N-terminal domain of apolipoprotein B has structural homology to lipovitellin and microsomal triglyceride transfer protein: a “lipid pocket” model for self-assembly of apoB-containing lipoprotein particles-Reference-Cited by-同舟云学术

N-terminal domain of apolipoprotein B has structural homology to lipovitellin and microsomal triglyceride transfer protein: a “lipid pocket” model for self-assembly of apoB-containing lipoprotein particles

Published:1999-08 Issue:8 Volume:40 Page:1401-1416
ISSN:0022-2275
Container-title:Journal of Lipid Research
language:en
Short-container-title:Journal of Lipid Research

Author:

Segrest Jere P.,Jones Martin K.,Dashti Nassrin

Publisher

Elsevier BV

Subject

Cell Biology,Endocrinology,Biochemistry

Reference33 articles.

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2. Role of intramolecular disulfide bond formation in the assembly and secretion of apolipoprotein B-100-containing lipoproteins;Shelness;J. Lipid Res.,1996

3. Folding of the aminoterminal domain of apolipoprotein B initiates microsomal triglyceride transfer protein-dependent lipid transfer to nascent very low density lipoprotein;Ingram;J. Biol. Chem.,1997

4. Identification of cysteine pairs within the amino-terminal 5% of apolipoprotein B essential for hepatic lipoprotein assembly and secretion;Huang;J. Biol. Chem.,1997

5. Functional analysis of disulfide linkages clustered within the amino terminus of human apolipoprotein B;Tran;J. Biol. Chem.,1998

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