ArticleBiophysical journal2005
Assembly of lipoprotein particles containing apolipoprotein-B: structural model for the nascent lipoprotein particle.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Century of Progress on the Structure of APOB-100 in Atherogenic Lipoproteins.Circulation research · 2026Review
- Article
- A New Structural Model of Apolipoprotein B100 Based on Computational Modeling and Cross Linking.International journal of molecular sciences · 2022Article
- Fibrinogen Gamma Chain Mutations Provoke Fibrinogen and Apolipoprotein B Plasma Deficiency and Liver Storage.International journal of molecular sciences · 2017Article
- Phospholipid transfer protein plays a major role in the initiation of apolipoprotein B-containing lipoprotein assembly in mouse primary hepatocytes.The Journal of biological chemistry · 2015Article
- Study of Protein Biomarkers of Diabetes Mellitus Type 2 and Therapy with Vitamin B1.Journal of diabetes research · 2015Review
- Surface tensiometry of apolipoprotein B domains at lipid interfaces suggests a new model for the initial steps in triglyceride-rich lipoprotein assembly.The Journal of biological chemistry · 2014Article
- Human LDL structural diversity studied by IR spectroscopy.PloS one · 2014Article
- Vitellogenin recognizes cell damage through membrane binding and shields living cells from reactive oxygen species.The Journal of biological chemistry · 2013Article
- Three-dimensional cryoEM reconstruction of native LDL particles to 16Å resolution at physiological body temperature.PloS one · 2011Article
- Apolipoprotein B-containing lipoprotein assembly in microsomal triglyceride transfer protein-deficient McA-RH7777 cells.Journal of lipid research · 2010Article
- Interfacial properties of apolipoprotein B292-593 (B6.4-13) and B611-782 (B13-17). Insights into the structure of the lipovitellin homology region in apolipoprotein B.Biochemistry · 2010Article
- Nonsynonymous mutations within APOB in human familial hypobetalipoproteinemia: evidence for feedback inhibition of lipogenesis and postendoplasmic reticulum degradation of apolipoprotein B.The Journal of biological chemistry · 2010Article
- Surface study of apoB1694-1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable.Journal of lipid research · 2009Article
- Circulatory lipid transport: lipoprotein assembly and function from an evolutionary perspective.Molecular and cellular biochemistry · 2009Review
- Structural and dynamic interfacial properties of the lipoprotein initiating domain of apolipoprotein B.Journal of lipid research · 2009Article
- Reconstituting initial events during the assembly of apolipoprotein B-containing lipoproteins in a cell-free system.Journal of molecular biology · 2008Article
- Charged amino acid residues 997-1000 of human apolipoprotein B100 are critical for the initiation of lipoprotein assembly and the formation of a stable lipidated primordial particle in McA-RH7777 cells.The Journal of biological chemistry · 2008Article
- Structural analysis of reconstituted lipoproteins containing the N-terminal domain of apolipoprotein B.Biophysical journal · 2007Article
- The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant.Infection and immunity · 2007Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Apolipoprotein B (apoB) is the major protein component of large lipoprotein particles that transport lipids and cholesterol. We have developed a detailed model of the first 1000 residues of apoB using standard sequence alignment programs (ClustalW and MACAW) and the MODELLER6 package for three-dimensional homology modeling. The validity of the apoB model was supported by conservation of disulfide bonds, location of all proline residues in turns and loops, and conservation of the hydrophobic faces of the two C-terminal amphipathic beta-sheets, betaA (residues 600-763) and betaB (residues 780-1000). This model suggests a lipid-pocket mechanism for initiation of lipoprotein particle assembly. In a previous model we suggested that microsomal triglyceride transfer protein might play a structural role in completion of the lipid pocket. We no longer think this likely, but instead propose a hairpin-bridge mechanism for lipid pocket completion. Salt-bridges between four tandem charged residues (717-720) in the turn of the hairpin-bridge and four tandem complementary residues (997-1000) at the C-terminus of the model lock the bridge in the closed position, enabling the deposition of an asymmetric bilayer within the lipid pocket.
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Registered trials
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