ArticleJournal of structural biology2011
Effects of phosphorylation on the self-assembly of native full-length porcine amelogenin and its regulation of calcium phosphate formation in vitro.
Article in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 75 citations in OpenAlex.
- Enamel matrix acidification caused by loss of amelogenin phosphorylation disrupts ameloblast pH-regulatory machinery.JBMR plus · 2026Article
- Application of Polymers in Advanced Materials for Enamel and Dentine Remineralization.ACS biomaterials science & engineering · 2026Review
- 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 Phosphorylation Affects Key Regulatory Genes in the Enamel Organ.Calcified tissue international · 2026Review
- Amelogenin enhances the reparative competence of trauma-affected periodontal ligament stem cells: implications for tooth autotransplantation.BMC oral health · 2026Article
- Article
- Reduction of Tooth Replacement Disproportionately Affects the Evolution of Enamel Matrix Proteins.Journal of molecular evolution · 2025Article
- Morphological study of remineralization of the eroded enamel lesions by tyrosine-rich amelogenin peptide.BMC oral health · 2024Article
- Role of amelogenin phosphorylation in regulating dental enamel formation.Matrix biology : journal of the International Society for Matrix Biology · 2024Article
- Developing Bioactive Hydrogels with Peptides for Dental Application.Biomedicines · 2024Article
- Effect of phosphate group on remineralization of early enamel caries regulated by amelogenin peptide.PloS one · 2024Article
- 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
- Loss of biological control of enamel mineralization in amelogenin-phosphorylation-deficient mice.Journal of structural biology · 2022Article
- Calcium interactions in amelogenin-derived peptide assembly.Frontiers in physiology · 2022Article
- Molecular Cloning of Mouse Homologue of Enamel Protein C4orf26 and Its Phosphorylation by FAM20C.Calcified tissue international · 2021Article
- Biomineralization of Enamel and Dentin Mediated by Matrix Proteins.Journal of dental research · 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
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The self-assembly of the predominant extracellular enamel matrix protein amelogenin plays an essential role in regulating the growth and organization of enamel mineral during early stages of dental enamel formation. The present study describes the effect of the phosphorylation of a single site on the full-length native porcine amelogenin P173 on self-assembly and on the regulation of spontaneous calcium phosphate formation in vitro. Studies were also conducted using recombinant non-phosphorylated (rP172) porcine amelogenin, along with the most abundant amelogenin cleavage product (P148) and its recombinant form (rP147). Amelogenin self-assembly was assessed using dynamic light scattering (DLS) and transmission electron microscopy (TEM). Using these approaches, we have shown that self-assembly of each amelogenin is very sensitive to pH and appears to be affected by both hydrophilic and hydrophobic interactions. Furthermore, our results suggest that the phosphorylation of the full-length porcine amelogenin P173 has a small but potentially important effect on its higher-order self-assembly into chain-like structures under physiological conditions of pH, temperature, and ionic strength. Although phosphorylation has a subtle effect on the higher-order assembly of full-length amelogenin, native phosphorylated P173 was found to stabilize amorphous calcium phosphate for extended periods of time, in sharp contrast to previous findings using non-phosphorylated rP172. The biological relevance of these findings is discussed.
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