ArticleBiomacromolecules2018
Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.
Article in Biomacromolecules, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- Amelogenin Phosphorylation Affects Protein-Protein Interactions In Vivo.Calcified tissue international · 2026Article
- 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
- Amyloid-induced mineralization: From biological systems to biomimetic materials.Bioactive materials · 2025Review
- SAXS of murine amelogenin identifies a persistent dimeric species from pH 5.0 to 8.0.Journal of structural biology · 2024Article
- Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
- Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin-Amelogenin Interactions.ACS biomaterials science & engineering · 2023Article
- High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 2023Article
- 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
- Advanced materials for enamel remineralization.Frontiers in bioengineering and biotechnology · 2022Review
- Calcium interactions in amelogenin-derived peptide assembly.Frontiers in physiology · 2022Article
- 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
- Biomineralization of Enamel and Dentin Mediated by Matrix Proteins.Journal of dental research · 2021Review
- Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.Molecules (Basel, Switzerland) · 2020Review
- Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020Review
- Protein nanoribbons template enamel mineralization.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin.International journal of molecular sciences · 2020Article
- Ameloblastin Binds to Phospholipid Bilayers via a Helix-Forming Motif within the Sequence Encoded by Exon 5.ACS omega · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Mechanisms of protein-guided mineralization in enamel, leading to organized fibrillar apatite nanocrystals, remain elusive. In vitro studies reveal recombinant human amelogenin (rH174), a matrix protein templating this process, self-assembles into a variety of structures. This study endeavors to clarify the self-assembly of rH174 in physiologically relevant conditions. Self-assembly in simulated enamel fluid was monitored up to 2 months. At alkali (7.3-8.7) and acidic (5.5-6.1) pH ranges, a distinct progression in formation was observed from nanospheres (17-23 nm) to intermediate-length nanorods, concluding with the formation of long 17-18 nm wide nanoribbons decorated with nanospheres. Assembly in acidic condition progressed quicker to nanoribbons with fewer persistent nanospheres. X-ray diffraction exhibited reflections characteristic of antiparallel β-sheets (4.7 and 9.65 Å), supporting the model of amyloid-like nanoribbon formation. This is the first observation of rH174 nanoribbons at alkaline pH as well as concurrent nanosphere formation, indicating both supramolecular structures are stable together under physiological conditions.
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Registered trials
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