PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 23721456-6 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 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 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 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 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 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 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 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 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 17474718-0 2007 Large disk intermediate precedes formation of apolipoprotein A-I-dimyristoylphosphatidylcholine small disks. Dimyristoylphosphatidylcholine 65-95 apolipoprotein A1 Homo sapiens 46-64 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 173-177 apolipoprotein A1 Homo sapiens 59-65 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 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 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 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 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 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 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 117-121 apolipoprotein A1 Homo sapiens 189-196 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 2985608-10 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 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 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 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 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 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 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 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 6432780-1 1984 Apolipoprotein A-I-dimyristoylphosphatidylcholine complex. Dimyristoylphosphatidylcholine 19-49 apolipoprotein A1 Homo sapiens 0-18 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 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 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 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 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 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 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 7356666-2 1980 Complexes of dimyristoyl phosphatidylcholine and human apo A-1. Dimyristoylphosphatidylcholine 13-44 apolipoprotein A1 Homo sapiens 55-62 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 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 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 57-61 apolipoprotein A1 Homo sapiens 99-105 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 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 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 apolipoprotein A1 Homo sapiens 94-100 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 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 192549-7 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 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 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 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 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