PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 154-158 apolipoprotein E Homo sapiens 45-50 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 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 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 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 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 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 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 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 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 E Homo sapiens 102-106 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 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 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 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 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 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 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 101-105 apolipoprotein E Homo sapiens 49-53 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 10751422-5 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 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 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 105-109 apolipoprotein E Homo sapiens 50-55 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 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 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 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 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 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 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 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 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 8610278-3 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 apolipoprotein E Homo sapiens 173-177 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 97-107 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