylphosphatidylcholine	8-39	apolipoprotein A1	Rattus norvegicus	49-56
6094531-5	1984	HDL and dimyristoyl phosphatidylcholine (DMPC) X apo-A-I complexes decreased binding by 80 and 65%, respectively.	Dimyristoylphosphatidylcholine	41-45	apolipoprotein A1	Rattus norvegicus	49-56
6094531-7	1984	However, DMPC X apo-E complexes did compete for the binding of the total HDL fraction that contained apo-E but to a lesser extent than did DMPC X apo-A-I.	Dimyristoylphosphatidylcholine	9-13	apolipoprotein E	Rattus norvegicus	16-21
6094531-7	1984	However, DMPC X apo-E complexes did compete for the binding of the total HDL fraction that contained apo-E but to a lesser extent than did DMPC X apo-A-I.	Dimyristoylphosphatidylcholine	9-13	apolipoprotein E	Rattus norvegicus	101-106
6094531-8	1984	DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein A1	Rattus norvegicus	12-19
6094531-8	1984	DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein A1	Rattus norvegicus	122-129
6094531-8	1984	DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein E	Rattus norvegicus	215-220
6094531-8	1984	DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes.	Dimyristoylphosphatidylcholine	115-119	apolipoprotein A1	Rattus norvegicus	12-19
6094531-8	1984	DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes.	Dimyristoylphosphatidylcholine	115-119	apolipoprotein A1	Rattus norvegicus	12-19
6094531-8	1984	DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes.	Dimyristoylphosphatidylcholine	115-119	apolipoprotein A1	Rattus norvegicus	12-19
6548649-9	1984	An increase of the rotational correlation times of the fluorescent probe and a higher order of its environment were detected after the interaction of alpha-lactalbumin with the dimyristoylphosphatidylcholine vesicles at acidic pH at 24.2 degrees C.	Dimyristoylphosphatidylcholine	177-207	lactalbumin alpha	Homo sapiens	150-167
6327714-7	1984	When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding.	Dimyristoylphosphatidylcholine	77-81	apolipoprotein E	Homo sapiens	164-170
6327714-7	1984	When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding.	Dimyristoylphosphatidylcholine	77-81	apolipoprotein E	Homo sapiens	204-210
6327714-7	1984	When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding.	Dimyristoylphosphatidylcholine	173-177	apolipoprotein E	Homo sapiens	164-170
6327714-7	1984	When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding.	Dimyristoylphosphatidylcholine	173-177	apolipoprotein E	Homo sapiens	164-170
6428456-2	1984	Apolipoprotein A-II spontaneously associates with dimyristoylphosphatidylcholine (DMPC)-cholesterol mixtures to give products whose composition is a sensitive function of temperature and cholesterol content.	Dimyristoylphosphatidylcholine	50-80	lipoprotein(a)	Homo sapiens	0-16
6428456-2	1984	Apolipoprotein A-II spontaneously associates with dimyristoylphosphatidylcholine (DMPC)-cholesterol mixtures to give products whose composition is a sensitive function of temperature and cholesterol content.	Dimyristoylphosphatidylcholine	82-86	lipoprotein(a)	Homo sapiens	0-16
6713599-4	1984	The complexes of TPO with dimyristoyl phosphatidyl choline (DMPC), DPPC, and distearoyl phosphatidyl choline (DSPC) bilayers showed transition temperatures (Tc) which were lower than the characteristic ones shown by liposomes with the respective phospholipids alone.	Dimyristoylphosphatidylcholine	26-58	LOW QUALITY PROTEIN: thyroid peroxidase	Bos taurus	17-20
6725265-8	1984	For complexes of DMPC/CO/apoB, the secondary structure shows less alpha-helix which correlates with the difference in surface lipid environment.	Dimyristoylphosphatidylcholine	17-21	apolipoprotein B	Homo sapiens	25-29
6424717-4	1984	alpha-Tocopherol transfers from apolipoprotein A-II/dimyristoylphosphatidylcholine recombinants with a half-time of 40 min and an activation energy of 17.2 kcal/mol.	Dimyristoylphosphatidylcholine	52-82	apolipoprotein A2	Bos taurus	32-51
6713599-4	1984	The complexes of TPO with dimyristoyl phosphatidyl choline (DMPC), DPPC, and distearoyl phosphatidyl choline (DSPC) bilayers showed transition temperatures (Tc) which were lower than the characteristic ones shown by liposomes with the respective phospholipids alone.	Dimyristoylphosphatidylcholine	60-64	LOW QUALITY PROTEIN: thyroid peroxidase	Bos taurus	17-20
6421327-1	1984	The formation of hybrid association products between apolipoprotein A-I and apolipoprotein A-II from human high-density lipoprotein was investigated in solutions of these apolipoprotein and in recombinant particles with dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	252-256	apolipoprotein A1	Homo sapiens	53-71
20815113-5	1984	In the presence of DMPC, thermal denaturation could be measured for apo A-I above 70-75 "C and for apo A-I1 and apo C above about 45 OC.	Dimyristoylphosphatidylcholine	19-23	apolipoprotein A1	Homo sapiens	68-75
6704114-1	1984	Cytochrome P-450, purified from liver microsomes of phenobarbital-treated rabbits, was incorporated into dimyristoylphosphatidylcholine liposomes.	Dimyristoylphosphatidylcholine	105-135	cytochrome P-450	Oryctolagus cuniculus	0-16
6849876-1	1983	The interactions of cytochrome b5 with dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine lipid bilayers have been studied with high-sensitivity differential scanning calorimetry and fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	39-69	cytochrome b5 type A	Homo sapiens	20-33
6318827-2	1984	The electron spin resonance spectrum of the spin-labeled protein was examined at different temperatures in: (a) whole erythrocyte ghosts; (b) ghosts depleted of spectrin and actin; (c) alkaline-treated ghosts; (d) vesicles made with purified band 3 reassociated with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	267-297	spindlin 1	Homo sapiens	44-48
6743304-0	1984	Reconstitution of the liver microsomal monooxygenase system in liposomes from dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	78-108	cytochrome P450 family 4 subfamily B member 1	Homo sapiens	28-52
6313653-4	1983	Only one of the five antibodies, referred to as 1D7, was found to inhibit binding, blocking greater than 90% of the receptor-binding activity of apo-E3 dimyristoylphosphatidyl-choline.	Dimyristoylphosphatidylcholine	152-183	apolipoprotein E	Homo sapiens	145-150
6411718-4	1983	SAA4 differed from the apolipoproteins in its ability to disrupt multilamellar dimyristoylphosphatidylcholine (DMPC) liposomes and generate bilayer discs.	Dimyristoylphosphatidylcholine	79-109	serum amyloid A4, constitutive	Homo sapiens	0-4
6411718-4	1983	SAA4 differed from the apolipoproteins in its ability to disrupt multilamellar dimyristoylphosphatidylcholine (DMPC) liposomes and generate bilayer discs.	Dimyristoylphosphatidylcholine	111-115	serum amyloid A4, constitutive	Homo sapiens	0-4
6411718-5	1983	Apo-A-I, apo-A-II, and apo-C-III reduced the turbidity of DMPC dispersions at protein:lipid molar ratios of 1:200.	Dimyristoylphosphatidylcholine	58-62	apolipoprotein A1	Homo sapiens	0-7
6411718-11	1983	In addition, SAA4 as well as the apolipoproteins broadened the range and increased the temperature of the gel-liquid crystal transition temperature of DMPC.	Dimyristoylphosphatidylcholine	151-155	serum amyloid A4, constitutive	Homo sapiens	13-17
6305968-1	1983	Highly purified beef adrenal cytochrome P-450 specific for cholesterol side chain cleavage (P-450-scc) has been reconstituted with sonicated vesicles containing cholesterol and either dimyristoyl phosphatidylcholine (DMPC) or dioleoyl phosphatidylcholine (DOPC).	Dimyristoylphosphatidylcholine	217-221	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	92-101
6421314-1	1984	Complexes formed between apolipoprotein A-I (apo A-I) and dimyristoylphosphatidylcholine (DMPC) or egg phosphatidylcholine have been studied by high-field 1H NMR, nondenaturing gradient gel electrophoresis, electron microscopy, and gel filtration chromatography.	Dimyristoylphosphatidylcholine	58-88	apolipoprotein A1	Homo sapiens	25-43
6421314-1	1984	Complexes formed between apolipoprotein A-I (apo A-I) and dimyristoylphosphatidylcholine (DMPC) or egg phosphatidylcholine have been studied by high-field 1H NMR, nondenaturing gradient gel electrophoresis, electron microscopy, and gel filtration chromatography.	Dimyristoylphosphatidylcholine	90-94	apolipoprotein A1	Homo sapiens	25-43
6421314-1	1984	Complexes formed between apolipoprotein A-I (apo A-I) and dimyristoylphosphatidylcholine (DMPC) or egg phosphatidylcholine have been studied by high-field 1H NMR, nondenaturing gradient gel electrophoresis, electron microscopy, and gel filtration chromatography.	Dimyristoylphosphatidylcholine	90-94	apolipoprotein A1	Homo sapiens	45-52
6421314-3	1984	As determined by electron microscopy and gel filtration of DMPC/apo A-I complexes, the size of the discoidal micelles produced appears to increase uniformly with an increasing lipid/protein ratio.	Dimyristoylphosphatidylcholine	59-63	apolipoprotein A1	Homo sapiens	64-71
6421314-4	1984	By electron microscopy, the diameters of isolated DMPC/apo A-I discoidal micelles range from approximately 89 A at a 40 molar ratio to 205 A at a 700 molar ratio.	Dimyristoylphosphatidylcholine	50-54	apolipoprotein A1	Homo sapiens	55-62
6525185-0	1984	Effect of the gel-liquid crystalline phase transition on the reduction of cytochrome P-450 reconstituted into dimyristoyl-phosphatidylcholine liposomes.	Dimyristoylphosphatidylcholine	110-141	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	74-90
6416305-0	1983	Pig apolipoprotein AI self-association and interaction with L-alpha-dimyristoylphosphatidylcholine as compared with human apolipoprotein AI.	Dimyristoylphosphatidylcholine	60-98	apolipoprotein A1	Sus scrofa	4-21
6882744-3	1983	A soluble apoB-dimyristoylphosphatidylcholine (DMPC) complex has been prepared by incubation of aqueous solutions of apoB-NaDC and DMPC-NaDC (2/1 w/w) at room temperature with detergent removal by extensive dialysis.	Dimyristoylphosphatidylcholine	47-51	apolipoprotein B	Homo sapiens	10-14
6882744-3	1983	A soluble apoB-dimyristoylphosphatidylcholine (DMPC) complex has been prepared by incubation of aqueous solutions of apoB-NaDC and DMPC-NaDC (2/1 w/w) at room temperature with detergent removal by extensive dialysis.	Dimyristoylphosphatidylcholine	47-51	apolipoprotein B	Homo sapiens	117-121
6882744-4	1983	A combination of gel chromatographic and density gradient fractionation of DMPC-apoB incubation mixtures demonstrates that a reasonably well-defined complex of DMPC and apoB is formed with a 4:1 w/w lipid:protein ratio.	Dimyristoylphosphatidylcholine	75-79	apolipoprotein B	Homo sapiens	80-84
6882744-4	1983	A combination of gel chromatographic and density gradient fractionation of DMPC-apoB incubation mixtures demonstrates that a reasonably well-defined complex of DMPC and apoB is formed with a 4:1 w/w lipid:protein ratio.	Dimyristoylphosphatidylcholine	75-79	apolipoprotein B	Homo sapiens	169-173
6882744-4	1983	A combination of gel chromatographic and density gradient fractionation of DMPC-apoB incubation mixtures demonstrates that a reasonably well-defined complex of DMPC and apoB is formed with a 4:1 w/w lipid:protein ratio.	Dimyristoylphosphatidylcholine	160-164	apolipoprotein B	Homo sapiens	80-84
6882744-7	1983	However, apoB that has been complexed with DMPC exhibits more alpha-helix.	Dimyristoylphosphatidylcholine	43-47	apolipoprotein B	Homo sapiens	9-13
6882744-9	1983	The behavior of apoB during its reassociation with phospholipid and the structural features of the DMPC-apoB particle are similar to those observed in the interaction of solubilized membrane proteins with lipid rather than that of other apo-lipoproteins.	Dimyristoylphosphatidylcholine	99-103	apolipoprotein B	Homo sapiens	104-108
6311617-5	1983	Hemoglobin encapsulated in egg phosphatidylcholine vesicles converts to methemoglobin within 2 days at 4 degrees C. By contrast, when a mixture of dimyristoyl phosphatidylcholine, cholesterol and dicetyl phosphate is used there is no acceleration in methemoglobin formation, and the preparation is stable for at least 14 days at 4 degrees C.	Dimyristoylphosphatidylcholine	147-178	hemoglobin subunit gamma 2	Homo sapiens	250-263
6301543-1	1983	The dynamic and conformational properties of the 2-methylene on the sn-2 chain of dimyristoylphosphatidylcholine have been investigated in small unilamellar vesicles.	Dimyristoylphosphatidylcholine	82-112	solute carrier family 38 member 5	Homo sapiens	68-72
6824658-3	1983	We investigated the interaction between alpha-lactalbumin and sonicated dimyristoylphosphatidylcholine at pH 4 and different temperatures.	Dimyristoylphosphatidylcholine	72-102	lactalbumin alpha	Homo sapiens	40-57
6838871-1	1983	The characteristics of small unilamellar, large unilamellar and large multilamellar vesicles of dimyristoylphosphatidylcholine and their interaction with alpha-lactalbumin are compared at pH 4.	Dimyristoylphosphatidylcholine	96-126	lactalbumin alpha	Homo sapiens	154-171
6838895-2	1983	Detergent-solubilized cytochrome b5 in solution and in a reconstituted system with dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	83-114	cytochrome b5 type A	Homo sapiens	22-35
6818987-4	1982	The initial velocities of the enzymatic reaction with purified human lecithin: cholesterol acyltransferase decreased in the order palmitoyloleoyl-PC greater than dipalmitoyl-PC greater than dimyristoyl-PC, at saturating micellar substrate levels.	Dimyristoylphosphatidylcholine	190-204	lecithin-cholesterol acyltransferase	Homo sapiens	69-106
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
7150552-0	1982	Nanosecond rotational motions of apolipoprotein C-I in solution and in complexes with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	86-116	apolipoprotein C1	Homo sapiens	33-51
7150552-1	1982	Human apolipoprotein C-I (apo C-I) in solution, in monomeric and oligomeric form, and in micellar complexes with dimyristoylphosphatidylcholine (DMPC), below and above the phase transition temperature of DMPC, was investigated with steady-state and time-resolved fluorescence methods.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein C1	Homo sapiens	6-24
7150552-1	1982	Human apolipoprotein C-I (apo C-I) in solution, in monomeric and oligomeric form, and in micellar complexes with dimyristoylphosphatidylcholine (DMPC), below and above the phase transition temperature of DMPC, was investigated with steady-state and time-resolved fluorescence methods.	Dimyristoylphosphatidylcholine	204-208	apolipoprotein C1	Homo sapiens	6-24
6810943-1	1982	The enthalpy, entropy and free energy of activation was measured for the transfer of the tryptophan residues of apolipoprotein A-I from a more hydrophobic environment of a lipoprotein particle containing dimyristoylphosphatidylcholine (with or without 12% cholesterol) to an aqueous solvent in the presence of varying concentrations of guanidinium chloride.	Dimyristoylphosphatidylcholine	204-234	apolipoprotein A1	Homo sapiens	112-130
6180771-7	1982	Fab fragments inhibited the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine vesicles and trioleoylglycerol emulsions to the same extent.	Dimyristoylphosphatidylcholine	71-101	FA complementation group B	Homo sapiens	0-3
7171597-3	1982	From the delta H dependence on protein concentration in proteoliposomes it was calculated that one cytochrome P-450 molecule influence 350 +/- 50 dimyristoylphosphatidylcholine (DMPC) molecules.	Dimyristoylphosphatidylcholine	146-176	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	99-115
7171597-3	1982	From the delta H dependence on protein concentration in proteoliposomes it was calculated that one cytochrome P-450 molecule influence 350 +/- 50 dimyristoylphosphatidylcholine (DMPC) molecules.	Dimyristoylphosphatidylcholine	178-182	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	99-115
7171597-4	1982	The electrostatic interaction of cytochrome P-450 and negatively charged phospholipid, phosphatidylinositol (PI), mixed with DMPC involves the temperature stabilization of proteoliposomes at a phase transition of phospholipid bilayers.	Dimyristoylphosphatidylcholine	125-129	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	33-49
7126647-8	1982	As with the heterogeneous antibodies, the monoclonal IgG1 is more efficient in mediating cellular uptake when the vesicles are in the "fluid" physical state (dimyristoylphosphatidylcholine at 37 degrees C) compared to "solid" (dipalmitoylphosphatidylcholine at 37 degrees C).	Dimyristoylphosphatidylcholine	158-188	immunoglobulin heavy constant gamma 1 (G1m marker)	Mus musculus	53-57
7150417-4	1982	We have introduced it into the hydrocarbon layer of dimyristoylphosphatidylcholine vesicles in order to study their interaction with alpha-lactalbumin (alpha-LA) as a function of pH and temperature.	Dimyristoylphosphatidylcholine	52-82	lactalbumin alpha	Homo sapiens	133-150
7150417-4	1982	We have introduced it into the hydrocarbon layer of dimyristoylphosphatidylcholine vesicles in order to study their interaction with alpha-lactalbumin (alpha-LA) as a function of pH and temperature.	Dimyristoylphosphatidylcholine	52-82	lactalbumin alpha	Homo sapiens	152-160
6180771-7	1982	Fab fragments inhibited the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine vesicles and trioleoylglycerol emulsions to the same extent.	Dimyristoylphosphatidylcholine	71-101	lipoprotein lipase	Bos taurus	28-46
6809042-6	1982	The energy barrier associated with this desorption step makes the binding of apo A-I to DMPC a thermodynamically irreversible process.	Dimyristoylphosphatidylcholine	88-92	apolipoprotein A1	Homo sapiens	77-84
6126513-8	1982	ACAT activity was five times higher when the liposomes were prepared from dioleoylphosphatidylcholine than from saturated phosphatidylcholines, including hydrogenated egg yolk, dimyristoyl or dipalmitoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	177-188	acetyl-Coenzyme A acetyltransferase 1	Mus musculus	0-4
6808278-4	1982	Incubation of the apo A-I-lipid complexes with HDL3 resulted in a complete breakdown of the discoidal structures and a transfer to DMPC and cholesterol to HDL3.	Dimyristoylphosphatidylcholine	131-135	apolipoprotein A1	Homo sapiens	18-25
7068619-5	1982	Moreover, delipidated apo-E is an inhibitory as apo-E complexed with dimyristoyl phosphatidylcholine or with sphingomyelin.	Dimyristoylphosphatidylcholine	69-100	apolipoprotein E	Homo sapiens	22-27
7068619-5	1982	Moreover, delipidated apo-E is an inhibitory as apo-E complexed with dimyristoyl phosphatidylcholine or with sphingomyelin.	Dimyristoylphosphatidylcholine	69-100	apolipoprotein E	Homo sapiens	48-53
6809042-0	1982	Mechanism of dissociation of human apolipoprotein A-I from complexes with dimyristoylphosphatidylcholine as studied by guanidine hydrochloride denaturation.	Dimyristoylphosphatidylcholine	74-104	apolipoprotein A1	Homo sapiens	35-53
6809042-3	1982	In both the denaturation and renaturation of 1:100 and 1:500 complexes, the final values of the molar ellipticity and the ratio of free to bound apo A-I at various concentrations of Gdn-HCl are dependent on the initial state of the lipid and protein; apo A-I is more resistant to denaturation when Gdn-HCl is added to existing complexes than to a mixture of apo A-I and DMPC.	Dimyristoylphosphatidylcholine	370-374	apolipoprotein A1	Homo sapiens	145-152
6809042-4	1982	There is an intermediate state in the denaturation pathway of apo A-I/DMPC complexes which is not present in the renaturation; the intermediate comprises partially unfold apo A-I molecules still associated with the complex by some of their apolar residues.	Dimyristoylphosphatidylcholine	70-74	apolipoprotein A1	Homo sapiens	62-69
6808278-1	1982	The interaction of human plasma high density lipoproteins (HDL3) with discoidal complexes of apolipoprotein A-I (apo A-I) and dimyristoyl phosphatidylcholine (DMPC) containing 0, 10, 20 or 30 mol % cholesterol was investigated.	Dimyristoylphosphatidylcholine	126-157	HDL3	Homo sapiens	59-63
6808278-1	1982	The interaction of human plasma high density lipoproteins (HDL3) with discoidal complexes of apolipoprotein A-I (apo A-I) and dimyristoyl phosphatidylcholine (DMPC) containing 0, 10, 20 or 30 mol % cholesterol was investigated.	Dimyristoylphosphatidylcholine	159-163	HDL3	Homo sapiens	59-63
6808278-4	1982	Incubation of the apo A-I-lipid complexes with HDL3 resulted in a complete breakdown of the discoidal structures and a transfer to DMPC and cholesterol to HDL3.	Dimyristoylphosphatidylcholine	131-135	HDL3	Homo sapiens	47-51
7093234-4	1982	The following results were obtained: (1) The rate of solute diffusion, which is decreased monotonically, in DMPC/DPPC MLV, by increasing the molar fractions of DPPC, exhibits maxima at 0.2 molar fraction of DSPC in DMPC/DSPC MLV and at 0.4 molar fraction of DBPC in DMPC/DBPC MLV.	Dimyristoylphosphatidylcholine	108-112	Y-box binding protein 2	Homo sapiens	258-262
7093234-4	1982	The following results were obtained: (1) The rate of solute diffusion, which is decreased monotonically, in DMPC/DPPC MLV, by increasing the molar fractions of DPPC, exhibits maxima at 0.2 molar fraction of DSPC in DMPC/DSPC MLV and at 0.4 molar fraction of DBPC in DMPC/DBPC MLV.	Dimyristoylphosphatidylcholine	108-112	Y-box binding protein 2	Homo sapiens	271-275
7053382-1	1982	The turkey erythrocyte membrane insulin receptor was solubilized and reconstituted into vesicles composed of either soy or dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	123-154	insulin receptor	Meleagris gallopavo	32-48
7084452-0	1982	Human C-apolipoproteins promote hydrolysis of dimyristoyl phosphatidylcholine by snake venom phospholipase A2.	Dimyristoylphosphatidylcholine	46-77	phospholipase A2 group IB	Homo sapiens	93-109
6461976-8	1982	Extensive restoration of the Ca2+-dependent ATPase activity has been achieved by oleic acid, a lysolecithin (myristoylglycerophosphocholine) and a lecithin (dimyristoylglycerophosphocholine).	Dimyristoylphosphatidylcholine	157-189	dynein axonemal heavy chain 8	Homo sapiens	44-50
7061462-0	1982	Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants.	Dimyristoylphosphatidylcholine	102-132	rhodopsin	Homo sapiens	92-101
7061462-1	1982	The technique of deuterium magnetic resonance was used to study the orientational order of the perdeuterated acyl chains of dimyristoylphosphatidylcholine (DMPC-d54) reconstituted with rhodopsin between 0 and 23 degrees C. This range includes the gel to liquid crystalline phase transition of DMPC-d54 at 20 degrees C. Molar lipid/protein (L/P) ratios of L/P = infinity, 150, 50, 30, and 12 were investigated.	Dimyristoylphosphatidylcholine	124-154	rhodopsin	Homo sapiens	185-194
7061462-1	1982	The technique of deuterium magnetic resonance was used to study the orientational order of the perdeuterated acyl chains of dimyristoylphosphatidylcholine (DMPC-d54) reconstituted with rhodopsin between 0 and 23 degrees C. This range includes the gel to liquid crystalline phase transition of DMPC-d54 at 20 degrees C. Molar lipid/protein (L/P) ratios of L/P = infinity, 150, 50, 30, and 12 were investigated.	Dimyristoylphosphatidylcholine	156-160	rhodopsin	Homo sapiens	185-194
6174152-3	1982	The effect was not seen upon the addition of poly(L-lysine) to this lipid nor does the myelin basic protein alter the phase transition properties of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	149-179	myelin basic protein	Bos taurus	87-107
7053382-10	1982	Solubilization studies with 1% beta-octylglucoside indicated, however, that the dimyristoyl phosphatidylcholine vesicles incorporated a slightly lesser amount of insulin receptor.	Dimyristoylphosphatidylcholine	80-111	insulin receptor	Meleagris gallopavo	162-178
6784753-0	1981	Physical properties of lipid-protein complexes formed by the interaction of dimyristoylphosphatidylcholine and human high-density apolipoprotein A-II.	Dimyristoylphosphatidylcholine	76-106	apolipoprotein A2	Homo sapiens	130-149
6799601-13	1982	ApoE purified and reconstituted into dimyristoyl phosphatidylcholine vesicles was a potent competitor for the remnant binding site.	Dimyristoylphosphatidylcholine	37-68	apolipoprotein E	Rattus norvegicus	0-4
6784753-1	1981	Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted.	Dimyristoylphosphatidylcholine	90-120	apolipoprotein A2	Homo sapiens	21-28
6784753-1	1981	Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted.	Dimyristoylphosphatidylcholine	122-126	apolipoprotein A2	Homo sapiens	0-19
6784753-1	1981	Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted.	Dimyristoylphosphatidylcholine	122-126	apolipoprotein A2	Homo sapiens	21-28
6784753-1	1981	Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted.	Dimyristoylphosphatidylcholine	90-120	apolipoprotein A2	Homo sapiens	0-19
6780564-0	1981	Interaction of apolipoprotein A-I with dimyristoylphosphatidylcholine particles of various sizes.	Dimyristoylphosphatidylcholine	39-69	APOAI	Bos taurus	15-33
6776110-1	1980	Interaction of apolipoprotein A-II from human plasma high density lipoproteins with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	84-114	apolipoprotein A2	Homo sapiens	15-34
6780564-7	1981	For the smaller DMPC vesicles, the vesicular complexes are saturated when 6 or 7 apo A-I molecules are bound per particle, which corresponds to 2,83 X 10(4) A2 of vesicle surface per apo A-I and an approximate 16% coverage of the surface by apo A-I.	Dimyristoylphosphatidylcholine	16-20	APOAI	Bos taurus	81-88
7213900-0	1981	Interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	38-69	lactalbumin alpha	Homo sapiens	15-32
7213900-3	1981	The interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles was studied as a function of temperature, pH and the molar ratio of phospholipid to protein.	Dimyristoylphosphatidylcholine	42-73	lactalbumin alpha	Homo sapiens	19-36
7213900-9	1981	A kinetic study of the interaction carried out around the transition temperature of dimyristoyl phosphatidylcholine as a function of pH shows that the speed of complex formation between alpha-lactalbumin and the lipid increases from neutral to acidic pH.	Dimyristoylphosphatidylcholine	84-115	lactalbumin alpha	Homo sapiens	186-203
6779866-4	1980	Binary mixtures of dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine at various proportions react maximally with apo A-I at the onset of the phase transition, as judged by comparison with published phase diagrams; in this case also, the rate of recombination was observed to decline for mixtures with higher phase transition temperatures.	Dimyristoylphosphatidylcholine	19-49	apolipoprotein A1	Homo sapiens	129-136
6784753-10	1981	The multiple lipid-protein species formed by apoA-II and DMPC suggest the possible existence of more than one macromolecular spices of lipid and apoA-II in the plasma.	Dimyristoylphosphatidylcholine	57-61	apolipoprotein A2	Homo sapiens	145-152
6784754-0	1981	Thermodynamics of lipid-protein interactions: Interaction of apolipoprotein A-II from human plasma high-density lipoproteins with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	130-160	apolipoprotein A2	Homo sapiens	61-80
7462634-3	1981	We have previously presented a model for CRP-membrane interactions using liposomes composed of dimyristoyl phosphatidylcholine (DMPC), cholesterol (CHOL), stearylamine (SA), and galactosyl ceramide.	Dimyristoylphosphatidylcholine	95-126	C-reactive protein	Homo sapiens	41-44
7462634-3	1981	We have previously presented a model for CRP-membrane interactions using liposomes composed of dimyristoyl phosphatidylcholine (DMPC), cholesterol (CHOL), stearylamine (SA), and galactosyl ceramide.	Dimyristoylphosphatidylcholine	128-132	C-reactive protein	Homo sapiens	41-44
7462634-7	1981	CRP binding to liposomes was dependent on the presence of SA in the membrane and could occur with dimyristoyl phosphatidylethanolamine in place of DMPC.	Dimyristoylphosphatidylcholine	147-151	C-reactive protein	Homo sapiens	0-3
6783071-0	1981	Raman spectroscopy of the thermal properties of reassembled high-density lipoprotein: apolipoprotein A-I complexes of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	118-148	apolipoprotein A1	Homo sapiens	86-104
7437421-0	1980	Interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	38-69	lactalbumin alpha	Homo sapiens	15-32
7437421-4	1980	The enthalpy changes associated with the interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles were measured as a function of the molar ratio of phospholipid to protein, pH and temperature.	Dimyristoylphosphatidylcholine	79-110	lactalbumin alpha	Homo sapiens	56-73
6776110-2	1980	ApoA-II and dimyristoylphosphatidylcholine (DMPC) spontaneously associate to give three different complexes whose structures are determined by the initial reactant concentration and by the reaction temperature with respect to Tc (23.9 degrees C), the gel to liquid crystalline transition temperature of DMPC.	Dimyristoylphosphatidylcholine	303-307	apolipoprotein A2	Homo sapiens	0-7
6768395-2	1980	Incubation at 37 degrees C for 4.5 h of HDL2b with discoidal complexes resulted in a transfer of DMPC from the discoidal complexes to the HDL2b, a release of lipid-free apolipoprotein A-I from the discoidal complexes during such transfer, and a dissociation of some apolipoprotein A-I from the HDL2b surface.	Dimyristoylphosphatidylcholine	97-101	apolipoprotein A1	Homo sapiens	266-284
6257278-8	1980	Upon addition of DMPC multilamellar liposomes to [13C]apoC-I in 1.6 M Gdn-HCl, the line width increased to 4.7 Hz and the T1 decreased to 380 ms.	Dimyristoylphosphatidylcholine	17-21	apolipoprotein C1	Homo sapiens	54-60
6774752-5	1980	Under all incubation conditions the apoprotein A-II associates more readily with cholesterol-DMPC vesicles than apoprotein A-I, as the kinetics are faster and the complex yield larger.	Dimyristoylphosphatidylcholine	93-97	NLR family pyrin domain containing 3	Homo sapiens	47-51
6774752-8	1980	According to these data the apoprotein A-II associates more readily than apoprotein A-I with cholesterol-DMPC vesicles to form protein-rich complexes, whilst the optimal apoprotein A-I-lipid association requires a more disordered lipid structure.	Dimyristoylphosphatidylcholine	105-109	NLR family pyrin domain containing 3	Homo sapiens	39-43
6774755-11	1980	The isolated pigeon apolipoprotein A-I was found bound to the phospholipid (dimyristoyl phosphatidylcholine) and there was no significant conformational change upon lipid binding as judged by CD.	Dimyristoylphosphatidylcholine	76-107	apolipoprotein A1	Homo sapiens	20-38
7356666-2	1980	Complexes of dimyristoyl phosphatidylcholine and human apo A-1.	Dimyristoylphosphatidylcholine	13-44	apolipoprotein A1	Homo sapiens	55-62
7354086-0	1980	Two types of complexes formed by the interaction of apolipoprotein A-I with vesicles of L-alpha-dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	88-126	apolipoprotein A1	Homo sapiens	52-70
7354087-0	1980	Kinetics and mechanism of apolipoprotein A-I interaction with L-alpha-dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	62-100	apolipoprotein A1	Homo sapiens	26-44
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	68-98	apolipoprotein A1	Homo sapiens	22-40
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	68-98	apolipoprotein A1	Homo sapiens	42-49
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	100-104	apolipoprotein A1	Homo sapiens	22-40
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	100-104	apolipoprotein A1	Homo sapiens	42-49
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein A1	Homo sapiens	42-49
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein A1	Homo sapiens	42-49
7354087-1	1980	The dynamics of human apolipoprotein A-I (apo A-I) interaction with dimyristoylphosphatidylcholine (DMPC) vesicles were investigated in a 4000:1 DMPC/apo A-I (mol/mol) mixture where all the protein is bound to DMPC in stable vesicular complexes, and in a 100:1 DMPC/apo A-I (mol/mol) mixture which gives micellar complexes at equilibrium.	Dimyristoylphosphatidylcholine	145-149	apolipoprotein A1	Homo sapiens	42-49
7354087-3	1980	The binding of apo A-I to DMPC vesicles is a very rapid process which takes only a few minutes, while the formation of micellar complexes takes several hours at 25 degrees C and involves saturated complexes of apo A-I .	Dimyristoylphosphatidylcholine	26-30	apolipoprotein A1	Homo sapiens	15-22
