PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16245954-0 2005 Role of oxysterol structure on the microdomain-induced microsolubilization of phospholipid membranes by apolipoprotein A-I. Oxysterols 8-17 apolipoprotein A1 Homo sapiens 104-122 22488423-5 2012 The ATP-binding cassette (ABC) transporters ABCA1 and ABCG1, and the scavenger receptor B type 1 mediate multiple intracellular signaling pathways as well as the efflux of cholesterol and/or oxysterols in response to apoA-I/HDL. Oxysterols 191-201 apolipoprotein A1 Homo sapiens 217-223 31382484-7 2019 Lipid subclass analyses revealed various oxysterols, sphingomyelins, and ceramides, species uniquely enriched in human plaques were significantly reduced by cholesterol acceptors, especially by apoA-I. Oxysterols 41-51 apolipoprotein A1 Homo sapiens 194-200 22488423-7 2012 SUMMARY: Current data suggest that in endothelial cells ABCA1 and ABCG1 mediate the activation of intracellular signaling pathways primarily through the efflux of cholesterol and oxysterols to apoA-I/HDL. Oxysterols 179-189 apolipoprotein A1 Homo sapiens 193-199 17053191-7 2006 Upregulation of ABCA1 with oxysterols increased apoA-I binding and internalization. Oxysterols 27-37 apolipoprotein A1 Homo sapiens 48-54 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. Oxysterols 211-220 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. Oxysterols 211-220 apolipoprotein A1 Homo sapiens 123-129 11035776-5 2000 We further demonstrate that expression of LXR alpha in NIH 3T3 fibroblasts and/or treatment of these cells with oxysterols is sufficient to stimulate cholesterol efflux to extracellular apolipoprotein AI. Oxysterols 112-122 apolipoprotein A1 Homo sapiens 186-203 11669638-1 2001 Cholesterol removal from lipid-loaded macrophages is an important, potentially antiatherogenic process, and we have previously shown that an oxysterol, 7-ketocholesterol (7K), can impair efflux to lipid-free apoprotein A-1 (apoA-1). Oxysterols 141-150 apolipoprotein A1 Homo sapiens 224-230 10933125-6 2000 Importantly, the effects of oxysterols, such as 7-ketocholesterol (7KC), on cholesterol and other lipid efflux by apoA-I needs to be investigated in any attempt to utilise apoA-I as an agent to stimulate efflux of lipids. Oxysterols 28-38 apolipoprotein A1 Homo sapiens 114-120 7744831-1 1995 In the present study, lecithin-cholesterol acyltransferase (LCAT) catalyzed esterification of oxysterols was investigated by using discoidal bilayer particles (DBP) containing various oxysterols, phosphatidylcholines, and apolipoprotein A-I. Oxysterols 94-104 apolipoprotein A1 Homo sapiens 222-240