ArticleNano letters2025
Direct Visualization of ATP-Binding Cassette Protein A1 Mediated Nascent High-Density Lipoprotein Biogenesis by High-Speed Atomic Force Microscopy.
Article in Nano letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- High-speed atomic force microscopy of membrane proteins: From dynamic imaging to integrative structural biology.Current opinion in structural biology · 2026Review
- Comparing multislice projections of MD simulations with cryo-EM exposes structural prediction errors.Biophysical journal · 2026Article
- Feedforward compensation of piezo nonlinearity for high-precision high-speed atomic force microscopy.Scientific reports · 2026Article
- Comparing Multislice Projections of MD Simulations with CryoEM Exposes Structural Prediction Errors.bioRxiv : the preprint server for biology · 2026Article
- Visualizing the Functional Dynamics of P-Glycoprotein and Its Modulation by Elacridar via High-Speed Atomic Force Microscopy.International journal of molecular sciences · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The ATP-binding cassette protein A1 (ABCA1) is crucial for high-density lipoprotein (HDL) formation, maintaining cholesterol homeostasis. However, the mechanism of ABCA1-mediated HDL formation remains unclear. Here, we reconstituted this process and directly visualized it using high-speed atomic force microscopy by employing a novel linker-based immobilization strategy for side-view imaging of ABCA1 nanodiscs. Our data revealed an approximately 1.6-fold volumetric expansion of the ABCA1 extracellular domain (ECD), coupled with a contraction of the ABCA1-embedded nanodisc, suggesting ATP-dependent transfer of over 300 lipids to the ECD for transient storage. Subsequent addition of apolipoprotein A-I, a major HDL protein, allowed ABCA1 to facilitate nascent HDL particle formation, as it does at the cell membrane. Notably, this study provides the first direct observation of a single ABC protein executing its unique functional cycle with submolecular spatial and subsecond temporal resolution, offering critical insights into "HDL biogenesis", with potential implications for ABCA1-targeted therapeutics for dyslipidemia.
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Registered trials
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