456381-4	1979	The transition temperature from gel-crystalline to liquid-crystalline phase in 24 degrees C for the dimyristoyl-phosphatidylcholine vesicles and is shifted to around 30 degrees C in the complexes between phosphatidylcholine and apoA-I, apoA-II, apoC-I, apoC-III proteins while the cooperativity of the transition is decreased.	Dimyristoylphosphatidylcholine	100-131	apolipoprotein A1	Homo sapiens	228-234
227881-7	1979	Emulgen 913, Tween 20, ethylene glycol, myristoyllysophosphatidylcholine, dimyristoylphosphatidylcholine, and phosphatidylethanolamine show the enhanced activity of cholesterol side chain cleavage reaction with cytochrome P-450scc, adrenodoxin, adrenodoxin reductase, and NADPH.	Dimyristoylphosphatidylcholine	74-104	cholesterol side-chain cleavage enzyme, mitochondrial	Bos taurus	211-230
227881-7	1979	Emulgen 913, Tween 20, ethylene glycol, myristoyllysophosphatidylcholine, dimyristoylphosphatidylcholine, and phosphatidylethanolamine show the enhanced activity of cholesterol side chain cleavage reaction with cytochrome P-450scc, adrenodoxin, adrenodoxin reductase, and NADPH.	Dimyristoylphosphatidylcholine	74-104	ferredoxin reductase	Bos taurus	245-266
94790-0	1979	Interaction between DMPC-vesicles and the peripheral protein alpha-lactalbumin [proceedings].	Dimyristoylphosphatidylcholine	20-24	lactalbumin alpha	Homo sapiens	61-78
456381-4	1979	The transition temperature from gel-crystalline to liquid-crystalline phase in 24 degrees C for the dimyristoyl-phosphatidylcholine vesicles and is shifted to around 30 degrees C in the complexes between phosphatidylcholine and apoA-I, apoA-II, apoC-I, apoC-III proteins while the cooperativity of the transition is decreased.	Dimyristoylphosphatidylcholine	100-131	apolipoprotein A2	Homo sapiens	236-243
21089-3	1977	The ionization behaviour of native apoA-I protein is compare to that of its complex with synthetic dimyristoyl lecithin in studies using calorimetric, potentiometric and spectrophotometric titration.	Dimyristoylphosphatidylcholine	99-119	apolipoprotein A1	Homo sapiens	35-41
220964-15	1979	When lipid-replaced enzymes were supplemented with 1,2-ditetradecanoyl-sn-glycero-3-phosphocholine and ubiquinone-10, reduction of cytochrome b was monophasic above the phase-transition temperature of the lipid but biphasic below it.	Dimyristoylphosphatidylcholine	51-98	cytochrome b	Bos taurus	131-143
214114-4	1978	0.1 mol cholesterol/mol dimyristoyl phosphatidylcholine (DMPC) were readily solubilized by apoHDL, apoA-1 or apoA-2.	Dimyristoylphosphatidylcholine	24-55	apolipoprotein A1	Homo sapiens	99-105
214114-4	1978	0.1 mol cholesterol/mol dimyristoyl phosphatidylcholine (DMPC) were readily solubilized by apoHDL, apoA-1 or apoA-2.	Dimyristoylphosphatidylcholine	24-55	apolipoprotein A2	Homo sapiens	109-115
214114-4	1978	0.1 mol cholesterol/mol dimyristoyl phosphatidylcholine (DMPC) were readily solubilized by apoHDL, apoA-1 or apoA-2.	Dimyristoylphosphatidylcholine	57-61	apolipoprotein A1	Homo sapiens	99-105
214114-4	1978	0.1 mol cholesterol/mol dimyristoyl phosphatidylcholine (DMPC) were readily solubilized by apoHDL, apoA-1 or apoA-2.	Dimyristoylphosphatidylcholine	57-61	apolipoprotein A2	Homo sapiens	109-115
214114-10	1978	Differential scanning calorimetry of cholesterol containing recombinants of DMPC/cholesterol/apoHDL or DMPC/cholesterol/apoA-1 showed, with increasing cholesterol content, a linear decrease in the enthalpy of the DMPC gel to liquid crystalline transition, extrapolating to zero enthalpy at 0.15 cholesterol/DMPC.	Dimyristoylphosphatidylcholine	103-107	apolipoprotein A1	Homo sapiens	120-126
214114-10	1978	Differential scanning calorimetry of cholesterol containing recombinants of DMPC/cholesterol/apoHDL or DMPC/cholesterol/apoA-1 showed, with increasing cholesterol content, a linear decrease in the enthalpy of the DMPC gel to liquid crystalline transition, extrapolating to zero enthalpy at 0.15 cholesterol/DMPC.	Dimyristoylphosphatidylcholine	103-107	apolipoprotein A1	Homo sapiens	120-126
214114-10	1978	Differential scanning calorimetry of cholesterol containing recombinants of DMPC/cholesterol/apoHDL or DMPC/cholesterol/apoA-1 showed, with increasing cholesterol content, a linear decrease in the enthalpy of the DMPC gel to liquid crystalline transition, extrapolating to zero enthalpy at 0.15 cholesterol/DMPC.	Dimyristoylphosphatidylcholine	103-107	apolipoprotein A1	Homo sapiens	120-126
20951-1	1977	Myelin basic protein associates with bilayer vesicles of pure egg phosphatidylcholine, L-alpha-dimyristoyl phosphatidylcholine and DL-alpha-dipalmitoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	87-126	myelin basic protein	Homo sapiens	0-20
221020-1	1979	Spin probes differing in the position of their paramagnetic centre are used to quench the fluorescence of pyrene derivatives and chlorophylls incorporated into dimyristoyl phosphatidylcholine membranes.	Dimyristoylphosphatidylcholine	160-191	spindlin 1	Homo sapiens	0-4
282617-0	1978	Rapid conformational changes of cytochrome P-450: effect of dimyristoyl lecithin.	Dimyristoylphosphatidylcholine	60-80	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	32-48
708375-5	1978	Further support for this theory was provided by the study of acetylcholinesterase binding to liposomes containing the phospholipid 1,2-dimyristoyl-sn-glycero-3-phosphocholine.	Dimyristoylphosphatidylcholine	131-174	acetylcholinesterase (Yt blood group)	Sus scrofa	61-81
746357-4	1978	With mixed vesicles of dimyristoyl phosphatidylcholine-cholesterol 20 micrometer of the fragments 32-57, 24-57 and 17-57 stimulated lecithin:cholesterol acyltransferase (LCAT) activity 50, 60, and 100%, respectively, of the value found for apolipoprotein C-I, while fragment 39-57 was inactive.	Dimyristoylphosphatidylcholine	23-54	lecithin-cholesterol acyltransferase	Homo sapiens	132-168
746357-4	1978	With mixed vesicles of dimyristoyl phosphatidylcholine-cholesterol 20 micrometer of the fragments 32-57, 24-57 and 17-57 stimulated lecithin:cholesterol acyltransferase (LCAT) activity 50, 60, and 100%, respectively, of the value found for apolipoprotein C-I, while fragment 39-57 was inactive.	Dimyristoylphosphatidylcholine	23-54	lecithin-cholesterol acyltransferase	Homo sapiens	170-174
21090-2	1977	Potentiometric titration of the native apo-A-II, apoC-I, apoC-III proteins and of their complexes with dimyristoyl lecithin.	Dimyristoylphosphatidylcholine	103-123	apolipoprotein A2	Homo sapiens	39-47
21090-2	1977	Potentiometric titration of the native apo-A-II, apoC-I, apoC-III proteins and of their complexes with dimyristoyl lecithin.	Dimyristoylphosphatidylcholine	103-123	apolipoprotein C1	Homo sapiens	49-55
19081-5	1977	At pH 3.1, the helical content of apoA-I is increased from 48 to 67% on binding to DMPC and the enthalpy of binding was -170 kcal/mol.	Dimyristoylphosphatidylcholine	83-87	apolipoprotein A1	Homo sapiens	34-40
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	107-138	lecithin-cholesterol acyltransferase	Homo sapiens	0-37
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	107-138	lecithin-cholesterol acyltransferase	Homo sapiens	39-43
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	107-138	apolipoprotein A1	Homo sapiens	74-92
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	107-138	apolipoprotein A1	Homo sapiens	94-100
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	140-144	lecithin-cholesterol acyltransferase	Homo sapiens	0-37
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	140-144	lecithin-cholesterol acyltransferase	Homo sapiens	39-43
199582-1	1977	Lecithin: cholesterol acyltransferase (LCAT) was more highly activated by apolipoprotein A-I (apoA-I) with dimyristoyl phosphatidylcholine (DMPC) than with dilinoleoyl phosphatidylcholine (DLPC) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate.	Dimyristoylphosphatidylcholine	140-144	apolipoprotein A1	Homo sapiens	94-100
19081-1	1977	Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	100-131	apolipoprotein A1	Homo sapiens	69-87
19081-1	1977	Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	100-131	apolipoprotein A1	Homo sapiens	89-95
19081-3	1977	At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%).	Dimyristoylphosphatidylcholine	45-76	apolipoprotein A1	Homo sapiens	29-35
19081-3	1977	At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%).	Dimyristoylphosphatidylcholine	78-82	apolipoprotein A1	Homo sapiens	29-35
196775-5	1977	In the electron spin resonance spectra obtained from spin-labeled lysolecithin solutions with various amounts of dimyristoyllecithin, the line width of broad signal arised from micellar spin-labeled lysolecithin broadened as increase of dimyristoyllecithin.	Dimyristoylphosphatidylcholine	113-132	spindlin 1	Homo sapiens	16-20
19081-3	1977	At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%).	Dimyristoylphosphatidylcholine	141-145	apolipoprotein A1	Homo sapiens	29-35
196775-5	1977	In the electron spin resonance spectra obtained from spin-labeled lysolecithin solutions with various amounts of dimyristoyllecithin, the line width of broad signal arised from micellar spin-labeled lysolecithin broadened as increase of dimyristoyllecithin.	Dimyristoylphosphatidylcholine	113-132	spindlin 1	Homo sapiens	53-57
196775-5	1977	In the electron spin resonance spectra obtained from spin-labeled lysolecithin solutions with various amounts of dimyristoyllecithin, the line width of broad signal arised from micellar spin-labeled lysolecithin broadened as increase of dimyristoyllecithin.	Dimyristoylphosphatidylcholine	113-132	spindlin 1	Homo sapiens	53-57
196775-5	1977	In the electron spin resonance spectra obtained from spin-labeled lysolecithin solutions with various amounts of dimyristoyllecithin, the line width of broad signal arised from micellar spin-labeled lysolecithin broadened as increase of dimyristoyllecithin.	Dimyristoylphosphatidylcholine	237-256	spindlin 1	Homo sapiens	16-20
196775-5	1977	In the electron spin resonance spectra obtained from spin-labeled lysolecithin solutions with various amounts of dimyristoyllecithin, the line width of broad signal arised from micellar spin-labeled lysolecithin broadened as increase of dimyristoyllecithin.	Dimyristoylphosphatidylcholine	237-256	spindlin 1	Homo sapiens	53-57
196775-5	1977	In the electron spin resonance spectra obtained from spin-labeled lysolecithin solutions with various amounts of dimyristoyllecithin, the line width of broad signal arised from micellar spin-labeled lysolecithin broadened as increase of dimyristoyllecithin.	Dimyristoylphosphatidylcholine	237-256	spindlin 1	Homo sapiens	53-57
193555-11	1977	The maximal-binding enthalpies of DMPC to apoHDL, apoA-I, and apoA-II were lower for the baboon than for the human apoprotein.	Dimyristoylphosphatidylcholine	34-38	apolipoprotein A-I	Papio anubis	50-56
193555-11	1977	The maximal-binding enthalpies of DMPC to apoHDL, apoA-I, and apoA-II were lower for the baboon than for the human apoprotein.	Dimyristoylphosphatidylcholine	34-38	apolipoprotein A2	Homo sapiens	62-69
193554-0	1977	Physical properties of the dimyristoylphosphatidylcholine vesicle and of complexes formed by its interaction with apolipoprotein C-III.	Dimyristoylphosphatidylcholine	27-57	apolipoprotein C3	Homo sapiens	114-134
191455-1	1977	The major protein components from human and bovine high density serum lipoproteins (apo-A-I proteins) were investigated in their interactions with L-alpha-myristoyl lysophosphatidylcholine and L-alpha-dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	193-232	apolipoprotein A1	Homo sapiens	84-91
192549-2	1977	The enthalpy changes on binding dimyristoyl lecithin and lysolecithin to either the human or the baboon native apoA-I protein were measured in a microcalorimeter.	Dimyristoylphosphatidylcholine	32-52	apolipoprotein A-I	Papio anubis	111-117
192549-7	1977	After preincubation of the apoA-I protein with lysolecithin, the enthalpy changes measured on subsequent binding of dimyristoyl lecithin were shifted towards more exothermal values compared to the curve for the native apoprotein.	Dimyristoylphosphatidylcholine	116-136	apolipoprotein A1	Homo sapiens	27-33
182212-2	1976	The existence of distinct regions of mismatch in molecular packing at the interfaces of the fluid and ordered domains during the phase transition of dimyristoylphosphatidylcholine vesicles has been demonstrated by measuring the temperature dependence of the permeability to a spin-label cation and comparing this with a statistical mechanical calculation of the fraction of interfacial lipid.	Dimyristoylphosphatidylcholine	149-179	spindlin 1	Homo sapiens	276-280
833505-1	1977	We have studied the lipid binding of apoC-III with two types of mixed vesicles of DMPC (dimyristoyl phosphatidylcholine) and DPPC (dipalmitoyl phosphatidyl-choline).	Dimyristoylphosphatidylcholine	82-86	apolipoprotein C3	Homo sapiens	37-45
833505-1	1977	We have studied the lipid binding of apoC-III with two types of mixed vesicles of DMPC (dimyristoyl phosphatidylcholine) and DPPC (dipalmitoyl phosphatidyl-choline).	Dimyristoylphosphatidylcholine	88-119	apolipoprotein C3	Homo sapiens	37-45
833505-4	1977	Combining DMPC:DPPC macroscopic mixtures with apoC-III above the transition temperature, Tc 23 degrees C, of DMPC produces an isolatable complex consisting of 4:1 DMPC:DPPC.	Dimyristoylphosphatidylcholine	109-113	apolipoprotein C3	Homo sapiens	46-54
833505-4	1977	Combining DMPC:DPPC macroscopic mixtures with apoC-III above the transition temperature, Tc 23 degrees C, of DMPC produces an isolatable complex consisting of 4:1 DMPC:DPPC.	Dimyristoylphosphatidylcholine	109-113	apolipoprotein C3	Homo sapiens	46-54
833505-6	1977	Spectral analysis of apoC-III in the presence of the micromixtures reveals a single transition, which occurs between the respective thermal transitions of DMPC (23 degrees C) and DPPC (41 degrees C).	Dimyristoylphosphatidylcholine	155-159	apolipoprotein C3	Homo sapiens	21-29
189808-1	1977	Water-soluble spin labels were used to study dimyristoyllecithin (DML) phospholipid multilayers.	Dimyristoylphosphatidylcholine	45-64	spindlin 1	Homo sapiens	14-18
189808-1	1977	Water-soluble spin labels were used to study dimyristoyllecithin (DML) phospholipid multilayers.	Dimyristoylphosphatidylcholine	66-69	spindlin 1	Homo sapiens	14-18
188642-1	1976	The interaction of synthetic dimyristoyl phosphatidylcholine (lecithin) liposomes with isolated apoC-I and apoC-III proteins from very low density lipoproteins has been studied by microcalorimetry.	Dimyristoylphosphatidylcholine	29-60	apolipoprotein C1	Homo sapiens	96-102
188642-1	1976	The interaction of synthetic dimyristoyl phosphatidylcholine (lecithin) liposomes with isolated apoC-I and apoC-III proteins from very low density lipoproteins has been studied by microcalorimetry.	Dimyristoylphosphatidylcholine	29-60	apolipoprotein C3	Homo sapiens	107-115
33374166-0	2020	DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy.	Dimyristoylphosphatidylcholine	0-4	cystatin C	Homo sapiens	61-71
182205-0	1976	Structure of an apolipoprotein-phospholipid complex: apoC-III induced changes in the physical properties of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	108-138	apolipoprotein C3	Homo sapiens	53-61
182205-1	1976	The effect of ApoC-III, a major apoprotein constituent of human very low density lipoproteins, on the physical properties of dimyristoylphosphatidylcholine (DMPC) vesicles has been studied by magnetic resonance and fluorescence techniques.	Dimyristoylphosphatidylcholine	125-155	apolipoprotein C3	Homo sapiens	14-22
182205-1	1976	The effect of ApoC-III, a major apoprotein constituent of human very low density lipoproteins, on the physical properties of dimyristoylphosphatidylcholine (DMPC) vesicles has been studied by magnetic resonance and fluorescence techniques.	Dimyristoylphosphatidylcholine	157-161	apolipoprotein C3	Homo sapiens	14-22
182205-2	1976	The sharp gel-liquid crystalline transition usually observed at 23 C in DMPC  is both broadened and elevated when ApoC-III is bound as determined (a) from measurements of microscopic viscosity by pyrene excimer fluorescence, (b) from the distribution of di-tert-butyl nitroxide between the bulk aqueous phase and the fluid lipid phase, and (c) from the motion of fatty acyl chains of spin-labeled phosphatdylcholine.	Dimyristoylphosphatidylcholine	72-76	apolipoprotein C3	Homo sapiens	114-122
182205-3	1976	Experiments involving the translocation of ascorbate and charged nitroxide ions and the movement of paramagnetic Eu 3+ ions indicate that when ApoC-III binds to DMPC vesicles, it increases their permeability or destroys their original bilayer structure.	Dimyristoylphosphatidylcholine	161-165	apolipoprotein C3	Homo sapiens	143-151
182205-5	1976	Taken together, the data indicate that ApoC-III binding to DMPC not only decreases the acyl chain motion of individual lipid molecules, but also induces break-down of bilamellar vesicular structure to give significantly smaller complexes.	Dimyristoylphosphatidylcholine	59-63	apolipoprotein C3	Homo sapiens	39-47
1182173-8	1975	A Ca2+- and Mg2+-induced shift in the transition temperature and an increase in the enthalpy change was also observed in a 1:1 mixture of dimyristoyl phosphatidylglycerol and dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	175-206	mucin 7, secreted	Homo sapiens	12-15
1182173-13	1975	The leak of ions from liposomes of a 1:1 mixture of dimyristoyl phosphatidylglycerol and dimyristoyl phosphatidylcholine in the vicinity of the phase transition temperature was considerably less in the presence of Ca2+ than in the presence of Mg2+.	Dimyristoylphosphatidylcholine	89-120	mucin 7, secreted	Homo sapiens	243-246
182250-8	1976	The sequential binding of DMPC to apo AI and apo AII suggests the existence of cooperativity between the two apoproteins in phospholipid binding as apo AII promotes the incorporation of apo AI into a protein-phospholipid complex.	Dimyristoylphosphatidylcholine	26-30	apolipoprotein A1	Homo sapiens	34-40
182250-8	1976	The sequential binding of DMPC to apo AI and apo AII suggests the existence of cooperativity between the two apoproteins in phospholipid binding as apo AII promotes the incorporation of apo AI into a protein-phospholipid complex.	Dimyristoylphosphatidylcholine	26-30	apolipoprotein A2	Homo sapiens	148-155
1125198-2	1975	Dimyristoyllecithin with myristic acid as 2% of the lipid was found to fuse rapidly at temperatures between 17 and 20 degrees, and dimyristoyllecithin with 4% lauric acid was found to fuse rapidly at temperatures between 11 and 15 degrees, while dimyristoyllecithin with 4% palmitic acid did not fuse at an appreciable rate anywhere in the range 17-37 degrees.	Dimyristoylphosphatidylcholine	0-19	Polykaryocytosis inducer	Homo sapiens	71-75
1125198-2	1975	Dimyristoyllecithin with myristic acid as 2% of the lipid was found to fuse rapidly at temperatures between 17 and 20 degrees, and dimyristoyllecithin with 4% lauric acid was found to fuse rapidly at temperatures between 11 and 15 degrees, while dimyristoyllecithin with 4% palmitic acid did not fuse at an appreciable rate anywhere in the range 17-37 degrees.	Dimyristoylphosphatidylcholine	131-150	Polykaryocytosis inducer	Homo sapiens	184-188
1125198-2	1975	Dimyristoyllecithin with myristic acid as 2% of the lipid was found to fuse rapidly at temperatures between 17 and 20 degrees, and dimyristoyllecithin with 4% lauric acid was found to fuse rapidly at temperatures between 11 and 15 degrees, while dimyristoyllecithin with 4% palmitic acid did not fuse at an appreciable rate anywhere in the range 17-37 degrees.	Dimyristoylphosphatidylcholine	131-150	Polykaryocytosis inducer	Homo sapiens	184-188
1138874-8	1975	Although there were some minor differences between phosphatidylglycerol and cardiolipin synthesis, in general, saturated shorter chain CDP-diglycerides (dilauroyl and dimyristoyl) were better substrates than the longer chain dipalmitoyl and distearoyl homologues.	Dimyristoylphosphatidylcholine	167-178	cut-like homeobox 1	Rattus norvegicus	135-138
33195218-4	2020	In order to probe the influence of a peptide, a transmembrane sequence of the transferrin receptor (TFRC) protein, on the dynamics of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) large unilamellar vesicles (LUVs) on a nanosecond time scale, high-resolution QENS experiments and complementary MD simulations have been utilized.	Dimyristoylphosphatidylcholine	134-177	transferrin receptor	Homo sapiens	78-98
32810603-4	2020	Approach We used biophysical and physiological assays of the function of APOA1P A variants, i.e., rHDL formation via dimyristoylphosphatidylcholine (DMPC) microsolubilization, activation of lecithin: cholesterol acyltransferase, cholesterol efflux from human monocyte-derived macrophages (THP-1) to each variant, and comparison of the size and composition of HDL from APOA1-/- mice receiving adeno-associated virus delivery of each human variant.	Dimyristoylphosphatidylcholine	117-147	apolipoprotein A1	Homo sapiens	73-78
32810603-4	2020	Approach We used biophysical and physiological assays of the function of APOA1P A variants, i.e., rHDL formation via dimyristoylphosphatidylcholine (DMPC) microsolubilization, activation of lecithin: cholesterol acyltransferase, cholesterol efflux from human monocyte-derived macrophages (THP-1) to each variant, and comparison of the size and composition of HDL from APOA1-/- mice receiving adeno-associated virus delivery of each human variant.	Dimyristoylphosphatidylcholine	149-153	apolipoprotein A1	Homo sapiens	73-78
32810603-8	2020	CONCLUSION: Studies of DMPC microsolubilization show that proline residues are essential to the optimal interaction of APOA1 with membranes, the initial step in cholesterol efflux and HDL production.	Dimyristoylphosphatidylcholine	23-27	apolipoprotein A-I	Mus musculus	119-124
33195218-4	2020	In order to probe the influence of a peptide, a transmembrane sequence of the transferrin receptor (TFRC) protein, on the dynamics of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) large unilamellar vesicles (LUVs) on a nanosecond time scale, high-resolution QENS experiments and complementary MD simulations have been utilized.	Dimyristoylphosphatidylcholine	134-177	transferrin receptor	Homo sapiens	100-104
33195218-4	2020	In order to probe the influence of a peptide, a transmembrane sequence of the transferrin receptor (TFRC) protein, on the dynamics of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) large unilamellar vesicles (LUVs) on a nanosecond time scale, high-resolution QENS experiments and complementary MD simulations have been utilized.	Dimyristoylphosphatidylcholine	179-183	transferrin receptor	Homo sapiens	78-98
33195218-4	2020	In order to probe the influence of a peptide, a transmembrane sequence of the transferrin receptor (TFRC) protein, on the dynamics of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) large unilamellar vesicles (LUVs) on a nanosecond time scale, high-resolution QENS experiments and complementary MD simulations have been utilized.	Dimyristoylphosphatidylcholine	179-183	transferrin receptor	Homo sapiens	100-104
31913846-5	2020	A reduction in DMPC clearance activity of apoE2 and apoE3 but not apoE4 was observed.	Dimyristoylphosphatidylcholine	15-19	apolipoprotein E	Homo sapiens	42-47
32710882-6	2020	Herein, we used TNAP-harboring proteoliposomes made of either pure dimyristoylphosphatidylcholine (DMPC) or DMPC mixed with either Chol, SM or both of them as MV biomimetic systems to evaluate how the composition modulates the lipid microenvironment and, in turn, TNAP incorporation into the lipid bilayer by means of calorimetry.	Dimyristoylphosphatidylcholine	99-103	TNAP	Homo sapiens	16-20
32710882-6	2020	Herein, we used TNAP-harboring proteoliposomes made of either pure dimyristoylphosphatidylcholine (DMPC) or DMPC mixed with either Chol, SM or both of them as MV biomimetic systems to evaluate how the composition modulates the lipid microenvironment and, in turn, TNAP incorporation into the lipid bilayer by means of calorimetry.	Dimyristoylphosphatidylcholine	108-112	TNAP	Homo sapiens	16-20
32407776-2	2020	The DMPC single bilayer was deposited on the mica surface by Langmuir-Blodgett and Langmuir-Schaefer techniques combined.	Dimyristoylphosphatidylcholine	4-8	MHC class I polypeptide-related sequence A	Homo sapiens	45-49
32222378-5	2020	One day after preparing the DMPC/glucagon lipid bilayer sample, lipid bilayers were disrupted below the phase transition temperature (Tc).	Dimyristoylphosphatidylcholine	28-32	glucagon	Homo sapiens	33-41
32222378-6	2020	Membrane disruption was reduced 2 days after preparation due to the reduction of glucagon-DMPC interaction, and subsequently increased by 4 days and was reduced again by 7 days.	Dimyristoylphosphatidylcholine	90-94	glucagon	Homo sapiens	81-89
31913846-5	2020	A reduction in DMPC clearance activity of apoE2 and apoE3 but not apoE4 was observed.	Dimyristoylphosphatidylcholine	15-19	apolipoprotein E	Homo sapiens	52-57
32223124-3	2020	Here, we show that a dHDL-relevant complex can also be prepared by gently mixing 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and apoA-I or its mutants in ethanol/H2O solutions containing urea in the order of a few molar, and then incubating the mixture at the gel-liquid crystalline phase transition temperature in test tubes.	Dimyristoylphosphatidylcholine	81-124	Hdl	Drosophila melanogaster	21-25
32223124-3	2020	Here, we show that a dHDL-relevant complex can also be prepared by gently mixing 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and apoA-I or its mutants in ethanol/H2O solutions containing urea in the order of a few molar, and then incubating the mixture at the gel-liquid crystalline phase transition temperature in test tubes.	Dimyristoylphosphatidylcholine	126-130	Hdl	Drosophila melanogaster	21-25
31887238-4	2020	We have developed a new experimental triple-resonance NMR technique, which was applied to uniformly doubly ( 15 N,  13 C) labeled Pf1 coat protein in magnetically aligned DMPC/DHPC bicelles.	Dimyristoylphosphatidylcholine	171-175	PHD finger protein 12	Homo sapiens	130-133
31023964-5	2019	The DMPC clearance assay subsequently showed that rHDL protein mixtures could promote DMPC turbidity clearance when more apoA-V was included in the reaction mixtures, with apoAV-rHDL showing the strongest turbidity clearance ability (P<0.05 vs AI-rHDL).	Dimyristoylphosphatidylcholine	4-8	apolipoprotein A5	Homo sapiens	121-127
31339036-5	2019	Using instrumentation to measure the fluorescence anisotropy decay of site specifically labeled 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) Nanodiscs over a wide frequency range, we quantitate the binding of KRAS4b to Nanodiscs containing either 30% phosphatidylserine (PS) or 10% l-alpha-phosphatidylinositol 4,5-bisphosphate by measuring the rotational correlation time of the Nanodisc-KRAS4b complex.	Dimyristoylphosphatidylcholine	141-145	KRAS proto-oncogene, GTPase	Homo sapiens	215-221
31339036-5	2019	Using instrumentation to measure the fluorescence anisotropy decay of site specifically labeled 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) Nanodiscs over a wide frequency range, we quantitate the binding of KRAS4b to Nanodiscs containing either 30% phosphatidylserine (PS) or 10% l-alpha-phosphatidylinositol 4,5-bisphosphate by measuring the rotational correlation time of the Nanodisc-KRAS4b complex.	Dimyristoylphosphatidylcholine	141-145	KRAS proto-oncogene, GTPase	Homo sapiens	395-401
31448595-2	2019	The NMR results in combination with molecular dynamics simulations revealed that the PGP-Me chain appeared to exhibit behavior different from that of typical membrane lipids such as dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	182-212	phosphoglycolate phosphatase	Homo sapiens	85-88
31448595-2	2019	The NMR results in combination with molecular dynamics simulations revealed that the PGP-Me chain appeared to exhibit behavior different from that of typical membrane lipids such as dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	214-218	phosphoglycolate phosphatase	Homo sapiens	85-88
31023964-5	2019	The DMPC clearance assay subsequently showed that rHDL protein mixtures could promote DMPC turbidity clearance when more apoA-V was included in the reaction mixtures, with apoAV-rHDL showing the strongest turbidity clearance ability (P<0.05 vs AI-rHDL).	Dimyristoylphosphatidylcholine	86-90	apolipoprotein A5	Homo sapiens	121-127
31023964-5	2019	The DMPC clearance assay subsequently showed that rHDL protein mixtures could promote DMPC turbidity clearance when more apoA-V was included in the reaction mixtures, with apoAV-rHDL showing the strongest turbidity clearance ability (P<0.05 vs AI-rHDL).	Dimyristoylphosphatidylcholine	86-90	apolipoprotein A5	Homo sapiens	172-177
30976055-0	2019	Methionine Oxidation Changes the Mechanism of Abeta Peptide Binding to the DMPC Bilayer.	Dimyristoylphosphatidylcholine	75-79	amyloid beta precursor protein	Homo sapiens	46-51
31010668-4	2019	Our results indicate that bilayers composed of various lipids (DMPC, DPPC, and DSPC) with different thicknesses result in different orientations of the DCD oligomer when embedded in lipid bilayers.	Dimyristoylphosphatidylcholine	63-67	dermcidin	Homo sapiens	152-155
30976055-6	2019	Third, oxidation "polarizes" Abeta binding to the DMPC bilayer by strengthening the interactions of the C-terminus with lipids while largely releasing the rest of the peptide from bilayer.	Dimyristoylphosphatidylcholine	50-54	amyloid beta precursor protein	Homo sapiens	29-34
30976055-9	2019	Fifth, methionine oxidation reduces the affinity of Abeta binding to the DMPC bilayer by disrupting favorable intrapeptide interactions upon binding, which offset the gains from better hydration.	Dimyristoylphosphatidylcholine	73-77	amyloid beta precursor protein	Homo sapiens	52-57
30777306-0	2019	Methanol Accelerates DMPC Flip-Flop and Transfer: A SANS Study on Lipid Dynamics.	Dimyristoylphosphatidylcholine	21-25	USH1 protein network component sans	Homo sapiens	52-56
30156415-3	2018	First, the DMPC/PSM/cholesterol bilayer features favorable interactions of cholesterol with DMPC and, particularly, PSM lipids, which are supported by hydrogen bonds.	Dimyristoylphosphatidylcholine	11-15	folate hydrolase 1	Homo sapiens	16-19
30156415-3	2018	First, the DMPC/PSM/cholesterol bilayer features favorable interactions of cholesterol with DMPC and, particularly, PSM lipids, which are supported by hydrogen bonds.	Dimyristoylphosphatidylcholine	92-96	folate hydrolase 1	Homo sapiens	16-19
30156415-3	2018	First, the DMPC/PSM/cholesterol bilayer features favorable interactions of cholesterol with DMPC and, particularly, PSM lipids, which are supported by hydrogen bonds.	Dimyristoylphosphatidylcholine	11-15	folate hydrolase 1	Homo sapiens	116-119
30187138-4	2018	In this work, we therefore employed molecular dynamics (MD) simulations to investigate the binding mechanisms of HD5 on LPS in comparison to a bare DMPC lipid membrane.	Dimyristoylphosphatidylcholine	148-152	defensin alpha 5	Homo sapiens	113-116
29401436-1	2018	A membrane-bound form of Pf1 coat protein reconstituted in magnetically aligned DMPC/DHPC bicelles was used as a molecular probe to quantify for the viscosity of the lipid membrane interior by measuring the uniaxial rotational diffusion coefficient of the protein.	Dimyristoylphosphatidylcholine	80-84	PHD finger protein 12	Homo sapiens	25-28
29274874-4	2018	We demonstrate the efficacy of this method for a small membrane protein, sarcolipin, reconstituted in DMPC/POPC/DHPC oriented bicelles.	Dimyristoylphosphatidylcholine	102-106	sarcolipin	Homo sapiens	73-83
28737894-4	2017	Negatively charged, lipid (DMPC) stabilized AuNRs inhibit the formation of fibrils due to selective binding to the positevly charged amyloidogenic sequence of Abeta protein.	Dimyristoylphosphatidylcholine	27-31	amyloid beta precursor protein	Homo sapiens	159-164
