Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure.-Reference-Cited by-同舟云学术

Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure.

Published:1990-05 Issue:15 Volume:265 Page:8610-8617
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

von Eckardstein A,Funke H,Walter M,Altland K,Benninghoven A,Assmann G

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference67 articles.

1. Isolation and characterization of the human apolipoprotein A-I gene.

2. Lipid-Protein Interactions in High Density Lipoproteins

3. A protein cofactor of lecithin:Cholesterol acyltransferase

4. Interaction of high density lipoproteins with cholesteryl ester-laden macrophages: biochemical and morphological characterization of cell surface receptor binding, endocytosis and resecretion of high density lipoproteins by macrophages.

5. Identification of apolipoproteins involved in the interaction of human high density lipoprotein3 with receptors on cultured cells.

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