Title : Role of oxysterol structure on the microdomain-induced microsolubilization of phospholipid membranes by apolipoprotein A-I.

Pub. Date : 2005 Nov 1

PMID : 16245954






5 Functional Relationships(s)
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1 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. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
2 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. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
3 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. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
4 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. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
5 The rate of DMPC microsolubilization by apoA-I is highly dependent upon the presence of lattice defects in the membrane surface that occur due to imperfect packing of coexisting lipid phases. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens