Structural Analysis of Reconstituted Lipoproteins Containing the N-Terminal Domain of Apolipoprotein B
- 1 June 2007
- journal article
- Published by Elsevier BV in Biophysical Journal
- Vol. 92 (11), 4097-4108
- https://doi.org/10.1529/biophysj.106.101105
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Defining Lipid-Interacting Domains in the N-Terminal Region of Apolipoprotein BBiochemistry, 2006
- Apolipoprotein B is conformationally flexible but anchored at a triolein/water interface: A possible model for lipoprotein surfacesProceedings of the National Academy of Sciences of the United States of America, 2006
- Phospholipid Transfer Activity of Microsomal Triacylglycerol Transfer Protein Is Sufficient for the Assembly and Secretion of Apolipoprotein B LipoproteinsPublished by Elsevier BV ,2006
- The Interfacial Properties of ApoA-I and an Amphipathic -Helix Consensus Peptide of Exchangeable Apolipoproteins at the Triolein/Water InterfaceJournal of Biological Chemistry, 2005
- Identification of the Lipoprotein Initiating Domain of Apolipoprotein BPublished by Elsevier BV ,2003
- The structure of vitellogenin provides a molecular model for the assembly and secretion of atherogenic lipoproteinsJournal of Molecular Biology, 1999
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- apoB-100 has a pentapartite structure composed of three amphipathic alpha-helical domains alternating with two amphipathic beta-strand domains. Detection by the computer program LOCATE.Arteriosclerosis and Thrombosis: A Journal of Vascular Biology, 1994
- Mechanism of microsomal triglyceride transfer protein catalyzed lipid transportBiochemistry, 1993
- Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 Å resolutionJournal of Molecular Biology, 1988