ArticleJournal of structural biology2013
CryoTEM study of effects of phosphorylation on the hierarchical assembly of porcine amelogenin and its regulation of mineralization in vitro.
Article in Journal of structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 30 citations in OpenAlex.
- Amelogenin Phosphorylation Affects Protein-Protein Interactions In Vivo.Calcified tissue international · 2026Article
- Amelogenin Phosphorylation Affects Key Regulatory Genes in the Enamel Organ.Calcified tissue international · 2026Review
- 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
- Effect of phosphate group on remineralization of early enamel caries regulated by amelogenin peptide.PloS one · 2024Article
- 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
- 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
- DNA nanostructures as templates for biomineralization.Nature reviews. Chemistry · 2021Review
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- Amelogenin phosphorylation regulates tooth enamel formation by stabilizing a transient amorphous mineral precursor.The Journal of biological chemistry · 2020Article
- Proteolysis by MMP20 Prevents Aberrant Mineralization in Secretory Enamel.Journal of dental research · 2019Article
- Ameloblastin Binds to Phospholipid Bilayers via a Helix-Forming Motif within the Sequence Encoded by Exon 5.ACS omega · 2019Article
- 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
- Dynamic interactions of amelogenin with hydroxyapatite surfaces are dependent on protein phosphorylation and solution pH.Colloids and surfaces. B, Biointerfaces · 2016Article
- MMP20 Proteolysis of Native Amelogenin Regulates Mineralization In Vitro.Journal of dental research · 2016Article
- Microscopy techniques for investigating the control of organic constituents on biomineralization.MRS bulletin · 2015Article
- Understanding nanocalcification: a role suggested for crystal ghosts.Marine drugs · 2014Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Amelogenin, the major extracellular enamel matrix protein, plays a critical role in regulating the growth and organization of enamel. Assembly and mineralization of full-length native (P173) and recombinant (rP172) porcine amelogenins were studied by cryogenic Transmission Electron Microscopy (cryoTEM). The cryoTEM revealed that both native and recombinant porcine amelogenins undergo step-wise self-assembly. Although the overall structural organization of P173 and rP172 oligomers was similar and resembled oligomers of murine recombinant amelogenin rM179, there were subtle differences suggesting that a single phosphorylated serine present in P173 might affect amelogenin self-assembly. Our mineralization studies demonstrated that both P173 and rP172 oligomers stabilize initial mineral clusters. Importantly, however, rP172 regulated the organization of initial mineral clusters into linear chains and guided the formation of parallel arrays of elongated mineral particles, which are the hallmark of enamel structural organization. These results are similar to those obtained previously using full-length recombinant murine amelogenin (Fang et al., 2011a). In contrast to that seen with rP172, phosphorylated P173 strongly inhibits mineralization for extended periods of time. We propose that these differences might be due to the differences in the structural organization and charge distribution between P173 and rP172. Overall our studies indicate that self-assembly of amelogenin and the mechanisms of its control over mineralization might be universal across different mammalian species. Our data also provide new insight into the effect of phosphorylation on amelogenin self-assembly and its regulation of mineralization.
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