Antibodies to the carboxyl terminus of human apolipoprotein A-I. The putative cellular binding domain of high density lipoprotein 3 and carboxyl-terminal structural homology between apolipoproteins A-I and A-II.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
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1. Deletion of the propeptide of apolipoprotein A-I reduces protein expression but stimulates effective conversion of preβ-high density lipoprotein to α-high density lipoprotein;Journal of Lipid Research;2000-11
2. Identification of an ApoA-I Ligand Domain That Interacts with High-Affinity Binding Sites on HepG2 Cells;Biochemical and Biophysical Research Communications;2000-01
3. A Single Amino Acid Deletion in the Carboxy Terminal of Apolipoprotein A-I Impairs Lipid Binding and Cellular Interaction;Arteriosclerosis, Thrombosis, and Vascular Biology;2000-01
4. Effectivity of Expression of Mature Forms of Mutant Human Apolipoprotein A-I;Protein Expression and Purification;1999-11
5. Branched synthetic peptide constructs mimic cellular binding and efflux of apolipoprotein AI in reconstituted high density lipoproteins;Atherosclerosis;1998-12
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