28847504-4	2017	2) Most strikingly, while WT-PFN1 only weakly interacts with DMPC/DHPC bicelle without altering the native structure, C71G-PFN1 acquires abnormal capacity in strongly interacting with DMPC/DHPC bicelle and DPC micelle, energetically driven by transforming the highly disordered unfolded state into a non-native helical structure, similar to what has been previously observed on ALS-causing SOD1 mutants.	Dimyristoylphosphatidylcholine	61-65	profilin 1	Homo sapiens	29-33
28847504-4	2017	2) Most strikingly, while WT-PFN1 only weakly interacts with DMPC/DHPC bicelle without altering the native structure, C71G-PFN1 acquires abnormal capacity in strongly interacting with DMPC/DHPC bicelle and DPC micelle, energetically driven by transforming the highly disordered unfolded state into a non-native helical structure, similar to what has been previously observed on ALS-causing SOD1 mutants.	Dimyristoylphosphatidylcholine	184-188	profilin 1	Homo sapiens	123-127
29121535-6	2018	X-ray diffraction studies on DMPC and DMPE showed that none of these complexes interacted with DMPE and only Cu-L1 interacted with DMPC.	Dimyristoylphosphatidylcholine	131-135	cullin 1	Homo sapiens	109-114
29121535-7	2018	This difference was explained by the fact that Cu-L1Me complex is more voluminous than Cu-L1 because it has two additional methyl groups; on the other hand, DMPC molecule has three methyl groups in its bulky terminal amino end.	Dimyristoylphosphatidylcholine	157-161	cullin 1	Homo sapiens	47-52
28644829-10	2017	As expected, DMPC/apoAI-NT/apoE-CT discoidal particles did not elicit LDLr binding ability, and promoted SR-B1 mediated cellular uptake of lipids to a limited extent.	Dimyristoylphosphatidylcholine	13-17	scavenger receptor class B member 1	Homo sapiens	105-110
28303107-10	2017	The distribution of the inter-phosphate and hydrophobic thicknesses showed that stretching of the DMPC annular layer around AQP0 surface is the mechanism that compensates the hydrophobic mismatch in this system.	Dimyristoylphosphatidylcholine	98-102	major intrinsic protein of lens fiber	Homo sapiens	124-128
28351228-5	2017	However, Wnt3A activity was preserved or enhanced in PEGylated 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) liposomes but not in PEGylated 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) liposomes.	Dimyristoylphosphatidylcholine	187-191	Wnt family member 3A	Homo sapiens	9-14
28476091-4	2017	The MD simulations show that SPF is inserted spontaneously in a transmembrane orientation in both 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayers resulting in thinning of the bilayers near the peptides, which drives the peptide aggregation.	Dimyristoylphosphatidylcholine	98-141	SEC14 like lipid binding 2	Homo sapiens	29-32
28387359-1	2017	The expression, functional reconstitution and first NMR characterization of the human growth hormone secretagogue (GHS) receptor reconstituted into either DMPC or POPC membranes is described.	Dimyristoylphosphatidylcholine	155-159	growth hormone secretagogue receptor	Homo sapiens	86-128
28303107-3	2017	EC and room-temperature molecular dynamics (MD) of dimyristoylglycerophosphocholine (DMPC) annular lipids around AQP0 show similarities, however, crystal-packing and temperature might affect the protein surface or the lipids distribution.	Dimyristoylphosphatidylcholine	51-83	major intrinsic protein of lens fiber	Homo sapiens	113-117
27782404-6	2016	Melting temperatures (Tm), heat capacities (DeltaCp), and calorimetric enthalpies (DeltaHcal) for denaturation of CYP3A4 each increased with an increasing fraction of DMPC, with a maximum at 50% DMPC, before decreasing at 75% DMPC.	Dimyristoylphosphatidylcholine	167-171	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	114-120
28303107-3	2017	EC and room-temperature molecular dynamics (MD) of dimyristoylglycerophosphocholine (DMPC) annular lipids around AQP0 show similarities, however, crystal-packing and temperature might affect the protein surface or the lipids distribution.	Dimyristoylphosphatidylcholine	85-89	major intrinsic protein of lens fiber	Homo sapiens	113-117
27782404-6	2016	Melting temperatures (Tm), heat capacities (DeltaCp), and calorimetric enthalpies (DeltaHcal) for denaturation of CYP3A4 each increased with an increasing fraction of DMPC, with a maximum at 50% DMPC, before decreasing at 75% DMPC.	Dimyristoylphosphatidylcholine	195-199	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	114-120
27782404-6	2016	Melting temperatures (Tm), heat capacities (DeltaCp), and calorimetric enthalpies (DeltaHcal) for denaturation of CYP3A4 each increased with an increasing fraction of DMPC, with a maximum at 50% DMPC, before decreasing at 75% DMPC.	Dimyristoylphosphatidylcholine	195-199	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	114-120
27529357-1	2016	Apolipoprotein C-III (ApoC-III) is found on high-density lipoproteins (HDLs) and remodels 1,2-dimyristoyl-sn-glycero-3-phosphocholine vesicles into HDL-like particles known as nanodiscs.	Dimyristoylphosphatidylcholine	90-133	apolipoprotein C3	Homo sapiens	0-20
27529357-1	2016	Apolipoprotein C-III (ApoC-III) is found on high-density lipoproteins (HDLs) and remodels 1,2-dimyristoyl-sn-glycero-3-phosphocholine vesicles into HDL-like particles known as nanodiscs.	Dimyristoylphosphatidylcholine	90-133	apolipoprotein C3	Homo sapiens	22-30
26829620-3	2016	The results of the spectroscopic measurements showed that the tilt angle of acyl chains obtained for deuterated DMPC bilayers supported on the beta-Tg-modified gold is significantly lower than that reported previously for DMPC bilayers deposited directly on Au(111) electrodes.	Dimyristoylphosphatidylcholine	112-116	pro-platelet basic protein	Homo sapiens	143-150
27493032-7	2016	The DMPC surface density was quantified from the relative Raman scattering intensities of C18 and phospholipid acyl chains and found to be ~40% of a DMPC vesicle membrane.	Dimyristoylphosphatidylcholine	4-8	Bardet-Biedl syndrome 9	Homo sapiens	90-93
26822505-5	2016	As a result, Abeta adsorbed along the localized DMPC lipid on the mixture lipid membranes, whereas it was adsorbed homogeneously on the pure DMPC and beta-CG membranes.	Dimyristoylphosphatidylcholine	48-52	amyloid beta precursor protein	Homo sapiens	13-18
26822505-6	2016	Moreover, amino acid fragments that mainly existed in the n-terminal of Abeta (1-40) peptide were strongly detected on the localized DMPC region.	Dimyristoylphosphatidylcholine	133-137	amyloid beta precursor protein	Homo sapiens	72-77
26947182-5	2016	(1) Binding to the DMPS bilayer triggers the formation of stable helix in the Abeta C-terminal, although the helix-inducing effect caused by DMPS lipids is weaker than that of DMPC.	Dimyristoylphosphatidylcholine	176-180	amyloid beta precursor protein	Homo sapiens	78-83
26947182-6	2016	(2) Compared to the DMPC-bound Abeta monomer, the anionic bilayer weakens intrapeptide interactions, particularly, formed by charged amino acids.	Dimyristoylphosphatidylcholine	20-24	amyloid beta precursor protein	Homo sapiens	31-36
26947182-8	2016	In contrast, these interactions play minor role in Abeta binding to the DMPC bilayer.	Dimyristoylphosphatidylcholine	72-76	amyloid beta precursor protein	Homo sapiens	51-56
26947182-10	2016	The opposite scenario applies to Abeta binding to the DMPC bilayer.	Dimyristoylphosphatidylcholine	54-58	amyloid beta precursor protein	Homo sapiens	33-38
26829620-4	2016	Moreover, tilt angles of ~18  were obtained for d54-DMPC bilayers on beta-Tg self-assembled monolayers (SAMs) at positive potentials, which are similar to the values calculated for h-DMPC deposited on bare gold in the desorbed state and to those observed for a stack of hydrated DMPC bilayers.	Dimyristoylphosphatidylcholine	52-56	pro-platelet basic protein	Homo sapiens	69-76
25634301-4	2015	Here we report an essential step toward that goal: extensive assignments of backbone and side chain resonances for VDAC in DMPC lipid bilayers via magic angle spinning nuclear magnetic resonance (MAS NMR).	Dimyristoylphosphatidylcholine	123-127	voltage dependent anion channel 1	Homo sapiens	115-119
27081463-9	2016	Moreover, the highest level of IFN- gamma and IL-4 was observed in the splenocytes of mice immunized with ISCOMATRIX DMPC or ISCOMATRIX DSPC, respectively.	Dimyristoylphosphatidylcholine	117-121	interferon gamma	Mus musculus	31-41
27081463-9	2016	Moreover, the highest level of IFN- gamma and IL-4 was observed in the splenocytes of mice immunized with ISCOMATRIX DMPC or ISCOMATRIX DSPC, respectively.	Dimyristoylphosphatidylcholine	117-121	interleukin 4	Mus musculus	46-50
27081463-11	2016	However, our results indicated that ISCOMATRIX EPC, DMPC or DSPC generated a mixed Th1/Th2 response that was not protective.	Dimyristoylphosphatidylcholine	52-56	negative elongation factor complex member C/D, Th1l	Mus musculus	83-86
26074009-3	2015	Here, a small-angle neutron scattering study of the interaction of melittin with lipid bilayers made of mixtures of dimyristoylphosphatidylcholine (DMPC) and cholesterol (Chol) is presented.	Dimyristoylphosphatidylcholine	116-146	melittin	Apis mellifera	67-75
26074009-3	2015	Here, a small-angle neutron scattering study of the interaction of melittin with lipid bilayers made of mixtures of dimyristoylphosphatidylcholine (DMPC) and cholesterol (Chol) is presented.	Dimyristoylphosphatidylcholine	148-152	melittin	Apis mellifera	67-75
26181234-6	2015	We find that DMPC/DHPC bicelles dramatically increase the thermal stability of the rhodopsin mutants G90V and N55K.	Dimyristoylphosphatidylcholine	13-17	rhodopsin	Homo sapiens	83-92
25863059-1	2015	Diacylglycerol (DAG)-induced activation of phosphatidylinositol-phospholipase C (PI-PLC) was studied with vesicles containing PI, either pure or in mixtures with dimyristoyl phosphatidylcholine, distearoyl phosphatidylcholine, sphingomyelin, or galactosylceramide, used as substrates.	Dimyristoylphosphatidylcholine	162-193	phospholipase C gamma 1	Homo sapiens	81-87
25634301-5	2015	VDAC reconstituted into DMPC lipid bilayers spontaneously forms two-dimensional lipid crystals, showing remarkable spectral resolution (0.5-0.3 ppm for (13)C line widths and <0.5 ppm (15)N line widths at 750 MHz).	Dimyristoylphosphatidylcholine	24-28	voltage dependent anion channel 1	Homo sapiens	0-4
25634301-10	2015	The reported assignments allow us to compare predicted torsion angles for VDAC prepared in DMPC 2D lipid crystals, DMPC liposomes, and LDAO-solubilized samples to address the possible effects of the membrane mimetic environment on the conformation of the protein.	Dimyristoylphosphatidylcholine	91-95	voltage dependent anion channel 1	Homo sapiens	74-78
24915638-8	2014	Triton X-100 imparts correct geometrical space during sPLA2 catalyzing DMPC, releasing lysophospholipid and acidic myristoyl acid, which in turn alters the hydrophobic environment prevailing around ANS-DMPC, which leads to weakening of the electrostatic ion pair interaction between DMPC and ANS ensuing decrease in fluorescence.	Dimyristoylphosphatidylcholine	71-75	phospholipase A2 group X	Homo sapiens	54-59
25037005-6	2014	Therefore, we conclude that Abeta monomer bound to the DMPC bilayer fails to perturb the bilayer structure in both leaflets.	Dimyristoylphosphatidylcholine	55-59	amyloid beta precursor protein	Homo sapiens	28-33
25037005-7	2014	Limited scope of structural perturbations in the DMPC bilayer caused by Abeta monomer may constitute the molecular basis of its low cytotoxicity.	Dimyristoylphosphatidylcholine	49-53	amyloid beta precursor protein	Homo sapiens	72-77
25037005-0	2014	Binding of Abeta peptide creates lipid density depression in DMPC bilayer.	Dimyristoylphosphatidylcholine	61-65	amyloid beta precursor protein	Homo sapiens	11-16
25037005-1	2014	Using isobaric-isothermal replica exchange molecular dynamics and all-atom explicit water model we study the impact of Abeta monomer binding on the equilibrium properties of DMPC bilayer.	Dimyristoylphosphatidylcholine	174-178	amyloid beta precursor protein	Homo sapiens	119-124
24915638-8	2014	Triton X-100 imparts correct geometrical space during sPLA2 catalyzing DMPC, releasing lysophospholipid and acidic myristoyl acid, which in turn alters the hydrophobic environment prevailing around ANS-DMPC, which leads to weakening of the electrostatic ion pair interaction between DMPC and ANS ensuing decrease in fluorescence.	Dimyristoylphosphatidylcholine	202-206	phospholipase A2 group X	Homo sapiens	54-59
24915638-8	2014	Triton X-100 imparts correct geometrical space during sPLA2 catalyzing DMPC, releasing lysophospholipid and acidic myristoyl acid, which in turn alters the hydrophobic environment prevailing around ANS-DMPC, which leads to weakening of the electrostatic ion pair interaction between DMPC and ANS ensuing decrease in fluorescence.	Dimyristoylphosphatidylcholine	202-206	phospholipase A2 group X	Homo sapiens	54-59
24915638-9	2014	These characteristic fluorescence changes between DMPC and ANS in response to sPLA2 catalysis are well documented and validated in this study.	Dimyristoylphosphatidylcholine	50-54	phospholipase A2 group X	Homo sapiens	78-83
24840721-2	2014	In the present study, ND were assembled from apolipoprotein A-I, the zwitterionic glycerophospholipid 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), and the synthetic cationic lipid 1,2-dimyristoyl-3-trimethylammonium-propane (DMTAP).	Dimyristoylphosphatidylcholine	147-151	apolipoprotein A1	Homo sapiens	45-63
25098179-3	2014	By combining two structurally sensitive optical methods, circular dichroism (CD) and deep-ultraviolet resonance Raman spectroscopy (dUVRR), we have identified distinct structural fluctuations in melittin correlated with increased and decreased 1,2-dimyristoyl-sn-glycero-3-phosphocholine bilayer fluidities.	Dimyristoylphosphatidylcholine	244-287	melittin	Apis mellifera	195-203
24526609-6	2014	A kinetic study using dimyristoyl phosphatidylcholine (DMPC) liposomes indicated that N-Hcy-apoA-I showed increased lipid-binding activity compared to wild-type apoA-I.	Dimyristoylphosphatidylcholine	22-53	apolipoprotein A1	Homo sapiens	92-98
24526609-6	2014	A kinetic study using dimyristoyl phosphatidylcholine (DMPC) liposomes indicated that N-Hcy-apoA-I showed increased lipid-binding activity compared to wild-type apoA-I.	Dimyristoylphosphatidylcholine	55-59	apolipoprotein A1	Homo sapiens	92-98
23895253-8	2014	Only salivary SOD and GR activities were significantly different in the CP and DMCP groups.	Dimyristoylphosphatidylcholine	79-83	glutathione-disulfide reductase	Homo sapiens	22-24
24530897-3	2014	P45 peptide showed lower surface activity and less extent of penetration into 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dimyristoyl-sn-glycero-3-phospho-L-serine (DMPS) (3:2, mol/mol) lipid monolayers than P58 and P59.	Dimyristoylphosphatidylcholine	78-121	nuclear factor, erythroid 2	Homo sapiens	0-3
24530897-3	2014	P45 peptide showed lower surface activity and less extent of penetration into 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dimyristoyl-sn-glycero-3-phospho-L-serine (DMPS) (3:2, mol/mol) lipid monolayers than P58 and P59.	Dimyristoylphosphatidylcholine	123-127	nuclear factor, erythroid 2	Homo sapiens	0-3
24655512-4	2014	This work aims to characterize the structure and dynamics of caveolin-1 (D82-S136; Cav182-136) in a DMPC bilayer using NMR, fluorescence emission measurements, and molecular dynamics simulations.	Dimyristoylphosphatidylcholine	100-104	caveolin 1	Homo sapiens	61-71
24623336-2	2014	The molecular mobility of the human neuropeptide Y receptor type 2 reconstituted into dimyristoylphosphatidylcholine (DMPC) membranes was investigated by means of solid-state NMR spectroscopy.	Dimyristoylphosphatidylcholine	86-116	neuropeptide Y receptor Y2	Homo sapiens	36-66
24623336-2	2014	The molecular mobility of the human neuropeptide Y receptor type 2 reconstituted into dimyristoylphosphatidylcholine (DMPC) membranes was investigated by means of solid-state NMR spectroscopy.	Dimyristoylphosphatidylcholine	118-122	neuropeptide Y receptor Y2	Homo sapiens	36-66
24299979-2	2014	In present work, we investigated the secondary structure and topology of the peptides associated to Slc11a1-TM2, TM3 and TM4 (wildtype peptides and function-relating mutants) in the phospholipid vesicles (DMPC, DMPG and their mixtures) using circular dichroism, fluorescence spectroscopy and differential scanning calorimetry.	Dimyristoylphosphatidylcholine	205-209	solute carrier family 11 member 1	Homo sapiens	100-107
24299979-6	2014	The E139A substitution of TM3 significantly impairs the pH dependence of the buried depth of TM3 and causes a pronounced increase in helicity in all DMPG-containing lipid vesicles at pH 5.5 and 7 and in DMPC at pH 4.	Dimyristoylphosphatidylcholine	203-207	tropomyosin 3	Homo sapiens	26-29
24296790-8	2014	Incorporation of Cum-Chl into the dimyristoylphosphatidylcholine (DMPC) lipid bilayer membrane results in a significant enhancement of monomeric fluorescence intensity.	Dimyristoylphosphatidylcholine	34-64	chordin like 1	Homo sapiens	21-24
24822411-5	2014	The DSC showed further results that the strong effects of ginsenoside Rb1 and Rh2 on DMPC, which both have obviously reduced the DMPC molecular phase transition temperature, thus increasing the fluidity of bilayers.	Dimyristoylphosphatidylcholine	85-89	RB transcriptional corepressor 1	Homo sapiens	70-73
24822411-5	2014	The DSC showed further results that the strong effects of ginsenoside Rb1 and Rh2 on DMPC, which both have obviously reduced the DMPC molecular phase transition temperature, thus increasing the fluidity of bilayers.	Dimyristoylphosphatidylcholine	85-89	Rh associated glycoprotein	Homo sapiens	78-81
24822411-5	2014	The DSC showed further results that the strong effects of ginsenoside Rb1 and Rh2 on DMPC, which both have obviously reduced the DMPC molecular phase transition temperature, thus increasing the fluidity of bilayers.	Dimyristoylphosphatidylcholine	129-133	RB transcriptional corepressor 1	Homo sapiens	70-73
24822411-5	2014	The DSC showed further results that the strong effects of ginsenoside Rb1 and Rh2 on DMPC, which both have obviously reduced the DMPC molecular phase transition temperature, thus increasing the fluidity of bilayers.	Dimyristoylphosphatidylcholine	129-133	Rh associated glycoprotein	Homo sapiens	78-81
24355622-4	2014	Here, free radicals 5-DOXYL stearic acid, TEMPOL, and CAT-1 were added to uniformly (15)N-labeled Pf1 coat protein reconstituted in DMPC/DHPC bicelles, and their effect on the longitudinal relaxation times (T1Z) was investigated.	Dimyristoylphosphatidylcholine	132-136	PHD finger protein 12	Homo sapiens	98-101
24296790-8	2014	Incorporation of Cum-Chl into the dimyristoylphosphatidylcholine (DMPC) lipid bilayer membrane results in a significant enhancement of monomeric fluorescence intensity.	Dimyristoylphosphatidylcholine	66-70	chordin like 1	Homo sapiens	21-24
24201377-4	2014	We compared the apoA-I configuration in D-HDL reconstituted with dimyristoylphosphatidylcholine by both procedures using fluorescence resonance energy transfer measurements with apoA-I tryptophan mutants and fluorescently labeled cysteine mutants.	Dimyristoylphosphatidylcholine	65-95	apolipoprotein A1	Homo sapiens	16-22
25323428-1	2014	BACKGROUND: The aim of this study was to investigate the association between the dialysate MCP-1 (dMCP-1) and systemic inflammatory and nutritional markers in peritoneal dialysis (PD) patients.	Dimyristoylphosphatidylcholine	98-102	C-C motif chemokine ligand 2	Homo sapiens	91-96
23349207-2	2013	The overall shape of both particles is discoidal with the low-resolution structure of apoA1 visualized as an open, contorted, and out of plane conformation with three arms in nascent HDL/dimyristoyl phosphatidylcholine without cholesterol (nHDL(DMPC)) and two arms in nascent HDL/dimyristoyl phosphatidylcholine with cholesterol (nHDL(DMPC+Chol)).	Dimyristoylphosphatidylcholine	187-218	apolipoprotein A1	Homo sapiens	86-91
23584361-4	2013	The presence of the surfactant caused changes in the temperature of the DMPC phase transition, as revealed using FTIR and DRS measurements.	Dimyristoylphosphatidylcholine	72-76	sushi repeat containing protein X-linked	Homo sapiens	122-125
23721456-3	2013	DSC studies reveal multiple phases or domains that can be classified as virtual DMPC, which contains a small amount of DMPC that slightly reduces the melting temperature (Tm), a boundary phase that is adjacent to the apo A-I or apo A-II that circumscribes the discoidal rHDL, and a mixed FC/DMPC phase that has a Tm that increases with FC mole percent.	Dimyristoylphosphatidylcholine	80-84	apolipoprotein A1	Homo sapiens	217-224
23721456-3	2013	DSC studies reveal multiple phases or domains that can be classified as virtual DMPC, which contains a small amount of DMPC that slightly reduces the melting temperature (Tm), a boundary phase that is adjacent to the apo A-I or apo A-II that circumscribes the discoidal rHDL, and a mixed FC/DMPC phase that has a Tm that increases with FC mole percent.	Dimyristoylphosphatidylcholine	80-84	apolipoprotein A2	Homo sapiens	228-236
23721456-6	2013	For rHDL (apo A-II) compared to rHDL (apo A-I), this occurs in spite of the reduced number of helical regions that mediate binding to the DMPC surface.	Dimyristoylphosphatidylcholine	138-142	apolipoprotein A2	Homo sapiens	10-18
23721456-6	2013	For rHDL (apo A-II) compared to rHDL (apo A-I), this occurs in spite of the reduced number of helical regions that mediate binding to the DMPC surface.	Dimyristoylphosphatidylcholine	138-142	apolipoprotein A1	Homo sapiens	10-17
23721456-7	2013	This effect is attributed to the very high lipophilicity of apo A-II and the reduction in the polarity of the interface between DMPC and the aqueous phase with an increasing FC mole percent, an effect that is expected to increase the strength of the hydrophobic associations with the nonpolar face of the amphipathic helices of apo A-II.	Dimyristoylphosphatidylcholine	128-132	apolipoprotein A2	Homo sapiens	328-336
23969702-4	2013	Bovine apoA-I showed the weakest binding ability of dimyristoyl phosphatidylcholine; however, bovine apoA-I formed slightly larger reconstituted HDL (rHDL) particles with palmitoyl oleoyl phosphatidylcholine, with a higher number of apoA-I-containing particles.	Dimyristoylphosphatidylcholine	52-83	APOAI	Bos taurus	7-13
23969702-4	2013	Bovine apoA-I showed the weakest binding ability of dimyristoyl phosphatidylcholine; however, bovine apoA-I formed slightly larger reconstituted HDL (rHDL) particles with palmitoyl oleoyl phosphatidylcholine, with a higher number of apoA-I-containing particles.	Dimyristoylphosphatidylcholine	52-83	APOAI	Bos taurus	101-107
23969702-4	2013	Bovine apoA-I showed the weakest binding ability of dimyristoyl phosphatidylcholine; however, bovine apoA-I formed slightly larger reconstituted HDL (rHDL) particles with palmitoyl oleoyl phosphatidylcholine, with a higher number of apoA-I-containing particles.	Dimyristoylphosphatidylcholine	52-83	APOAI	Bos taurus	101-107
23349207-2	2013	The overall shape of both particles is discoidal with the low-resolution structure of apoA1 visualized as an open, contorted, and out of plane conformation with three arms in nascent HDL/dimyristoyl phosphatidylcholine without cholesterol (nHDL(DMPC)) and two arms in nascent HDL/dimyristoyl phosphatidylcholine with cholesterol (nHDL(DMPC+Chol)).	Dimyristoylphosphatidylcholine	245-249	apolipoprotein A1	Homo sapiens	86-91
23349207-2	2013	The overall shape of both particles is discoidal with the low-resolution structure of apoA1 visualized as an open, contorted, and out of plane conformation with three arms in nascent HDL/dimyristoyl phosphatidylcholine without cholesterol (nHDL(DMPC)) and two arms in nascent HDL/dimyristoyl phosphatidylcholine with cholesterol (nHDL(DMPC+Chol)).	Dimyristoylphosphatidylcholine	335-339	apolipoprotein A1	Homo sapiens	86-91
23349207-4	2013	Modeling studies indicate that apoA1 is folded onto itself in nHDL(DMPC), making a large hairpin, which was also confirmed independently by both cross-linking mass spectrometry and hydrogen-deuterium exchange (HDX) mass spectrometry analyses.	Dimyristoylphosphatidylcholine	67-71	apolipoprotein A1	Homo sapiens	31-36
23053007-1	2013	Using implicit solvent atomistic model and replica exchange molecular dynamics, we study binding of Abeta monomer to zwitterionic dimyristoylphosphatidylcholine (DMPC) lipid monolayer.	Dimyristoylphosphatidylcholine	162-166	amyloid beta precursor protein	Homo sapiens	100-105
23042146-1	2013	All-atom simulations are carried out on ErbB1/B2 and EphA1 transmembrane helix dimers in lipid bilayers starting from their solution/DMPC bicelle NMR structures.	Dimyristoylphosphatidylcholine	133-137	epidermal growth factor receptor	Homo sapiens	40-48
23042146-1	2013	All-atom simulations are carried out on ErbB1/B2 and EphA1 transmembrane helix dimers in lipid bilayers starting from their solution/DMPC bicelle NMR structures.	Dimyristoylphosphatidylcholine	133-137	EPH receptor A1	Homo sapiens	53-58
23053007-4	2013	We show that binding to the DMPC monolayer causes a dramatic conformational transition in Abeta monomer, resulting in chain extension, loss of intrapeptide interactions, and formation of beta-structure.	Dimyristoylphosphatidylcholine	28-32	amyloid beta precursor protein	Homo sapiens	90-95
23103361-8	2013	Rat apoE converts DMPC vesicles to smaller DMPC/apoE complexes with a first order rate constant of 0.12 min(-1).	Dimyristoylphosphatidylcholine	18-22	apolipoprotein E	Rattus norvegicus	4-8
23261466-3	2013	Based on our earlier study demonstrating that apoA-I mimetic peptide 4F forms discoidal complex with 1,2-dimyristoyl-sn-glycero-3-phosphocholine, we hypothesized that lipid complexes of 4F would be able to bind PON1 and enhance its activity and stability.	Dimyristoylphosphatidylcholine	101-144	apolipoprotein A1	Homo sapiens	46-52
23261466-3	2013	Based on our earlier study demonstrating that apoA-I mimetic peptide 4F forms discoidal complex with 1,2-dimyristoyl-sn-glycero-3-phosphocholine, we hypothesized that lipid complexes of 4F would be able to bind PON1 and enhance its activity and stability.	Dimyristoylphosphatidylcholine	101-144	paraoxonase 1	Homo sapiens	211-215
23103361-8	2013	Rat apoE converts DMPC vesicles to smaller DMPC/apoE complexes with a first order rate constant of 0.12 min(-1).	Dimyristoylphosphatidylcholine	18-22	apolipoprotein E	Rattus norvegicus	48-52
23103361-8	2013	Rat apoE converts DMPC vesicles to smaller DMPC/apoE complexes with a first order rate constant of 0.12 min(-1).	Dimyristoylphosphatidylcholine	43-47	apolipoprotein E	Rattus norvegicus	4-8
23103361-8	2013	Rat apoE converts DMPC vesicles to smaller DMPC/apoE complexes with a first order rate constant of 0.12 min(-1).	Dimyristoylphosphatidylcholine	43-47	apolipoprotein E	Rattus norvegicus	48-52
23025327-5	2012	At this stoichiometry, apo A-II forms rHDL from DMPC and FC.	Dimyristoylphosphatidylcholine	48-52	apolipoprotein A2	Homo sapiens	23-31
23025327-6	2012	Contrary to our hypothesis, apo A-II, like apo A-I, reacts poorly with DMPC containing >=20 mol % FC.	Dimyristoylphosphatidylcholine	71-75	apolipoprotein A2	Homo sapiens	28-36
23025327-10	2012	On the basis of our data, we propose a model in which apo A-I and apo A-II bind to DMPC via surface defects that disappear at 20 mol % FC.	Dimyristoylphosphatidylcholine	83-87	NLR family pyrin domain containing 3	Homo sapiens	70-74
22435461-2	2012	MAS spectra reveal a well-structured VDAC1 in 2D crystals of dimyristoylphosphatidylcholine (DMPC) and diphytanoylphosphatidylcholine (DPhPC), and their temperature dependence suggests that the VDAC structure does not change conformation above and below the lipid phase transition temperature.	Dimyristoylphosphatidylcholine	61-91	voltage dependent anion channel 1	Homo sapiens	37-42
22579757-5	2012	In a bicellar DMPC/DHPC environment, the ErbB4 membrane-spanning alpha-helices (651-678)(2) form a right-handed parallel dimer through the N-terminal double GG4-like motif A(655)GxxGG(660) in a fashion that is believed to permit proper kinase domain activation.	Dimyristoylphosphatidylcholine	14-18	erb-b2 receptor tyrosine kinase 4	Homo sapiens	41-46
22119777-5	2012	Here, we report the reconstitution of functional VDAC-2 in lauryldimethylamine-oxide (LDAO) detergent micelles and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipid bilayer nanodiscs.	Dimyristoylphosphatidylcholine	115-158	voltage dependent anion channel 2	Homo sapiens	49-55
22119777-5	2012	Here, we report the reconstitution of functional VDAC-2 in lauryldimethylamine-oxide (LDAO) detergent micelles and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipid bilayer nanodiscs.	Dimyristoylphosphatidylcholine	160-164	voltage dependent anion channel 2	Homo sapiens	49-55
22398364-4	2012	GD3:DMPC lipid bilayers possess lipid chain characteristics that are indiscernible from those present in the lactosylceramide:DMPC bilayer, while possessing different structural head groups, indicating that the head group has little influence on the underlying lipid structure.	Dimyristoylphosphatidylcholine	126-130	GRDX	Homo sapiens	0-3
22398364-0	2012	Use of attenuated total reflectance Fourier transform infrared spectroscopy to study lactosylceramide and GD3 DMPC bilayers.	Dimyristoylphosphatidylcholine	110-114	GRDX	Homo sapiens	106-109
22398364-4	2012	GD3:DMPC lipid bilayers possess lipid chain characteristics that are indiscernible from those present in the lactosylceramide:DMPC bilayer, while possessing different structural head groups, indicating that the head group has little influence on the underlying lipid structure.	Dimyristoylphosphatidylcholine	4-8	GRDX	Homo sapiens	0-3
22435461-2	2012	MAS spectra reveal a well-structured VDAC1 in 2D crystals of dimyristoylphosphatidylcholine (DMPC) and diphytanoylphosphatidylcholine (DPhPC), and their temperature dependence suggests that the VDAC structure does not change conformation above and below the lipid phase transition temperature.	Dimyristoylphosphatidylcholine	93-97	voltage dependent anion channel 1	Homo sapiens	37-42
22240027-1	2012	Hybrid liposomes (HLs), composed of l-alpha-dimyristoylphosphatidylcholine (DMPC) and polyoxyethylene(23) dodecyl ether, have selectively inhibited the growth of human hepatocellular carcinoma (HCC) cells without affecting normal hepatocytes to trigger apoptosis via caspase-3 activation.	Dimyristoylphosphatidylcholine	76-80	caspase 3	Homo sapiens	267-276
21796706-4	2012	Advanced glycation end-products up-regulated the expression of Bad and Bax and down-regulated Bcl-2 proteins, and pretreatment with DMPC significantly down-regulated Bad and Bax while up-regulating Bcl-2 expressions.	Dimyristoylphosphatidylcholine	132-136	BCL2 associated X, apoptosis regulator	Homo sapiens	71-74
21796706-4	2012	Advanced glycation end-products up-regulated the expression of Bad and Bax and down-regulated Bcl-2 proteins, and pretreatment with DMPC significantly down-regulated Bad and Bax while up-regulating Bcl-2 expressions.	Dimyristoylphosphatidylcholine	132-136	BCL2 apoptosis regulator	Homo sapiens	94-99
21796706-4	2012	Advanced glycation end-products up-regulated the expression of Bad and Bax and down-regulated Bcl-2 proteins, and pretreatment with DMPC significantly down-regulated Bad and Bax while up-regulating Bcl-2 expressions.	Dimyristoylphosphatidylcholine	132-136	BCL2 associated X, apoptosis regulator	Homo sapiens	174-177
21796706-4	2012	Advanced glycation end-products up-regulated the expression of Bad and Bax and down-regulated Bcl-2 proteins, and pretreatment with DMPC significantly down-regulated Bad and Bax while up-regulating Bcl-2 expressions.	Dimyristoylphosphatidylcholine	132-136	BCL2 apoptosis regulator	Homo sapiens	198-203
21796706-6	2012	More importantly, these increases of ICAM-1 and TGF-beta1 expressions were reduced meaningfully with the pretreatment of DMPC.	Dimyristoylphosphatidylcholine	121-125	intercellular adhesion molecule 1	Homo sapiens	37-43
21796706-6	2012	More importantly, these increases of ICAM-1 and TGF-beta1 expressions were reduced meaningfully with the pretreatment of DMPC.	Dimyristoylphosphatidylcholine	121-125	transforming growth factor beta 1	Homo sapiens	48-57
