PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2512989-1 1989 Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods. Dimyristoylphosphatidylcholine 69-112 apolipoprotein A2 Homo sapiens 6-25 2512989-1 1989 Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods. Dimyristoylphosphatidylcholine 69-112 apolipoprotein A2 Homo sapiens 27-35 2512989-1 1989 Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods. Dimyristoylphosphatidylcholine 114-118 apolipoprotein A2 Homo sapiens 6-25 2512989-1 1989 Human apolipoprotein A-II (apo A-II) in solution and associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) was investigated by a combination of absorbance and fluorescence methods. Dimyristoylphosphatidylcholine 114-118 apolipoprotein A2 Homo sapiens 27-35 2512989-7 1989 Similar measurements also revealed that the microenvironments around tyrosines of apo A-II bound to DMPC in the gel phase are different from those observed in the liquid crystalline phase. Dimyristoylphosphatidylcholine 100-104 apolipoprotein A2 Homo sapiens 82-90 2512990-4 1989 The kinetics of hydrolysis of apo A-II associated with 1,2-dimyristoyl-sn-glycero-3-phosphocholine showed several differences. Dimyristoylphosphatidylcholine 55-98 apolipoprotein A2 Homo sapiens 30-38 6776110-1 1980 Interaction of apolipoprotein A-II from human plasma high density lipoproteins with dimyristoylphosphatidylcholine. Dimyristoylphosphatidylcholine 84-114 apolipoprotein A2 Homo sapiens 15-34 6784753-1 1981 Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted. Dimyristoylphosphatidylcholine 90-120 apolipoprotein A2 Homo sapiens 21-28 6784753-1 1981 Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted. Dimyristoylphosphatidylcholine 122-126 apolipoprotein A2 Homo sapiens 0-19 6784753-1 1981 Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted. Dimyristoylphosphatidylcholine 122-126 apolipoprotein A2 Homo sapiens 21-28 6784753-10 1981 The multiple lipid-protein species formed by apoA-II and DMPC suggest the possible existence of more than one macromolecular spices of lipid and apoA-II in the plasma. Dimyristoylphosphatidylcholine 57-61 apolipoprotein A2 Homo sapiens 145-152 6784754-0 1981 Thermodynamics of lipid-protein interactions: Interaction of apolipoprotein A-II from human plasma high-density lipoproteins with dimyristoylphosphatidylcholine. Dimyristoylphosphatidylcholine 130-160 apolipoprotein A2 Homo sapiens 61-80 6784753-0 1981 Physical properties of lipid-protein complexes formed by the interaction of dimyristoylphosphatidylcholine and human high-density apolipoprotein A-II. Dimyristoylphosphatidylcholine 76-106 apolipoprotein A2 Homo sapiens 130-149 6784753-1 1981 Apolipoprotein A-II (apoA-II) from human plasma high-density lipoproteins associates with dimyristoylphosphatidylcholine (DMPC) to give complexes whose structure is determined by the temperature at which the reaction is conducted. Dimyristoylphosphatidylcholine 90-120 apolipoprotein A2 Homo sapiens 0-19 6776110-2 1980 ApoA-II and dimyristoylphosphatidylcholine (DMPC) spontaneously associate to give three different complexes whose structures are determined by the initial reactant concentration and by the reaction temperature with respect to Tc (23.9 degrees C), the gel to liquid crystalline transition temperature of DMPC. Dimyristoylphosphatidylcholine 303-307 apolipoprotein A2 Homo sapiens 0-7 214114-4 1978 0.1 mol cholesterol/mol dimyristoyl phosphatidylcholine (DMPC) were readily solubilized by apoHDL, apoA-1 or apoA-2. Dimyristoylphosphatidylcholine 24-55 apolipoprotein A2 Homo sapiens 109-115 456381-4 1979 The transition temperature from gel-crystalline to liquid-crystalline phase in 24 degrees C for the dimyristoyl-phosphatidylcholine vesicles and is shifted to around 30 degrees C in the complexes between phosphatidylcholine and apoA-I, apoA-II, apoC-I, apoC-III proteins while the cooperativity of the transition is decreased. Dimyristoylphosphatidylcholine 100-131 apolipoprotein A2 Homo sapiens 236-243 214114-4 1978 0.1 mol cholesterol/mol