ReviewNew biotechnology2015
Ferritin family proteins and their use in bionanotechnology.
Review in New biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 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
73 citing papers in PubMed, 197 citations in OpenAlex.
- Immobilization-driven enhancement of CNT-binding peptide affinity: substantial shift from the free-state.RSC advances · 2026Article
- A deep dive into ferritin nanoparticle advancements: experimental and computational perspectives.Discover nano · 2026Review
- Metalloprotein-Based Nanomedicines: Design Strategies, Functional Mechanisms, and Biomedical Applications.International journal of molecular sciences · 2026Review
- Molecular Mechanisms and Biomedical Applications of Ferritin Nanocages: A Comprehensive Review of Self-Assembly, Engineering, and Multifunctional Delivery Platforms.International journal of nanomedicine · 2026Review
- Semisynthetic Ferritin Nanocages for Flexible, Site-Specific Targeting and Ligand-Free Activation of Membrane Receptors.Nano letters · 2025Article
- 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
- Controlling nanocage assembly, towards developing a one-health "plug & play" platform for targeted therapy.Chemical communications (Cambridge, England) · 2025Review
- Structural Insight Into a Human H Ferritin@Gold-Monocarbene Adduct: Aurophilicity Revealed in a Biological Context.Angewandte Chemie (International ed. in English) · 2025Article
- High-Fidelity In Vitro Packaging of Diverse Synthetic Cargo into Encapsulin Protein Cages.Angewandte Chemie (International ed. in English) · 2025Article
- Design and application of ferritin-based nanomedicine for targeted cancer therapy.Nanomedicine (London, England) · 2025Review
- Magnetizing Biotech-Advances in (In Vivo) Magnetic Enzyme Immobilization.Engineering in life sciences · 2025Review
- The Dps Protein ProtectsInternational journal of molecular sciences · 2025Article
- Advanced technologies for the development of infectious disease vaccines.Nature reviews. Drug discovery · 2024Review
- EngineeringVaccines · 2024Review
- Tyrosinase-Mediated Conjugation for Antigen Display on Ferritin Nanoparticles.Bioconjugate chemistry · 2024Article
- Self-Assembled Ferritin Nanoparticles for Delivery of Antigens and Development of Vaccines: From Structure and Property to Applications.Molecules (Basel, Switzerland) · 2024Review
- Review
- Adapting Ferritin, a Naturally Occurring Protein Cage, to Modulate Intrinsic Agonism of OX40.Bioconjugate chemistry · 2024Article
- Strategies for developing self-assembled nanoparticle vaccines against SARS-CoV-2 infection.Frontiers in immunology · 2024Review
13 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
2 authors at 1 institution in 1 country.
Funding
Abstract
Ferritin family proteins are found in all kingdoms of life and act to store iron within a protein cage and to protect the cell from oxidative damage caused by the Fenton reaction. The structural and biochemical features of the ferritins have been widely exploited in bionanotechnology applications: from the production of metal nanoparticles; as templates for semi-conductor production; and as scaffolds for vaccine design and drug delivery. In this review we first discuss the structural properties of the main ferritin family proteins, and describe how their organisation specifies their functions. Second, we describe materials science applications of ferritins that rely on their ability to sequester metal within their cavities. Finally, we explore the use of ferritin as a container for drug delivery and as a scaffold for the production of vaccines.
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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.