22172806-3	2012	Aligned experiments indicate that the transmembrane domain of wild-type PLB has a helical tilt of 13 +-4  in DMPC/DHPC bicelles.	Dimyristoylphosphatidylcholine	109-113	phospholamban	Homo sapiens	72-75
22197371-5	2012	Remarkably, spontaneous insertion of BclXL into DMPC/DHPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine/1,2-dihexanoyl-sn-glycero-3-phosphocholine) bicelles results in a dramatic conformational change such that it can no longer recognize the BH3 ligands in what has come to be known as the "hit-and-run" mechanism.	Dimyristoylphosphatidylcholine	48-52	BCL2 like 1	Homo sapiens	37-42
22197371-5	2012	Remarkably, spontaneous insertion of BclXL into DMPC/DHPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine/1,2-dihexanoyl-sn-glycero-3-phosphocholine) bicelles results in a dramatic conformational change such that it can no longer recognize the BH3 ligands in what has come to be known as the "hit-and-run" mechanism.	Dimyristoylphosphatidylcholine	59-102	BCL2 like 1	Homo sapiens	37-42
21712092-3	2011	Our approach results in rapid, high-yield production of structurally and functionally competent apoE4 as evidenced by secondary structure measurements, thermal and chemical melting profiles and the kinetic profile of solubilization of dimyristoyl-phosphatidylcholine (DMPC) vesicles.	Dimyristoylphosphatidylcholine	235-266	apolipoprotein E	Homo sapiens	96-101
21872568-4	2012	We have employed replica exchange molecular dynamics computer simulations to study a doubly lipidated heptapeptide, corresponding to the C-terminus of the human N-Ras protein, incorporated into a dimyristoylphosphatidylcholine lipid bilayer.	Dimyristoylphosphatidylcholine	196-226	NRAS proto-oncogene, GTPase	Homo sapiens	161-166
22008704-6	2012	RESULTS: Activity of APOA5 variants on LPL-mediated 1,2-dimyristoyl-sn-glycero-3-phosphocholine hydrolysis was reduced by 17 to 74% in comparison to wild type APOA5 (P<0.0001).	Dimyristoylphosphatidylcholine	52-95	apolipoprotein A5	Homo sapiens	21-26
22008704-6	2012	RESULTS: Activity of APOA5 variants on LPL-mediated 1,2-dimyristoyl-sn-glycero-3-phosphocholine hydrolysis was reduced by 17 to 74% in comparison to wild type APOA5 (P<0.0001).	Dimyristoylphosphatidylcholine	52-95	lipoprotein lipase	Homo sapiens	39-42
21712092-3	2011	Our approach results in rapid, high-yield production of structurally and functionally competent apoE4 as evidenced by secondary structure measurements, thermal and chemical melting profiles and the kinetic profile of solubilization of dimyristoyl-phosphatidylcholine (DMPC) vesicles.	Dimyristoylphosphatidylcholine	268-272	apolipoprotein E	Homo sapiens	96-101
21553808-8	2011	We have employed peptide amide hydrogen-deuterium exchange mass spectrometry (DXMS) to characterize the association of Lp-PLA(2) with dimyristoylphosphatidylcholine (DMPC) vesicles and found that specific residues 113-120 in one of the enzyme"s surface-disposed hydrophobic alpha-helices likely mediate liposome binding.	Dimyristoylphosphatidylcholine	134-164	phospholipase A2 group VII	Homo sapiens	119-127
21699199-8	2011	Lipid binding, as measured by turbidity clearance of unilamellar vesicles of DMPC, is faster at acidic pH values and consistent with our previous hypothesis that it is only the monomeric form of apoE that binds lipid tightly.	Dimyristoylphosphatidylcholine	77-81	apolipoprotein E	Homo sapiens	195-199
21553808-8	2011	We have employed peptide amide hydrogen-deuterium exchange mass spectrometry (DXMS) to characterize the association of Lp-PLA(2) with dimyristoylphosphatidylcholine (DMPC) vesicles and found that specific residues 113-120 in one of the enzyme"s surface-disposed hydrophobic alpha-helices likely mediate liposome binding.	Dimyristoylphosphatidylcholine	166-170	phospholipase A2 group VII	Homo sapiens	119-127
21395305-3	2011	The fluorescence experiments reported that the Trp side chain of [Trp8]SP inserts into the hydrophobic core of the SDS micelles and DMPG liposomes but faces the DMPC hydrophilic region, indicating that electrostatic interactions between membrane and SP are essential for the alpha-helical fold.	Dimyristoylphosphatidylcholine	161-165	tachykinin precursor 1	Homo sapiens	71-73
21442718-10	2011	Upon probing the interaction of the DMPC-cholesterol-glycolipid bilayer with MAG a slight decrease in the capacity of the adsorbed lipid film is observed.	Dimyristoylphosphatidylcholine	36-40	myelin associated glycoprotein	Homo sapiens	77-80
22022488-5	2011	Binding of PDC-109 with dimyristoylphosphatidylcholine membranes containing 25 mol% cholesterol showed an initial increase in the association constant as well as enthalpy and entropy of binding with increase in temperature, whereas the values decreased with further increase in temperature.	Dimyristoylphosphatidylcholine	24-54	seminal plasma protein PDC-109	Bos taurus	11-18
21322570-6	2011	Measurements of the time dependence of turbidity clearance of small unilamellar vesicles of dimyristoyl-sn-glycero-3-phosphocholine (DMPC) upon addition of apoE show that higher molecular weight oligomers bind poorly if at all.	Dimyristoylphosphatidylcholine	133-137	apolipoprotein E	Homo sapiens	156-160
21408153-8	2011	Cholesterol incorporation into DMPC membranes led to a decrease in the CLA of PDC-109-lipid recombinants, which could be attributed to reduced accessibility of hydrophobic surfaces to the substrate protein(s).	Dimyristoylphosphatidylcholine	31-35	seminal plasma protein PDC-109	Bos taurus	78-85
21211814-1	2011	The interaction of new bivalent NOP receptor antagonists with dodecyl phosphatidylcholine micelles and DMPC/cholesterol liposomes was investigated in solution by high resolution NMR.	Dimyristoylphosphatidylcholine	103-107	opioid related nociceptin receptor 1	Homo sapiens	32-35
21219628-6	2011	Dimyristoylphosphatidylcholine turbidity clearance assay showed that apoE4-(72-166) maintains the highest lipid-binding capacity.	Dimyristoylphosphatidylcholine	0-30	apolipoprotein E	Homo sapiens	69-74
22649687-4	2011	In the present work, heteronuclear NMR spectroscopy and molecular dynamics simulations were used to demonstrate that the two most widely used media (detergent DPC micelles and lipid DMPC/DHPC bicelles) enable to perform structural studies of the specific interactions between transmembrane alpha-helices by the example of dimerizing the transmembrane domain of the bitopic protein glycophorin A.	Dimyristoylphosphatidylcholine	182-186	glycophorin A (MNS blood group)	Homo sapiens	381-394
21336227-6	2011	An average of nearly 1 mug of DMPC was eluted into ATF within the first 10 h. Elution was about five times faster in ATF than in water.	Dimyristoylphosphatidylcholine	30-34	glial cell derived neurotrophic factor	Homo sapiens	51-54
21336227-6	2011	An average of nearly 1 mug of DMPC was eluted into ATF within the first 10 h. Elution was about five times faster in ATF than in water.	Dimyristoylphosphatidylcholine	30-34	glial cell derived neurotrophic factor	Homo sapiens	117-120
21408153-6	2011	Presence of DMPC was found to increase the CLA of PDC-109 significantly, which could be due to the considerable exposure of hydrophobic regions on the lipid-protein recombinants, which can interact productively with the nonnative structures of target proteins, resulting in their protection.	Dimyristoylphosphatidylcholine	12-16	seminal plasma protein PDC-109	Bos taurus	50-57
21426773-1	2011	OBJECTIVE: To evaluate the effect of non-surgical periodontal therapy on periodontal status, glycemic control and the level of serum interleukin (IL)-6 in type 2 diabetic patients with chronic periodontitis (DMCP).	Dimyristoylphosphatidylcholine	208-212	interleukin 6	Homo sapiens	133-151
20518532-6	2010	Adsorption of Fg to surfaces coated with a neutral lipid, dimyristoylphosphatidylcholine (DMPC), and a cationic lipid, dioctadecyldimethylammonium bromide (DOMA), from a range of solution concentrations has been studied using a quartz crystal microbalance (QCM).	Dimyristoylphosphatidylcholine	58-88	fibrinogen beta chain	Homo sapiens	14-16
20961099-3	2010	Using solid-state nuclear magnetic resonance spectroscopy, we have now determined the conformation, dynamics, oligomeric state, and topology of a human alpha-defensin, HNP-1, in DMPC/DMPG bilayers.	Dimyristoylphosphatidylcholine	178-182	HNP1	Homo sapiens	168-173
21117173-1	2010	The effect of PDC-109 binding to dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles (MLVs) and supported membranes was investigated by (31)P NMR spectroscopy and atomic force microscopy.	Dimyristoylphosphatidylcholine	33-63	seminal plasma protein PDC-109	Bos taurus	14-21
21117173-1	2010	The effect of PDC-109 binding to dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles (MLVs) and supported membranes was investigated by (31)P NMR spectroscopy and atomic force microscopy.	Dimyristoylphosphatidylcholine	65-69	seminal plasma protein PDC-109	Bos taurus	14-21
20532386-3	2010	Here we present the results of molecular dynamics simulations of PR3 anchored at three different phospholipid bilayers: DMPC, DMPG and an equimolar mixture of DMPC/DMPG.	Dimyristoylphosphatidylcholine	120-124	proteinase 3	Homo sapiens	65-68
20532386-3	2010	Here we present the results of molecular dynamics simulations of PR3 anchored at three different phospholipid bilayers: DMPC, DMPG and an equimolar mixture of DMPC/DMPG.	Dimyristoylphosphatidylcholine	159-163	proteinase 3	Homo sapiens	65-68
21117173-3	2010	Binding of PDC-109 to MLVs of DMPC and DPPG induced the formation of an isotropic signal in their (31)P NMR spectra, which increased with increasing protein/lipid ratio and temperature, consistent with protein-induced disruption of the MLVs and the formation of small unilamellar vesicles or micelles but not inverse hexagonal or cubic phases.	Dimyristoylphosphatidylcholine	30-34	seminal plasma protein PDC-109	Bos taurus	11-18
20836507-1	2010	The present work demonstrates the modulation of excited state intramolecular proton transfer (ESIPT) emission of 1-hydroxy-2-naphthaldehyde (HN12) upon its interaction with the liposomal vesicles/bilayer of dimyristoyl-l-alpha-phosphatidylcholine (DMPC) and dimyristoyl-l-alpha-phosphatidylglycerol (DMPG) and its subsequent implementation as an efficient molecular reporter for probing of microheterogeneous environments of lipid-bilayer system.	Dimyristoylphosphatidylcholine	248-252	MT-RNR2 like 12 (pseudogene)	Homo sapiens	141-145
20836507-2	2010	Modifications on the emission profile of HN12 in terms of remarkable emission intensity enhancement coupled with a hypsochromic shift induced by the presence of DMPC and DMPG membranes have been interpreted to be vivid manifestations of the interactions between the two partners.	Dimyristoylphosphatidylcholine	161-165	MT-RNR2 like 12 (pseudogene)	Homo sapiens	41-45
20351248-6	2010	We studied the structure of Nogo-66 alone and in the presence of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles and dodecylphosphocholine (DPC) micelles as membrane mimetics.	Dimyristoylphosphatidylcholine	110-114	reticulon 4	Homo sapiens	28-32
19782154-4	2010	It was found that neither patch plays a significant functional role in the ability of apoA-I to accept cholesterol in an ABCA1-dependent manner, but that the hydrophobic patch did affect the ability of apoA-I to clear DMPC liposomes.	Dimyristoylphosphatidylcholine	218-222	apolipoprotein A1	Homo sapiens	202-208
20045042-6	2010	In the present paper, the differential scanning calorimetry technique has been used to study the interaction of TMS with a biomembrane model constituted by dimyristoylphosphatidylcholine multilamellar vesicles.	Dimyristoylphosphatidylcholine	156-186	thymidylate synthetase	Homo sapiens	112-115
20030366-6	2010	The triple repeat LA3-5 showed the expected interaction with ApoE(1-191).DMPC, but surprisingly CR16-18 did not interact with this form of ApoE.	Dimyristoylphosphatidylcholine	73-77	apolipoprotein E	Homo sapiens	61-65
20030366-7	2010	To understand these differences in ApoE binding affinity, we introduced mutations of conserved residues from LA5 into CR18 and produced a CR16-18 variant capable of binding ApoE(1-191).DMPC.	Dimyristoylphosphatidylcholine	185-189	apolipoprotein E	Homo sapiens	35-39
20030366-7	2010	To understand these differences in ApoE binding affinity, we introduced mutations of conserved residues from LA5 into CR18 and produced a CR16-18 variant capable of binding ApoE(1-191).DMPC.	Dimyristoylphosphatidylcholine	185-189	WAS/WASL interacting protein family member 3	Homo sapiens	138-142
20030366-7	2010	To understand these differences in ApoE binding affinity, we introduced mutations of conserved residues from LA5 into CR18 and produced a CR16-18 variant capable of binding ApoE(1-191).DMPC.	Dimyristoylphosphatidylcholine	185-189	apolipoprotein E	Homo sapiens	173-177
19925783-2	2010	In this study, atomic force microscopy was applied to characterise the association of CYP2C9 to dimyristoylphosphatidylcholine (DMPC) supported phospholipid bilayers.	Dimyristoylphosphatidylcholine	96-126	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	86-92
19925783-2	2010	In this study, atomic force microscopy was applied to characterise the association of CYP2C9 to dimyristoylphosphatidylcholine (DMPC) supported phospholipid bilayers.	Dimyristoylphosphatidylcholine	128-132	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	86-92
19925783-3	2010	CYP2C9 was found to exclusively localise in the gel domains of partially melted DMPC bilayers.	Dimyristoylphosphatidylcholine	80-84	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	0-6
19700415-4	2010	We found that cholesterol stabilizes relatively unstable complexes; for example, incorporation of 10-30 mol% cholesterol in apoC-I:dimyristoyl phosphatidylcholine complexes increased their kinetic stability by deltaDeltaG* congruent with 1 kcal/mol.	Dimyristoylphosphatidylcholine	131-162	apolipoprotein C1	Homo sapiens	124-130
19396372-4	2009	The myristoylated Galpha(i) subunit (Galpha-mir) was reconstituted in 1,2-dimiristoyl-sn-glycerophosphocoline (DMPC) bilayers, as a mimic of the drug target.	Dimyristoylphosphatidylcholine	111-115	succinate-CoA ligase GDP/ADP-forming subunit alpha	Homo sapiens	18-24
19683598-2	2009	The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein.	Dimyristoylphosphatidylcholine	138-168	seminal plasma protein PDC-109	Bos taurus	65-74
19683598-2	2009	The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein.	Dimyristoylphosphatidylcholine	138-168	seminal plasma protein PDC-109	Bos taurus	65-72
19683598-2	2009	The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein.	Dimyristoylphosphatidylcholine	170-174	seminal plasma protein PDC-109	Bos taurus	65-74
19683598-2	2009	The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein.	Dimyristoylphosphatidylcholine	170-174	seminal plasma protein PDC-109	Bos taurus	65-72
19683598-3	2009	The degree of quenching achieved by different quenchers with PDC-109/B bound to Lyso-PC and DMPC membranes was significantly higher as compared to the full PDC-109 protein, indicating that membrane binding afforded considerably lesser protection to the tryptophan residues of domain B as compared to those in the full PDC-109 protein.	Dimyristoylphosphatidylcholine	92-96	seminal plasma protein PDC-109	Bos taurus	61-70
19683598-3	2009	The degree of quenching achieved by different quenchers with PDC-109/B bound to Lyso-PC and DMPC membranes was significantly higher as compared to the full PDC-109 protein, indicating that membrane binding afforded considerably lesser protection to the tryptophan residues of domain B as compared to those in the full PDC-109 protein.	Dimyristoylphosphatidylcholine	92-96	seminal plasma protein PDC-109	Bos taurus	61-68
19683598-4	2009	Finally, changes in red-edge excitation shift (REES) seen with PDC-109/B upon binding to DMPC membranes and Lyso-PC micelles were smaller that the corresponding changes in the REES values observed for the full PDC-109.	Dimyristoylphosphatidylcholine	89-93	seminal plasma protein PDC-109	Bos taurus	63-72
19683598-4	2009	Finally, changes in red-edge excitation shift (REES) seen with PDC-109/B upon binding to DMPC membranes and Lyso-PC micelles were smaller that the corresponding changes in the REES values observed for the full PDC-109.	Dimyristoylphosphatidylcholine	89-93	seminal plasma protein PDC-109	Bos taurus	63-70
18984910-2	2009	In this study, we employed a LC-MS/MS assay to demonstrate that residues 38-51 of apoC-I are significantly protected from proteolysis in the presence of 1,2-dimyristoyl-3-sn-glycero-phosphocholine (DMPC).	Dimyristoylphosphatidylcholine	198-202	apolipoprotein C1	Homo sapiens	82-88
18984910-5	2009	In contrast to wild-type apoC-I (WT), which binds DMPC vesicles with an apparent Kd [Kd(app)] of 0.89 microM, apoC-I(F42A) and apoC-I(F46A) possess 2-fold weaker affinities for DMPC with Kd(app) of 1.52 microM and 1.58 microM, respectively.	Dimyristoylphosphatidylcholine	50-54	apolipoprotein C1	Homo sapiens	25-31
18984910-5	2009	In contrast to wild-type apoC-I (WT), which binds DMPC vesicles with an apparent Kd [Kd(app)] of 0.89 microM, apoC-I(F42A) and apoC-I(F46A) possess 2-fold weaker affinities for DMPC with Kd(app) of 1.52 microM and 1.58 microM, respectively.	Dimyristoylphosphatidylcholine	177-181	apolipoprotein C1	Homo sapiens	25-31
18984910-6	2009	However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively.	Dimyristoylphosphatidylcholine	107-111	apolipoprotein C1	Homo sapiens	9-15
18984910-6	2009	However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively.	Dimyristoylphosphatidylcholine	107-111	apolipoprotein C1	Homo sapiens	23-29
18984910-6	2009	However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively.	Dimyristoylphosphatidylcholine	107-111	apolipoprotein C1	Homo sapiens	23-29
18984910-6	2009	However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively.	Dimyristoylphosphatidylcholine	107-111	apolipoprotein C1	Homo sapiens	23-29
18984910-7	2009	Sedimentation velocity studies subsequently show that the protein/DMPC complexes formed by these apoC-I mutants sediment at 6.5S, 6.7S, 6.5S, and 8.0S, respectively.	Dimyristoylphosphatidylcholine	66-70	apolipoprotein C1	Homo sapiens	97-103
19413971-5	2009	In zwitterionic 1,2-dimyristoyl-sn-glycero-3-phosphocholine membranes, the myristoyl chain of Src was significantly longer and appears "stiffer" than the phospholipid chains.	Dimyristoylphosphatidylcholine	16-59	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	94-97
19825998-8	2009	The ability of apoA-V(1-146) to solubilize dimyristoylphosphatidylcholine vesicles at a rate faster than full-length apoA-V suggests that N- and C-terminal interactions in the full-length protein modulate its lipid binding properties.	Dimyristoylphosphatidylcholine	43-73	apolipoprotein A5	Homo sapiens	15-21
19456103-4	2009	Fluorescence measurements suggested that DMPC possesses a lower entropy in nanodiscs than in vesicles, because apoA-I molecules, which surround the bilayer, force closer lipid packing, but allow water penetration to the acyl chain ends.	Dimyristoylphosphatidylcholine	41-45	apolipoprotein A1	Homo sapiens	111-117
19098283-3	2009	The addition of dimyristoylphosphatidylcholine (DMPC) to isolated LDL induced a decrease in the alpha-helical content of apoB and increased the immunoreactivity of the apoB C terminus toward monoclonal antibodies in the region.	Dimyristoylphosphatidylcholine	16-46	apolipoprotein B	Mus musculus	121-125
19098283-3	2009	The addition of dimyristoylphosphatidylcholine (DMPC) to isolated LDL induced a decrease in the alpha-helical content of apoB and increased the immunoreactivity of the apoB C terminus toward monoclonal antibodies in the region.	Dimyristoylphosphatidylcholine	16-46	apolipoprotein B	Mus musculus	168-172
19098283-3	2009	The addition of dimyristoylphosphatidylcholine (DMPC) to isolated LDL induced a decrease in the alpha-helical content of apoB and increased the immunoreactivity of the apoB C terminus toward monoclonal antibodies in the region.	Dimyristoylphosphatidylcholine	48-52	apolipoprotein B	Mus musculus	121-125
19098283-3	2009	The addition of dimyristoylphosphatidylcholine (DMPC) to isolated LDL induced a decrease in the alpha-helical content of apoB and increased the immunoreactivity of the apoB C terminus toward monoclonal antibodies in the region.	Dimyristoylphosphatidylcholine	48-52	apolipoprotein B	Mus musculus	168-172
19396372-4	2009	The myristoylated Galpha(i) subunit (Galpha-mir) was reconstituted in 1,2-dimiristoyl-sn-glycerophosphocoline (DMPC) bilayers, as a mimic of the drug target.	Dimyristoylphosphatidylcholine	111-115	succinate-CoA ligase GDP/ADP-forming subunit alpha	Homo sapiens	37-43
19326075-4	2009	Furthermore, increasing the molar ratio of apoC-III in rHDL enhanced the surfactant-like properties and the ability to lyse dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	124-155	apolipoprotein C3	Homo sapiens	43-51
19138679-3	2009	We found that Abeta (1-40) strongly perturbed the bilayer structure of dimyristoylphosphatidylcholine (DMPC), to form a non-lamellar phase (most likely micellar).	Dimyristoylphosphatidylcholine	71-101	amyloid beta precursor protein	Homo sapiens	14-19
19138679-3	2009	We found that Abeta (1-40) strongly perturbed the bilayer structure of dimyristoylphosphatidylcholine (DMPC), to form a non-lamellar phase (most likely micellar).	Dimyristoylphosphatidylcholine	103-107	amyloid beta precursor protein	Homo sapiens	14-19
19138679-5	2009	The difference of the isotropic peak intensity between DMPC/Abeta and DMPC/GM1/Abeta suggests a specific interaction between Abeta and GM1.	Dimyristoylphosphatidylcholine	55-59	amyloid beta precursor protein	Homo sapiens	60-65
19138679-5	2009	The difference of the isotropic peak intensity between DMPC/Abeta and DMPC/GM1/Abeta suggests a specific interaction between Abeta and GM1.	Dimyristoylphosphatidylcholine	70-74	amyloid beta precursor protein	Homo sapiens	79-84
19138679-5	2009	The difference of the isotropic peak intensity between DMPC/Abeta and DMPC/GM1/Abeta suggests a specific interaction between Abeta and GM1.	Dimyristoylphosphatidylcholine	70-74	amyloid beta precursor protein	Homo sapiens	79-84
19138679-6	2009	We show that in the DMPC/GM1/Abeta system there are three lipid phases, namely a lamellar phase, a hexagonal phase and non-oriented lipids.	Dimyristoylphosphatidylcholine	20-24	amyloid beta precursor protein	Homo sapiens	29-34
18959431-7	2008	These structural changes are associated with a slower rate of solubilization of DMPC vesicles by apoE4-mut1 and reduced binding of the protein to emulsion particles compared with WT apoE4.	Dimyristoylphosphatidylcholine	80-84	apolipoprotein E	Homo sapiens	97-107
19159271-0	2009	Interactions between DMPC liposomes and the serum blood proteins HSA and IgG.	Dimyristoylphosphatidylcholine	21-25	albumin	Homo sapiens	65-68
19159271-1	2009	The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements.	Dimyristoylphosphatidylcholine	122-170	albumin	Homo sapiens	63-82
18959431-5	2008	To better understand how these mutations improve the function of apoE4, we investigated the conformation and stability of apoE4-mut1 and apoE4-mut2 and their binding to dimyristoyl phosphatidylcholine (DMPC) vesicles and to triglyceride (TG)-rich emulsion particles.	Dimyristoylphosphatidylcholine	202-206	apolipoprotein E	Homo sapiens	122-127
18959431-5	2008	To better understand how these mutations improve the function of apoE4, we investigated the conformation and stability of apoE4-mut1 and apoE4-mut2 and their binding to dimyristoyl phosphatidylcholine (DMPC) vesicles and to triglyceride (TG)-rich emulsion particles.	Dimyristoylphosphatidylcholine	202-206	apolipoprotein E	Homo sapiens	137-147
18959431-7	2008	These structural changes are associated with a slower rate of solubilization of DMPC vesicles by apoE4-mut1 and reduced binding of the protein to emulsion particles compared with WT apoE4.	Dimyristoylphosphatidylcholine	80-84	apolipoprotein E	Homo sapiens	97-102
18452333-3	2008	For DMPC-based biomembranes, polymers whose PPO chain length is less than that of the bilayer thickness insert weakly into the membrane with the PEO blocks on the same side of the bilayer, leading to delocalization of the PEO at the membrane-water interface.	Dimyristoylphosphatidylcholine	4-8	protoporphyrinogen oxidase	Homo sapiens	44-47
18939592-3	2008	Differential scanning calorimetry (DSC) of vesicles formed from DMPC shows that the gel-to-fluid phase transition temperature is lower for vesicles containing this ortho-substituted PCB.	Dimyristoylphosphatidylcholine	64-68	pyruvate carboxylase	Homo sapiens	182-185
18939592-4	2008	Atomic force microscopy (AFM) shows that, whereas supported bilayers of DMPC containing this ortho-substituted PCB display two melting points, bilayers containing the coplanar PCB display just a single melting point.	Dimyristoylphosphatidylcholine	72-76	pyruvate carboxylase	Homo sapiens	111-114
18642906-2	2008	Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein.	Dimyristoylphosphatidylcholine	45-49	apolipoprotein A1	Homo sapiens	73-91
18402784-7	2008	Upon binding of PDC-109 to DMPC membranes and Lyso-PC micelles the REES values were reduced to 2.5 and 1.0 nm, respectively, which could be due to the penetration of some parts of the protein, especially the segment containing Trp-90 into the membrane interior, where the red-edge effects are considerably reduced.	Dimyristoylphosphatidylcholine	27-31	seminal plasma protein PDC-109	Bos taurus	16-23
18393425-0	2008	STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface.	Dimyristoylphosphatidylcholine	59-102	sulfotransferase family 1A member 3	Homo sapiens	0-3
18406360-1	2008	Formation of discoidal high density lipoproteins (rHDL) by apolipoprotein A-I (apoA-I) mediated solubilization of dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles (MLV) was dramatically affected by bilayer cholesterol concentration.	Dimyristoylphosphatidylcholine	114-145	apolipoprotein A1	Homo sapiens	59-77
18406360-1	2008	Formation of discoidal high density lipoproteins (rHDL) by apolipoprotein A-I (apoA-I) mediated solubilization of dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles (MLV) was dramatically affected by bilayer cholesterol concentration.	Dimyristoylphosphatidylcholine	114-145	apolipoprotein A1	Homo sapiens	79-85
18406360-1	2008	Formation of discoidal high density lipoproteins (rHDL) by apolipoprotein A-I (apoA-I) mediated solubilization of dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles (MLV) was dramatically affected by bilayer cholesterol concentration.	Dimyristoylphosphatidylcholine	147-151	apolipoprotein A1	Homo sapiens	59-77
18406360-1	2008	Formation of discoidal high density lipoproteins (rHDL) by apolipoprotein A-I (apoA-I) mediated solubilization of dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles (MLV) was dramatically affected by bilayer cholesterol concentration.	Dimyristoylphosphatidylcholine	147-151	apolipoprotein A1	Homo sapiens	79-85
18406360-4	2008	At a high ratio of DMPC/apoA-I (10/1 mg DMPC/mg apoA-I, 420/1 mol/mol), changing the temperature and cholesterol concentration yielded rHDL that varied greatly in size, phospholipid/protein ratio, mol% cholesterol, and number of apoA-I molecules per particle.	Dimyristoylphosphatidylcholine	19-23	apolipoprotein A1	Homo sapiens	48-54
18406360-4	2008	At a high ratio of DMPC/apoA-I (10/1 mg DMPC/mg apoA-I, 420/1 mol/mol), changing the temperature and cholesterol concentration yielded rHDL that varied greatly in size, phospholipid/protein ratio, mol% cholesterol, and number of apoA-I molecules per particle.	Dimyristoylphosphatidylcholine	19-23	apolipoprotein A1	Homo sapiens	48-54
18366234-3	2008	Higher SOD-like activity was obtained in the case of DLPC and DMPC liposomes, in which the ligands were well-dispersed on the membrane in the liquid crystalline phase.	Dimyristoylphosphatidylcholine	62-66	superoxide dismutase 1	Homo sapiens	7-10
18366234-5	2008	On the basis of the above results, the co-induction of the SOD and POD activities to eliminate the superoxide and also hydrogen peroxide as a one-pot reaction was finally performed by using the Mn-HPyP-modified DMPC liposome, resulting in an increase in the efficiency of the elimination of both superoxide and hydrogen peroxide.	Dimyristoylphosphatidylcholine	211-215	superoxide dismutase 1	Homo sapiens	59-62
26621095-7	2008	We then compared amino acid association constants, the partitioning of a series of model pentapeptides, the partitioning and orientation of WALP23 in DOPC lipid bilayers and a series of KALP peptides in dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine (DPPC) bilayers.	Dimyristoylphosphatidylcholine	203-233	anosmin 2, pseudogene	Homo sapiens	186-190
18393425-0	2008	STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface.	Dimyristoylphosphatidylcholine	104-108	sulfotransferase family 1A member 3	Homo sapiens	0-3
18201068-6	2008	In addition, the solubilization of dimyristoylphosphatidylcholine multilamellar vesicles is more rapid with apoE4 than with apoE3; removal of the C-terminal helices significantly affected solubilization rates with both isoforms.	Dimyristoylphosphatidylcholine	35-65	apolipoprotein E	Homo sapiens	108-113
18201068-6	2008	In addition, the solubilization of dimyristoylphosphatidylcholine multilamellar vesicles is more rapid with apoE4 than with apoE3; removal of the C-terminal helices significantly affected solubilization rates with both isoforms.	Dimyristoylphosphatidylcholine	35-65	apolipoprotein E	Homo sapiens	124-129
18068665-5	2008	Using lipid vesicles made of DMPG/DMPC at a molar ratio of 1:1 at 10mg/ml in the presence of different non-muscle myosin II concentrations showed a variation of the main phase transition of the lipid vesicle at around 23 degrees C. With increasing concentrations of non-muscle myosin II the thermotropic properties of the lipid vesicle changed, which is indicative of protein-lipid interaction/insertion.	Dimyristoylphosphatidylcholine	34-38	myosin heavy chain 14	Homo sapiens	114-120
18068665-5	2008	Using lipid vesicles made of DMPG/DMPC at a molar ratio of 1:1 at 10mg/ml in the presence of different non-muscle myosin II concentrations showed a variation of the main phase transition of the lipid vesicle at around 23 degrees C. With increasing concentrations of non-muscle myosin II the thermotropic properties of the lipid vesicle changed, which is indicative of protein-lipid interaction/insertion.	Dimyristoylphosphatidylcholine	34-38	myosin heavy chain 14	Homo sapiens	277-283
17964533-5	2008	The onset of the hydrolytic activity of cobra-venom sPLA2 towards mixed monolayers of dimyristoyl-PC (DMPC)/cholesterol 2:1 (mol/mol) has been determined using infrared reflection-absorption spectroscopy (IRRAS) and polarization-modulated (PM-) IRRAS.	Dimyristoylphosphatidylcholine	86-100	phospholipase A2 group X	Homo sapiens	52-57
17964533-5	2008	The onset of the hydrolytic activity of cobra-venom sPLA2 towards mixed monolayers of dimyristoyl-PC (DMPC)/cholesterol 2:1 (mol/mol) has been determined using infrared reflection-absorption spectroscopy (IRRAS) and polarization-modulated (PM-) IRRAS.	Dimyristoylphosphatidylcholine	102-106	phospholipase A2 group X	Homo sapiens	52-57
17964533-9	2008	The surface pressure that is critical for sPLA2 activation correlates with the critical miscibility pressure according to the phase diagram of DMPC and cholesterol.	Dimyristoylphosphatidylcholine	143-147	phospholipase A2 group X	Homo sapiens	42-47
17880077-3	2007	Recently, the structure of the full-length H-ras protein in a DMPC bilayer has been computationally characterized.	Dimyristoylphosphatidylcholine	62-66	HRas proto-oncogene, GTPase	Homo sapiens	43-48
18221016-7	2008	Correlation of secondary structure changes with lipid transition temperature during heating suggested that the MiRP1 C-terminus incorporates into DMPC bilayers.	Dimyristoylphosphatidylcholine	146-150	potassium voltage-gated channel subfamily E regulatory subunit 2	Homo sapiens	111-116
17996895-5	2007	We show that opsin can also be directly purified in DMPC/DHPC bicelles to give correctly folded functional opsin, as shown by the ability to regenerate rhodopsin to approximately 70% yield.	Dimyristoylphosphatidylcholine	52-56	rhodopsin	Homo sapiens	152-161
17557790-2	2007	Here, we applied a combination of experimental and computational techniques to determine structural and dynamical details of the lipid chain modifications of an N-ras heptapeptide in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes.	Dimyristoylphosphatidylcholine	183-226	NRAS proto-oncogene, GTPase	Homo sapiens	161-166
17557790-2	2007	Here, we applied a combination of experimental and computational techniques to determine structural and dynamical details of the lipid chain modifications of an N-ras heptapeptide in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes.	Dimyristoylphosphatidylcholine	228-232	NRAS proto-oncogene, GTPase	Homo sapiens	161-166
17880077-4	2007	Here, the atomic interactions between the H-ras membrane anchor and the DMPC bilayer are investigated in detail.	Dimyristoylphosphatidylcholine	72-76	HRas proto-oncogene, GTPase	Homo sapiens	42-47
17603006-8	2007	The rate increase is modeled with the assumption that the binding of PLA2 to DMPC interface is cooperatively promoted by bile salt followed by allosteric k(cat)(*)-activation of the bound enzyme by the anionic interface.	Dimyristoylphosphatidylcholine	77-81	phospholipase A2 group IB	Homo sapiens	69-73
17685646-1	2007	The interaction of hydrophobically modified copolymers of acrylamide and acrylic acid, designated as PAM-C12-AA (X%) (X% indicates the percentage of acrylic acid unit and X = 5, 10, 20), with dimyristoylphosphatidylcholine (DMPC) vesicles has been studied.	Dimyristoylphosphatidylcholine	192-222	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	101-104
17603006-4	2007	The PLA2-catalyzed rate of hydrolysis of zwitterionic dimyristoylphosphatidylcholine (DMPC) vesicles depends on the concentration and structure of the bile salt.	Dimyristoylphosphatidylcholine	86-90	phospholipase A2 group IB	Homo sapiens	4-8
17715945-7	2007	Monomeric and wild-type apoE display similar lipid-binding activities in dimyristoylphosphatidylcholine clearance assays and formation of reconstituted high-density lipoproteins.	Dimyristoylphosphatidylcholine	73-103	apolipoprotein E	Homo sapiens	24-28
17685646-1	2007	The interaction of hydrophobically modified copolymers of acrylamide and acrylic acid, designated as PAM-C12-AA (X%) (X% indicates the percentage of acrylic acid unit and X = 5, 10, 20), with dimyristoylphosphatidylcholine (DMPC) vesicles has been studied.	Dimyristoylphosphatidylcholine	224-228	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	101-104
17488074-4	2007	Here, we present the first solid-state NMR studies on holo-cyt b5 in a membrane environment, namely, macroscopically oriented DMPC:DHPC bicelles.	Dimyristoylphosphatidylcholine	126-130	cytochrome b5 type A	Homo sapiens	59-65
17369413-3	2007	Specifically, we focus on the N-terminal 6.4-17% of apoB (B6.4-17) complexed with the phospholipid dimyristoylphosphatidylcholine in vitro.	Dimyristoylphosphatidylcholine	99-129	apolipoprotein B	Homo sapiens	52-56
17474718-0	2007	Large disk intermediate precedes formation of apolipoprotein A-I-dimyristoylphosphatidylcholine small disks.	Dimyristoylphosphatidylcholine	65-95	apolipoprotein A1	Homo sapiens	46-64
17474718-1	2007	Small approximately 8.5 nm disks formed spontaneously when dimyristoylphosphatidylcholine (DMPC) large unilamellar vesicles (LUVs) were incubated with apolipoprotein A-I (apoA-I) (100:1 molar ratio).	Dimyristoylphosphatidylcholine	59-89	apolipoprotein A1	Homo sapiens	151-169
17401142-8	2007	Truncated apoA-V displayed an attenuated ability to solubilize l-alpha-dimyristoylphosphatidylcholine phospholipid vesicles compared with full-length apoA-V, whereas a peptide corresponding to the deleted C-terminal segment displayed markedly enhanced kinetics.	Dimyristoylphosphatidylcholine	63-101	apolipoprotein A5	Homo sapiens	10-16
17474718-1	2007	Small approximately 8.5 nm disks formed spontaneously when dimyristoylphosphatidylcholine (DMPC) large unilamellar vesicles (LUVs) were incubated with apolipoprotein A-I (apoA-I) (100:1 molar ratio).	Dimyristoylphosphatidylcholine	91-95	apolipoprotein A1	Homo sapiens	151-169
17474718-1	2007	Small approximately 8.5 nm disks formed spontaneously when dimyristoylphosphatidylcholine (DMPC) large unilamellar vesicles (LUVs) were incubated with apolipoprotein A-I (apoA-I) (100:1 molar ratio).	Dimyristoylphosphatidylcholine	91-95	apolipoprotein A1	Homo sapiens	171-177
17474718-4	2007	The reaction kinetics of apoA-I with DMPC LUVs was monitored by fluorescence resonance energy transfer, and two phases were observed, supporting the presence of the intermediate in the formation of small disks.	Dimyristoylphosphatidylcholine	37-41	apolipoprotein A1	Homo sapiens	25-31
17474718-5	2007	The lipid dynamics of LUVs and disks were assayed, revealing the presence of sequestered lipid-protein domains upon apoA-I binding to DMPC LUVs.	Dimyristoylphosphatidylcholine	134-138	apolipoprotein A1	Homo sapiens	116-122
17474718-7	2007	We propose that apoA-I binds with DMPC LUVs to form small lipid-protein domains on the LUV; then the domains are released to form large disks, which can mature in the presence of additional apoA-I to form small disks.	Dimyristoylphosphatidylcholine	34-38	apolipoprotein A1	Homo sapiens	16-22
17442288-2	2007	The disruption of DMPC multilamellar vesicles (MLV"s) with monomyristoylphosphatidylcholine (lysoPC), a product of hydrolysis of phospholipase A(2) (PLA(2)), is more efficient at 18 degrees C, where DMPC MLV"s are known to be in the ripple P(beta") phase, than at 10 degrees C (L(beta") flat gel phase).	Dimyristoylphosphatidylcholine	18-22	phospholipase A2 group IB	Homo sapiens	129-147
17442288-2	2007	The disruption of DMPC multilamellar vesicles (MLV"s) with monomyristoylphosphatidylcholine (lysoPC), a product of hydrolysis of phospholipase A(2) (PLA(2)), is more efficient at 18 degrees C, where DMPC MLV"s are known to be in the ripple P(beta") phase, than at 10 degrees C (L(beta") flat gel phase).	Dimyristoylphosphatidylcholine	18-22	phospholipase A2 group IB	Homo sapiens	149-155
17442288-2	2007	The disruption of DMPC multilamellar vesicles (MLV"s) with monomyristoylphosphatidylcholine (lysoPC), a product of hydrolysis of phospholipase A(2) (PLA(2)), is more efficient at 18 degrees C, where DMPC MLV"s are known to be in the ripple P(beta") phase, than at 10 degrees C (L(beta") flat gel phase).	Dimyristoylphosphatidylcholine	199-203	phospholipase A2 group IB	Homo sapiens	129-147
17557268-3	2007	We measured the serum (sMCP-1) and dialysate MCP-1 (dMCP-1) concentrations of stable peritoneal dialysis (PD) patients and studied various factors affecting MCP-1 production.	Dimyristoylphosphatidylcholine	52-56	C-C motif chemokine ligand 2	Homo sapiens	45-50
17326667-2	2007	To investigate the molecular basis for this phenomenon we explored the ability of apolipoprotein A-V, in most experiments complexed to disks of dimyristoylphosphatidylcholine, to interact with two members of the low density lipoprotein receptor family, the low density lipoprotein receptor-related protein and the mosaic type-1 receptor, SorLA.	Dimyristoylphosphatidylcholine	144-174	apolipoprotein A5	Homo sapiens	82-100
17341095-0	2007	Role of secondary structure in protein-phospholipid surface interactions: reconstitution and denaturation of apolipoprotein C-I:DMPC complexes.	Dimyristoylphosphatidylcholine	128-132	apolipoprotein C1	Homo sapiens	109-127
17258176-4	2007	Using reconstituted lipoprotein particles of apoE3 N-terminal (NT) domain and dimyristoylphosphatidylcholine (DMPC), maximal LDLR binding was observed at DMPC:apoE3-NT ratios >2.5:1 (w/w).	Dimyristoylphosphatidylcholine	110-114	low density lipoprotein receptor	Homo sapiens	125-129
17258176-4	2007	Using reconstituted lipoprotein particles of apoE3 N-terminal (NT) domain and dimyristoylphosphatidylcholine (DMPC), maximal LDLR binding was observed at DMPC:apoE3-NT ratios >2.5:1 (w/w).	Dimyristoylphosphatidylcholine	110-114	apolipoprotein E	Homo sapiens	159-164
17258176-4	2007	Using reconstituted lipoprotein particles of apoE3 N-terminal (NT) domain and dimyristoylphosphatidylcholine (DMPC), maximal LDLR binding was observed at DMPC:apoE3-NT ratios >2.5:1 (w/w).	Dimyristoylphosphatidylcholine	78-108	low density lipoprotein receptor	Homo sapiens	125-129
17258176-4	2007	Using reconstituted lipoprotein particles of apoE3 N-terminal (NT) domain and dimyristoylphosphatidylcholine (DMPC), maximal LDLR binding was observed at DMPC:apoE3-NT ratios >2.5:1 (w/w).	Dimyristoylphosphatidylcholine	154-158	apolipoprotein E	Homo sapiens	45-50
17258176-4	2007	Using reconstituted lipoprotein particles of apoE3 N-terminal (NT) domain and dimyristoylphosphatidylcholine (DMPC), maximal LDLR binding was observed at DMPC:apoE3-NT ratios >2.5:1 (w/w).	Dimyristoylphosphatidylcholine	154-158	low density lipoprotein receptor	Homo sapiens	125-129
17258176-6	2007	In the case of apoE3-NT, lipid particles comprised of a mixture of DMPC and DMPS, a DMPS concentration dependent inhibition of LDLR binding activity was observed.	Dimyristoylphosphatidylcholine	67-71	apolipoprotein E	Homo sapiens	15-20
17258176-6	2007	In the case of apoE3-NT, lipid particles comprised of a mixture of DMPC and DMPS, a DMPS concentration dependent inhibition of LDLR binding activity was observed.	Dimyristoylphosphatidylcholine	67-71	low density lipoprotein receptor	Homo sapiens	127-131
17627601-0	2007	Molecular dynamics simulations of C-terminal decapeptide of gastrin-releasing peptide in DMPC bilayers: structure, stability and orientation of the peptide hormone within the bilayers.	Dimyristoylphosphatidylcholine	89-93	gastrin releasing peptide	Homo sapiens	60-85
17263520-0	2007	Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer.	Dimyristoylphosphatidylcholine	76-115	HRas proto-oncogene, GTPase	Homo sapiens	57-62
17263520-4	2007	Here, the structure of the full-length H-Ras protein in complex with a 1,2-dimyristoylglycero-3-phosphocholine (DMPC) bilayer obtained from modeling and all-atom explicit solvent molecular dynamics simulations, as well as experimental validation of the main results, are presented.	Dimyristoylphosphatidylcholine	71-110	HRas proto-oncogene, GTPase	Homo sapiens	39-44
17263520-4	2007	Here, the structure of the full-length H-Ras protein in complex with a 1,2-dimyristoylglycero-3-phosphocholine (DMPC) bilayer obtained from modeling and all-atom explicit solvent molecular dynamics simulations, as well as experimental validation of the main results, are presented.	Dimyristoylphosphatidylcholine	112-116	HRas proto-oncogene, GTPase	Homo sapiens	39-44
17110109-2	2007	The concentrations of cytokines (IFN-gamma, IL-12) were significantly increased in the presence of HL25 ([DMPC] = 100 microM, [C12(EO)25] = 10 microM) and the maximum values attained were 13-14 times higher compared with those of control, though the viability and proliferation of hPBMCs were decreased under the same conditions.	Dimyristoylphosphatidylcholine	106-110	interferon gamma	Homo sapiens	33-42
17627601-3	2007	The biologically active C-terminal decapeptide of GRP (GRP10) was studied in explicit DMPC bilayers using molecular dynamics simulations.	Dimyristoylphosphatidylcholine	86-90	gastrin releasing peptide	Homo sapiens	50-53
17627601-3	2007	The biologically active C-terminal decapeptide of GRP (GRP10) was studied in explicit DMPC bilayers using molecular dynamics simulations.	Dimyristoylphosphatidylcholine	86-90	gastrin releasing peptide	Homo sapiens	55-60
16877761-5	2006	Here, we have demonstrated that PGLa is able to assume such an I-state in a 1:1 mixture with magainin 2 at a peptide-to-lipid ratio as low as 1:100 in dimyristoylphosphatidylcholine/dimyristoylphosphatidylglycerol model membranes.	Dimyristoylphosphatidylcholine	151-181	prepro-PGLa S homeolog	Xenopus laevis	32-36
17144661-7	2006	Ste14p activity was monitored by an in vitro methyltransferase assay in reconstituted vesicle dispersions composed of DMPC, C20BAS/E.	Dimyristoylphosphatidylcholine	118-122	protein-S-isoprenylcysteine carboxyl O-methyltransferase	Saccharomyces cerevisiae S288C	0-6
17054379-5	2006	Because experimental data do not distinguish clearly helix-helix packing, molecular dynamics (MD) simulations are used to investigate the energetic factors that drive Neu TM-TM interactions of the wild and the oncogenic receptor (Val664/Glu mutation) in DMPC or in POPC environments.	Dimyristoylphosphatidylcholine	254-258	erb-b2 receptor tyrosine kinase 2	Homo sapiens	167-170
17002280-9	2006	Using kinetic analysis of the DMPC clearance assay, we show that the identified phospholipid binding sequences all map to the surface of the lipid binding pocket in the B17 model based on the homologous protein, lipovitellin.	Dimyristoylphosphatidylcholine	30-34	NADH:ubiquinone oxidoreductase subunit B6	Homo sapiens	169-172
16814496-1	2006	High sensitivity differential scanning calorimetry (HSDSC) has been used to study the interaction of the model proteins lactate dehydrogenase (LDH) and tyrosinase with dimyristoylphosphatidylcholine (DMPC) liposomes, and relate this to the thermal and physical stability of the proteins.	Dimyristoylphosphatidylcholine	168-198	tyrosinase	Homo sapiens	152-162
16814496-1	2006	High sensitivity differential scanning calorimetry (HSDSC) has been used to study the interaction of the model proteins lactate dehydrogenase (LDH) and tyrosinase with dimyristoylphosphatidylcholine (DMPC) liposomes, and relate this to the thermal and physical stability of the proteins.	Dimyristoylphosphatidylcholine	200-204	tyrosinase	Homo sapiens	152-162
16814496-2	2006	On heating, both LDH and tyrosinase denatured irreversibly in a time-dependent manner and modified the phase transition behaviour of DMPC liposomes at all concentrations investigated.	Dimyristoylphosphatidylcholine	133-137	tyrosinase	Homo sapiens	25-35
16235222-6	2005	These results are obtained from phosphatidylcholine spin probes with the nitroxide systematically stepped down the sn-2 chain, in fully hydrated bilayer membranes of dimyristoyl phosphatidylcholine (DMPC)-containing cholesterol.	Dimyristoylphosphatidylcholine	199-203	solute carrier family 38 member 5	Homo sapiens	115-119
16467279-6	2006	In competition binding assays, unlabeled apoE3-NT DMPC inhibited AEDANS-apoE DMPC binding to sLDLR more effectively than low density lipoprotein.	Dimyristoylphosphatidylcholine	77-81	apolipoprotein E	Homo sapiens	41-46
16467279-6	2006	In competition binding assays, unlabeled apoE3-NT DMPC inhibited AEDANS-apoE DMPC binding to sLDLR more effectively than low density lipoprotein.	Dimyristoylphosphatidylcholine	77-81	apolipoprotein E	Homo sapiens	41-45
16285025-7	2006	Secondary structure of Neu(TM35) was retained in DMPC (dimyristoylphosphatidylcholine)/DCPC (dicaproylphosphatidylcholine) membrane bicelles, and evidences for dimers/oligomers in the lipid bilayer were found.	Dimyristoylphosphatidylcholine	49-53	erb-b2 receptor tyrosine kinase 2	Homo sapiens	23-26
16285025-7	2006	Secondary structure of Neu(TM35) was retained in DMPC (dimyristoylphosphatidylcholine)/DCPC (dicaproylphosphatidylcholine) membrane bicelles, and evidences for dimers/oligomers in the lipid bilayer were found.	Dimyristoylphosphatidylcholine	55-85	erb-b2 receptor tyrosine kinase 2	Homo sapiens	23-26
16183881-3	2005	Atomic force microscopy of supported 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) bilayers in the presence of MSI-78 provides images of the membrane thinning process at a high spatial resolution.	Dimyristoylphosphatidylcholine	37-80	RB binding protein 4, chromatin remodeling factor	Homo sapiens	116-119
16183881-3	2005	Atomic force microscopy of supported 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) bilayers in the presence of MSI-78 provides images of the membrane thinning process at a high spatial resolution.	Dimyristoylphosphatidylcholine	82-86	RB binding protein 4, chromatin remodeling factor	Homo sapiens	116-119
16183881-8	2005	This picture is consistent with concentration-dependent 31P and 2H NMR spectra of MSI-78 in mechanically aligned DMPC bilayers.	Dimyristoylphosphatidylcholine	113-117	RB binding protein 4, chromatin remodeling factor	Homo sapiens	82-85
16540478-6	2006	The C-terminal truncated apoE-(1-191) and apoE-(1-231) proteins greatly lost lipid binding ability as illustrated by the dimyristoylphosphatidylcholine turbidity clearance.	Dimyristoylphosphatidylcholine	121-151	apolipoprotein E	Homo sapiens	25-29
16540478-6	2006	The C-terminal truncated apoE-(1-191) and apoE-(1-231) proteins greatly lost lipid binding ability as illustrated by the dimyristoylphosphatidylcholine turbidity clearance.	Dimyristoylphosphatidylcholine	121-151	apolipoprotein E	Mus musculus	42-46
16467279-4	2006	Incubation of sLDLR with AEDANS-Trp-null apoE3-NT dimyristoylphosphatidylcholine (DMPC) disks, but not lipid-free AEDANS-apoE, induced an enhancement in AEDANS fluorescence emission intensity (excitation, 280 nm) consistent with intermolecular energy transfer from excited Trp in sLDLR to receptor-bound apoE.	Dimyristoylphosphatidylcholine	50-80	apolipoprotein E	Homo sapiens	41-46
16467279-4	2006	Incubation of sLDLR with AEDANS-Trp-null apoE3-NT dimyristoylphosphatidylcholine (DMPC) disks, but not lipid-free AEDANS-apoE, induced an enhancement in AEDANS fluorescence emission intensity (excitation, 280 nm) consistent with intermolecular energy transfer from excited Trp in sLDLR to receptor-bound apoE.	Dimyristoylphosphatidylcholine	50-80	apolipoprotein E	Homo sapiens	41-45
16467279-4	2006	Incubation of sLDLR with AEDANS-Trp-null apoE3-NT dimyristoylphosphatidylcholine (DMPC) disks, but not lipid-free AEDANS-apoE, induced an enhancement in AEDANS fluorescence emission intensity (excitation, 280 nm) consistent with intermolecular energy transfer from excited Trp in sLDLR to receptor-bound apoE.	Dimyristoylphosphatidylcholine	82-86	apolipoprotein E	Homo sapiens	41-46
16467279-4	2006	Incubation of sLDLR with AEDANS-Trp-null apoE3-NT dimyristoylphosphatidylcholine (DMPC) disks, but not lipid-free AEDANS-apoE, induced an enhancement in AEDANS fluorescence emission intensity (excitation, 280 nm) consistent with intermolecular energy transfer from excited Trp in sLDLR to receptor-bound apoE.	Dimyristoylphosphatidylcholine	82-86	apolipoprotein E	Homo sapiens	41-45
16467279-6	2006	In competition binding assays, unlabeled apoE3-NT DMPC inhibited AEDANS-apoE DMPC binding to sLDLR more effectively than low density lipoprotein.	Dimyristoylphosphatidylcholine	50-54	apolipoprotein E	Homo sapiens	41-46
16467279-6	2006	In competition binding assays, unlabeled apoE3-NT DMPC inhibited AEDANS-apoE DMPC binding to sLDLR more effectively than low density lipoprotein.	Dimyristoylphosphatidylcholine	50-54	apolipoprotein E	Homo sapiens	41-45
16808151-3	2006	The selective inhibition of paraoxonase activity by palmitoyl-lysoPG, characterized by noncompetitiveness and charge interaction, was also observed with HDL- or dimyristoylphosphatidylcholine (DMPC)-bound PON1.	Dimyristoylphosphatidylcholine	161-191	paraoxonase 1	Homo sapiens	205-209
16808151-7	2006	Separately, lysoPC stimulation was less remarkable for DMPC-bound PON1 than for either dimyristoylphosphatidylserine (DMPS)- or dimyristoylphosphatidylglycerol-bound PON1, suggesting a tight association between PON1 and DMPC.	Dimyristoylphosphatidylcholine	55-59	paraoxonase 1	Homo sapiens	66-70
16808151-8	2006	In support of this, the stimulatory role of apolipoprotein A-I was less prominent for DMPC-bound PON1 than for DMPS-bound PON1.	Dimyristoylphosphatidylcholine	86-90	apolipoprotein A1	Homo sapiens	44-62
16808151-8	2006	In support of this, the stimulatory role of apolipoprotein A-I was less prominent for DMPC-bound PON1 than for DMPS-bound PON1.	Dimyristoylphosphatidylcholine	86-90	paraoxonase 1	Homo sapiens	97-101
16679530-4	2006	PMCA was photolabeled in mixed micelles containing detergent, the phosphatidylcholine photoactivatable analog 1-palmitoyl-2-[9-[2"-[125I]iodo-4"- (trifluoromethyldiazirinyl)-benzyloxycarbonyl]-nonaoyl]-sn-glycero-3-phosphocholine, and different amounts of dimyristoyl phosphatidylcholine (PC).	Dimyristoylphosphatidylcholine	256-287	ATPase plasma membrane Ca2+ transporting 2	Homo sapiens	0-4
16679536-2	2006	The micellization process of dimirystoil phosphatidylcholine liposomes (MLV-DMPC) by apo A-I in the presence of LPS was characterized.	Dimyristoylphosphatidylcholine	76-80	apolipoprotein A1	Homo sapiens	85-92
16679536-3	2006	Apo A-I may interact with MLV-DMPC at the lipid transition temperature, forming micellar complexes.	Dimyristoylphosphatidylcholine	30-34	apolipoprotein A1	Homo sapiens	0-7
16245954-2	2005	The kinetics of microsolubilization of dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles by apolipoprotein A-I (apoA-I) to form discoidal high-density lipoproteins (rHDL) was dramatically affected by oxysterol chemical structure.	Dimyristoylphosphatidylcholine	39-69	apolipoprotein A1	Homo sapiens	103-121
16245954-2	2005	The kinetics of microsolubilization of dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles by apolipoprotein A-I (apoA-I) to form discoidal high-density lipoproteins (rHDL) was dramatically affected by oxysterol chemical structure.	Dimyristoylphosphatidylcholine	39-69	apolipoprotein A1	Homo sapiens	123-129
16245954-2	2005	The kinetics of microsolubilization of dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles by apolipoprotein A-I (apoA-I) to form discoidal high-density lipoproteins (rHDL) was dramatically affected by oxysterol chemical structure.	Dimyristoylphosphatidylcholine	71-75	apolipoprotein A1	Homo sapiens	103-121
16245954-2	2005	The kinetics of microsolubilization of dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles by apolipoprotein A-I (apoA-I) to form discoidal high-density lipoproteins (rHDL) was dramatically affected by oxysterol chemical structure.	Dimyristoylphosphatidylcholine	71-75	apolipoprotein A1	Homo sapiens	123-129
16245954-7	2005	The rate of DMPC microsolubilization by apoA-I is highly dependent upon the presence of lattice defects in the membrane surface that occur due to imperfect packing of coexisting lipid phases.	Dimyristoylphosphatidylcholine	12-16	apolipoprotein A1	Homo sapiens	40-46
16032847-1	2005	DMPC vesicles were injected into a 50 mM NaF solution in water, and the kinetics of a monolayer formation at the air-solution interface was investigated by measuring changes of the film pressure, pi, as a function of time.	Dimyristoylphosphatidylcholine	0-4	C-X-C motif chemokine ligand 8	Homo sapiens	41-44
15588256-6	2005	Electron microscopy and non-denaturing PAGE analysis of DMPC (dimyristoylphosphatidylcholine)--apoE CT domain lipoprotein complexes revealed discoidal complexes with a diameter of approx.	Dimyristoylphosphatidylcholine	56-60	apolipoprotein E	Homo sapiens	95-99
15588256-6	2005	Electron microscopy and non-denaturing PAGE analysis of DMPC (dimyristoylphosphatidylcholine)--apoE CT domain lipoprotein complexes revealed discoidal complexes with a diameter of approx.	Dimyristoylphosphatidylcholine	62-92	apolipoprotein E	Homo sapiens	95-99
16153106-3	2005	For dimyristoyl-sn-glycero-3-phosphocholine (DMPC)-based biomembrane structures, polymers whose PPO chain length approximates that of the acyl chains of the lipid bilayer yield highly ordered, expanded lamellar structures consistent with well-integrated (into the lipid bilayer) PPO blocks.	Dimyristoylphosphatidylcholine	45-49	protoporphyrinogen oxidase	Homo sapiens	96-99
16153106-3	2005	For dimyristoyl-sn-glycero-3-phosphocholine (DMPC)-based biomembrane structures, polymers whose PPO chain length approximates that of the acyl chains of the lipid bilayer yield highly ordered, expanded lamellar structures consistent with well-integrated (into the lipid bilayer) PPO blocks.	Dimyristoylphosphatidylcholine	45-49	protoporphyrinogen oxidase	Homo sapiens	279-282
16086582-4	2005	Similarly, Bcl-2-C adopted a structure with a predominance of intermolecularly bound pleated beta-sheet in the absence of membranes, with alpha-helix as the main component in the presence of DMPC and POPG, but intermolecular beta-sheet in the presence of EYPC and cholesterol.	Dimyristoylphosphatidylcholine	191-195	BCL2 apoptosis regulator	Homo sapiens	11-18
16042399-5	2005	Circular dichroism, Trp fluorescence, and light scattering data show that molar concentrations of NaCl or Na(2)SO(4) increase the apparent melting temperature of apoC-1:DMPC complexes by up to 20 degrees C and decelerate protein unfolding.	Dimyristoylphosphatidylcholine	169-173	apolipoprotein C1	Homo sapiens	162-168
16042399-8	2005	Thus, the dominant electrostatic interactions in apoC-1:DMPC disks are destabilizing.	Dimyristoylphosphatidylcholine	56-60	apolipoprotein C1	Homo sapiens	49-55
15654121-2	2005	Here, we show that treatment of plasma with dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles generates prebeta(1)-apoA-I-containing lipoproteins (LpA-I)-like particles similar to those of native plasma.	Dimyristoylphosphatidylcholine	44-75	apolipoprotein A1	Homo sapiens	127-133
15654121-2	2005	Here, we show that treatment of plasma with dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles generates prebeta(1)-apoA-I-containing lipoproteins (LpA-I)-like particles similar to those of native plasma.	Dimyristoylphosphatidylcholine	77-81	apolipoprotein A1	Homo sapiens	127-133
15654121-8	2005	Removal of apoA-I-containing lipoproteins from normolipidemic plasma drastically reduced free cholesterol efflux mediated by DMPC-treated plasma.	Dimyristoylphosphatidylcholine	125-129	apolipoprotein A1	Homo sapiens	11-17
15654121-10	2005	These results indicate that DMPC enrichment of normal plasma resulted in the redistribution of apoA-I from alpha-HDL to prebeta-HDL, allowing for more efficient ABCA1-mediated cellular lipid release.	Dimyristoylphosphatidylcholine	28-32	apolipoprotein A1	Homo sapiens	95-101
15654121-10	2005	These results indicate that DMPC enrichment of normal plasma resulted in the redistribution of apoA-I from alpha-HDL to prebeta-HDL, allowing for more efficient ABCA1-mediated cellular lipid release.	Dimyristoylphosphatidylcholine	28-32	ATP binding cassette subfamily A member 1	Homo sapiens	161-166
15588256-10	2005	Fluorescence quenching analysis of DMPC-apoE CT domain discoidal complexes by spin-labelled stearic acid indicated a relatively superficial location of the native tryptophan residues with respect to the plane of the phospholipid bilayer.	Dimyristoylphosphatidylcholine	35-39	apolipoprotein E	Homo sapiens	40-44
15240475-3	2004	PLA(2) is shown to have higher activity toward the ripple phase compared to the gel phase in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes, indicating its preference for this highly curved membrane morphology.	Dimyristoylphosphatidylcholine	93-136	phospholipase A2 group IB	Homo sapiens	0-6
15708851-10	2005	In dimyristoylphosphatidylcholine/pyrene-R61C/E255C/apoE4 discoidal complexes, pyrene excimer fluorescence emission was retained.	Dimyristoylphosphatidylcholine	3-33	apolipoprotein E	Homo sapiens	52-57
15681655-0	2005	Kinetic stabilization and fusion of apolipoprotein A-2:DMPC disks: comparison with apoA-1 and apoC-1.	Dimyristoylphosphatidylcholine	55-59	apolipoprotein A2	Homo sapiens	36-54
15654128-2	2005	We analyzed here apoA-I interaction with dimyristoylphosphatidylcholine/distearoylphosphatidylcholine (DMPC/DSPC) bilayers at a temperature showing phase coexistence.	Dimyristoylphosphatidylcholine	41-71	apolipoprotein A1	Homo sapiens	17-23
15654128-2	2005	We analyzed here apoA-I interaction with dimyristoylphosphatidylcholine/distearoylphosphatidylcholine (DMPC/DSPC) bilayers at a temperature showing phase coexistence.	Dimyristoylphosphatidylcholine	103-107	apolipoprotein A1	Homo sapiens	17-23
15476409-7	2004	Characterization by density gradient ultracentrifugation and visualization by negative staining electron microscopy demonstrated that [1-44]apoA-I interacts with dimyristoylphosphatidylcholine (DMPC) over a wide range of lipid:peptide ratios from 1:1 to 12:1 (w/w).	Dimyristoylphosphatidylcholine	162-192	apolipoprotein A1	Homo sapiens	140-146
15476409-7	2004	Characterization by density gradient ultracentrifugation and visualization by negative staining electron microscopy demonstrated that [1-44]apoA-I interacts with dimyristoylphosphatidylcholine (DMPC) over a wide range of lipid:peptide ratios from 1:1 to 12:1 (w/w).	Dimyristoylphosphatidylcholine	194-198	apolipoprotein A1	Homo sapiens	140-146
15476409-10	2004	When bound to DMPC, [1-44]apoA-I has approximately 60% helical structure, independent of whether it forms discoidal or vesicular complexes.	Dimyristoylphosphatidylcholine	14-18	apolipoprotein A1	Homo sapiens	26-32
15476409-15	2004	The helix length of 5 [1-44]apoA-I molecules in lipid-bound form is just long enough to wrap around the DMPC bilayer disk once.	Dimyristoylphosphatidylcholine	104-108	apolipoprotein A1	Homo sapiens	28-34
15654128-7	2005	Next, apoA-I was incubated with DMPC/DSPC small unilamellar vesicles, and products were isolated and quantified.	Dimyristoylphosphatidylcholine	32-36	apolipoprotein A1	Homo sapiens	6-12
15766290-6	2005	ApoA-I-(44-186) induced solubilization of dimyristoylphosphatidylcholine vesicles at a rate comparable to that of full-length apoA-I, displayed lipoprotein binding ability, and was an acceptor of ABCA1-mediated cholesterol efflux from cultured macrophages.	Dimyristoylphosphatidylcholine	42-72	apolipoprotein A1	Homo sapiens	0-6
15751982-6	2005	Solid-state NMR methods were used to examine the size and heterogeneity of Ala-PLB and TM-Ala-PLB labeled with (13)C and (2)H in the transmembrane domain and incorporated into dimyristoylphosphatidylcholine (DMPC) bilayers.	Dimyristoylphosphatidylcholine	176-206	phospholamban	Homo sapiens	94-97
15530449-4	2004	According to 31P NMR, the lamellar morphology of the DMPC bilayer remains intact in the presence of B18.	Dimyristoylphosphatidylcholine	53-57	NADH:ubiquinone oxidoreductase subunit B7	Homo sapiens	100-103
15210365-2	2004	The effect of CSA on model membranes such as dimyristoyl phosphatidylcholine (DMPC) bilayers was studied using small-angle X-ray diffraction and differential scanning calorimetry (DSC).	Dimyristoylphosphatidylcholine	45-76	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	14-17
15210365-2	2004	The effect of CSA on model membranes such as dimyristoyl phosphatidylcholine (DMPC) bilayers was studied using small-angle X-ray diffraction and differential scanning calorimetry (DSC).	Dimyristoylphosphatidylcholine	78-82	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	14-17
15210365-3	2004	CSA abolishes the pretransition and affects the transition of DMPC model membranes in a concentration-related manner as is shown by DSC.	Dimyristoylphosphatidylcholine	62-66	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	0-3
15210365-7	2004	In conclusion, CSA, as both small-angle X-ray diffraction and DSC show, affects in a concentration-wise manner the DMPC model membranes and perturbs the bilayer, in particular the acyl chain region.	Dimyristoylphosphatidylcholine	115-119	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	15-18
15240475-3	2004	PLA(2) is shown to have higher activity toward the ripple phase compared to the gel phase in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes, indicating its preference for this highly curved membrane morphology.	Dimyristoylphosphatidylcholine	138-142	phospholipase A2 group IB	Homo sapiens	0-6
15240475-8	2004	Bulk high-performance liquid chromatography measurements indicate that PLA(2) preferentially hydrolyzes DMPC in the DMPC/DSPC ripples.	Dimyristoylphosphatidylcholine	104-108	phospholipase A2 group IB	Homo sapiens	71-77
15240475-8	2004	Bulk high-performance liquid chromatography measurements indicate that PLA(2) preferentially hydrolyzes DMPC in the DMPC/DSPC ripples.	Dimyristoylphosphatidylcholine	116-120	phospholipase A2 group IB	Homo sapiens	71-77
