ArticleACS nano2020
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways.
Article in ACS nano, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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Who cites it
27 citing papers in PubMed.
- Article
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- Atomistic characterization of the maturation mechanisms in the HIV-1 capsid domain.Nature communications · 2026Article
- Zooming into Disease at the Nanoscale: High-Speed Atomic Force Microscopy in Biomedical Discovery.ACS nano · 2026Review
- Using atomic force microscopy for physical virology: touching and manipulating single virus particles.Biophysical reviews · 2026Review
- Article
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Structural Basis for Alternative Self-Assembly Pathways Leading to Different Human Immunodeficiency Virus Capsid-Like Nanoparticles.ACS nano · 2024Article
- Light-driven eco-evolutionary dynamics in a synthetic replicator system.Nature chemistry · 2024Article
- Atomic Force Microscopy of Viruses.Sub-cellular biochemistry · 2024Review
- Theoretical Studies on Assembly, Physical Stability, and Dynamics of Viruses.Sub-cellular biochemistry · 2024Review
- Understanding Virus Structure and Dynamics through Molecular Simulations.Journal of chemical theory and computation · 2023Review
- Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action.Microscopy (Oxford, England) · 2023Review
- Article
- Artificial Protein Cage with Unusual Geometry and Regularly Embedded Gold Nanoparticles.Nano letters · 2022Article
- Review
- Review
- Antiviral compounds modulate elasticity, strength and material fatigue of a virus capsid framework.Biophysical journal · 2022Article
- High-speed atomic force microscopy reveals a three-state elevator mechanism in the citrate transporter CitS.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Direct visualization of pathways followed by single molecules while they spontaneously self-assemble into supramolecular biological machines may provide fundamental knowledge to guide molecular therapeutics and the bottom-up design of nanomaterials and nanodevices. Here, high-speed atomic force microscopy is used to visualize self-assembly of the bidimensional lattice of protein molecules that constitutes the framework of the mature human immunodeficiency virus capsid. By real-time imaging of the assembly reaction, individual transient intermediates and reaction pathways followed by single molecules could be revealed. As when assembling a jigsaw puzzle, the capsid protein lattice is randomly built. Lattice patches grow independently from separate nucleation events whereby individual molecules follow different paths. Protein subunits can be added individually, while others form oligomers before joining a lattice or are occasionally removed from the latter. Direct real-time imaging of supramolecular self-assembly has revealed a complex, chaotic process involving multiple routes followed by individual molecules that are inaccessible to bulk (averaging) techniques.
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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.