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Expression and activity of the nucleotide-binding domains of the human ABCA1 transporter
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Characterization of the ABCA transporter subfamily: Identification of prokaryotic and eukaryotic members, phylogeny and topology
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Effect of mutations of N- and C-terminal charged residues on the activity of LCAT.
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Three arginine residues in apolipoprotein A-I are critical for activation of lecithin: cholesterol acyltransferase.
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Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT).
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Displacement of apo A-I from HDL by apo A-II or its C-terminal helix promotes the formation of pre-beta(1) migrating particles and decreases LCAT activation.
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The C-terminal helix of human apolipoprotein AII promotes the fusion of unilamellar liposomes and displaces apolipoprotein AI from high-density lipoproteins.
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A proposed architecture for lecithin cholesterol acyl transferase (LCAT): Identification of the catalytic triad and molecular modeling.