ArticleProceedings of the National Academy of Sciences of the United States of America2024
Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed.
- Molecular insights into dynamic RNA quaternary assemblies.RNA biology · 2026Review
- Development and immunogenicity of adenoviral Fc-fused FMDV virus-like particle vaccine in swine.The veterinary quarterly · 2025Article
- Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024Review
- Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance.ACS nano · 2024Article
- Pore engineering as a general strategy to improve protein-based enzyme nanoreactor performance.bioRxiv : the preprint server for biology · 2024Article
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion.Protein science : a publication of the Protein Society · 2024Article
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Funding
Abstract
Protein capsids are a widespread form of compartmentalization in nature. Icosahedral symmetry is ubiquitous in capsids derived from spherical viruses, as this geometry maximizes the internal volume that can be enclosed within. Despite the strong preference for icosahedral symmetry, we show that simple point mutations in a virus-like capsid can drive the assembly of unique symmetry-reduced structures. Starting with the encapsulin from
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