ReviewBiochimica et biophysica acta2010
The ferritin superfamily: Supramolecular templates for materials synthesis.
Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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
63 citing papers in PubMed.
- Immobilization-driven enhancement of CNT-binding peptide affinity: substantial shift from the free-state.RSC advances · 2026Article
- Cavity acidification limits ferritin iron biomineralization.Journal of inorganic biochemistry · 2026Article
- Peptide cages: bioinspired supramolecular architectures for next-generation applications.Chemical science · 2026Review
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- Coherent X-rays reveal anomalous molecular diffusion and cage effects in crowded protein solutions.Nature communications · 2025Article
- A role for Dps ferritin activity in long-term survival ofMicrobiology spectrum · 2025Article
- Beyond the Walls of Troy: A Scoping Review on Pharmacological Strategies to Enhance Drug Delivery Across the Blood-Brain Barrier and Blood-Tumor Barrier.International journal of molecular sciences · 2025Article
- Article
- Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024Review
- Development and Use of Human RecombinantACS applied bio materials · 2024Article
- Use of virus-like particles and nanoparticle-based vaccines for combating picornavirus infections.Veterinary research · 2024Review
- Self-Assembled Ferritin Nanoparticles for Delivery of Antigens and Development of Vaccines: From Structure and Property to Applications.Molecules (Basel, Switzerland) · 2024Review
- Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Encapsulated Ferritin-like Proteins: A Structural Perspective.Biomolecules · 2024Review
- Review
- Mobility Selective Ion Soft-Landing and Characterization Enabled Using Structures for Lossless Ion Manipulation.Analytical chemistry · 2024Article
- Computational design and investigation of the monomeric spike SARS-CoV-2-ferritin nanocage vaccine stability and interactions.Frontiers in molecular biosciences · 2024Article
- Untapped Potential of Deep Eutectic Solvents for the Synthesis of Bioinspired Inorganic-Organic Materials.Chemistry of materials : a publication of the American Chemical Society · 2023Review
- Magnetite-Based Biosensors and Molecular Logic Gates: From Magnetite Synthesis to Application.Biosensors · 2023Review
- Vaccination Strategies Based on Bacterial Self-Assembling Proteins as Antigen Delivery Nanoscaffolds.Vaccines · 2022Review
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Members of the ferritin superfamily are multi-subunit cage-like proteins with a hollow interior cavity. These proteins possess three distinct surfaces, i.e. interior and exterior surfaces of the cages and interface between subunits. The interior cavity provides a unique reaction environment in which the interior reaction is separated from the external environment. In biology the cavity is utilized for sequestration of irons and biomineralization as a mechanism to render Fe inert and sequester it from the external environment. Material scientists have been inspired by this system and exploited a range of ferritin superfamily proteins as supramolecular templates to encapsulate nanoparticles and/or as well-defined building blocks for fabrication of higher order assembly. Besides the interior cavity, the exterior surface of the protein cages can be modified without altering the interior characteristics. This allows us to deliver the protein cages to a targeted tissue in vivo or to achieve controlled assembly on a solid substrate to fabricate higher order structures. Furthermore, the interface between subunits is utilized for manipulating chimeric self-assembly of the protein cages and in the generation of symmetry-broken Janus particles. Utilizing these ideas, the ferritin superfamily has been exploited for development of a broad range of materials with applications from biomedicine to electronics.
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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.