ArticlePloS one2011
Amelogenin supramolecular assembly in nanospheres defined by a complex helix-coil-PPII helix 3D-structure.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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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
32 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review.International journal of molecular sciences · 2021Pooled it
- Serine-16 Phosphorylation, C-Terminal Truncation, and Ion-Specific Interactions Coordinate Amelogenin Nanoribbon Formation.Calcified tissue international · 2026Article
- Optimization of Functional Toothpaste Formulation Containing Nano-Hydroxyapatite and Birch Extract for Daily Oral Care.Materials (Basel, Switzerland) · 2023Article
- Sodium/(calcium + potassium) exchanger NCKX4 optimizes KLK4 activity in the enamel matrix microenvironment to regulate ECM modeling.Frontiers in physiology · 2023Article
- Residue-Specific Insights into the Intermolecular Protein-Protein Interfaces Driving Amelogenin Self-Assembly in Solution.Biochemistry · 2022Article
- Highly acidic pH facilitates enamel protein self-assembly, apatite crystal growth and enamel protein interactions in the early enamel matrix.Frontiers in physiology · 2022Article
- Mechanisms of Enamel Mineralization Guided by Amelogenin Nanoribbons.Journal of dental research · 2021Review
- Amelogenesis: Transformation of a protein-mineral matrix into tooth enamel.Journal of structural biology · 2021Review
- A N-Terminus Domain Determines Amelogenin's Stability to Guide the Development of Mouse Enamel Matrix.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2021Article
- The Amelogenin-Derived Peptide TVH-19 Promotes Dentinal Tubule Occlusion and Mineralization.Polymers · 2021Article
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- Identification of Key Functional Motifs of Native Amelogenin Protein for Dental Enamel Remineralisation.Molecules (Basel, Switzerland) · 2020Review
- Enamel biomimetics-fiction or future of dentistry.International journal of oral science · 2019Review
- Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite.Biophysical journal · 2018Article
- Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method.Archives of oral biology · 2018Article
- Article
- Integrative Temporo-Spatial, Mineralogic, Spectroscopic, and Proteomic Analysis of Postnatal Enamel Development in Teeth with Limited Growth.Frontiers in physiology · 2017Article
- Posttranslational Amelogenin Processing and Changes in Matrix Assembly during Enamel Development.Frontiers in physiology · 2017Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- TGF-β1 autocrine signalling and enamel matrix components.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Tooth enamel, the hardest material in the human body, is formed within a self-assembled matrix consisting mostly of amelogenin proteins. Here we have determined the complete mouse amelogenin structure under physiological conditions and defined interactions between individual domains. NMR spectroscopy revealed four major amelogenin structural motifs, including an N-terminal assembly of four α-helical segments (S9-V19, T21-P33, Y39-W45, V53-Q56), an elongated random coil region interrupted by two 3(10) helices (∼P60-Q117), an extended proline-rich PPII-helical region (P118-L165), and a charged hydrophilic C-terminus (L165-D180). HSQC experiments demonstrated ipsilateral interactions between terminal domains of individual amelogenin molecules, i.e. N-terminal interactions with corresponding N-termini and C-terminal interactions with corresponding C-termini, while the central random coil domain did not engage in interactions. Our HSQC spectra of the full-length amelogenin central domain region completely overlapped with spectra of the monomeric Amel-M fragment, suggesting that the central amelogenin coil region did not involve in assembly, even in assembled nanospheres. This finding was confirmed by analytical ultracentrifugation experiments. We conclude that under conditions resembling those found in the developing enamel protein matrix, amelogenin molecules form complex 3D-structures with N-terminal α-helix-like segments and C-terminal PPII-helices, which self-assemble through ipsilateral interactions at the N-terminus of the molecule.
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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.