PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19124026-5 2009 Data on the conformation, mobility, distance, and surface exposure of regions revealed by the cysteine probes were modeled into the molecular envelope of apoE bound to dipalmitoylphosphatidylcholine that had been determined by X-ray analysis. 1,2-Dipalmitoylphosphatidylcholine 168-198 apolipoprotein E Homo sapiens 154-158 17308333-0 2007 Apolipoprotein E*dipalmitoylphosphatidylcholine particles are ellipsoidal in solution. 1,2-Dipalmitoylphosphatidylcholine 17-47 apolipoprotein E Homo sapiens 0-16 17308333-5 2007 In contrast to a widely accepted discoidal model of apoA-I bound to dimyristoylphosphatidylcholine, which is based on solution studies, an X-ray diffraction study of apoE bound to dipalmitoylphosphatidylcholine (DPPC) indicated that apoE*DPPC particles are quasi-spheroidal and that the packing of the phospholipid core is similar to a micelle. 1,2-Dipalmitoylphosphatidylcholine 180-210 apolipoprotein E Homo sapiens 166-170 17308333-6 2007 Using small-angle X-ray scattering, we show that apoE*DPPC particles in solution are ellipsoidal and that the shape of the phospholipid core is compatible with a twisted-bilayer model. 1,2-Dipalmitoylphosphatidylcholine 54-58 apolipoprotein E Homo sapiens 49-53 10924113-5 2000 All apoC-III proteins bound to the apoE:DPPC complexes; the amount of apoE displaced from the complex was dependent on the apoC-III lipid binding affinity. 1,2-Dipalmitoylphosphatidylcholine 40-44 apolipoprotein E Homo sapiens 35-39 16278220-0 2006 Model of biologically active apolipoprotein E bound to dipalmitoylphosphatidylcholine. 1,2-Dipalmitoylphosphatidylcholine 55-85 apolipoprotein E Homo sapiens 29-45 11687228-5 2001 For complexes with all three apolipoproteins studied, at T<T(t) the probe mobility in the lipid phase of rHDL was significantly higher compared to pure DPPC bilayer. 1,2-Dipalmitoylphosphatidylcholine 155-159 apolipoprotein E Homo sapiens 29-44 16511213-4 2005 To test this possibility, apoE4 complexed with the phospholipid dipalmitoylphosphatidylcholine was chosen. 1,2-Dipalmitoylphosphatidylcholine 64-94 apolipoprotein E Homo sapiens 26-31 10924113-5 2000 All apoC-III proteins bound to the apoE:DPPC complexes; the amount of apoE displaced from the complex was dependent on the apoC-III lipid binding affinity. 1,2-Dipalmitoylphosphatidylcholine 40-44 apolipoprotein E Homo sapiens 70-74 1718450-6 1991 Monoclonal antibody 3D12F11 (subclass IgG1) showed a high affinity for the apoE (Kd = 3.5 +/- 0.5 nM) without any effect on the apoprotein binding to heparin-Sepharose and apoE-induced destruction of dipalmitoylphosphatidylcholine liposomes. 1,2-Dipalmitoylphosphatidylcholine 200-230 apolipoprotein E Homo sapiens 75-79 9275298-4 1997 Association of apoE3 with DPPC resulted in a more structured state of the apolipoprotein molecule versus the soluble apolipoprotein; this state was characterized by parallel orientation of alpha-helixes of apoE3 and DPPC acyl chains. 1,2-Dipalmitoylphosphatidylcholine 26-30 apolipoprotein E Homo sapiens 15-20 9275298-4 1997 Association of apoE3 with DPPC resulted in a more structured state of the apolipoprotein molecule versus the soluble apolipoprotein; this state was characterized by parallel orientation of alpha-helixes of apoE3 and DPPC acyl chains. 1,2-Dipalmitoylphosphatidylcholine 26-30 apolipoprotein E Homo sapiens 74-88 9275298-4 1997 Association of apoE3 with DPPC resulted in a more structured state of the apolipoprotein molecule versus the soluble apolipoprotein; this state was characterized by parallel orientation of alpha-helixes of apoE3 and DPPC acyl chains. 1,2-Dipalmitoylphosphatidylcholine 26-30 apolipoprotein E Homo sapiens 206-211 9275298-6 1997 The transformation of discoidal apoE3-DPPC-Chol complexes into spherical particles was induced by LCAT and accumulation of cholesteryl esters was approximately 62% of the total cholesterol. 1,2-Dipalmitoylphosphatidylcholine 38-42 apolipoprotein E Homo sapiens 32-37 9275298-8 1997 Discoidal apoE3-DPPC complexes incorporated unesterified cholesterol released from Chol-loaded J774 macrophages. 1,2-Dipalmitoylphosphatidylcholine 16-20 apolipoprotein E Homo sapiens 10-15 9219896-12 1997 (2) The relative response of trans-PA fluorescence intensity to temperature-induced phase transition of DPPC in apoA-I/DPPC/Chol complexes was decreased as a function of apolipoprotein content in a non-monotonic fashion with a transition midpoint at a mol ratio DPPC/A-I of 250:1, probably indicating two different modes of apolipoprotein/DPPC interaction in different sized complexes. 1,2-Dipalmitoylphosphatidylcholine 104-108 apolipoprotein E Homo sapiens 170-184 9219896-12 1997 (2) The relative response of trans-PA fluorescence intensity to temperature-induced phase transition of DPPC in apoA-I/DPPC/Chol complexes was decreased as a function of apolipoprotein content in a non-monotonic fashion with a transition midpoint at a mol ratio DPPC/A-I of 250:1, probably indicating two different modes of apolipoprotein/DPPC interaction in different sized complexes. 1,2-Dipalmitoylphosphatidylcholine 119-123 apolipoprotein E Homo sapiens 170-184 9219896-12 1997 (2) The relative response of trans-PA fluorescence intensity to temperature-induced phase transition of DPPC in apoA-I/DPPC/Chol complexes was decreased as a function of apolipoprotein content in a non-monotonic fashion with a transition midpoint at a mol ratio DPPC/A-I of 250:1, probably indicating two different modes of apolipoprotein/DPPC interaction in different sized complexes. 1,2-Dipalmitoylphosphatidylcholine 119-123 apolipoprotein E Homo sapiens 170-184 9219896-12 1997 (2) The relative response of trans-PA fluorescence intensity to temperature-induced phase transition of DPPC in apoA-I/DPPC/Chol complexes was decreased as a function of apolipoprotein content in a non-monotonic fashion with a transition midpoint at a mol ratio DPPC/A-I of 250:1, probably indicating two different modes of apolipoprotein/DPPC interaction in different sized complexes. 1,2-Dipalmitoylphosphatidylcholine 119-123 apolipoprotein E Homo sapiens 170-184