ArticleProtein science : a publication of the Protein Society2024
Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Multivalent recognition of ferritin by full-length NCOA4 enables robust ferritinophagy.Protein science : a publication of the Protein Society · 2026Article
- Geometric Confinement in Solid-State Nanopores Enables Single-Molecule Discrimination of Ferritin Subunits and Translocation Bias.Nano letters · 2026Article
- Ferritin iron uptake and oxidation are dynamically modulated by nucleotide phosphate architecture via electrostatic gating.International journal of biological macromolecules · 2026Article
- The assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Molecular Mechanisms and Biomedical Applications of Ferritin Nanocages: A Comprehensive Review of Self-Assembly, Engineering, and Multifunctional Delivery Platforms.International journal of nanomedicine · 2026Review
- Controlling nanocage assembly, towards developing a one-health "plug & play" platform for targeted therapy.Chemical communications (Cambridge, England) · 2025Review
- AI-based quality assessment methods for protein structure models from cryo-EM.Current research in structural biology · 2025Review
- A Brief History of Ferritin, an Ancient and Versatile Protein.International journal of molecular sciences · 2024Review
- Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Despite ferritin's critical role in regulating cellular and systemic iron levels, our understanding of the structure and assembly mechanism of isoferritins, discovered over eight decades ago, remains limited. Unveiling how the composition and molecular architecture of hetero-oligomeric ferritins confer distinct functionality to isoferritins is essential to understanding how the structural intricacies of H and L subunits influence their interactions with cellular machinery. In this study, ferritin heteropolymers with specific H to L subunit ratios were synthesized using a uniquely engineered plasmid design, followed by high-resolution cryo-electron microscopy analysis and deep learning-based amino acid modeling. Our structural examination revealed unique architectural features during the self-assembly mechanism of heteropolymer ferritins and demonstrated a significant preference for H-L heterodimer formation over H-H or L-L homodimers. Unexpectedly, while dimers seem essential building blocks in the protein self-assembly process, the overall mechanism of ferritin self-assembly is observed to proceed randomly through diverse pathways. The physiological significance of these findings is discussed including how ferritin microheterogeneity could represent a tissue-specific adaptation process that imparts distinctive tissue-specific functions to isoferritins.
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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.