ArticleNature cardiovascular research2022
Cholesterol efflux mechanism revealed by structural analysis of human ABCA1 conformational states.
Article in Nature cardiovascular research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 34 citations in OpenAlex.
- Lipid transport mechanisms in human ABCA family transporters: a structural perspective.Biochemical Society transactions · 2026Review
- ABCA1-mediated lipid efflux restrains oxidative stress and neuroinflammation after spinal cord injury.Journal of neuroinflammation · 2026Article
- Balancing cholesterol metabolism in the liver and gut: perspectives in health and disease.Nature reviews. Gastroenterology & hepatology · 2026Review
- ABCA1-Mediated Structural Diversity of HDL Subspecies and Their Proposed Roles in Cardioprotection.Arteriosclerosis, thrombosis, and vascular biology · 2026Review
- RORα: a critical nexus in the crosstalk between cholesterol metabolism and macrophage polarization.Frontiers in immunology · 2026Review
- Synthesis and evaluation of 5, 6-dihydro-8Journal of enzyme inhibition and medicinal chemistry · 2025Article
- Direct Visualization of ATP-Binding Cassette Protein A1 Mediated Nascent High-Density Lipoprotein Biogenesis by High-Speed Atomic Force Microscopy.Nano letters · 2025Article
- Revisiting the Role of the Leucine Plug/Valve in the Human ABCG2 Multidrug Transporter.International journal of molecular sciences · 2025Article
- Lipidome disruption in Alzheimer's disease brain: detection, pathological mechanisms, and therapeutic implications.Molecular neurodegeneration · 2025Review
- Role ofCurrent medicinal chemistry · 2025Review
- ATP-Binding Cassette and Solute Carrier Transporters: Understanding Their Mechanisms and Drug Modulation Through Structural and Modeling Approaches.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Does Exercise Affect Cancer via Reverse Cholesterol Transport Process? A Hypothesis Which Needs to Be Clarified by Researchers.Advanced pharmaceutical bulletin · 2024Article
- Cryo-EM structures of Myomaker reveal a molecular basis for myoblast fusion.Nature structural & molecular biology · 2023Article
- Structural basis for abscisic acid efflux mediated by ABCG25 in Arabidopsis thaliana.Nature plants · 2023Article
- Is reverse cholesterol transport regulated by active cholesterol?Journal of lipid research · 2023Review
- Activity and Structural Dynamics of Human ABCA1 in a Lipid Membrane.Journal of molecular biology · 2023Article
- Biomedical Advances in ABCA1 Transporter: From Bench to Bedside.Biomedicines · 2023Review
- Cholesterol-Lowering Activity of Vitisin A Is Mediated by Inhibiting Cholesterol Biosynthesis and Enhancing LDL Uptake in HepG2 Cells.International journal of molecular sciences · 2023Article
- Efficacy and underlying mechanisms of berberine against lipid metabolic diseases: a review.Frontiers in pharmacology · 2023Review
- New insights into cholesterol efflux via ABCA1.Nature cardiovascular research · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
ATP-binding cassette transporter A1 (ABCA1) utilizes energy derived from ATP hydrolysis to export cholesterol and phospholipids from macrophages. ABCA1 plays a central role in the biosynthesis of high-density lipoprotein (HDL), which mediates reverse cholesterol transport and prevents detrimental lipid deposition. Mutations in ABCA1 cause Tangier disease characterized by a remarkable reduction in the amount of HDL in blood. Here we present cryo-electron microscopy structures of human ABCA1 in ATP-bound and nucleotide-free states. Structural comparison reveals that ATP molecules pull the nucleotide-binding domains together, inducing movements of transmembrane helices 1, 2, 7 and 8 through a series of salt-bridge interactions. Subsequently, extracellular domains (ECDs) undergo a rotation and introduce conformational changes in the ECD-transmembrane interface. In addition, while we observe a sterol-like molecule in ECDs, no such density was observed in the structure of an HDL-deficiency mutant ABCA1
Identifiers
What OpenQuestion holds
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.