12950167-2	2003	It was found that the initial rate of association of apoE2, apoE3, apoE4, and a mutant form apoE4R158M to multilamellar DMPC vesicles was similar and was reduced and eventually diminished by gradual deletion of the carboxy terminal segments.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein E	Homo sapiens	53-58
15109264-10	2004	DMPC-binding assays demonstrate an identical vesicle clearance rate shared by both the mutant and the wild-type apoE C-terminal domain.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein E	Homo sapiens	112-116
14504179-8	2003	Adding 1.0 mg/mL DMPC to the drinking water of 6-month-old apoE-null male mice for 8 weeks significantly reduced aortic sinus lesion area (P=0.0031) and en face whole aorta lesion area (P=0.001), whereas adding the same concentrations of soy or egg lecithin did not significantly alter lesion area.	Dimyristoylphosphatidylcholine	17-21	apolipoprotein E	Mus musculus	59-63
14504179-9	2003	Jejunal apoA-I synthesis and plasma apoA-I levels were increased 2- to 3-fold in mice receiving DMPC but not soy or egg lecithin.	Dimyristoylphosphatidylcholine	96-100	apolipoprotein A-I	Mus musculus	8-14
14504179-9	2003	Jejunal apoA-I synthesis and plasma apoA-I levels were increased 2- to 3-fold in mice receiving DMPC but not soy or egg lecithin.	Dimyristoylphosphatidylcholine	96-100	apolipoprotein A-I	Mus musculus	36-42
14504179-10	2003	CONCLUSIONS: DMPC (but not lecithin) raises HDL cholesterol and apoA-I, improves HDL function, and prevents lesions or causes their regression in apoE-null mice.	Dimyristoylphosphatidylcholine	13-17	apolipoprotein A-I	Mus musculus	64-70
14504179-10	2003	CONCLUSIONS: DMPC (but not lecithin) raises HDL cholesterol and apoA-I, improves HDL function, and prevents lesions or causes their regression in apoE-null mice.	Dimyristoylphosphatidylcholine	13-17	apolipoprotein E	Mus musculus	146-150
12956604-0	2003	Molecular dynamics simulations of the transmembrane domain of the oncogenic ErbB2 receptor dimer in a DMPC bilayer.	Dimyristoylphosphatidylcholine	102-106	erb-b2 receptor tyrosine kinase 2	Homo sapiens	76-81
12956604-1	2003	Molecular dynamics simulations of an atomic model of the transmembrane domain of the oncogenic ErbB2 receptor dimer embedded in an explicit dimyristoylphosphatidylcholine (DMPC) bilayer were performed for more than 4 ns.	Dimyristoylphosphatidylcholine	140-170	erb-b2 receptor tyrosine kinase 2	Homo sapiens	95-100
14609337-4	2003	The effects of mutations on the ability of apoA-I to form bilayer disk complexes with dimyristoyl phosphatidylcholine (DMPC) that resemble nascent HDL were analyzed by density gradient ultracentrifugation and electron microscopy (EM).	Dimyristoylphosphatidylcholine	86-117	apolipoprotein A1	Homo sapiens	43-49
14609337-4	2003	The effects of mutations on the ability of apoA-I to form bilayer disk complexes with dimyristoyl phosphatidylcholine (DMPC) that resemble nascent HDL were analyzed by density gradient ultracentrifugation and electron microscopy (EM).	Dimyristoylphosphatidylcholine	119-123	apolipoprotein A1	Homo sapiens	43-49
14609337-8	2003	CD and EM studies of the apoA-I/DMPC complexes at different pH demonstrated that changes in the net charge or in the charge distribution on the apoA-I molecule have critical effects on the conformation and lipid-binding ability of the protein.	Dimyristoylphosphatidylcholine	32-36	apolipoprotein A1	Homo sapiens	25-31
14609337-8	2003	CD and EM studies of the apoA-I/DMPC complexes at different pH demonstrated that changes in the net charge or in the charge distribution on the apoA-I molecule have critical effects on the conformation and lipid-binding ability of the protein.	Dimyristoylphosphatidylcholine	32-36	apolipoprotein A1	Homo sapiens	144-150
14606878-3	2003	For dimyristoyl-sn-glycero-3-phosphocholine (DMPC)-based biomembrane structures, polymers possessing a PPO chain length commensurate with the acyl chain dimensions of the lipid bilayer yield highly ordered, swollen lamellar structures consistent with well-integrated (into the lipid bilayer) PPO blocks.	Dimyristoylphosphatidylcholine	45-49	protoporphyrinogen oxidase	Homo sapiens	103-106
14606878-3	2003	For dimyristoyl-sn-glycero-3-phosphocholine (DMPC)-based biomembrane structures, polymers possessing a PPO chain length commensurate with the acyl chain dimensions of the lipid bilayer yield highly ordered, swollen lamellar structures consistent with well-integrated (into the lipid bilayer) PPO blocks.	Dimyristoylphosphatidylcholine	45-49	protoporphyrinogen oxidase	Homo sapiens	292-295
14606878-4	2003	Triblock copolymers of lesser PPO chain length yield materials with structural characteristics similar to a simple dispersion of DMPC in water.	Dimyristoylphosphatidylcholine	129-133	protoporphyrinogen oxidase	Homo sapiens	30-33
14504179-0	2003	Oral synthetic phospholipid (DMPC) raises high-density lipoprotein cholesterol levels, improves high-density lipoprotein function, and markedly reduces atherosclerosis in apolipoprotein E-null mice.	Dimyristoylphosphatidylcholine	29-33	apolipoprotein E	Mus musculus	171-187
14504179-3	2003	We tested DMPC in vivo in apolipoprotein (apo) E-null mice.	Dimyristoylphosphatidylcholine	10-14	apolipoprotein E	Mus musculus	26-48
14504179-5	2003	Eight weeks later, HDL cholesterol levels and apoA-I levels were markedly increased in the mice that received DMPC.	Dimyristoylphosphatidylcholine	110-114	apolipoprotein A-I	Mus musculus	46-52
14504179-7	2003	Adding 1.0 mg/mL of DMPC to the drinking water of 10-month-old apoE-null female mice for 5 weeks caused regression of aortic sinus lesions (P=0.003).	Dimyristoylphosphatidylcholine	20-24	apolipoprotein E	Mus musculus	63-67
12810715-5	2003	Fluorescence spectroscopy of recombinant human apoA-V provided evidence of tertiary folding, and light scattering studies indicated that apoA-V transforms dimyristoylphosphatidylcholine vesicles into discoidal complexes with an efficiency similar to that of apoA-I.	Dimyristoylphosphatidylcholine	155-185	apolipoprotein A5	Homo sapiens	137-143
12950167-2	2003	It was found that the initial rate of association of apoE2, apoE3, apoE4, and a mutant form apoE4R158M to multilamellar DMPC vesicles was similar and was reduced and eventually diminished by gradual deletion of the carboxy terminal segments.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein E	Homo sapiens	60-65
12950167-2	2003	It was found that the initial rate of association of apoE2, apoE3, apoE4, and a mutant form apoE4R158M to multilamellar DMPC vesicles was similar and was reduced and eventually diminished by gradual deletion of the carboxy terminal segments.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein E	Homo sapiens	67-72
12588864-4	2003	Nuclear magnetic resonance measurements showed that, in apoE3-dimyristoyl phosphatidylcholine discs, Lys-143 and -146 in the N-terminal domain and Lys-233 in the C-terminal domain have unusually low pK(a) values, indicating high positive electrostatic potential around these residues.	Dimyristoylphosphatidylcholine	62-93	apolipoprotein E	Homo sapiens	56-61
12719234-6	2003	The dissociation rate constant (k(-1)) for the DMPC/PDC-109 system was found to be 2.7 x 10(-2) s(-1) whereas the k(-1) values obtained with DMPG and DMPA was about three to four times higher.	Dimyristoylphosphatidylcholine	47-51	seminal plasma protein PDC-109	Bos taurus	52-59
12719234-7	2003	From the kinetic data, the association constant for the binding of PDC-109 to DMPC was estimated as 2.1 x 10(7) M(-1).	Dimyristoylphosphatidylcholine	78-82	seminal plasma protein PDC-109	Bos taurus	67-74
12719234-9	2003	Thus the higher affinity of PDC-109 for choline phospholipids is reflected in a faster association rate constant and a slower dissociation rate constant for DMPC as compared to the other phospholipids.	Dimyristoylphosphatidylcholine	157-161	seminal plasma protein PDC-109	Bos taurus	28-35
12719234-11	2003	Analysis of the activation parameters indicates that the interaction of PDC-109 with DMPC membranes is favored by a strong entropic contribution, whereas negative entropic contribution is primarily responsible for the rather weak interaction of this protein with DMPA and DMPG.	Dimyristoylphosphatidylcholine	85-89	seminal plasma protein PDC-109	Bos taurus	72-79
12899628-8	2003	ApoA-V interacts with bilayer vesicles of dimyristoylphosphatidylcholine to form discoidal complexes with diameters in the range of 15-20 nm.	Dimyristoylphosphatidylcholine	42-72	apolipoprotein A5	Homo sapiens	0-6
12364553-1	2002	We examined the effects of apolipoprotein E (apoE) domain structure and polymorphism on the kinetics of solubilization (clearance) of dimyristoyl-phosphatidylcholine multilamellar vesicles.	Dimyristoylphosphatidylcholine	134-165	apolipoprotein E	Homo sapiens	45-49
12633731-1	2003	The self-association state of human plasma apolipoprotein E (apoE) in solution and in complexes with dimyristoylphosphatidylcholine (DMPC) varying in stoichiometry was studied in sub-micromolar concentration range by gel filtration, fluorescence anisotropy, fluorescence quenching and energy transfer measurements with apolipoprotein labeled with lysine-specific fluorescent dyes.	Dimyristoylphosphatidylcholine	101-131	apolipoprotein E	Homo sapiens	43-59
12633731-1	2003	The self-association state of human plasma apolipoprotein E (apoE) in solution and in complexes with dimyristoylphosphatidylcholine (DMPC) varying in stoichiometry was studied in sub-micromolar concentration range by gel filtration, fluorescence anisotropy, fluorescence quenching and energy transfer measurements with apolipoprotein labeled with lysine-specific fluorescent dyes.	Dimyristoylphosphatidylcholine	101-131	apolipoprotein E	Homo sapiens	61-65
12633731-1	2003	The self-association state of human plasma apolipoprotein E (apoE) in solution and in complexes with dimyristoylphosphatidylcholine (DMPC) varying in stoichiometry was studied in sub-micromolar concentration range by gel filtration, fluorescence anisotropy, fluorescence quenching and energy transfer measurements with apolipoprotein labeled with lysine-specific fluorescent dyes.	Dimyristoylphosphatidylcholine	101-131	apolipoprotein E	Homo sapiens	43-57
12633731-1	2003	The self-association state of human plasma apolipoprotein E (apoE) in solution and in complexes with dimyristoylphosphatidylcholine (DMPC) varying in stoichiometry was studied in sub-micromolar concentration range by gel filtration, fluorescence anisotropy, fluorescence quenching and energy transfer measurements with apolipoprotein labeled with lysine-specific fluorescent dyes.	Dimyristoylphosphatidylcholine	133-137	apolipoprotein E	Homo sapiens	43-57
12633731-3	2003	Within DMPC:apoE discoidal complex (125:1) the apolipoprotein association state seems to be intermediate between that in solution and in larger vesicular complex (1000:1); for both complexes, the degree of exposure of fluorescein chromophores into water phase decreased.	Dimyristoylphosphatidylcholine	7-11	apolipoprotein E	Homo sapiens	47-61
12615683-5	2003	Circular dichroism studies of a synthetic peptide spanning human apoB amino acids 4372-4392, both in the absence and presence of dimyristoylphosphatidylcholine, confirmed the alpha-helical nature of the sequence.	Dimyristoylphosphatidylcholine	129-159	apolipoprotein B	Homo sapiens	65-69
12646385-9	2003	When the zwitterionic dimyristoylphosphatidylcholine (DMPC) was employed as the model lipid surface, interaction of apoE-NT isoforms with the lipid substrate was slow.	Dimyristoylphosphatidylcholine	54-58	apolipoprotein E	Homo sapiens	116-120
12364553-4	2002	In contrast, the more flexible interhelical connections in apoA-I and the 10 kDa C-terminal domain of apoE promoted rapid solubilization of dimyristoyl-phosphatidylcholine (DMPC) multilamellar vesicles (mLV).	Dimyristoylphosphatidylcholine	140-171	apolipoprotein A1	Homo sapiens	59-65
12364553-4	2002	In contrast, the more flexible interhelical connections in apoA-I and the 10 kDa C-terminal domain of apoE promoted rapid solubilization of dimyristoyl-phosphatidylcholine (DMPC) multilamellar vesicles (mLV).	Dimyristoylphosphatidylcholine	140-171	apolipoprotein E	Homo sapiens	102-106
12364553-4	2002	In contrast, the more flexible interhelical connections in apoA-I and the 10 kDa C-terminal domain of apoE promoted rapid solubilization of dimyristoyl-phosphatidylcholine (DMPC) multilamellar vesicles (mLV).	Dimyristoylphosphatidylcholine	173-177	apolipoprotein A1	Homo sapiens	59-65
12364553-4	2002	In contrast, the more flexible interhelical connections in apoA-I and the 10 kDa C-terminal domain of apoE promoted rapid solubilization of dimyristoyl-phosphatidylcholine (DMPC) multilamellar vesicles (mLV).	Dimyristoylphosphatidylcholine	173-177	apolipoprotein E	Homo sapiens	102-106
12124275-8	2002	These results are supported by the enhanced activity of PC-PLC upon exceeding T(m) of DMPC large unilamellar vesicles (diameter approximately 0.1 microm) used as a substrate.	Dimyristoylphosphatidylcholine	86-90	heparan sulfate proteoglycan 2	Homo sapiens	59-62
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
12173940-2	2002	The apoA-I deletion delta(144-165) leads to a red shift in the wavelength of maximum fluorescence and a reduction in the alpha-helical content, the stability, the initial rate of association with DMPC liposomes, and the size of the discoidal particles.	Dimyristoylphosphatidylcholine	196-200	apolipoprotein A1	Homo sapiens	4-10
12297311-2	2002	The selectivity of PDC-109 for different spin-labelled phospholipids and sterol probes in dimyristoylphosphatidylcholine (DMPC) host matrix has been characterized earlier by EPR spectroscopy [Ramakrishnan, M., Anbazhagan, V., Pratap, T.V., Marsh, D. and Swamy, M.J. (2001) Biophys.	Dimyristoylphosphatidylcholine	90-120	seminal plasma protein PDC-109	Bos taurus	19-26
12297311-2	2002	The selectivity of PDC-109 for different spin-labelled phospholipids and sterol probes in dimyristoylphosphatidylcholine (DMPC) host matrix has been characterized earlier by EPR spectroscopy [Ramakrishnan, M., Anbazhagan, V., Pratap, T.V., Marsh, D. and Swamy, M.J. (2001) Biophys.	Dimyristoylphosphatidylcholine	122-126	seminal plasma protein PDC-109	Bos taurus	19-26
12297311-5	2002	In this report the effect of cholesterol on the interaction of PDC-109 with DMPC membranes has been investigated by spin-label EPR spectroscopy.	Dimyristoylphosphatidylcholine	76-80	seminal plasma protein PDC-109	Bos taurus	63-70
11969413-3	2002	In the presence of increasing concentrations of L-alpha-dimyristoylphosphatidylcholine (L-alpha-DMPC) lipid vesicles, a dramatic increase in a minimum at 198 nm is observed in the CD spectra of Hst3.	Dimyristoylphosphatidylcholine	48-86	histatin 3	Homo sapiens	194-198
12044170-1	2002	Thermal unfolding of discoidal complexes of apolipoprotein (apo) C-1 with dimyristoyl phosphatidylcholine (DMPC) reveals a novel mechanism of lipoprotein stabilization that is based on kinetics rather than thermodynamics.	Dimyristoylphosphatidylcholine	74-105	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	65-68
12044170-1	2002	Thermal unfolding of discoidal complexes of apolipoprotein (apo) C-1 with dimyristoyl phosphatidylcholine (DMPC) reveals a novel mechanism of lipoprotein stabilization that is based on kinetics rather than thermodynamics.	Dimyristoylphosphatidylcholine	107-111	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	65-68
12044170-6	2002	Consequently, apoC-1/DMPC disks are kinetically but not thermodynamically stable.	Dimyristoylphosphatidylcholine	21-25	apolipoprotein C1	Homo sapiens	14-20
12044170-7	2002	To explore the origins of this kinetic stability, we utilized dynode voltage measured in CD experiments that shows temperature-dependent contribution from UV light scattering of apoC-1/DMPC complexes (d approximately 20 nm).	Dimyristoylphosphatidylcholine	185-189	apolipoprotein C1	Homo sapiens	178-184
12144351-1	2002	The structure and interactions of the 1-24 fragment of the adrenocorticotropin hormone, ACTH (1-24), with membrane have been studied by molecular dynamics (MD) simulation in an NPT ensembles in two explicit membrane mimics, a dodecylphosphocholine (DPC) micelle and a dimyristoylphosphatidylcholine (DMPC) bilayer.	Dimyristoylphosphatidylcholine	268-298	proopiomelanocortin	Homo sapiens	88-92
12144351-1	2002	The structure and interactions of the 1-24 fragment of the adrenocorticotropin hormone, ACTH (1-24), with membrane have been studied by molecular dynamics (MD) simulation in an NPT ensembles in two explicit membrane mimics, a dodecylphosphocholine (DPC) micelle and a dimyristoylphosphatidylcholine (DMPC) bilayer.	Dimyristoylphosphatidylcholine	300-304	proopiomelanocortin	Homo sapiens	88-92
11969413-3	2002	In the presence of increasing concentrations of L-alpha-dimyristoylphosphatidylcholine (L-alpha-DMPC) lipid vesicles, a dramatic increase in a minimum at 198 nm is observed in the CD spectra of Hst3.	Dimyristoylphosphatidylcholine	88-100	histatin 3	Homo sapiens	194-198
11969413-4	2002	The NMR data of Hst3 in the presence of L-alpha-DMPC lipid vesicles reveal the proximity of residues Y(10) and S(20), indicating the existence of a more compact structure.	Dimyristoylphosphatidylcholine	40-52	histatin 3	Homo sapiens	16-20
11951953-2	2002	Differential scanning calorimetry showed that BaP, at concentrations as low as 2 mol% in mixtures with dimyristoylphosphatidylcholine (DMPC), dipalmitoylphosphatidylcholine, and distearoylphosphatidylcholine, abolished the pretransition and broadened and shifted to lower temperatures the main gel-to-liquid crystalline phase transition.	Dimyristoylphosphatidylcholine	103-133	prohibitin 2	Homo sapiens	46-49
12007094-3	2002	GPA has been reconstituted into liposomes formed from dimyristoylphosphatidylcholine, dimyristoylphosphatidylserine, cholesterol, and a bola-amphiphilic phospholipidic photoactivatable probe (radioactive probe 1) by a detergent-mediated method.	Dimyristoylphosphatidylcholine	54-84	glycophorin A (MNS blood group)	Homo sapiens	0-3
11566792-1	2001	The interaction of the major acidic bovine seminal plasma protein, PDC-109, with dimyristoylphosphatidylcholine (DMPC) membranes has been investigated by spin-label electron spin resonance spectroscopy.	Dimyristoylphosphatidylcholine	81-111	seminal plasma protein PDC-109	Bos taurus	43-74
11718669-2	2001	In this study the activity of PLA(2) towards large unilamellar vesicles composed of DPPC:SMPC and DMPC:DSPC:SMPC is investigated using fluorescence and HPLC techniques.	Dimyristoylphosphatidylcholine	98-102	phospholipase A2 group IB	Homo sapiens	30-36
11951953-2	2002	Differential scanning calorimetry showed that BaP, at concentrations as low as 2 mol% in mixtures with dimyristoylphosphatidylcholine (DMPC), dipalmitoylphosphatidylcholine, and distearoylphosphatidylcholine, abolished the pretransition and broadened and shifted to lower temperatures the main gel-to-liquid crystalline phase transition.	Dimyristoylphosphatidylcholine	135-139	prohibitin 2	Homo sapiens	46-49
11951953-5	2002	Fitting of this band resulted in the presence of three components in the case of samples containing BaP, centered at 1,742, 1,727, and 1,704 cm(-1) (only two components, at 1,742 and 1,727 cm(-1), were observed for pure DMPC).	Dimyristoylphosphatidylcholine	220-224	prohibitin 2	Homo sapiens	100-103
11951953-7	2002	Small-angle x-ray diffraction showed that incorporation of 10 mol% BaP into DMPC increased bilayer thickness from 66.7 to 71 A in the gel state and from 58.9 to 60.9 A in the fluid phase.	Dimyristoylphosphatidylcholine	76-80	prohibitin 2	Homo sapiens	67-70
15080496-5	2002	INF-alpha was encapsulated in different liposomal formulations, Dimyristoylphosphatidylcholine (DMPC), Dioleyl-phosphatidyl-ethanolamine/Dimyristoylphosphatidylcholine (DOPE/DMPC) and DOPE/Dimyristoylphosphatidylglycerol (DOPE/DMPG).	Dimyristoylphosphatidylcholine	64-94	interferon alpha 17	Homo sapiens	0-9
15080496-5	2002	INF-alpha was encapsulated in different liposomal formulations, Dimyristoylphosphatidylcholine (DMPC), Dioleyl-phosphatidyl-ethanolamine/Dimyristoylphosphatidylcholine (DOPE/DMPC) and DOPE/Dimyristoylphosphatidylglycerol (DOPE/DMPG).	Dimyristoylphosphatidylcholine	96-100	interferon alpha 17	Homo sapiens	0-9
15080496-5	2002	INF-alpha was encapsulated in different liposomal formulations, Dimyristoylphosphatidylcholine (DMPC), Dioleyl-phosphatidyl-ethanolamine/Dimyristoylphosphatidylcholine (DOPE/DMPC) and DOPE/Dimyristoylphosphatidylglycerol (DOPE/DMPG).	Dimyristoylphosphatidylcholine	174-178	interferon alpha 17	Homo sapiens	0-9
15080496-12	2002	The results indicate that the MT-IIA mRNA level depends on the liposomal formulation of INF-alpha, and the sustained-time effect of the INF-alpha encapsulated in DMPC liposomes is parallel to that of nonencapsulated INF-alpha over a period of 36 hours.	Dimyristoylphosphatidylcholine	162-166	interferon alpha 17	Homo sapiens	136-145
15080496-12	2002	The results indicate that the MT-IIA mRNA level depends on the liposomal formulation of INF-alpha, and the sustained-time effect of the INF-alpha encapsulated in DMPC liposomes is parallel to that of nonencapsulated INF-alpha over a period of 36 hours.	Dimyristoylphosphatidylcholine	162-166	interferon alpha 17	Homo sapiens	136-145
11566792-1	2001	The interaction of the major acidic bovine seminal plasma protein, PDC-109, with dimyristoylphosphatidylcholine (DMPC) membranes has been investigated by spin-label electron spin resonance spectroscopy.	Dimyristoylphosphatidylcholine	113-117	seminal plasma protein PDC-109	Bos taurus	43-74
11566792-3	2001	Binding of PDC-109 at high protein/lipid ratios (PDC-109:DMPC = 1:2, w/w) results in a considerable decrease in the chain segmental mobility of the lipid as seen by spin-label electron spin resonance spectroscopy.	Dimyristoylphosphatidylcholine	57-61	seminal plasma protein PDC-109	Bos taurus	11-18
11566792-4	2001	A further interesting new observation is that, at high concentrations, PDC-109 is capable of (partially) solubilizing DMPC bilayers.	Dimyristoylphosphatidylcholine	118-122	seminal plasma protein PDC-109	Bos taurus	71-78
11566792-5	2001	The selectivity of PDC-109 in its interaction with membrane lipids was investigated by using different spin-labeled phospholipid and steroid probes in the DMPC host membrane.	Dimyristoylphosphatidylcholine	155-159	seminal plasma protein PDC-109	Bos taurus	19-26
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	16-47	apolipoprotein E	Homo sapiens	123-128
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	16-47	apolipoprotein E	Homo sapiens	133-138
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	16-47	low density lipoprotein receptor	Homo sapiens	152-156
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	49-53	apolipoprotein E	Homo sapiens	123-128
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	49-53	apolipoprotein E	Homo sapiens	133-138
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	49-53	low density lipoprotein receptor	Homo sapiens	152-156
11369796-2	2001	When present in dimyristoyl phosphatidylcholine (DMPC) complexes, the 22-kDa amino-terminal fragments (residues 1;-191) of apoE3 and apoE4 bound to the LDLR with approximately 100-fold greater affinity than the 22-kDa fragment of apoE2.	Dimyristoylphosphatidylcholine	49-53	apolipoprotein E	Homo sapiens	230-235
11369796-3	2001	The pK(a) values of lysines (K) at positions 143 and 146 in the LDLR-binding region in DMPC-associated 22-kDa apoE fragments were 9.4 and 9.9 in apoE2, 9.5 and 9.2 in apoE3, and 9.9 and 9.4 in apoE4, respectively.	Dimyristoylphosphatidylcholine	87-91	low density lipoprotein receptor	Homo sapiens	64-68
11369796-3	2001	The pK(a) values of lysines (K) at positions 143 and 146 in the LDLR-binding region in DMPC-associated 22-kDa apoE fragments were 9.4 and 9.9 in apoE2, 9.5 and 9.2 in apoE3, and 9.9 and 9.4 in apoE4, respectively.	Dimyristoylphosphatidylcholine	87-91	apolipoprotein E	Homo sapiens	110-114
11369796-3	2001	The pK(a) values of lysines (K) at positions 143 and 146 in the LDLR-binding region in DMPC-associated 22-kDa apoE fragments were 9.4 and 9.9 in apoE2, 9.5 and 9.2 in apoE3, and 9.9 and 9.4 in apoE4, respectively.	Dimyristoylphosphatidylcholine	87-91	apolipoprotein E	Homo sapiens	145-150
11369796-3	2001	The pK(a) values of lysines (K) at positions 143 and 146 in the LDLR-binding region in DMPC-associated 22-kDa apoE fragments were 9.4 and 9.9 in apoE2, 9.5 and 9.2 in apoE3, and 9.9 and 9.4 in apoE4, respectively.	Dimyristoylphosphatidylcholine	87-91	apolipoprotein E	Homo sapiens	167-172
11369796-3	2001	The pK(a) values of lysines (K) at positions 143 and 146 in the LDLR-binding region in DMPC-associated 22-kDa apoE fragments were 9.4 and 9.9 in apoE2, 9.5 and 9.2 in apoE3, and 9.9 and 9.4 in apoE4, respectively.	Dimyristoylphosphatidylcholine	87-91	apolipoprotein E	Homo sapiens	193-198
11386681-1	2001	To describe the action mechanisms of Bacteriochlorin a (BCA), a second generation photosensitizer, in phosphate buffer (PB) and in dimyristoyl phosphatidylcholine (DMPC) liposomes we carried out oxygen consumption and ESR measurements.	Dimyristoylphosphatidylcholine	164-168	B cell linker	Homo sapiens	56-59
11386681-3	2001	Incorporation of BCA in DMPC liposomes, by promoting the monomerization of BCA, increased 9-fold the oxygen consumption in comparison to the value in PB.	Dimyristoylphosphatidylcholine	24-28	B cell linker	Homo sapiens	17-20
11386681-1	2001	To describe the action mechanisms of Bacteriochlorin a (BCA), a second generation photosensitizer, in phosphate buffer (PB) and in dimyristoyl phosphatidylcholine (DMPC) liposomes we carried out oxygen consumption and ESR measurements.	Dimyristoylphosphatidylcholine	131-162	B cell linker	Homo sapiens	37-54
11386681-3	2001	Incorporation of BCA in DMPC liposomes, by promoting the monomerization of BCA, increased 9-fold the oxygen consumption in comparison to the value in PB.	Dimyristoylphosphatidylcholine	24-28	B cell linker	Homo sapiens	75-78
11386681-1	2001	To describe the action mechanisms of Bacteriochlorin a (BCA), a second generation photosensitizer, in phosphate buffer (PB) and in dimyristoyl phosphatidylcholine (DMPC) liposomes we carried out oxygen consumption and ESR measurements.	Dimyristoylphosphatidylcholine	131-162	B cell linker	Homo sapiens	56-59
11386681-1	2001	To describe the action mechanisms of Bacteriochlorin a (BCA), a second generation photosensitizer, in phosphate buffer (PB) and in dimyristoyl phosphatidylcholine (DMPC) liposomes we carried out oxygen consumption and ESR measurements.	Dimyristoylphosphatidylcholine	164-168	B cell linker	Homo sapiens	37-54
11386681-4	2001	The use of specific singlet oxygen quenchers (Azide and 9,10-Anthracenedipropionic acid) in ESR and oxygen consumption experiments allowed us to assert that BCA was mainly a type II sensitizer when it was incorporated in DMPC.	Dimyristoylphosphatidylcholine	221-225	B cell linker	Homo sapiens	157-160
11386681-5	2001	Finally, the cell survival of WiDr cells after a PDT treatment was measured for cells incubated with BCA in cell culture medium and cells incubated with BCA in DMPC.	Dimyristoylphosphatidylcholine	160-164	B cell linker	Homo sapiens	153-156
11015229-3	2000	Further, similar conclusions are reached when the ESR spectra of the N-acyl PE spin-labels in dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylethanolamine (DMPE) host matrixes are compared with those of phosphatidylcholine spin-labels in these two lipids.	Dimyristoylphosphatidylcholine	94-124	spindlin 1	Homo sapiens	79-83
11160365-1	2001	The N-terminal 17% of apolipoprotein B (apoB-17) readily associates with dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles (MLV) to form large (240-A diameter) discoidal particles.	Dimyristoylphosphatidylcholine	73-103	apolipoprotein B	Homo sapiens	40-44
11160365-1	2001	The N-terminal 17% of apolipoprotein B (apoB-17) readily associates with dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles (MLV) to form large (240-A diameter) discoidal particles.	Dimyristoylphosphatidylcholine	105-109	apolipoprotein B	Homo sapiens	22-38
11160365-1	2001	The N-terminal 17% of apolipoprotein B (apoB-17) readily associates with dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles (MLV) to form large (240-A diameter) discoidal particles.	Dimyristoylphosphatidylcholine	105-109	apolipoprotein B	Homo sapiens	40-44
11160365-10	2001	When apoB-17 bound to emulsions was incubated with DMPC MLV at 26 degrees C for 18 h, it remained bound to the emulsions, indicating that once bound to these emulsions it is unable to exchange off and solubilize DMPC into discs.	Dimyristoylphosphatidylcholine	51-55	apolipoprotein B	Homo sapiens	5-9
11160365-10	2001	When apoB-17 bound to emulsions was incubated with DMPC MLV at 26 degrees C for 18 h, it remained bound to the emulsions, indicating that once bound to these emulsions it is unable to exchange off and solubilize DMPC into discs.	Dimyristoylphosphatidylcholine	212-216	apolipoprotein B	Homo sapiens	5-9
11160365-1	2001	The N-terminal 17% of apolipoprotein B (apoB-17) readily associates with dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles (MLV) to form large (240-A diameter) discoidal particles.	Dimyristoylphosphatidylcholine	73-103	apolipoprotein B	Homo sapiens	22-38
10921925-3	2000	As shown by (1)H,(13)C heteronuclear single quantum coherence nuclear magnetic resonance, lysine resonances in the lipid-free fragment were poorly resolved over a wide pH range, whereas in apoE3.dimyristoyl phosphatidylcholine (DMPC) discs, the lysine microenvironments and protein conformation were significantly altered.	Dimyristoylphosphatidylcholine	195-226	apolipoprotein E	Homo sapiens	189-194
10921925-6	2000	In apoE3.DMPC complexes, however, all eight lysines were resolved, and the pK(a) values were 9.2-11.1.	Dimyristoylphosphatidylcholine	9-13	apolipoprotein E	Homo sapiens	3-8
10921925-8	2000	Shift reagent experiments with potassium ferricyanide showed that Lys-143 and Lys-146 were much more accessible to the ferricyanide anion in the apoE3.DMPC complex than in the lipid-free state.	Dimyristoylphosphatidylcholine	151-155	apolipoprotein E	Homo sapiens	145-150
10921925-10	2000	This increased exposure and the greater positive electrostatic potential created by interaction with DMPC may explain why lipid association is required for high affinity binding of apoE to the low density lipoprotein receptor.	Dimyristoylphosphatidylcholine	101-105	apolipoprotein E	Homo sapiens	181-185
10921925-10	2000	This increased exposure and the greater positive electrostatic potential created by interaction with DMPC may explain why lipid association is required for high affinity binding of apoE to the low density lipoprotein receptor.	Dimyristoylphosphatidylcholine	101-105	low density lipoprotein receptor	Homo sapiens	193-225
11052821-1	2000	Oncolipin is a multilamellar liposomal (dimyristoyl phosphatidylcholine) formulation of interleukin 2 (IL-2) and human serum albumin (HSA) with distinct surface characteristics which may influence its biological activities.	Dimyristoylphosphatidylcholine	40-71	interleukin 2	Mus musculus	88-101
11052821-1	2000	Oncolipin is a multilamellar liposomal (dimyristoyl phosphatidylcholine) formulation of interleukin 2 (IL-2) and human serum albumin (HSA) with distinct surface characteristics which may influence its biological activities.	Dimyristoylphosphatidylcholine	40-71	interleukin 2	Mus musculus	103-107
11052821-1	2000	Oncolipin is a multilamellar liposomal (dimyristoyl phosphatidylcholine) formulation of interleukin 2 (IL-2) and human serum albumin (HSA) with distinct surface characteristics which may influence its biological activities.	Dimyristoylphosphatidylcholine	40-71	albumin	Mus musculus	119-132
11015229-3	2000	Further, similar conclusions are reached when the ESR spectra of the N-acyl PE spin-labels in dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylethanolamine (DMPE) host matrixes are compared with those of phosphatidylcholine spin-labels in these two lipids.	Dimyristoylphosphatidylcholine	126-130	spindlin 1	Homo sapiens	79-83
