ArticleNature chemistry2014
Structure of a designed protein cage that self-assembles into a highly porous cube.
Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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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
108 citing papers in PubMed.
- Review
- I53-50: Engineered icosahedral protein cage for modular vaccine nanoplatform.Journal of microbiology (Seoul, Korea) · 2026Review
- Engineering complexity into protein-based biomaterials for biomedical applications.Nature reviews. Materials · 2026Article
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Construction of artificial organellesChemical science · 2025Review
- Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Computational design of bifaceted protein nanomaterials.Nature materials · 2025Article
- Automatic design and optimization of MRI-based neurochemical sensors via reinforcement learning.Discover nano · 2025Article
- Modular protein frameworks via supramolecular synthons.Biophysical reviews · 2025Review
- Protein design of two-component tubular assemblies similar to cytoskeletons.Nature communications · 2025Article
- Local structural flexibility drives oligomorphism in computationally designed protein assemblies.Nature structural & molecular biology · 2025Article
- Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Article
- Article
- A suite of designed protein cages using machine learning and protein fragment-based protocols.Structure (London, England : 1993) · 2024Article
- Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation.Acta crystallographica. Section F, Structural biology communications · 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
- An interaction network approach predicts protein cage architectures in bionanotechnology.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
48 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Natural proteins can be versatile building blocks for multimeric, self-assembling structures. Yet, creating protein-based assemblies with specific geometries and chemical properties remains challenging. Highly porous materials represent particularly interesting targets for designed assembly. Here, we utilize a strategy of fusing two natural protein oligomers using a continuous alpha-helical linker to design a novel protein that self assembles into a 750 kDa, 225 Å diameter, cube-shaped cage with large openings into a 130 Å diameter inner cavity. A crystal structure of the cage showed atomic-level agreement with the designed model, while electron microscopy, native mass spectrometry and small angle X-ray scattering revealed alternative assembly forms in solution. These studies show that accurate design of large porous assemblies with specific shapes is feasible, while further specificity improvements will probably require limiting flexibility to select against alternative forms. These results provide a foundation for the design of advanced materials with applications in bionanotechnology, nanomedicine and material sciences.
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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.