PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24866239-4 2014 Pyrene-labeled recombinant human apoE3 displayed a robust ability to stimulate ABCA1-mediated cholesterol efflux from cholesterol-loaded J774 macrophages (which do not express apoE), comparable to that elicited by unlabeled apoE3. pyrene 0-6 apolipoprotein E Homo sapiens 33-37 24866239-0 2014 A pyrene based fluorescence approach to study conformation of apolipoprotein E3 in macrophage-generated nascent high density lipoprotein. pyrene 2-8 apolipoprotein E Homo sapiens 62-79 24866239-3 2014 The objective of this study is to understand the conformation adopted by apoE3 in macrophage-generated nHDL using a fluorescence spectroscopic approach involving pyrene. pyrene 162-168 apolipoprotein E Homo sapiens 73-78 24866239-4 2014 Pyrene-labeled recombinant human apoE3 displayed a robust ability to stimulate ABCA1-mediated cholesterol efflux from cholesterol-loaded J774 macrophages (which do not express apoE), comparable to that elicited by unlabeled apoE3. pyrene 0-6 apolipoprotein E Homo sapiens 33-38 24866239-4 2014 Pyrene-labeled recombinant human apoE3 displayed a robust ability to stimulate ABCA1-mediated cholesterol efflux from cholesterol-loaded J774 macrophages (which do not express apoE), comparable to that elicited by unlabeled apoE3. pyrene 0-6 apolipoprotein E Homo sapiens 224-229 24866239-8 2014 A significant extent of pyrene excimer emission was noted in nHDL, indicative of spatial proximity between Cys112 on neighboring apoE3 molecules similar to that noted in reconstituted HDL. pyrene 24-30 apolipoprotein E Homo sapiens 129-134 24866239-11 2014 A similar organization of the C-terminal tail of apoE on nHDL was noted when pyrene-apoEA277C(201-299) was used as the cholesterol acceptor. pyrene 77-83 apolipoprotein E Homo sapiens 49-53 20073510-0 2010 Pyrene fluorescence analysis offers new insights into the conformation of the lipoprotein-binding domain of human apolipoprotein E. pyrene 0-6 apolipoprotein E Homo sapiens 114-130 22730894-4 2012 Pyrene excimer fluorescence together with gel filtration chromatography indicated that there are extensive intermolecular helix-helix contacts through the C-terminal helices of apoE4. pyrene 0-6 apolipoprotein E Homo sapiens 177-182 22730894-5 2012 Comparison of increases in pyrene fluorescence upon binding of pyrene-labeled apoE4 to egg phosphatidylcholine small unilamellar vesicles suggests a two-step lipid-binding process; apoE4 initially binds to a lipid surface through the C-terminal helices followed by the slower conformational reorganization of the N-terminal helix bundle domain. pyrene 27-33 apolipoprotein E Homo sapiens 78-83 22730894-5 2012 Comparison of increases in pyrene fluorescence upon binding of pyrene-labeled apoE4 to egg phosphatidylcholine small unilamellar vesicles suggests a two-step lipid-binding process; apoE4 initially binds to a lipid surface through the C-terminal helices followed by the slower conformational reorganization of the N-terminal helix bundle domain. pyrene 27-33 apolipoprotein E Homo sapiens 181-186 22730894-5 2012 Comparison of increases in pyrene fluorescence upon binding of pyrene-labeled apoE4 to egg phosphatidylcholine small unilamellar vesicles suggests a two-step lipid-binding process; apoE4 initially binds to a lipid surface through the C-terminal helices followed by the slower conformational reorganization of the N-terminal helix bundle domain. pyrene 63-69 apolipoprotein E Homo sapiens 78-83 22730894-5 2012 Comparison of increases in pyrene fluorescence upon binding of pyrene-labeled apoE4 to egg phosphatidylcholine small unilamellar vesicles suggests a two-step lipid-binding process; apoE4 initially binds to a lipid surface through the C-terminal helices followed by the slower conformational reorganization of the N-terminal helix bundle domain. pyrene 63-69 