10651809-8	2000	In studies of apoLp-III-DMPC disc complexes, far-UV CD spectroscopy revealed an increase in alpha-helix content to approximately 85% and a ninefold increase in the GdnHCl-induced denaturation transition midpoint to 3 M. In studies of lipid interaction, apoLp-III was shown to disrupt both negatively charged and zwitterionic phospholipid bilayer vesicles, transforming them into discoidal complexes.	Dimyristoylphosphatidylcholine	24-28	apolipophorin III	Bombyx mori	14-23
10964416-6	2000	Catalytically, DAGK showed a strong preference for bicelles containing 3-(cholamidopropyl)dimethylammonio-2-hydroxy-1-propanesulfonate (CHAPSO) as the detergentcomponent relative to short-chained phosphatidylcholine.DAGK also exhibited a preference for dimyristoylphosphatidylcholine or dipalmitoylphosphatidylcholine bicelles relative to those of dilauroylphosphatidylcholine.	Dimyristoylphosphatidylcholine	253-283	diacylglycerol kinase alpha	Homo sapiens	15-19
10801877-1	2000	Conformational reorganization of the amino-terminal four-helix bundle (22-kDa fragment) of apolipoprotein E (apoE) in binding to the phospholipid dimyristoylphosphatidylcholine (DMPC) to form discoidal particles was investigated by introducing single, double, and triple interhelical disulfide bonds to restrict the opening of the bundle.	Dimyristoylphosphatidylcholine	178-182	apolipoprotein E	Homo sapiens	91-107
10801877-1	2000	Conformational reorganization of the amino-terminal four-helix bundle (22-kDa fragment) of apolipoprotein E (apoE) in binding to the phospholipid dimyristoylphosphatidylcholine (DMPC) to form discoidal particles was investigated by introducing single, double, and triple interhelical disulfide bonds to restrict the opening of the bundle.	Dimyristoylphosphatidylcholine	178-182	apolipoprotein E	Homo sapiens	109-113
10801877-2	2000	Interaction of apoE with DMPC was assessed by vesicle disruption, turbidimetric clearing, and gel filtration assays.	Dimyristoylphosphatidylcholine	25-29	apolipoprotein E	Homo sapiens	15-19
10801877-3	2000	The results indicate that the formation of apoE.DMPC discoidal particles occurs in a series of steps.	Dimyristoylphosphatidylcholine	48-52	apolipoprotein E	Homo sapiens	43-47
10858447-7	2000	When complexed with dimyristoylphosphatidylcholine, the N-terminal and C-terminal CNBr fragments of apoA-I each bound to SR-BI in a saturable, high affinity manner, and each cross-linked efficiently to mSR-BI.	Dimyristoylphosphatidylcholine	20-50	apolipoprotein A-I	Mus musculus	100-106
10858447-7	2000	When complexed with dimyristoylphosphatidylcholine, the N-terminal and C-terminal CNBr fragments of apoA-I each bound to SR-BI in a saturable, high affinity manner, and each cross-linked efficiently to mSR-BI.	Dimyristoylphosphatidylcholine	20-50	scavenger receptor class B, member 1	Mus musculus	121-126
10858447-7	2000	When complexed with dimyristoylphosphatidylcholine, the N-terminal and C-terminal CNBr fragments of apoA-I each bound to SR-BI in a saturable, high affinity manner, and each cross-linked efficiently to mSR-BI.	Dimyristoylphosphatidylcholine	20-50	scavenger receptor class B, member 1	Mus musculus	202-208
10651809-3	2000	Near-UV CD spectra obtained in buffer or complexed with dimyristoylglycerophosphocholine (DMPC), provided evidence that apoLp-III alpha-helices reorient upon interaction with lipid, indicative of a protein conformational change.	Dimyristoylphosphatidylcholine	56-88	apolipophorin III	Bombyx mori	120-129
10651809-3	2000	Near-UV CD spectra obtained in buffer or complexed with dimyristoylglycerophosphocholine (DMPC), provided evidence that apoLp-III alpha-helices reorient upon interaction with lipid, indicative of a protein conformational change.	Dimyristoylphosphatidylcholine	90-94	apolipophorin III	Bombyx mori	120-129
11012677-5	2000	In contrast, the phase transition temperature of positively charged dimyristoylphosphatidylcholine/sphingosine multilamellar vesicles (molar ratio 9 : 1, respectively) is increased by approximately 2.4 degrees C and the half width of the enthalpy peak broadened from 1.9 to 5.6 degrees C in the presence of P17 (protein : lipid molar ratio 1 : 47).	Dimyristoylphosphatidylcholine	68-98	assembly	Enterobacteria phage PRD1	307-310
10920009-4	2000	Rotational correlation times of 1-2 micros for purified spin-labeled bovine rhodopsin in lipid membranes led to viscosities of 2.2 poise for bilayers of dimyristoylphosphatidylcholine (28 degrees C) and 3.0 poise for the specific mixture of lipids used to reconstitute LacS (30 degrees C).	Dimyristoylphosphatidylcholine	153-183	rhodopsin	Bos taurus	76-85
10751422-2	2000	To this end, we examined the in vitro binding of apoE complexed with dimyristoylphosphatidylcholine (DMPC) to human aortic Bg before and after glycosaminoglycan (GAG) depletion.	Dimyristoylphosphatidylcholine	69-99	apolipoprotein E	Homo sapiens	49-53
10751422-2	2000	To this end, we examined the in vitro binding of apoE complexed with dimyristoylphosphatidylcholine (DMPC) to human aortic Bg before and after glycosaminoglycan (GAG) depletion.	Dimyristoylphosphatidylcholine	69-99	biglycan	Homo sapiens	123-125
10751422-2	2000	To this end, we examined the in vitro binding of apoE complexed with dimyristoylphosphatidylcholine (DMPC) to human aortic Bg before and after glycosaminoglycan (GAG) depletion.	Dimyristoylphosphatidylcholine	101-105	apolipoprotein E	Homo sapiens	49-53
10751422-2	2000	To this end, we examined the in vitro binding of apoE complexed with dimyristoylphosphatidylcholine (DMPC) to human aortic Bg before and after glycosaminoglycan (GAG) depletion.	Dimyristoylphosphatidylcholine	101-105	biglycan	Homo sapiens	123-125
10751422-3	2000	In a solid-phase assay, apoE.DMPC bound to Bg and GAG-depleted protein core in a similar manner, suggesting a protein-protein mode of interaction.	Dimyristoylphosphatidylcholine	29-33	apolipoprotein E	Homo sapiens	24-28
10751422-3	2000	In a solid-phase assay, apoE.DMPC bound to Bg and GAG-depleted protein core in a similar manner, suggesting a protein-protein mode of interaction.	Dimyristoylphosphatidylcholine	29-33	biglycan	Homo sapiens	43-45
10751422-5	2000	A recombinant apoE fragment representing the C-terminal 10-kDa domain, complexed with DMPC, bound as efficiently as full-length apoE, whereas the N-terminal 22-kDa domain was inactive.	Dimyristoylphosphatidylcholine	86-90	apolipoprotein E	Homo sapiens	14-18
23345710-11	2000	Thetheoretical analysis performed shows that a sequence of shapetransformations in the DMPC/NaC mixed systems is determined by thesynergism of four major factors: detergent/lipid ratio, temperature (acylchain melting), DMPC and NaC mixing, and reorientation of NaC molecules inmixed aggregates.	Dimyristoylphosphatidylcholine	87-91	synuclein alpha	Homo sapiens	92-95
23345710-11	2000	Thetheoretical analysis performed shows that a sequence of shapetransformations in the DMPC/NaC mixed systems is determined by thesynergism of four major factors: detergent/lipid ratio, temperature (acylchain melting), DMPC and NaC mixing, and reorientation of NaC molecules inmixed aggregates.	Dimyristoylphosphatidylcholine	87-91	synuclein alpha	Homo sapiens	228-231
23345710-11	2000	Thetheoretical analysis performed shows that a sequence of shapetransformations in the DMPC/NaC mixed systems is determined by thesynergism of four major factors: detergent/lipid ratio, temperature (acylchain melting), DMPC and NaC mixing, and reorientation of NaC molecules inmixed aggregates.	Dimyristoylphosphatidylcholine	87-91	synuclein alpha	Homo sapiens	228-231
23345710-11	2000	Thetheoretical analysis performed shows that a sequence of shapetransformations in the DMPC/NaC mixed systems is determined by thesynergism of four major factors: detergent/lipid ratio, temperature (acylchain melting), DMPC and NaC mixing, and reorientation of NaC molecules inmixed aggregates.	Dimyristoylphosphatidylcholine	219-223	synuclein alpha	Homo sapiens	92-95
10651809-8	2000	In studies of apoLp-III-DMPC disc complexes, far-UV CD spectroscopy revealed an increase in alpha-helix content to approximately 85% and a ninefold increase in the GdnHCl-induced denaturation transition midpoint to 3 M. In studies of lipid interaction, apoLp-III was shown to disrupt both negatively charged and zwitterionic phospholipid bilayer vesicles, transforming them into discoidal complexes.	Dimyristoylphosphatidylcholine	24-28	apolipophorin III	Bombyx mori	253-262
10651809-9	2000	Characterization of apoLp-III-DMPC discs, using 5-doxyl or 12-doxyl stearic acid as lipid-based quenching agents, revealed that Trp40 localizes near the phospholipid polar head groups.	Dimyristoylphosphatidylcholine	30-34	apolipophorin III	Bombyx mori	20-29
10651809-10	2000	KSV values for acrylamide and KI quenching of intrinsic fluorescence of apoLp-III-DMPC discs indicate that Trp40 is embedded in the lipid milieu, with little or no accessibility to the aqueous quenchers.	Dimyristoylphosphatidylcholine	82-86	apolipophorin III	Bombyx mori	72-81
11081405-7	2000	Based on the optimum position determined from the continuum solvent model, two atomic models of the PGHS-1 anchoring domain associated with an explicit dimyristoylphosphatidylcholine (DMPC) bilayer differing by the thickness of the membrane bilayer were constructed.	Dimyristoylphosphatidylcholine	152-182	prostaglandin-endoperoxide synthase 1	Homo sapiens	100-106
11081405-7	2000	Based on the optimum position determined from the continuum solvent model, two atomic models of the PGHS-1 anchoring domain associated with an explicit dimyristoylphosphatidylcholine (DMPC) bilayer differing by the thickness of the membrane bilayer were constructed.	Dimyristoylphosphatidylcholine	184-188	prostaglandin-endoperoxide synthase 1	Homo sapiens	100-106
11081405-11	2000	The phosphate headgroup of one DMPC molecule disposed at the center of the spiral formed by helices A, B, C and D interacts strongly with Arg120, a residue on helix D that has previously been identified as being important in the activity of PGHS-1.	Dimyristoylphosphatidylcholine	31-35	prostaglandin-endoperoxide synthase 1	Homo sapiens	241-247
10479618-3	1999	After dialysis of detergent-solubilized porin in the presence of dimyristoylphosphatidylcholine at lipid-to-protein ratios between 0.2 and 0.5 (percentage by weight), mostly multilamellar crystals were obtained.	Dimyristoylphosphatidylcholine	65-95	voltage dependent anion channel 1	Homo sapiens	40-45
10543393-4	1999	Normal apoA-I and apoA-I(R151C)Paris cleared DMPC emulsions at equal rates.	Dimyristoylphosphatidylcholine	45-49	apolipoprotein A-I	Mus musculus	7-13
10543393-4	1999	Normal apoA-I and apoA-I(R151C)Paris cleared DMPC emulsions at equal rates.	Dimyristoylphosphatidylcholine	45-49	apolipoprotein A-I	Mus musculus	18-24
10600503-3	1999	In contrast with caveolin-1, a component of GEMs that requires cholesterol for its integration into artificial membranes, MAL incorporation took place with dimyristoylphosphatidylcholine as the only lipid component.	Dimyristoylphosphatidylcholine	156-186	mal, T cell differentiation protein	Canis lupus familiaris	122-125
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
10587458-5	1999	The electron spin resonance (ESR) spectrum of N-biotinyl phosphatidylethanolamine spin-labeled at the C-14 position of the sn-2 chain consists of two components in fluid-phase membranes of dimyristoylphosphatidylcholine containing the proteolipid.	Dimyristoylphosphatidylcholine	189-219	spindlin 1	Homo sapiens	13-17
10587458-5	1999	The electron spin resonance (ESR) spectrum of N-biotinyl phosphatidylethanolamine spin-labeled at the C-14 position of the sn-2 chain consists of two components in fluid-phase membranes of dimyristoylphosphatidylcholine containing the proteolipid.	Dimyristoylphosphatidylcholine	189-219	spindlin 1	Homo sapiens	82-86
10103046-6	1999	In calorimetric assays, using lipid vesicles of mixed DMPC/DMPG, increasing PR3 concentrations (protein/lipid molar ratio from 0 to 1 : 110) induced a significant decrease of the main chain transition enthalpy and a shift in chain melting temperatures which is indicative of partial insertion of PR3 into the hydrophobic region of the lipid membranes.	Dimyristoylphosphatidylcholine	54-58	proteinase 3	Homo sapiens	76-79
10103046-8	1999	The molar affinity of PR3, HNE, and MPO to lipid vesicles of different DMPC/DMPG ratios was then determined by spectrophotometry.	Dimyristoylphosphatidylcholine	71-75	proteinase 3	Homo sapiens	22-25
10103046-4	1999	We investigated the interaction of purified human PR3 with mixtures of zwitterionic (dimyristoyl-L-alpha-phosphatidylcholine, DMPC) and anionic (dimyristoyl-L-alpha-phosphatidylglycerol, DMPG) phospholipids in reconstituted lipid bilayers using differential scanning calorimetry and lipid photolabeling, and measured the affinity of this interaction using spectrophotometry.	Dimyristoylphosphatidylcholine	126-130	proteinase 3	Homo sapiens	50-53
10103046-8	1999	The molar affinity of PR3, HNE, and MPO to lipid vesicles of different DMPC/DMPG ratios was then determined by spectrophotometry.	Dimyristoylphosphatidylcholine	71-75	myeloperoxidase	Homo sapiens	36-39
10103046-9	1999	At a DMPC/DMPG ratio of 1 : 1, molar affinities of PR3, Kd = 4.5 +/- 0.3 microm; HNE, 14.5 +/- 1.2 microm; and MPO, 50 +/- 5 microm (n = 3) were estimated.	Dimyristoylphosphatidylcholine	5-9	proteinase 3	Homo sapiens	51-54
10064737-4	1999	However, both apoA-I(P165R) and apoA-I(R160L)Oslo showed a reduced capacity to clear a turbid emulsion of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	106-136	apolipoprotein A-I	Mus musculus	14-20
10064737-4	1999	However, both apoA-I(P165R) and apoA-I(R160L)Oslo showed a reduced capacity to clear a turbid emulsion of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	106-136	apolipoprotein A-I	Mus musculus	14-19
10080109-5	1999	The critical mole ratio of unionized CFX:DMPC, Rec, for solubilization was estimated to be 0.12.	Dimyristoylphosphatidylcholine	41-45	RBPJ pseudogene 4	Homo sapiens	47-50
10064737-4	1999	However, both apoA-I(P165R) and apoA-I(R160L)Oslo showed a reduced capacity to clear a turbid emulsion of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	138-142	apolipoprotein A-I	Mus musculus	14-20
10064737-4	1999	However, both apoA-I(P165R) and apoA-I(R160L)Oslo showed a reduced capacity to clear a turbid emulsion of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	138-142	apolipoprotein A-I	Mus musculus	14-19
10357263-9	1999	The amount of fibrinogen adsorbed on every MAPC polymer surface was reduced by addition of the DMPC liposome in the fibrinogen solution.	Dimyristoylphosphatidylcholine	95-99	fibrinogen beta chain	Homo sapiens	14-24
9929493-1	1999	Lipid activation of protein kinase C alpha (PKC alpha) was studied by using a model mixture containing 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 1, 2-dimyristoyl-sn-glycero-3-phosphoserine (DMPS), and 1, 2-dimyristoyl-sn-glycerol (1,2-DMG).	Dimyristoylphosphatidylcholine	103-147	protein kinase C alpha	Homo sapiens	20-42
9929493-1	1999	Lipid activation of protein kinase C alpha (PKC alpha) was studied by using a model mixture containing 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 1, 2-dimyristoyl-sn-glycero-3-phosphoserine (DMPS), and 1, 2-dimyristoyl-sn-glycerol (1,2-DMG).	Dimyristoylphosphatidylcholine	103-147	protein kinase C alpha	Homo sapiens	44-53
9929493-1	1999	Lipid activation of protein kinase C alpha (PKC alpha) was studied by using a model mixture containing 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 1, 2-dimyristoyl-sn-glycero-3-phosphoserine (DMPS), and 1, 2-dimyristoyl-sn-glycerol (1,2-DMG).	Dimyristoylphosphatidylcholine	149-153	protein kinase C alpha	Homo sapiens	20-42
9929493-1	1999	Lipid activation of protein kinase C alpha (PKC alpha) was studied by using a model mixture containing 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 1, 2-dimyristoyl-sn-glycero-3-phosphoserine (DMPS), and 1, 2-dimyristoyl-sn-glycerol (1,2-DMG).	Dimyristoylphosphatidylcholine	149-153	protein kinase C alpha	Homo sapiens	44-53
9929495-5	1999	In the Lalpha phase near full hydration, PtP is 30.8 A for pure DLPC, 32.1 A for the DLPC/gD mixture, 35.3 A for pure DMPC, and 32.7 A for the DMPC/gD mixture.	Dimyristoylphosphatidylcholine	118-122	protein tyrosine phosphatase receptor type U	Homo sapiens	41-44
9929495-5	1999	In the Lalpha phase near full hydration, PtP is 30.8 A for pure DLPC, 32.1 A for the DLPC/gD mixture, 35.3 A for pure DMPC, and 32.7 A for the DMPC/gD mixture.	Dimyristoylphosphatidylcholine	143-147	protein tyrosine phosphatase receptor type U	Homo sapiens	41-44
9925654-4	1999	dimyristoylphosphatidylcholine displayed a defective binding to the low density lipoprotein (LDL) receptor.	Dimyristoylphosphatidylcholine	0-30	low density lipoprotein receptor	Homo sapiens	68-106
10505789-3	1999	Purified Thy-1 was reconstituted into lipid bilayer vesicles of dimyristoyl-phosphatidylcholine (DMPC) alone or in combination with galactosylceramide (GC).	Dimyristoylphosphatidylcholine	64-95	Thy-1 cell surface antigen	Homo sapiens	9-14
10505789-3	1999	Purified Thy-1 was reconstituted into lipid bilayer vesicles of dimyristoyl-phosphatidylcholine (DMPC) alone or in combination with galactosylceramide (GC).	Dimyristoylphosphatidylcholine	97-101	Thy-1 cell surface antigen	Homo sapiens	9-14
10505789-4	1999	The ability of Thy-1 to perturb the gel to a liquid-crystalline phase transition of DMPC was examined by differential scanning calorimetry.	Dimyristoylphosphatidylcholine	84-88	Thy-1 cell surface antigen	Homo sapiens	15-20
10357263-9	1999	The amount of fibrinogen adsorbed on every MAPC polymer surface was reduced by addition of the DMPC liposome in the fibrinogen solution.	Dimyristoylphosphatidylcholine	95-99	fibrinogen beta chain	Homo sapiens	116-126
10357263-10	1999	The number of platelets adhered on the MAPC polymer was also decreased when the DMPC liposome was present in the fibrinogen solution during pretreatment.	Dimyristoylphosphatidylcholine	80-84	fibrinogen beta chain	Homo sapiens	113-123
9774231-8	1998	The superactive analog des-Gly10[D-Trp6,Pro9-NHEt]GnRH exhibited the ability to transport Ca2+ ions across large unilamellar vesicles of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	137-167	transient receptor potential cation channel subfamily C member 6	Homo sapiens	35-39
9869654-8	1999	Interaction of AEDANS-apoE3(1-183) with dimyristoylphosphatidylcholine to form disk particles, or with detergent micelles, resulted in large decreases in the efficiency of energy transfer.	Dimyristoylphosphatidylcholine	40-70	apolipoprotein E	Homo sapiens	22-27
9826612-1	1998	The change in vertical location of spin-labeled N-biotinyl phosphatidylethanolamine in fluid-phase dimyristoyl phosphatidylcholine bilayer membranes, on binding avidin to the biotinyl headgroup, has been investigated by progressive saturation electron spin resonance measurements.	Dimyristoylphosphatidylcholine	99-130	spindlin 1	Homo sapiens	35-39
10472056-4	1999	In the fluid phase near full hydration, PtP is 30.8 A for pure DLPC, 32.1 A for DLPC/gramicidin mixture, 35.3 A for pure DMPC and 32.7 A for a DMPC/gramicidin mixture.	Dimyristoylphosphatidylcholine	121-125	protein tyrosine phosphatase receptor type U	Homo sapiens	40-43
10472056-4	1999	In the fluid phase near full hydration, PtP is 30.8 A for pure DLPC, 32.1 A for DLPC/gramicidin mixture, 35.3 A for pure DMPC and 32.7 A for a DMPC/gramicidin mixture.	Dimyristoylphosphatidylcholine	143-147	protein tyrosine phosphatase receptor type U	Homo sapiens	40-43
9826613-6	1998	However, alpha-tocopherol has a dramatic inhibitory effect on the rate of association of apolipoprotein A-I with dimyristoylphosphatidylcholine, a process that occurs through the insertion of the protein into preformed defects in the lipid surface.	Dimyristoylphosphatidylcholine	113-143	apolipoprotein A1	Homo sapiens	89-107
9826613-7	1998	It is proposed that alpha-tocopherol inhibits the rate of association of apolipoprotein A-I with dimyristoylphosphatidylcholine by inserting into defects within the lipid surface, thereby reducing the size and/or number of sites for insertion of apolipoprotein A-I.	Dimyristoylphosphatidylcholine	97-127	apolipoprotein A1	Homo sapiens	73-91
9826613-7	1998	It is proposed that alpha-tocopherol inhibits the rate of association of apolipoprotein A-I with dimyristoylphosphatidylcholine by inserting into defects within the lipid surface, thereby reducing the size and/or number of sites for insertion of apolipoprotein A-I.	Dimyristoylphosphatidylcholine	97-127	apolipoprotein A1	Homo sapiens	246-264
9774231-8	1998	The superactive analog des-Gly10[D-Trp6,Pro9-NHEt]GnRH exhibited the ability to transport Ca2+ ions across large unilamellar vesicles of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	137-167	gonadotropin releasing hormone 1	Homo sapiens	50-54
9548943-5	1998	However, upon the insertion of the negatively charged lipid DMPG at 1:1 molar ratio into the DMPC bilayers, myosin was found to interact electrostatically with the liposomes, thereby affecting significantly both the quadrupole splittings and spin-lattice relaxation rates of the alpha-, beta-, and gamma-deuterons in labeled DMPC.	Dimyristoylphosphatidylcholine	93-97	myosin heavy chain 14	Homo sapiens	108-114
9733956-9	1998	Involvement of electrostatic attraction between the acidic phosphate of DMPG and cationic residues in apoB is suggested by the finding that increasing the content of dimyristoylphosphatidylcholine (DMPC) in DMPG liposomes reduced their aggregation and at XDMPC=0.50 no response was evident.	Dimyristoylphosphatidylcholine	166-196	apolipoprotein B	Homo sapiens	102-106
9733956-9	1998	Involvement of electrostatic attraction between the acidic phosphate of DMPG and cationic residues in apoB is suggested by the finding that increasing the content of dimyristoylphosphatidylcholine (DMPC) in DMPG liposomes reduced their aggregation and at XDMPC=0.50 no response was evident.	Dimyristoylphosphatidylcholine	198-202	apolipoprotein B	Homo sapiens	102-106
9685717-1	1998	The linoleic acids embedded in the SUVs of soy-PC, DMPC, and DPPC served as substrate for soybean lipoxygenase-1 (L-1).	Dimyristoylphosphatidylcholine	51-55	seed linoleate 13S-lipoxygenase-1	Glycine max	98-112
9685717-1	1998	The linoleic acids embedded in the SUVs of soy-PC, DMPC, and DPPC served as substrate for soybean lipoxygenase-1 (L-1).	Dimyristoylphosphatidylcholine	51-55	seed linoleate 13S-lipoxygenase-1	Glycine max	114-117
9685717-3	1998	The Km values of L-1 for the linoleic acids in soy-PC, DMPC, and DPPC vesicles were 0.07, 0.09, and 0.11 mM, respectively, being comparable with that for Tween-20 micellar linoleic acid.	Dimyristoylphosphatidylcholine	55-59	seed linoleate 13S-lipoxygenase-1	Glycine max	17-20
9548943-6	1998	Monitoring DMPG-d5 in mixed DMPC/DMPG bilayers revealed a direct electrostatic interaction of DMPG with the protein, where positively charged lysine residues located at the tail domain of myosin provide the necessary sites for the interaction to occur.	Dimyristoylphosphatidylcholine	28-32	myosin heavy chain 14	Homo sapiens	188-194
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
9699892-4	1998	Here we have investigated whether purified plasma apo E, complexed with dimyristoyl phosphatidylcholine (DMPC) vesicles, can inhibit cytokine-induced vascular cell adhesion molecule-1 (VCAM-1) expression in human umbilical vein endothelial cells (HUVECs).	Dimyristoylphosphatidylcholine	72-103	apolipoprotein E	Homo sapiens	50-55
9699892-4	1998	Here we have investigated whether purified plasma apo E, complexed with dimyristoyl phosphatidylcholine (DMPC) vesicles, can inhibit cytokine-induced vascular cell adhesion molecule-1 (VCAM-1) expression in human umbilical vein endothelial cells (HUVECs).	Dimyristoylphosphatidylcholine	72-103	vascular cell adhesion molecule 1	Homo sapiens	150-183
9699892-4	1998	Here we have investigated whether purified plasma apo E, complexed with dimyristoyl phosphatidylcholine (DMPC) vesicles, can inhibit cytokine-induced vascular cell adhesion molecule-1 (VCAM-1) expression in human umbilical vein endothelial cells (HUVECs).	Dimyristoylphosphatidylcholine	72-103	vascular cell adhesion molecule 1	Homo sapiens	185-191
9699892-4	1998	Here we have investigated whether purified plasma apo E, complexed with dimyristoyl phosphatidylcholine (DMPC) vesicles, can inhibit cytokine-induced vascular cell adhesion molecule-1 (VCAM-1) expression in human umbilical vein endothelial cells (HUVECs).	Dimyristoylphosphatidylcholine	105-109	apolipoprotein E	Homo sapiens	50-55
9699892-4	1998	Here we have investigated whether purified plasma apo E, complexed with dimyristoyl phosphatidylcholine (DMPC) vesicles, can inhibit cytokine-induced vascular cell adhesion molecule-1 (VCAM-1) expression in human umbilical vein endothelial cells (HUVECs).	Dimyristoylphosphatidylcholine	105-109	vascular cell adhesion molecule 1	Homo sapiens	150-183
9699892-4	1998	Here we have investigated whether purified plasma apo E, complexed with dimyristoyl phosphatidylcholine (DMPC) vesicles, can inhibit cytokine-induced vascular cell adhesion molecule-1 (VCAM-1) expression in human umbilical vein endothelial cells (HUVECs).	Dimyristoylphosphatidylcholine	105-109	vascular cell adhesion molecule 1	Homo sapiens	185-191
9699892-6	1998	However, preincubations with physiological concentrations (10-100 microg protein/ml) of apo E DMPC did not downregulate VCAM-1 expression, even with extended preincubation times.	Dimyristoylphosphatidylcholine	94-98	apolipoprotein E	Homo sapiens	88-93
9643348-6	1998	ApoE-Leiden and its truncated variants formed larger DMPC discs than did intact or truncated apoE3 or apoE2.	Dimyristoylphosphatidylcholine	53-57	apolipoprotein E	Homo sapiens	0-4
9548943-5	1998	However, upon the insertion of the negatively charged lipid DMPG at 1:1 molar ratio into the DMPC bilayers, myosin was found to interact electrostatically with the liposomes, thereby affecting significantly both the quadrupole splittings and spin-lattice relaxation rates of the alpha-, beta-, and gamma-deuterons in labeled DMPC.	Dimyristoylphosphatidylcholine	325-329	myosin heavy chain 14	Homo sapiens	108-114
9490006-3	1998	Bovine rhodopsin containing 11-cis retinal, specifically deuterated at its methyl groups at the C19 or C20 position, was uniaxially oriented in DMPC bilayers.	Dimyristoylphosphatidylcholine	144-148	rhodopsin	Bos taurus	7-16
9535703-13	1998	Recombinant apoA-I was shown to be functional in lipoprotein binding as well as to possess an ability to transform bilayer vesicles of dimyristoylphosphatidylcholine into discoidal complexes.	Dimyristoylphosphatidylcholine	135-165	apolipoprotein AI	Gallus gallus	12-18
9548597-7	1998	LDL receptor binding activities were studied using recombinant apoE loaded to dimyristoylphosphatidylcholine (DMPC) vesicles and to VLDL and from an apoE-deficient individual.	Dimyristoylphosphatidylcholine	78-108	low density lipoprotein receptor	Homo sapiens	0-12
9548597-7	1998	LDL receptor binding activities were studied using recombinant apoE loaded to dimyristoylphosphatidylcholine (DMPC) vesicles and to VLDL and from an apoE-deficient individual.	Dimyristoylphosphatidylcholine	110-114	low density lipoprotein receptor	Homo sapiens	0-12
9144088-4	1997	DMPC, but not BBSM, also generated particles with mobility similar to pre beta(2)-HDL; These species were demonstrably different from the discoidal complexes formed by reaction of DMPC with purified apoA-I.	Dimyristoylphosphatidylcholine	0-4	APOAI	Bos taurus	199-205
9442017-5	1998	Importantly, PtdIns(3,4,5)P3, but not PtdIns(4,5)P2, markedly enhances the ARF exchange activity of GRP1 in a reaction mixture containing dimyristoylphosphatidylcholine micelles, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid, and a low concentration of sodium cholate.	Dimyristoylphosphatidylcholine	138-168	Rud3p	Saccharomyces cerevisiae S288C	100-104
9505319-2	1998	We prepared various kinds of IL-2-containing liposomes made by the hydration of powdered dimyristoyl-phosphatidylcholine with aqueous recombinant IL-2 followed by the combination with galactose residues to facilitate the selective uptake by liver parenchymal cells bearing galactose receptors.	Dimyristoylphosphatidylcholine	89-120	interleukin 2	Mus musculus	29-33
9315611-1	1997	Binding and localization of the vasodilator and antitumor drug coactivator dipyridamole (DIP) and one of its derivatives, RA25, to phospholipid vesicles of DMPC (dimyristoylphosphatidylcholine) and DPPC (dipalmitoylphosphatidylcholine) was studied using fluorescence spectroscopy as well as quenching of fluorescence.	Dimyristoylphosphatidylcholine	156-160	RA25	Homo sapiens	122-126
9315611-1	1997	Binding and localization of the vasodilator and antitumor drug coactivator dipyridamole (DIP) and one of its derivatives, RA25, to phospholipid vesicles of DMPC (dimyristoylphosphatidylcholine) and DPPC (dipalmitoylphosphatidylcholine) was studied using fluorescence spectroscopy as well as quenching of fluorescence.	Dimyristoylphosphatidylcholine	162-192	RA25	Homo sapiens	122-126
9321809-3	1997	DMPC/apoA-1 but not apoA-1 alone or DMPC alone was found to suppress both impairment of endothelium-dependent arterial relaxation and vasocontraction caused by ox-LDL in the isolated porcine coronary arterial rings suspended in organ chambers.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein A1	Homo sapiens	5-11
9321809-4	1997	DMPC/apoA-1 absorbed lysophosphatidylcholine (LPC) from ox-LDL and decreased the transfer of LPC from ox-LDL to the surface membrane of the cultured endothelial cells, but apoA-1 alone and DMPC alone had no effect.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein A1	Homo sapiens	5-11
9321809-4	1997	DMPC/apoA-1 absorbed lysophosphatidylcholine (LPC) from ox-LDL and decreased the transfer of LPC from ox-LDL to the surface membrane of the cultured endothelial cells, but apoA-1 alone and DMPC alone had no effect.	Dimyristoylphosphatidylcholine	0-4	apolipoprotein A1	Homo sapiens	172-178
9211897-3	1997	HDL and dimyristoyl phosphatidylcholine binding assays using the variant apoA-I forms have shown that replacement of specific carboxyl-terminal hydrophobic residues Leu222, Phe225, and Phe229 with lysines, as well as replacement of Leu211, Leu214, Leu218, and Leu219 with valines, diminished the ability of apoA-I to bind to HDL and to lyse dimyristoyl phosphatidylcholine liposomes.	Dimyristoylphosphatidylcholine	8-39	apolipoprotein A1	Homo sapiens	73-79
9492317-7	1998	1H-NMR selective line broadening was apparent for several of the angiotensin II protons upon titration of an aqueous sample with less than stoichiometric amounts of 1,2-dimyristoyl-sn-glycero-3-phosphocholine bilayer vesicles.	Dimyristoylphosphatidylcholine	165-208	angiotensinogen	Homo sapiens	65-79
9369499-1	1997	To analyze whether specific protein-lipid interactions or physical features of the membrane contribute to cytochrome P450SCC (CYP11A1) activation by lipids, dimyristoylphosphatidylcholine/cardiolipin and dimyristoylphosphatidylcholine/branched phosphatidylcholine vesicles of defined acyl chain structure were studied for their ability to stimulate the side chain cleavage activity of the enzyme.	Dimyristoylphosphatidylcholine	157-187	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	126-133
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
8995232-9	1997	Direct confirmation that apoE stimulates NO synthase was obtained by use of L-[3H]arginine; platelets pretreated with apoE x DMPC produced markedly more L-[3H]citrulline (0.71 +/- 0.1 pmol/h/10(9) platelets) than controls (0.18 +/- 0.03; p < 0.05).	Dimyristoylphosphatidylcholine	125-129	apolipoprotein E	Homo sapiens	25-29
9048564-5	1997	Kinetics of association of these proteins with DMPC are similar for delta (100-143) and Rec.-apoA-I (t 1/2 of 4.0 and 4.4 min, respectively) but appear significantly reduced for delta (122-165) and delta (144-186) (t 1/2 of 7.5 and 6.9 min, respectively).	Dimyristoylphosphatidylcholine	47-51	apolipoprotein A1	Homo sapiens	93-99
8995232-3	1997	Here we show that purified apoE (10-50 microg/ml), complexed with phospholipid vesicles (dimyristoylphosphatidylcholine, DMPC), suppresses platelet aggregation induced by ADP, epinephrine, or collagen.	Dimyristoylphosphatidylcholine	89-119	apolipoprotein E	Homo sapiens	27-31