dimyristoyl phosphatidylcholine (DMPC) were readily solubilized by apoHDL, apoA-1 or apoA-2. Dimyristoylphosphatidylcholine 57-61 apolipoprotein A2 Homo sapiens 109-115 23025327-5 2012 At this stoichiometry, apo A-II forms rHDL from DMPC and FC. Dimyristoylphosphatidylcholine 48-52 apolipoprotein A2 Homo sapiens 23-31 193555-11 1977 The maximal-binding enthalpies of DMPC to apoHDL, apoA-I, and apoA-II were lower for the baboon than for the human apoprotein. Dimyristoylphosphatidylcholine 34-38 apolipoprotein A2 Homo sapiens 62-69 182250-8 1976 The sequential binding of DMPC to apo AI and apo AII suggests the existence of cooperativity between the two apoproteins in phospholipid binding as apo AII promotes the incorporation of apo AI into a protein-phospholipid complex. Dimyristoylphosphatidylcholine 26-30 apolipoprotein A2 Homo sapiens 148-155 23721456-3 2013 DSC studies reveal multiple phases or domains that can be classified as virtual DMPC, which contains a small amount of DMPC that slightly reduces the melting temperature (Tm), a boundary phase that is adjacent to the apo A-I or apo A-II that circumscribes the discoidal rHDL, and a mixed FC/DMPC phase that has a Tm that increases with FC mole percent. Dimyristoylphosphatidylcholine 80-84 apolipoprotein A2 Homo sapiens 228-236 23721456-6 2013 For rHDL (apo A-II) compared to rHDL (apo A-I), this occurs in spite of the reduced number of helical regions that mediate binding to the DMPC surface. Dimyristoylphosphatidylcholine 138-142 apolipoprotein A2 Homo sapiens 10-18 23721456-7 2013 This effect is attributed to the very high lipophilicity of apo A-II and the reduction in the polarity of the interface between DMPC and the aqueous phase with an increasing FC mole percent, an effect that is expected to increase the strength of the hydrophobic associations with the nonpolar face of the amphipathic helices of apo A-II. Dimyristoylphosphatidylcholine 128-132 apolipoprotein A2 Homo sapiens 328-336 21090-2 1977 Potentiometric titration of the native apo-A-II, apoC-I, apoC-III proteins and of their complexes with dimyristoyl lecithin. Dimyristoylphosphatidylcholine 103-123 apolipoprotein A2 Homo sapiens 39-47 23025327-6 2012 Contrary to our hypothesis, apo A-II, like apo A-I, reacts poorly with DMPC containing >=20 mol % FC. Dimyristoylphosphatidylcholine 71-75 apolipoprotein A2 Homo sapiens 28-36 7957205-4 1994 Kinetics of association to dimyristoylglycerophosphocholine (Myr2GroPCho) vesicles showed that recombinant apoA-II exhibited the same pattern of association as human plasma apoA-II. Dimyristoylphosphatidylcholine 27-59 apolipoprotein A2 Homo sapiens 107-114 15681655-0 2005 Kinetic stabilization and fusion of apolipoprotein A-2:DMPC disks: comparison with apoA-1 and apoC-1. Dimyristoylphosphatidylcholine 55-59 apolipoprotein A2 Homo sapiens 36-54 7957205-4 1994 Kinetics of association to dimyristoylglycerophosphocholine (Myr2GroPCho) vesicles showed that recombinant apoA-II exhibited the same pattern of association as human plasma apoA-II. Dimyristoylphosphatidylcholine 27-59 apolipoprotein A2 Homo sapiens 173-180 8844260-3 1996 The lipid binding properties of apoA-II(18-30)+ were assessed using optical spectroscopy in the presence of sodium dodecyl sulfate (SDS), dodecylphosphocholine (DPC), tetradecyltrimethyl ammonium chloride (TMA) and dimyristoylphosphatidylcholine (DMPC). Dimyristoylphosphatidylcholine 215-245 apolipoprotein A2 Homo sapiens 32-39 8844260-3 1996 The lipid binding properties of apoA-II(18-30)+ were assessed using optical spectroscopy in the presence of sodium dodecyl sulfate (SDS), dodecylphosphocholine (DPC), tetradecyltrimethyl ammonium chloride (TMA) and dimyristoylphosphatidylcholine (DMPC). Dimyristoylphosphatidylcholine 247-251 apolipoprotein A2 Homo sapiens 32-39 8844260-4 1996 The fluorescence emission spectra and the circular dichroism data suggested that apoA-II(18-30)+ interacted most strongly with SDS and most weakly with DMPC. Dimyristoylphosphatidylcholine 152-156 apolipoprotein A2 Homo sapiens 81-88