ReviewJournal of structural biology2020
Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.
Review in Journal of structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed.
- Nanoparticle Saltwater Fish Powder and Cell Protein Pathways in Enamel Density Enhancement.European journal of dentistry · 2026Article
- Human Enamel Formation: A Scoping Review for Oral Health Professionals.Dentistry journal · 2026Review
- Effect of conditioned medium derived from a clone cell of epithelial rests of Malassez on enamel crystallization in tooth germs.Medical molecular morphology · 2026Article
- Regenerative Strategies in Pediatric Dentistry: A Comprehensive Overview of Tissue Engineering from Past to Future.Advances in experimental medicine and biology · 2026Review
- Biomimetic Mineralization of Keratin Scaffolds for Enamel Regeneration.Advanced healthcare materials · 2025Article
- Reduction of Tooth Replacement Disproportionately Affects the Evolution of Enamel Matrix Proteins.Journal of molecular evolution · 2025Article
- Antimicrobial, remineralization, and infiltration: advanced strategies for interrupting dental caries.Medical review (2021) · 2025Review
- The role of the TGF-β1 signaling pathway in the process of amelogenesis.Frontiers in physiology · 2025Review
- Ameloblastin binding to biomimetic models of cell membranes - A continuum of intrinsic disorder.Archives of oral biology · 2025Article
- Chickpea NCR13 disulfide cross-linking variants exhibit profound differences in antifungal activity and modes of action.PLoS pathogens · 2024Article
- SAXS of murine amelogenin identifies a persistent dimeric species from pH 5.0 to 8.0.Journal of structural biology · 2024Article
- Unraveling Nanomaterials in Biomimetic Mineralization of Dental Hard Tissue: Focusing on Advantages, Mechanisms, and Prospects.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Structure of biomimetic casein micelles: Critical tests of the hydrophobic colloid and multivalent-binding models using recombinant deuterated and phosphorylated β-casein.Journal of structural biology: X · 2024Article
- Polycarboxy/Sulfo Betaine-Calcium Phosphate Hybrid Materials with a Remineralization Potential.Materials (Basel, Switzerland) · 2023Article
- Mechanistic Insights into Bioengineered Antibiofilm Enamel Pellicles.Journal of dental research · 2023Article
- Resolving protein-mineral interfacial interactions duringMaterials today. Advances · 2023Article
- High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 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
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Amelogenin, a protein critical to enamel formation, is presented as a model for understanding how the structure of biomineralization proteins orchestrate biomineral formation. Amelogenin is the predominant biomineralization protein in the early stages of enamel formation and contributes to the controlled formation of hydroxyapatite (HAP) enamel crystals. The resulting enamel mineral is one of the hardest tissues in the human body and one of the hardest biominerals in nature. Structural studies have been hindered by the lack of techniques to evaluate surface adsorbed proteins and by amelogenin's disposition to self-assemble. Recent advancements in solution and solid state nuclear magnetic resonance (NMR) spectroscopy, atomic force microscopy (AFM), and recombinant isotope labeling strategies are now enabling detailed structural studies. These recent studies, coupled with insights from techniques such as CD and IR spectroscopy and computational methodologies, are contributing to important advancements in our structural understanding of amelogenesis. In this review we focus on recent advances in solution and solid state NMR spectroscopy and in situ AFM that reveal new insights into the secondary, tertiary, and quaternary structure of amelogenin by itself and in contact with HAP. These studies have increased our understanding of the interface between amelogenin and HAP and how amelogenin controls enamel formation.
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