PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27529357-1 2016 Apolipoprotein C-III (ApoC-III) is found on high-density lipoproteins (HDLs) and remodels 1,2-dimyristoyl-sn-glycero-3-phosphocholine vesicles into HDL-like particles known as nanodiscs. Dimyristoylphosphatidylcholine 90-133 apolipoprotein C3 Homo sapiens 0-20 27529357-1 2016 Apolipoprotein C-III (ApoC-III) is found on high-density lipoproteins (HDLs) and remodels 1,2-dimyristoyl-sn-glycero-3-phosphocholine vesicles into HDL-like particles known as nanodiscs. Dimyristoylphosphatidylcholine 90-133 apolipoprotein C3 Homo sapiens 22-30 3355846-0 1988 Probucol reduces the rate of association of apolipoprotein C-III with dimyristoylphosphatidylcholine. Dimyristoylphosphatidylcholine 70-100 apolipoprotein C3 Homo sapiens 44-64 19326075-4 2009 Furthermore, increasing the molar ratio of apoC-III in rHDL enhanced the surfactant-like properties and the ability to lyse dimyristoyl phosphatidylcholine. Dimyristoylphosphatidylcholine 124-155 apolipoprotein C3 Homo sapiens 43-51 3355846-1 1988 The effect of low concentrations of probucol and cholesterol on the association of dimyristoylphosphatidylcholine with human plasma apolipoprotein C-III was studied. Dimyristoylphosphatidylcholine 83-113 apolipoprotein C3 Homo sapiens 132-152 3355846-2 1988 Liposomes of dimyristoylphosphatidylcholine with or without probucol or cholesterol were prepared by swelling the lipids in buffer at 37 degrees C. The association of apolipoprotein C-III with the liposomes was determined at 24 degrees C by measuring the rate of clearing of turbidity at 400 nm following addition of protein. Dimyristoylphosphatidylcholine 13-43 apolipoprotein C3 Homo sapiens 167-187 833505-1 1977 We have studied the lipid binding of apoC-III with two types of mixed vesicles of DMPC (dimyristoyl phosphatidylcholine) and DPPC (dipalmitoyl phosphatidyl-choline). Dimyristoylphosphatidylcholine 82-86 apolipoprotein C3 Homo sapiens 37-45 193554-0 1977 Physical properties of the dimyristoylphosphatidylcholine vesicle and of complexes formed by its interaction with apolipoprotein C-III. Dimyristoylphosphatidylcholine 27-57 apolipoprotein C3 Homo sapiens 114-134 833505-1 1977 We have studied the lipid binding of apoC-III with two types of mixed vesicles of DMPC (dimyristoyl phosphatidylcholine) and DPPC (dipalmitoyl phosphatidyl-choline). Dimyristoylphosphatidylcholine 88-119 apolipoprotein C3 Homo sapiens 37-45 833505-4 1977 Combining DMPC:DPPC macroscopic mixtures with apoC-III above the transition temperature, Tc 23 degrees C, of DMPC produces an isolatable complex consisting of 4:1 DMPC:DPPC. Dimyristoylphosphatidylcholine 109-113 apolipoprotein C3 Homo sapiens 46-54 833505-4 1977 Combining DMPC:DPPC macroscopic mixtures with apoC-III above the transition temperature, Tc 23 degrees C, of DMPC produces an isolatable complex consisting of 4:1 DMPC:DPPC. Dimyristoylphosphatidylcholine 109-113 apolipoprotein C3 Homo sapiens 46-54 833505-6 1977 Spectral analysis of apoC-III in the presence of the micromixtures reveals a single transition, which occurs between the respective thermal transitions of DMPC (23 degrees C) and DPPC (41 degrees C). Dimyristoylphosphatidylcholine 155-159 apolipoprotein C3 Homo sapiens 21-29 188642-1 1976 The interaction of synthetic dimyristoyl phosphatidylcholine (lecithin) liposomes with isolated apoC-I and apoC-III proteins from very low density lipoproteins has been studied by microcalorimetry. Dimyristoylphosphatidylcholine 29-60 apolipoprotein C3 Homo sapiens 107-115 182205-0 1976 Structure of an apolipoprotein-phospholipid complex: apoC-III induced changes in the physical properties of dimyristoylphosphatidylcholine. Dimyristoylphosphatidylcholine 108-138 apolipoprotein C3 Homo sapiens 53-61 182205-1 1976 The effect of ApoC-III, a major apoprotein constituent of human very low density lipoproteins, on the physical properties of dimyristoylphosphatidylcholine (DMPC) vesicles has been studied by magnetic resonance and fluorescence techniques. Dimyristoylphosphatidylcholine 125-155 apolipoprotein C3 Homo sapiens 14-22 182205-1 1976 The effect of ApoC-III, a major apoprotein constituent of human very low density lipoproteins, on the physical properties of dimyristoylphosphatidylcholine (DMPC) vesicles has been studied by magnetic resonance and fluorescence techniques. Dimyristoylphosphatidylcholine 157-161 apolipoprotein C3 Homo sapiens 14-22 182205-2 1976 The sharp gel-liquid crystalline transition usually observed at 23 C in DMPC is both broadened and elevated when ApoC-III is bound as determined (a) from measurements of microscopic viscosity by pyrene excimer fluorescence, (b) from the distribution of di-tert-butyl nitroxide between the bulk aqueous phase and the fluid lipid phase, and (c) from the motion of fatty acyl chains of spin-labeled phosphatdylcholine. Dimyristoylphosphatidylcholine 72-76 apolipoprotein C3 Homo sapiens 114-122 182205-3 1976 Experiments involving the translocation of ascorbate and charged nitroxide ions and the movement of paramagnetic Eu 3+ ions indicate that when ApoC-III binds to DMPC vesicles, it increases their permeability or destroys their original bilayer structure. Dimyristoylphosphatidylcholine 161-165 apolipoprotein C3 Homo sapiens 143-151 182205-5 1976 Taken together, the data indicate that ApoC-III binding to DMPC not only decreases the acyl chain motion of individual lipid molecules, but also induces break-down of bilamellar vesicular structure to give significantly smaller complexes. Dimyristoylphosphatidylcholine 59-63 apolipoprotein C3 Homo sapiens 39-47