ReviewBiomacromolecules2019
Protein Assemblies: Nature-Inspired and Designed Nanostructures.
Review in Biomacromolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed.
- A Generative Neuro-Symbolic AI for Protein Sequence Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Impact of solvent forces and broken symmetry on the assembly of designed proteins at a liquid-solid interface.Nature communications · 2026Article
- Construction of artificial organellesChemical science · 2025Review
- Structural polymorphism of two-dimensional lattices assembled from baculoviral capsid proteins.Virologica Sinica · 2025Article
- Living/controlled supramolecular protein polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Synergestic Protein-Green synthesized Nanoparticles Nanosystems: A Sustainable and Safe Approach for Cancer Theranostics.Nanotheranostics · 2025Review
- Heterotelechelic Organometallic PEG Reagents Enable Modular Access to Complex Bioconjugates.ACS macro letters · 2024Article
- Single-molecule digital sizing of proteins in solution.Nature communications · 2024Article
- Modeling reveals the strength of weak interactions in stacked-ring assembly.Biophysical journal · 2024Article
- Glucose-Triggered Gelation of Supramolecular Peptide Nanocoils with Glucose-Binding Motifs.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome.Structure (London, England : 1993) · 2023Article
- Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Single-Molecule Sizing through Nanocavity Confinement.Nano letters · 2023Article
- Article
- Dissecting the general mechanisms of protein cage self-assembly by coarse-grained simulations.Protein science : a publication of the Protein Society · 2023Article
- Recombinant vaccines in 2022: a perspective from the cell factory.Microbial cell factories · 2022Review
- Understanding Supramolecular Assembly of Supercharged Proteins.ACS central science · 2022Article
- An In Silico Methodology That Facilitates Decision Making in the Engineering of Nanoscale Protein Materials.International journal of molecular sciences · 2022Article
- Peptides for Vaccine Development.ACS applied bio materials · 2022Review
- Rational Design of Self-Assembling Supramolecular Protein Nanostructures Utilizing the Cucurbit[8]Uril Macrocyclic Host.Methods in molecular biology (Clifton, N.J.) · 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
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ordered protein assemblies are attracting interest as next-generation biomaterials with a remarkable range of structural and functional properties, leading to potential applications in biocatalysis, materials templating, drug delivery and vaccine development. This Review covers ordered protein assemblies including protein nanowires/nanofibrils, nanorings, nanotubes, designed two- and three-dimensional ordered protein lattices and protein-like cages including polyhedral virus-like cage structures. The main focus is on designed ordered protein assemblies, in which the spatial organization of the proteins is controlled by tailored noncovalent interactions (including metal ion binding interactions, electrostatic interactions and ligand-receptor interactions among others) or by careful design of modified (mutant) proteins or de novo constructs. The modification of natural protein assemblies including bacterial S-layers and cage-like and rod-like viruses to impart novel function, e.g. enzymatic activity, is also considered. A diversity of structures have been created using distinct approaches, and this Review provides a summary of the state-of-the-art in the development of these systems, which have exceptional potential as advanced bionanomaterials for a diversity of applications.
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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.