ReviewComparative biochemistry and physiology. Part A, Molecular & integrative physiology2010
The helix bundle: a reversible lipid binding motif.
Review in Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- Tardigrades' cytoplasmic abundant heat soluble proteins serve as membrane protectors during dehydration.Research square · 2025Article
- Apolipoprotein A (ApoA) in Neurological Disorders: Connections and Insights.International journal of molecular sciences · 2025Review
- An ELISA-based method forPeerJ · 2024Article
- Binding of perilipin 3 to membranes containing diacylglycerol is mediated by conserved residues within its PAT domain.The Journal of biological chemistry · 2023Article
- Insights into the C-terminal domain of apolipoprotein E from chimera studies with apolipophorin III.Molecular and cellular biochemistry · 2023Article
- Engineered rHDL Nanoparticles as a Suitable Platform for Theranostic Applications.Molecules (Basel, Switzerland) · 2022Article
- Fragments ofBBA advances · 2021Article
- Reconfiguring Nature's Cholesterol Accepting Lipoproteins as Nanoparticle Platforms for Transport and Delivery of Therapeutic and Imaging Agents.Nanomaterials (Basel, Switzerland) · 2020Review
- Dual binding motifs underpin the hierarchical association of perilipins1-3 with lipid droplets.Molecular biology of the cell · 2019Article
- Charged Residues in the C-Terminal Domain of Apolipoprotein A-I Modulate Oligomerization.Biochemistry · 2018Article
- Expression of the C-terminal domain of human apolipoprotein A-I using a chimeric apolipoprotein.Protein expression and purification · 2017Article
- Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.Science advances · 2017Article
- Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity.Biochimica et biophysica acta. Biomembranes · 2017Article
- The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome.Scientific reports · 2017Article
- The Conformation of Interfacially Adsorbed Ranaspumin-2 Is an Arrested State on the Unfolding Pathway.Biophysical journal · 2016Article
- Deletion of the N- or C-Terminal Helix of Apolipophorin III To Create a Four-Helix Bundle Protein.Biochemistry · 2016Article
- ApoA1 and ApoA1-specific self-antibodies in cardiovascular disease.Laboratory investigation; a journal of technical methods and pathology · 2016Review
- Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella.Biomolecular NMR assignments · 2016Article
- Mechanism of Lipid Binding of Human Apolipoprotein E3 by Hydrogen/Deuterium Exchange/Mass Spectrometry and Fluorescence Polarization.Protein and peptide letters · 2016Article
- The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Apolipoproteins are the protein components of lipoproteins that have the innate ability to inter convert between a lipid-free and a lipid-bound form in a facile manner, a remarkable property conferred by the helix bundle motif. Composed of a series of four or five amphipathic alpha-helices that fold to form a helix bundle, this motif allows the en face orientation of the hydrophobic faces of the alpha-helices in the protein interior in the lipid-free state. A conformational switch then permits helix-helix interactions to be substituted by helix-lipid interactions upon lipid binding interaction. This review compares the apolipoprotein high-resolution structures and the factors that trigger this switch in insect apolipophorin III and the mammalian apolipoproteins, apolipoprotein E and apolipoprotein A-I, pointing out the commonalities and key differences in the mode of lipid interaction. Further insights into the lipid-bound conformation of apolipoproteins are required to fully understand their functional role under physiological conditions.
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Registered trials
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.