apolipoprotein E Homo sapiens 181-186 22730894-8 2012 However, monitoring pyrene fluorescence upon binding to HDL(3) suggests that not only apoE-lipid interactions but also protein-protein interactions are important for apoE4 binding to HDL(3). pyrene 20-26 apolipoprotein E Homo sapiens 166-171 22779734-0 2012 The extent of pyrene excimer fluorescence emission is a reflector of distance and flexibility: analysis of the segment linking the LDL receptor-binding and tetramerization domains of apolipoprotein E3. pyrene 14-20 apolipoprotein E Homo sapiens 183-200 22779734-9 2012 This study offers new insights into the conformation of tetrameric apoE and presents the use of pyrene as a powerful probe for studying protein spatial organization. pyrene 96-102 apolipoprotein E Homo sapiens 67-71 20073510-5 2010 Pyrene was covalently attached to single cysteine-containing recombinant human apoE CT at position 223 or 255 to probe the first predicted helical segment and at position 277 to monitor the terminal predicted helical segment. pyrene 0-6 apolipoprotein E Homo sapiens 79-83 20073510-6 2010 Regardless of the location of the probe, all three pyrene-labeled apoE CT variants display an intense and dramatic fluorescence excimer band at 460 nm, a signature feature of pyrene, which indicates that two pyrene moieties are within 10 A of each other. pyrene 51-57 apolipoprotein E Homo sapiens 66-70 20073510-6 2010 Regardless of the location of the probe, all three pyrene-labeled apoE CT variants display an intense and dramatic fluorescence excimer band at 460 nm, a signature feature of pyrene, which indicates that two pyrene moieties are within 10 A of each other. pyrene 175-181 apolipoprotein E Homo sapiens 66-70 20073510-6 2010 Regardless of the location of the probe, all three pyrene-labeled apoE CT variants display an intense and dramatic fluorescence excimer band at 460 nm, a signature feature of pyrene, which indicates that two pyrene moieties are within 10 A of each other. pyrene 175-181 apolipoprotein E Homo sapiens 66-70 15708851-0 2005 Examination of lipid-bound conformation of apolipoprotein E4 by pyrene excimer fluorescence. pyrene 64-70 apolipoprotein E Homo sapiens 43-60 15708851-8 2005 Pyrene excimer fluorescence was noted in lipid-free pyrene-R61C/E255C/apoE4 in mixtures containing excess wild-type apoE4, which was attributed to intramolecular spatial proximity between these specified sites. pyrene 0-6 apolipoprotein E Homo sapiens 70-75 15708851-8 2005 Pyrene excimer fluorescence was noted in lipid-free pyrene-R61C/E255C/apoE4 in mixtures containing excess wild-type apoE4, which was attributed to intramolecular spatial proximity between these specified sites. pyrene 0-6 apolipoprotein E Homo sapiens 116-121 15708851-8 2005 Pyrene excimer fluorescence was noted in lipid-free pyrene-R61C/E255C/apoE4 in mixtures containing excess wild-type apoE4, which was attributed to intramolecular spatial proximity between these specified sites. pyrene 52-58 apolipoprotein E Homo sapiens 70-75 15708851-8 2005 Pyrene excimer fluorescence was noted in lipid-free pyrene-R61C/E255C/apoE4 in mixtures containing excess wild-type apoE4, which was attributed to intramolecular spatial proximity between these specified sites. pyrene 52-58 apolipoprotein E Homo sapiens 116-121 15708851-9 2005 Upon disruption of tertiary interaction, a large decrease in excimer fluorescence emission was noted in pyrene-R61C/E255C/apoE4. pyrene 104-110 apolipoprotein E Homo sapiens 122-127 15708851-10 2005 In dimyristoylphosphatidylcholine/pyrene-R61C/E255C/apoE4 discoidal complexes, pyrene excimer fluorescence emission was retained. pyrene 34-40 apolipoprotein E Homo sapiens 52-57 15708851-10 2005 In dimyristoylphosphatidylcholine/pyrene-R61C/E255C/apoE4 discoidal complexes, pyrene excimer fluorescence emission was retained. pyrene 79-85 apolipoprotein E Homo sapiens 52-57