ArticleEuropean journal of oral sciences2011
Effect of phosphorylation on the interaction of calcium with leucine-rich amelogenin peptide.
Article in European journal of oral sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 21 citations in OpenAlex.
- Amelogenin Phosphorylation Affects Protein-Protein Interactions In Vivo.Calcified tissue international · 2026Article
- Article
- Effect of phosphate group on remineralization of early enamel caries regulated by amelogenin peptide.PloS one · 2024Article
- 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
- 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
- Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020Review
- Amelogenin phosphorylation regulates tooth enamel formation by stabilizing a transient amorphous mineral precursor.The Journal of biological chemistry · 2020Article
- Dose-Dependent Rescue of KO Amelogenin Enamel by TransgenesFrontiers in physiology · 2017Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Dynamic interactions of amelogenin with hydroxyapatite surfaces are dependent on protein phosphorylation and solution pH.Colloids and surfaces. B, Biointerfaces · 2016Article
- The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution.Journal of structural biology · 2015Article
- The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength.Frontiers in physiology · 2014Article
- Role of mineralization inhibitors in the regulation of hard tissue biomineralization: relevance to initial enamel formation and maturation.Frontiers in physiology · 2014Review
- CryoTEM study of effects of phosphorylation on the hierarchical assembly of porcine amelogenin and its regulation of mineralization in vitro.Journal of structural biology · 2013Article
- Phosphorylation and ionic strength alter the LRAP-HAP interface in the N-terminus.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Amelogenin undergoes self-assembly and plays an essential role in guiding enamel mineral formation. The leucine-rich amelogenin peptide (LRAP) is an alternative splice product of the amelogenin gene and is composed of the N terminus (containing the only phosphate group) and the C terminus of full-length amelogenin. This study was conducted to investigate further the role of phosphorylation in LRAP self-assembly in the presence and absence of calcium using small angle X-ray scattering (SAXS). Consistent with our previous dynamic light-scattering findings for phosphorylated (+P) and non-phosphorylated (-P) LRAP, SAXS analyses revealed radii of gyration (R(g)) for LRAP(-P) (46.3-48.0 Å) that were larger than those for LRAP(+P) (25.0-27.4 Å) at pH 7.4. However, added calcium (up to 2.5 mM) induced significant increases in the R(g) of LRAP(+P) (up to 46.4 Å), while it had relatively little effect on LRAP(-P) particle size. Furthermore, SAXS analyses suggested compact folded structures for LRAP(-P) in the presence and absence of calcium, whereas the conformation of LRAP(+P) changed from an unfolded structure to a more compact structure upon the addition of calcium. We conclude that the single phosphate group in LRAP(+P) induces functionally important conformational changes, suggesting that phosphorylation may also influence amelogenin conformation and protein-mineral interactions during the early stages of amelogenesis.
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