ArticleJournal of structural biology2007
pH triggered self-assembly of native and recombinant amelogenins under physiological pH and temperature in vitro.
Article in Journal of structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 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
66 citing papers in PubMed, 86 citations in OpenAlex.
- 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
- Clinical evaluation of open flap debridement with or without Emdogain® in treating intrabony defects.Bioinformation · 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
- Role of amelogenin phosphorylation in regulating dental enamel formation.Matrix biology : journal of the International Society for Matrix Biology · 2024Article
- Physicochemical understanding of biomineralization by molecular vibrational spectroscopy: From mechanism to nature.Exploration (Beijing, China) · 2023Review
- High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 2023Article
- Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth.Scientific reports · 2022Article
- Residue-Specific Insights into the Intermolecular Protein-Protein Interfaces Driving Amelogenin Self-Assembly in Solution.Biochemistry · 2022Article
- Loss of biological control of enamel mineralization in amelogenin-phosphorylation-deficient mice.Journal of structural biology · 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
- 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
- Control of Calcium Phosphate Nucleation and Transformation through Interactions of Enamelin and Amelogenin Exhibits the "Goldilocks Effect".Crystal growth & design · 2018Article
- Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite.Biophysical journal · 2018Article
- Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.Biomacromolecules · 2018Article
- DENTAL ENAMEL FORMATION AND IMPLICATIONS FOR ORAL HEALTH AND DISEASE.Physiological reviews · 2017Review
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Preparative SDS PAGE as an Alternative to His-Tag Purification of Recombinant Amelogenin.Frontiers in physiology · 2017Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Self-assembly of the extracellular matrix protein amelogenin is believed to play an essential role in regulating the growth and organization of enamel crystals during enamel formation. This study examines the effect of temperature and pH on amelogenin self-assembly under physiological pH conditions in vitro, using dynamic light scattering, turbidity measurements, and transmission electron microscopy. Full-length recombinant amelogenins from mouse (rM179) and pig (rP172) were investigated, along with proteolytic cleavage products (rM166 and native P148) lacking the hydrophilic C-terminus of parent molecules. Results indicated that the self-assembly of full-length amelogenin is primarily triggered by pH in the temperature range from 13 to 37 degrees C and not by temperature. Furthermore, very large assemblies of all proteins studied formed through the rearrangement of similarly sized nanospherical particles, although at different pH values: pH 7.7 (P148), pH 7.5 (rM166), pH 7.2 (rP172), and pH 7.2 (rM179). Structural differences were also observed. The full-length molecules formed apparently tightly connected elongated, high-aspect ratio assemblies comprised of small spheres, while the amelogenin cleavage products appeared as loosely associated spherical particles, suggesting that the hydrophilic C-terminus plays an essential role in higher-order amelogenin assembly. Hence, tightly controlled pH values during secretory amelogenesis may serve to regulate the functions of both full-length and cleaved amelogenins.
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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.