ArticleACS nano2018
Modular Self-Assembly of Protein Cage Lattices for Multistep Catalysis.
Article in ACS nano, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 112 citations in OpenAlex.
- Review
- Reversible Assembly of Virus-Like Particles (VLPs) into Higher-Order Structures Controlled by Oxidation and Reduction of Linker Protein.ACS applied bio materials · 2026Article
- Computer Simulations Show That Liquid-Liquid Phase Separation Enhances Self-Assembly.ACS nano · 2025Article
- Colloidal Crystallization of Virus-Like Particles with Polycations.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Modular protein frameworks via supramolecular synthons.Biophysical reviews · 2025Review
- Confinement-Induced Metastable Supramolecular Assembly: Dynamic Built-in Electric Field Driving Deep Mineralization of Organic Pollutants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance.ACS nano · 2024Article
- Article
- Coupling Peptide-Based Encapsulation of Enzymes with Bacteria for Paraoxon Bioremediation.ACS applied materials & interfaces · 2024Article
- Mechanistic Insights Behind the Self-Assembly of Human Insulin under the Influence of Surface-Engineered Gold Nanoparticles.ACS chemical neuroscience · 2024Article
- Pore engineering as a general strategy to improve protein-based enzyme nanoreactor performance.bioRxiv : the preprint server for biology · 2024Article
- Supramolecular Synthons in Protein-Ligand Frameworks.Crystal growth & design · 2024Article
- Virus-like particle encapsulation of functional proteins: advances and applications.Theranostics · 2024Review
- Engineering and Bio/Nanotechnological Applications of Virus Particles.Sub-cellular biochemistry · 2024Review
- Enhancing Multistep Reactions: Biomimetic Design of Substrate Channeling Using P22 Virus-Like Particles.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Quantitative functionalization of biosynthetic caged protein materials.Quantitative biology (Beijing, China) · 2023Review
- Review
- High order assembly of multiple protein cages with homogeneous sizes and shapesChemical science · 2023Article
- Harnessing physicochemical properties of virus capsids for designing enzyme confined nanocompartments.Current opinion in virology · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 8 institutions in 2 countries.
Funding
Abstract
The assembly of individual molecules into hierarchical structures is a promising strategy for developing three-dimensional materials with properties arising from interaction between the individual building blocks. Virus capsids are elegant examples of biomolecular nanostructures, which are themselves hierarchically assembled from a limited number of protein subunits. Here, we demonstrate the bio-inspired modular construction of materials with two levels of hierarchy: the formation of catalytically active individual virus-like particles (VLPs) through directed self-assembly of capsid subunits with enzyme encapsulation, and the assembly of these VLP building blocks into three-dimensional arrays. The structure of the assembled arrays was successfully altered from an amorphous aggregate to an ordered structure, with a face-centered cubic lattice, by modifying the exterior surface of the VLP without changing its overall morphology, to modulate interparticle interactions. The assembly behavior and resultant lattice structure was a consequence of interparticle interaction between exterior surfaces of individual particles and thus independent of the enzyme cargos encapsulated within the VLPs. These superlattice materials, composed of two populations of enzyme-packaged VLP modules, retained the coupled catalytic activity in a two-step reaction for isobutanol synthesis. This study demonstrates a significant step toward the bottom-up fabrication of functional superlattice materials using a self-assembly process across multiple length scales and exhibits properties and function that arise from the interaction between individual building blocks.
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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.