8995232-9	1997	Direct confirmation that apoE stimulates NO synthase was obtained by use of L-[3H]arginine; platelets pretreated with apoE x DMPC produced markedly more L-[3H]citrulline (0.71 +/- 0.1 pmol/h/10(9) platelets) than controls (0.18 +/- 0.03; p < 0.05).	Dimyristoylphosphatidylcholine	125-129	apolipoprotein E	Homo sapiens	118-122
8995232-3	1997	Here we show that purified apoE (10-50 microg/ml), complexed with phospholipid vesicles (dimyristoylphosphatidylcholine, DMPC), suppresses platelet aggregation induced by ADP, epinephrine, or collagen.	Dimyristoylphosphatidylcholine	121-125	apolipoprotein E	Homo sapiens	27-31
8995232-4	1997	This effect was not due to sequestration of cholesterol from platelet membranes; apoE x DMPC chemically modified with cyclohexanedione (cyclohexanedione-apoE x DMPC) did not inhibit aggregation but nevertheless removed similar amounts of cholesterol as untreated complexes, about 2% during the aggregation period.	Dimyristoylphosphatidylcholine	88-92	apolipoprotein E	Homo sapiens	81-85
8995232-4	1997	This effect was not due to sequestration of cholesterol from platelet membranes; apoE x DMPC chemically modified with cyclohexanedione (cyclohexanedione-apoE x DMPC) did not inhibit aggregation but nevertheless removed similar amounts of cholesterol as untreated complexes, about 2% during the aggregation period.	Dimyristoylphosphatidylcholine	88-92	apolipoprotein E	Homo sapiens	153-157
8995232-4	1997	This effect was not due to sequestration of cholesterol from platelet membranes; apoE x DMPC chemically modified with cyclohexanedione (cyclohexanedione-apoE x DMPC) did not inhibit aggregation but nevertheless removed similar amounts of cholesterol as untreated complexes, about 2% during the aggregation period.	Dimyristoylphosphatidylcholine	160-164	apolipoprotein E	Homo sapiens	153-157
8995232-6	1997	Thus, apoE x DMPC markedly increased cGMP in ADP-stimulated platelets which correlated with the resulting inhibition of aggregation (r = 0.85; p < 0.01, n = 10), whereas cyclohexanedione-apoE x DMPC vesicles had no effect.	Dimyristoylphosphatidylcholine	13-17	apolipoprotein E	Homo sapiens	6-10
8995232-6	1997	Thus, apoE x DMPC markedly increased cGMP in ADP-stimulated platelets which correlated with the resulting inhibition of aggregation (r = 0.85; p < 0.01, n = 10), whereas cyclohexanedione-apoE x DMPC vesicles had no effect.	Dimyristoylphosphatidylcholine	13-17	apolipoprotein E	Homo sapiens	190-194
12232625-4	1996	The induction intensity of different kinds of lipids on colicin E(1) was in the following order: DMPG>DMPE>DMPC.	Dimyristoylphosphatidylcholine	113-117	small nucleolar RNA, H/ACA box 73A	Homo sapiens	64-68
8995232-6	1997	Thus, apoE x DMPC markedly increased cGMP in ADP-stimulated platelets which correlated with the resulting inhibition of aggregation (r = 0.85; p < 0.01, n = 10), whereas cyclohexanedione-apoE x DMPC vesicles had no effect.	Dimyristoylphosphatidylcholine	197-201	apolipoprotein E	Homo sapiens	6-10
9511970-7	1997	The C2-C1-O11-P fragment of the DMPC head group (theta1, alpha1, alpha2 torsions) is rigid while the P-O12-C11-C12 fragment (alpha3, alpha4, alpha5 torsions) is flexible.	Dimyristoylphosphatidylcholine	32-36	immunoglobulin binding protein 1	Homo sapiens	133-139
8703980-1	1996	Neurotensin derivatives having a dioctadecyl group were synthesized and immobilized on DMPC liposome to construct a multivalent-ligand system.	Dimyristoylphosphatidylcholine	87-91	neurotensin	Homo sapiens	0-11
8829604-1	1996	Complexes of alpha-lactalbumin (alpha-LA)1 with dimyristoylphosphatidylcholine (DMPC) or dipalmitoylphosphatidylcholine (DPPC) liposomes at pH 8 and at pH 2 have been obtained by means of gel filtration.	Dimyristoylphosphatidylcholine	48-78	lactalbumin alpha	Homo sapiens	13-30
8829604-1	1996	Complexes of alpha-lactalbumin (alpha-LA)1 with dimyristoylphosphatidylcholine (DMPC) or dipalmitoylphosphatidylcholine (DPPC) liposomes at pH 8 and at pH 2 have been obtained by means of gel filtration.	Dimyristoylphosphatidylcholine	80-84	lactalbumin alpha	Homo sapiens	13-30
9054055-3	1996	Here we demonstrate that platelet cholesterol depletion is an improbable explanation for the suppressive effect of apoE:DMPC on ADP-mediated platelet aggregation; only 0.5% of cholesterol was released prior to addition of ADP to initiate aggregation while lactoferrin, which does not accept cellular cholesterol, was also inhibitory.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein E	Homo sapiens	115-119
8620350-10	1996	Differential scanning calorimetry (DSC) studies showed that on a molar basis, apo A-I is about 10 times more effective than the most effective peptide analyzed in reducing the enthalpy of the gel-to-liquid crystalline phase transition of DMPC MLVs.	Dimyristoylphosphatidylcholine	238-242	apolipoprotein A1	Homo sapiens	78-85
8906881-1	1996	We present here results on 260 pico seconds (ps) molecular dynamics (MD) simulation of substance P (SP) in hydrated bilayer of dimyristoyl phosphatidyl choline (DMPC) (39 molecules of DMPC with 776 water molecules).	Dimyristoylphosphatidylcholine	127-159	tachykinin precursor 1	Homo sapiens	87-98
8906881-1	1996	We present here results on 260 pico seconds (ps) molecular dynamics (MD) simulation of substance P (SP) in hydrated bilayer of dimyristoyl phosphatidyl choline (DMPC) (39 molecules of DMPC with 776 water molecules).	Dimyristoylphosphatidylcholine	127-159	tachykinin precursor 1	Homo sapiens	100-102
8906881-1	1996	We present here results on 260 pico seconds (ps) molecular dynamics (MD) simulation of substance P (SP) in hydrated bilayer of dimyristoyl phosphatidyl choline (DMPC) (39 molecules of DMPC with 776 water molecules).	Dimyristoylphosphatidylcholine	161-165	tachykinin precursor 1	Homo sapiens	87-98
8906881-1	1996	We present here results on 260 pico seconds (ps) molecular dynamics (MD) simulation of substance P (SP) in hydrated bilayer of dimyristoyl phosphatidyl choline (DMPC) (39 molecules of DMPC with 776 water molecules).	Dimyristoylphosphatidylcholine	161-165	tachykinin precursor 1	Homo sapiens	100-102
8906881-1	1996	We present here results on 260 pico seconds (ps) molecular dynamics (MD) simulation of substance P (SP) in hydrated bilayer of dimyristoyl phosphatidyl choline (DMPC) (39 molecules of DMPC with 776 water molecules).	Dimyristoylphosphatidylcholine	184-188	tachykinin precursor 1	Homo sapiens	87-98
8808496-2	1996	Analyses of re-isolated ox-LDL showed that apo A-I was transferred from DMPC/apo A-I to ox-LDL, which accounted for 10% of the total protein of ox-LDL.	Dimyristoylphosphatidylcholine	72-76	apolipoprotein A-I	Mus musculus	43-50
8808496-2	1996	Analyses of re-isolated ox-LDL showed that apo A-I was transferred from DMPC/apo A-I to ox-LDL, which accounted for 10% of the total protein of ox-LDL.	Dimyristoylphosphatidylcholine	72-76	apolipoprotein A-I	Mus musculus	77-84
8889194-5	1996	From the decay of the fluorescence anisotropy in spherical bilayers of DMPC and POPC it is shown that t-COPA also correctly reflects the lipid order parameters, determined by 2H NMR techniques.	Dimyristoylphosphatidylcholine	71-75	COPI coat complex subunit alpha	Homo sapiens	104-108
8827524-6	1996	ProapoA-I self associated, interacted with dimyristoyl phosphatidylcholine vesicles, and formed secondary structures very similar to the lipid-free apoA-I.	Dimyristoylphosphatidylcholine	43-74	apolipoprotein A1	Homo sapiens	3-9
9231332-1	1996	A multivalent ligand system was constructed by coimmobilization of two kinds of peptide ligands, enkephalin and neurotensin derivatives having a dioctadecyl group, on dimyristoylphosphatidylcholine (DMPC) liposomes.	Dimyristoylphosphatidylcholine	167-197	neurotensin	Homo sapiens	112-123
9231332-1	1996	A multivalent ligand system was constructed by coimmobilization of two kinds of peptide ligands, enkephalin and neurotensin derivatives having a dioctadecyl group, on dimyristoylphosphatidylcholine (DMPC) liposomes.	Dimyristoylphosphatidylcholine	199-203	neurotensin	Homo sapiens	112-123
9231332-8	1996	Neurotensin derivatives coimmobilized with large amounts of Enk3D on the DMPC liposomes show higher affinity than the neurotensin derivatives immobilized alone.	Dimyristoylphosphatidylcholine	73-77	neurotensin	Homo sapiens	0-11
9231332-8	1996	Neurotensin derivatives coimmobilized with large amounts of Enk3D on the DMPC liposomes show higher affinity than the neurotensin derivatives immobilized alone.	Dimyristoylphosphatidylcholine	73-77	neurotensin	Homo sapiens	118-129
8819172-1	1996	alpha-Lactalbumin (alpha-LA) associates with dimyristoylphosphatidylcholine (DMPC) or egg lecithin (EPC) liposomes.	Dimyristoylphosphatidylcholine	45-75	lactalbumin alpha	Homo sapiens	0-17
8819172-1	1996	alpha-Lactalbumin (alpha-LA) associates with dimyristoylphosphatidylcholine (DMPC) or egg lecithin (EPC) liposomes.	Dimyristoylphosphatidylcholine	45-75	lactalbumin alpha	Homo sapiens	19-27
8819172-1	1996	alpha-Lactalbumin (alpha-LA) associates with dimyristoylphosphatidylcholine (DMPC) or egg lecithin (EPC) liposomes.	Dimyristoylphosphatidylcholine	77-81	lactalbumin alpha	Homo sapiens	0-17
8819172-1	1996	alpha-Lactalbumin (alpha-LA) associates with dimyristoylphosphatidylcholine (DMPC) or egg lecithin (EPC) liposomes.	Dimyristoylphosphatidylcholine	77-81	lactalbumin alpha	Homo sapiens	19-27
8819172-6	1996	At pH 2, where the protein inserts into the bilayer rapidly, the isolated DMPC-alpha-LA complex showed a distinct fluorescence thermal transition between 40 and 60 degrees C, consistent with a partially inserted form that possesses some degree of tertiary structure and unfolds cooperatively.	Dimyristoylphosphatidylcholine	74-78	lactalbumin alpha	Homo sapiens	79-87
8639617-4	1996	The results, for the gel phase, are consistent with interdigitation of the C26-CBS long acyl chain across the bilayer center of an all-trans-DMPC bilayer in which DMPC is less tilted than in the absence of CBS.	Dimyristoylphosphatidylcholine	141-145	cystathionine beta-synthase	Homo sapiens	79-82
8639617-4	1996	The results, for the gel phase, are consistent with interdigitation of the C26-CBS long acyl chain across the bilayer center of an all-trans-DMPC bilayer in which DMPC is less tilted than in the absence of CBS.	Dimyristoylphosphatidylcholine	163-167	cystathionine beta-synthase	Homo sapiens	79-82
8639617-8	1996	The thermotropic behavior of the lipid mixtures of C26-CBS at 8 mol % in DMPC or DPPC shows that the glycosphingolipid stabilizes the gel phase of the short chain length bilayer while it destabilizes the long chain length one.	Dimyristoylphosphatidylcholine	73-77	cystathionine beta-synthase	Homo sapiens	55-58
8639617-9	1996	Our results further demonstrate that, at this concentration, C26-CBS is completely miscible in DMPC and DPPC in the gel and the liquid crystalline phases.	Dimyristoylphosphatidylcholine	95-99	cystathionine beta-synthase	Homo sapiens	65-68
8639617-10	1996	The difference in behavior of C26-CBS in DMPC and DPPC is a consequence of the greater mismatch between the C26 chain length and the bilayer thickness of DPPC relative to DMPC.	Dimyristoylphosphatidylcholine	41-45	cystathionine beta-synthase	Homo sapiens	34-37
8639617-10	1996	The difference in behavior of C26-CBS in DMPC and DPPC is a consequence of the greater mismatch between the C26 chain length and the bilayer thickness of DPPC relative to DMPC.	Dimyristoylphosphatidylcholine	171-175	cystathionine beta-synthase	Homo sapiens	34-37
8662615-10	1996	Mature TC II-R dimerized upon insertion into synthetic phosphatidylcholine vesicles of different fatty acyl chain length (dimyristoyl, dipalmitoyl, and disteroyl phosphatidylcholine) in the absence or the presence of cholesterol at temperatures below or above their transition temperatures, respectively.	Dimyristoylphosphatidylcholine	122-133	transcobalamin 2	Homo sapiens	7-12
9054055-2	1996	Recently, apoE complexes with phospholipids (DMPC) were reported to inhibit thrombin-induced aggregation by sequestering platelet membrane cholesterol.	Dimyristoylphosphatidylcholine	45-49	apolipoprotein E	Homo sapiens	10-14
9054055-2	1996	Recently, apoE complexes with phospholipids (DMPC) were reported to inhibit thrombin-induced aggregation by sequestering platelet membrane cholesterol.	Dimyristoylphosphatidylcholine	45-49	coagulation factor II, thrombin	Homo sapiens	76-84
8610278-2	1995	Recently, apoE complexes with phospholipids (DMPC) were reported to inhibit thrombin-induced aggregation by sequestering platelet membrane cholesterol.	Dimyristoylphosphatidylcholine	45-49	apolipoprotein E	Homo sapiens	10-14
8610278-2	1995	Recently, apoE complexes with phospholipids (DMPC) were reported to inhibit thrombin-induced aggregation by sequestering platelet membrane cholesterol.	Dimyristoylphosphatidylcholine	45-49	coagulation factor II, thrombin	Homo sapiens	76-84
8610278-3	1995	Here we demonstrate that platelet cholesterol depletion is an improbable explanation for the suppressive effect of apoE:DMPC on ADP-mediated platelet aggregation; only 0.5% of cholesterol was released prior to addition of ADP to initiate aggregation while lactoferrin, which does not accept cellular cholesterol, was also inhibitory.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein E	Homo sapiens	115-119
8606364-1	1995	Relationships between the permeability coefficient (PHA) and partition coefficient (K m/w) of acetic acid and the surface density of DMPC:cholesterol bilayers have been investigated.	Dimyristoylphosphatidylcholine	133-137	lamin B receptor	Homo sapiens	52-55
7577918-2	1995	The rate of turbidity decrease following mixing of apo A-I(delta Ala190-Gln243) with dimyristoylphosphatidylcholine (DMPC) vesicles at 23 degrees C was 10-fold lower than that of the other apo A-I proteins, confirming that the carboxy-terminal region of apo A-I plays a role in rapid lipid binding.	Dimyristoylphosphatidylcholine	117-121	apolipoprotein A1	Homo sapiens	51-58
8563913-1	1995	Phospholipase A2 hydrolysis of dioleoylphosphatidylcholine, dimyristoylphosphatidylcholine or their equimolar mixture with sphingomyelin in liposomes exposed to gamma-radiation has been investigated.	Dimyristoylphosphatidylcholine	60-90	phospholipase A2 group IB	Homo sapiens	0-16
7577918-2	1995	The rate of turbidity decrease following mixing of apo A-I(delta Ala190-Gln243) with dimyristoylphosphatidylcholine (DMPC) vesicles at 23 degrees C was 10-fold lower than that of the other apo A-I proteins, confirming that the carboxy-terminal region of apo A-I plays a role in rapid lipid binding.	Dimyristoylphosphatidylcholine	117-121	apolipoprotein A1	Homo sapiens	189-196
7577918-2	1995	The rate of turbidity decrease following mixing of apo A-I(delta Ala190-Gln243) with dimyristoylphosphatidylcholine (DMPC) vesicles at 23 degrees C was 10-fold lower than that of the other apo A-I proteins, confirming that the carboxy-terminal region of apo A-I plays a role in rapid lipid binding.	Dimyristoylphosphatidylcholine	85-115	apolipoprotein A1	Homo sapiens	51-58
7577918-2	1995	The rate of turbidity decrease following mixing of apo A-I(delta Ala190-Gln243) with dimyristoylphosphatidylcholine (DMPC) vesicles at 23 degrees C was 10-fold lower than that of the other apo A-I proteins, confirming that the carboxy-terminal region of apo A-I plays a role in rapid lipid binding.	Dimyristoylphosphatidylcholine	117-121	apolipoprotein A1	Homo sapiens	189-196
7662677-6	1995	The transition temperatures determined by fluorescence polarization were higher for the DMPC complexes with intact apoE3 and with 22- and 10-kDa fragments (25.5 degrees C) than with the 22-kDa Thr57-->Cys variant (23.5 degrees C), suggesting that the variant fragment possessed the lowest affinity for lipid.	Dimyristoylphosphatidylcholine	88-92	apolipoprotein E	Homo sapiens	115-120
9384676-7	1995	MLVs composed of DMPC/DMPG (7:3) and SUVs composed of DPPC/DSPC (1:1) displayed high capacity for binding to caprylated TNF-SAM2.	Dimyristoylphosphatidylcholine	17-21	tumor necrosis factor	Homo sapiens	120-123
7744765-7	1995	ApoAI-(1-192) lysed dimyristoyl phosphatidylcholine liposomes slowly compared with apoAI but did form rHDL complexes with palmitoyloleoyl phosphatidylcholine or dipalmitoyl phosphatidylcholine when prepared by the sodium cholate dialysis method.	Dimyristoylphosphatidylcholine	20-51	apolipoprotein A1	Homo sapiens	0-5
8655189-6	1995	A linear relationship was obtained between log K (the partitioning of the beta-blocker in DMPC and also in octanol/water) and the potencies of these beta1-antagonists.	Dimyristoylphosphatidylcholine	90-94	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	149-154
7595090-11	1995	The relative orientation of the peptide and the phospholipid is the same as in a DMPC/apoA-I complex as the helices are oriented parallel to the acyl chains of the phospholipid.	Dimyristoylphosphatidylcholine	81-85	apolipoprotein A1	Homo sapiens	86-92
8180206-9	1994	Labeled, unbleached rhodopsin was purified by chromatography over hydroxyapatite and concanavalin A-agarose and reconstituted into dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	131-161	rhodopsin	Bos taurus	20-29
7493000-3	1995	Free myristic acid, released from DMPC upon PLA2 treatment, was anthrylmethylated with 9-anthryldiazomethane (ADAM) and determined by reversed-phase HPLC.	Dimyristoylphosphatidylcholine	34-38	phospholipase A2 group IB	Homo sapiens	44-48
7893721-1	1995	ATPase activities for the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum reconstituted in dimyristoylphosphatidylcholine [di(C14:0)PC] or dipalmitoylphosphatidylcholine [di(C16:0)PC] are very low at temperatures below 25 and 30 degrees C, respectively.	Dimyristoylphosphatidylcholine	99-129	dynein axonemal heavy chain 8	Homo sapiens	0-6
7893721-1	1995	ATPase activities for the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum reconstituted in dimyristoylphosphatidylcholine [di(C14:0)PC] or dipalmitoylphosphatidylcholine [di(C16:0)PC] are very low at temperatures below 25 and 30 degrees C, respectively.	Dimyristoylphosphatidylcholine	99-129	dynein axonemal heavy chain 8	Homo sapiens	33-39
7957205-4	1994	Kinetics of association to dimyristoylglycerophosphocholine (Myr2GroPCho) vesicles showed that recombinant apoA-II exhibited the same pattern of association as human plasma apoA-II.	Dimyristoylphosphatidylcholine	27-59	apolipoprotein A2	Homo sapiens	107-114
7957205-4	1994	Kinetics of association to dimyristoylglycerophosphocholine (Myr2GroPCho) vesicles showed that recombinant apoA-II exhibited the same pattern of association as human plasma apoA-II.	Dimyristoylphosphatidylcholine	27-59	apolipoprotein A2	Homo sapiens	173-180
8204624-1	1994	Glycophorin A (GPA) has been reconstituted into dimyristoylphosphatidylcholine vesicles and digested with proteinase K to identify the membrane domain and to characterize its structure and orientation.	Dimyristoylphosphatidylcholine	48-78	glycophorin A (MNS blood group)	Homo sapiens	0-19
7529287-1	1995	Lymphotoxin (LT or TNF-beta), a T cell-derived lymphokine with partial homology to TNF-alpha, was found to bind to dimyristoylphosphatidylcholine vesicles in a pH-dependent manner: binding increased with decreasing pH.	Dimyristoylphosphatidylcholine	115-145	lymphotoxin alpha	Homo sapiens	19-27
7529287-1	1995	Lymphotoxin (LT or TNF-beta), a T cell-derived lymphokine with partial homology to TNF-alpha, was found to bind to dimyristoylphosphatidylcholine vesicles in a pH-dependent manner: binding increased with decreasing pH.	Dimyristoylphosphatidylcholine	115-145	tumor necrosis factor	Homo sapiens	83-92
7811738-0	1995	Hydrolysis of DMPC or DPPC by pancreatic phospholipase A2 is slowed down when (perfluoroalkyl) alkanes are incorporated into the liposomal membrane.	Dimyristoylphosphatidylcholine	14-18	phospholipase A2 group IB	Homo sapiens	41-57
7706948-6	1995	The low density lipoprotein receptor-binding activity of purified apoE3" (Arg136-->His) when complexed with DMPC was slightly defective (80% of the activity of normal apoE).	Dimyristoylphosphatidylcholine	111-115	low density lipoprotein receptor	Homo sapiens	4-36
7706948-6	1995	The low density lipoprotein receptor-binding activity of purified apoE3" (Arg136-->His) when complexed with DMPC was slightly defective (80% of the activity of normal apoE).	Dimyristoylphosphatidylcholine	111-115	apolipoprotein E	Homo sapiens	66-71
7706948-6	1995	The low density lipoprotein receptor-binding activity of purified apoE3" (Arg136-->His) when complexed with DMPC was slightly defective (80% of the activity of normal apoE).	Dimyristoylphosphatidylcholine	111-115	apolipoprotein E	Homo sapiens	66-70
7918481-1	1994	The interaction of the actin-binding protein filamin with mixtures of zwitterionic and anionic phospholipids (DMPC, DMPG, PC, PS) was studied in reconstituted lipid monolayers and bilayers.	Dimyristoylphosphatidylcholine	110-114	filamin C	Homo sapiens	45-52
7918481-5	1994	Mixed DMPC/DMPG LUVETs showed a linear decrease of the main phase transition enthalpy and a significant shift in temperature for the solidus and liquidus lines with increasing mole fractions of reconstituted filamin.	Dimyristoylphosphatidylcholine	6-10	filamin C	Homo sapiens	208-215
8175773-9	1994	The beta-VLDL enriched in apoE or apoE-dimyristoylphosphatidylcholine complexes bound to isolated HSPG from McA-RH7777 cells or the rat liver to a very similar degree.	Dimyristoylphosphatidylcholine	39-69	apolipoprotein E	Rattus norvegicus	34-38
8117691-4	1994	ApoA-I-DMPC complexes also present two binding components comparable to the HDL3 binding sites.	Dimyristoylphosphatidylcholine	7-11	apolipoprotein A1	Homo sapiens	0-6
8175773-9	1994	The beta-VLDL enriched in apoE or apoE-dimyristoylphosphatidylcholine complexes bound to isolated HSPG from McA-RH7777 cells or the rat liver to a very similar degree.	Dimyristoylphosphatidylcholine	39-69	syndecan 2	Rattus norvegicus	98-102
8117691-4	1994	ApoA-I-DMPC complexes also present two binding components comparable to the HDL3 binding sites.	Dimyristoylphosphatidylcholine	7-11	HDL3	Homo sapiens	76-80
8305444-4	1994	AC2 is a synthetic chemical analog of the long-chain phospholipid, dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	67-97	adenylate cyclase 2	Homo sapiens	0-3
8106510-4	1994	After 18 h incubation with DMPC/apoA-I in a cell-free system, acetyl-LDL was re-isolated from DMPC/apoA-I by Sephacryl S-300 gel filtration chromatography.	Dimyristoylphosphatidylcholine	27-31	apolipoprotein A1	Rattus norvegicus	99-105
8106510-4	1994	After 18 h incubation with DMPC/apoA-I in a cell-free system, acetyl-LDL was re-isolated from DMPC/apoA-I by Sephacryl S-300 gel filtration chromatography.	Dimyristoylphosphatidylcholine	94-98	apolipoprotein A1	Rattus norvegicus	32-38
8106510-8	1994	These results indicate that transfer of DMPC from DMPC/apoA-I to acetyl-LDL weakens the ligand activity for the scavenger receptor due probably to a decrease in net negative charge.	Dimyristoylphosphatidylcholine	40-44	apolipoprotein A1	Rattus norvegicus	55-61
8106510-8	1994	These results indicate that transfer of DMPC from DMPC/apoA-I to acetyl-LDL weakens the ligand activity for the scavenger receptor due probably to a decrease in net negative charge.	Dimyristoylphosphatidylcholine	50-54	apolipoprotein A1	Rattus norvegicus	55-61
8305444-4	1994	AC2 is a synthetic chemical analog of the long-chain phospholipid, dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	99-103	adenylate cyclase 2	Homo sapiens	0-3
8373787-11	1993	NMR relaxation time measurements in the headgroup and chain region of DMPG and DMPC suggest that the lateral diffusion coefficient of the acidic lipid decreases significantly due to the coupling with MBP while the zwitterionic DMPC is not affected.	Dimyristoylphosphatidylcholine	79-83	myelin basic protein	Homo sapiens	200-203
8373775-2	1993	The DSC thermograms exhibited by DMPC/GM1 vesicles, either in the presence or in the absence of GPA, are resolvable into two components.	Dimyristoylphosphatidylcholine	33-37	glycophorin A (MNS blood group)	Homo sapiens	96-99
8011074-1	1994	Peptides corresponding to lipid binding domains of Apo B-100 were synthesized, purified, and incubated with dimyristoylphosphatidylcholine (DMPC) liposomes.	Dimyristoylphosphatidylcholine	108-138	apolipoprotein B	Homo sapiens	51-60
8011074-1	1994	Peptides corresponding to lipid binding domains of Apo B-100 were synthesized, purified, and incubated with dimyristoylphosphatidylcholine (DMPC) liposomes.	Dimyristoylphosphatidylcholine	140-144	apolipoprotein B	Homo sapiens	51-60
8118918-0	1993	The effects of the p-nitrophenyl esters of the even-numbered fatty acids from caproic (C6) to stearic (C18) on the main phase transition of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	140-170	Bardet-Biedl syndrome 9	Homo sapiens	103-106
8118918-1	1993	Differential scanning calorimetry (DSC) is employed in a study of the effects of the p-nitrophenyl esters of the even numbered fatty acids from C6 (caproic acid) to C18 (stearic acid) on the main phase transition of multilamellar suspensions of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	245-275	Bardet-Biedl syndrome 9	Homo sapiens	165-168
8118918-1	1993	Differential scanning calorimetry (DSC) is employed in a study of the effects of the p-nitrophenyl esters of the even numbered fatty acids from C6 (caproic acid) to C18 (stearic acid) on the main phase transition of multilamellar suspensions of dimyristoylphosphatidylcholine (DMPC).	Dimyristoylphosphatidylcholine	277-281	Bardet-Biedl syndrome 9	Homo sapiens	165-168
8428938-12	1993	Incubation of mouse peritoneal macrophages with apoA-I(Pro165-->Arg).DMPC complexes did also result in a 30% decreased efflux of radiolabeled cholesterol if compared to rHDL with the normal allele product from the same donor.	Dimyristoylphosphatidylcholine	72-76	apolipoprotein A-I	Mus musculus	48-54
8323946-10	1993	Apo A-IV helicity increased for the protein bound to DMPC or DPPC but the increase was more pronounced for the apo A-IV/DMPC particles.	Dimyristoylphosphatidylcholine	53-57	apolipoprotein A4	Homo sapiens	0-8
8323946-10	1993	Apo A-IV helicity increased for the protein bound to DMPC or DPPC but the increase was more pronounced for the apo A-IV/DMPC particles.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein A4	Homo sapiens	0-8
8323946-10	1993	Apo A-IV helicity increased for the protein bound to DMPC or DPPC but the increase was more pronounced for the apo A-IV/DMPC particles.	Dimyristoylphosphatidylcholine	120-124	apolipoprotein A4	Homo sapiens	111-119
8504138-5	1993	Based on competition between bovine serum albumin and the vesicles for the lysophospholipid, we estimated the partition coefficient to be about 5.10(-7) for palmitoyl lipids at 39 degrees C and about 9.10(-7) for myristoyl lipids at 22 degrees C. These values were able to rationalize the behavior of the lag time with dipalmitoylphosphatidylcholine vesicles, but they were unable to predict the behavior with dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	410-440	albumin	Homo sapiens	36-49
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
8428938-9	1993	In the present study, all apoA-I.DMPC complexes except those containing apoA-I(Pro165-->Arg) promoted cholesterol efflux as effectively as those containing normal apoA-I.	Dimyristoylphosphatidylcholine	33-37	apolipoprotein A-I	Mus musculus	26-32
8428938-10	1993	Cholesterol efflux from adipocytes obtained after 180 min of incubation with apoA-I(Pro165-->Arg).DMPC complexes was decreased by 30% although this variant was bound to adipocytes with normal affinity.	Dimyristoylphosphatidylcholine	101-105	apolipoprotein A-I	Mus musculus	77-83
8428938-11	1993	By contrast, apoA-I(Lys107-->Met).DMPC complexes were decreased in their binding affinity compared to normal apoA-I.DMPC complexes but normally promoted cholesterol efflux.	Dimyristoylphosphatidylcholine	37-41	apolipoprotein A-I	Mus musculus	13-19
8428938-11	1993	By contrast, apoA-I(Lys107-->Met).DMPC complexes were decreased in their binding affinity compared to normal apoA-I.DMPC complexes but normally promoted cholesterol efflux.	Dimyristoylphosphatidylcholine	37-41	apolipoprotein A-I	Mus musculus	112-118
8428938-11	1993	By contrast, apoA-I(Lys107-->Met).DMPC complexes were decreased in their binding affinity compared to normal apoA-I.DMPC complexes but normally promoted cholesterol efflux.	Dimyristoylphosphatidylcholine	119-123	apolipoprotein A-I	Mus musculus	13-19
8241397-1	1993	Using a heat conduction calorimeter with very high resolution (+/- 0.00005 J/degrees C.cm3), we have measured the specific heat CpL between 25 and 35 degrees C of dimyristoylphosphatidylcholine (DMPC) in aqueous dispersions.	Dimyristoylphosphatidylcholine	163-193	hephaestin	Homo sapiens	128-131
8241397-1	1993	Using a heat conduction calorimeter with very high resolution (+/- 0.00005 J/degrees C.cm3), we have measured the specific heat CpL between 25 and 35 degrees C of dimyristoylphosphatidylcholine (DMPC) in aqueous dispersions.	Dimyristoylphosphatidylcholine	195-199	hephaestin	Homo sapiens	128-131
8396448-0	1993	The kinetics and thermodynamics of bleaching of rhodopsin in dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	61-91	rhodopsin	Homo sapiens	48-57
8396448-11	1993	The results indicate that rhodopsin has extensive photochemical activity when reconstituted in dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	95-125	rhodopsin	Homo sapiens	26-35
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
19431857-3	1992	The binary phase diagram of DMPC-DMG mixtures displays three regions corresponding to the existence of compounds (C1 and C2, respectively) with approximately 1:1 and 1:2 mol/mol DMPC:DMG stoichiometries.	Dimyristoylphosphatidylcholine	28-32	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	114-167
1501242-4	1992	MBP caused a change in the temperature transition profiles of acidic liposomes (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidyl serine or an equimolar mixture of 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1,2-dimyristoyl-sn-glycero-3-phosphatidic acid) and induced their aggregation as shown by fluorescence resonance energy transfer experiments.	Dimyristoylphosphatidylcholine	161-204	myelin basic protein	Homo sapiens	0-3
1504094-1	1992	The interaction of the diabetes associated polypeptide (amylin) with dimyristoylphosphatidylcholine (DMPC) was assessed by measurements of turbidity (absorbance at 400 nm) and secondary structure by CD spectroscopy.	Dimyristoylphosphatidylcholine	69-99	islet amyloid polypeptide	Homo sapiens	56-62
1504094-1	1992	The interaction of the diabetes associated polypeptide (amylin) with dimyristoylphosphatidylcholine (DMPC) was assessed by measurements of turbidity (absorbance at 400 nm) and secondary structure by CD spectroscopy.	Dimyristoylphosphatidylcholine	101-105	islet amyloid polypeptide	Homo sapiens	56-62
1504094-6	1992	These data demonstrate that fundamental differences in the structures adopted by amylins from human and rat species exist in mixtures with DMPC and suggest that these differences may be related to the formation of amyloid fibrils in the human amylin peptide which are not observed in the rat peptide.	Dimyristoylphosphatidylcholine	139-143	islet amyloid polypeptide	Homo sapiens	81-87
1322696-4	1992	The reduction in Dlat of HLA molecules in DMPC liposomes is found to be sensitive to time and temperature.	Dimyristoylphosphatidylcholine	42-46	dihydrolipoamide S-acetyltransferase	Homo sapiens	17-21
1473215-8	1992	There was no significant difference (P > 0.5) between apoA-IV and control but a very significant difference (P < 0.001) between liposome (apoA-IV:DMPC) and control, suggesting that liposomes (apoA-IV:DMPC) play a role in reverse cholesterol transport.	Dimyristoylphosphatidylcholine	152-156	apolipoprotein A4	Homo sapiens	144-151
1473215-8	1992	There was no significant difference (P > 0.5) between apoA-IV and control but a very significant difference (P < 0.001) between liposome (apoA-IV:DMPC) and control, suggesting that liposomes (apoA-IV:DMPC) play a role in reverse cholesterol transport.	Dimyristoylphosphatidylcholine	152-156	apolipoprotein A4	Homo sapiens	144-151