ArticleBiomacromolecules2012
Self-assembly of filamentous amelogenin requires calcium and phosphate: from dimers via nanoribbons to fibrils.
Article in Biomacromolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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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.
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Who cites it
35 citing papers in PubMed, 56 citations in OpenAlex.
- Nanoparticle Saltwater Fish Powder and Cell Protein Pathways in Enamel Density Enhancement.European journal of dentistry · 2026Article
- Application of Polymers in Advanced Materials for Enamel and Dentine Remineralization.ACS biomaterials science & engineering · 2026Review
- Serine-16 Phosphorylation, C-Terminal Truncation, and Ion-Specific Interactions Coordinate Amelogenin Nanoribbon Formation.Calcified tissue international · 2026Article
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Biomimetic supramolecular protein matrix restores structure and properties of human dental enamel.Nature communications · 2025Article
- Amyloid-induced mineralization: From biological systems to biomimetic materials.Bioactive materials · 2025Review
- The role of the TGF-β1 signaling pathway in the process of amelogenesis.Frontiers in physiology · 2025Review
- SAXS of murine amelogenin identifies a persistent dimeric species from pH 5.0 to 8.0.Journal of structural biology · 2024Article
- Recombinant human enamelin produced in Escherichia coli promotes mineralization in vitro.BMC biotechnology · 2024Article
- Residue-Specific Insights into the Intermolecular Protein-Protein Interfaces Driving Amelogenin Self-Assembly in Solution.Biochemistry · 2022Article
- Amyloid-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Calcium interactions in amelogenin-derived peptide assembly.Frontiers in physiology · 2022Article
- Advances in biomineralization-inspired materials for hard tissue repair.International journal of oral science · 2021Review
- Mechanisms of Enamel Mineralization Guided by Amelogenin Nanoribbons.Journal of dental research · 2021Review
- A Brief History of the Discovery of Amelogenin Nanoribbons In Vitro and In Vivo.Journal of dental research · 2021Article
- Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold.International journal of molecular sciences · 2021Article
- Predicting a Kind of Unusual Multiple-States Dimerization-Modes Transformation in Protein PD-L1 System by Computational Investigation and a Generalized Rate Theory.Frontiers in chemistry · 2021Article
- Enamel synthesis explained.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Protein nanoribbons template enamel mineralization.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Significance and Utilisation of Biomimetic and Bioinspired Strategies in the Field of Biomedical Material Engineering: The Case of Calcium Phosphat-Protein Template Constructs.Materials (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Enamel matrix self-assembly has long been suggested as the driving force behind aligned nanofibrous hydroxyapatite formation. We tested if amelogenin, the main enamel matrix protein, can self-assemble into ribbon-like structures in physiologic solutions. Ribbons 17 nm wide were observed to grow several micrometers in length, requiring calcium, phosphate, and pH 4.0-6.0. The pH range suggests that the formation of ion bridges through protonated histidine residues is essential to self-assembly, supported by a statistical analysis of 212 phosphate-binding proteins predicting 12 phosphate-binding histidines. Thermophoretic analysis verified the importance of calcium and phosphate in self-assembly. X-ray scattering characterized amelogenin dimers with dimensions fitting the cross-section of the amelogenin ribbon, leading to the hypothesis that antiparallel dimers are the building blocks of the ribbons. Over 5-7 days, ribbons self-organized into bundles composed of aligned ribbons mimicking the structure of enamel crystallites in enamel rods. These observations confirm reports of filamentous organic components in developing enamel and provide a new model for matrix-templated enamel mineralization.
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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.