Structure and function of apolipoprotein A-I and high-density lipoprotein

被引：113

作者：

Segrest, JP

Li, L

Anantharamaiah, GM

Harvey, SC

Liadaki, KN

Zannis, V

机构：

[1] Univ Alabama, Med Ctr, Dept Med, Atherosclerosis Res Unit, Birmingham, AL 35294 USA

[2] Univ Alabama, Med Ctr, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA

[3] Univ Crete, Sch Med, Crete, Greece

[4] Univ Crete, Inst Mol Biol & Biotechnol, Crete, Greece

[5] Boston Univ, Sch Med, Cardiovasc Inst, Mol Genet Sect, Boston, MA 02118 USA

来源：

CURRENT OPINION IN LIPIDOLOGY | 2000年 / 11卷 / 02期

关键词：

D O I：

10.1097/00041433-200004000-00002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Structural biology and molecular modeling have provided intriguing insights into the atomic details of the lipid-associated structure of the major protein component of HDL, apo A-I. For the first time, an atomic resolution map is available for future studies of the molecular interactions of HDL in such biological processes as ABC1-regulated HDL assembly, LCAT activation, receptor binding, reverse lipid transport and HDL heterogeneity. Within the context of this paradigm, the current review summarizes the state of HDL research. Curr Opin Lipidol 11:105-115. (C) 2000 Lippincott Williams & Wilkins.

引用

页码：105 / 115

页数：11

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