ArticleThe Biochemical journal2005
Orientation and mode of lipid-binding interaction of human apolipoprotein E C-terminal domain.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 35 citations in OpenAlex.
- Apolipoprotein E Mimetic Peptide-Mediated Modulation of Lipid Homeostasis.Biomolecules · 2026Review
- Structural Change of ApoE-Lipid Nanoparticles Alters Receptor-Mediated Endocytosis and Induces Endosomal Disruption.Journal of the American Chemical Society · 2026Article
- Usefulness of plasma and apolipoprotein B-depleted serum samples in paraoxonase 1 assessment.Biochemistry and biophysics reports · 2025Article
- Apolipoprotein E3 Containing Nanodiscs as Vehicles for Transport and Targeted Delivery of Flavonoid Luteolin.ACS omega · 2024Article
- Molecular dynamics simulation of apolipoprotein E3 lipid nanodiscs.Biochimica et biophysica acta. Biomembranes · 2024Article
- Article
- Insights into the C-terminal domain of apolipoprotein E from chimera studies with apolipophorin III.Molecular and cellular biochemistry · 2023Article
- Endogenous Human Proteins Interfering with Amyloid Formation.Biomolecules · 2022Review
- ApoE Lipidation as a Therapeutic Target in Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Reconfiguring Nature's Cholesterol Accepting Lipoproteins as Nanoparticle Platforms for Transport and Delivery of Therapeutic and Imaging Agents.Nanomaterials (Basel, Switzerland) · 2020Review
- APOE in the normal brain.Neurobiology of disease · 2020Review
- The Genetic Variability ofGenes · 2019Review
- Lipidated apolipoprotein E4 structure and its receptor binding mechanism determined by a combined cross-linking coupled to mass spectrometry and molecular dynamics approach.PLoS computational biology · 2018Article
- IgG Antibody 3D Structures and Dynamics.Antibodies (Basel, Switzerland) · 2018Review
- Mechanism of Lipid Binding of Human Apolipoprotein E3 by Hydrogen/Deuterium Exchange/Mass Spectrometry and Fluorescence Polarization.Protein and peptide letters · 2016Article
- Optimized negative staining: a high-throughput protocol for examining small and asymmetric protein structure by electron microscopy.Journal of visualized experiments : JoVE · 2014Article
- Acrolein modification impairs key functional features of rat apolipoprotein E: identification of modified sites by mass spectrometry.Biochemistry · 2014Article
- Biochemical and biophysical characterization of recombinant rat apolipoprotein E: similarities to human apolipoprotein E3.Archives of biochemistry and biophysics · 2013Article
- Optimized negative-staining electron microscopy for lipoprotein studies.Biochimica et biophysica acta · 2013Review
- Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ApoE (apolipoprotein E) is an anti-atherogenic lipid transport protein that plays an integral role in lipoprotein metabolism and cholesterol homoeostasis. Lipid association educes critical functional features of apoE, mediating reduction in plasma and cellular cholesterol levels. The 10-kDa CT (C-terminal) domain of apoE facilitates helix-helix interactions in lipid-free state to promote apoE self-association and helix-lipid interactions during binding with lipoproteins, although the mode of lipid-binding interaction is not well understood. We investigated the mode of lipid-binding interaction and orientation of apoE CT domain on reconstituted lipoproteins. Isolated recombinant human apoE CT domain (residues 201-299) possesses a strong ability to interact with phospholipid vesicles, yielding lipoprotein particles with an apparent molecular mass of approximately 600 kDa, while retaining the overall alpha-helical content. Electron microscopy and non-denaturing PAGE analysis of DMPC (dimyristoylphosphatidylcholine)--apoE CT domain lipoprotein complexes revealed discoidal complexes with a diameter of approx. 17 nm. Cross-linking apoE CT domain on discoidal particles yielded dimeric species as the major product. Attenuated total reflectance Fourier transform IR spectroscopy of phospholipid-apoE CT domain complexes reveals that the helical axis is oriented perpendicular to fatty acyl chains of the phospholipid. Fluorescence quenching analysis of DMPC-apoE CT domain discoidal complexes by spin-labelled stearic acid indicated a relatively superficial location of the native tryptophan residues with respect to the plane of the phospholipid bilayer. Taken together, we propose that apoE CT domain interacts with phospholipid vesicles, forming a long extended helix that circumscribes the discoidal bilayer lipoprotein complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.