ArticleJournal of dental research2011
Leucine-rich amelogenin peptides regulate mineralization in vitro.
Article in Journal of dental research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.
- Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review.International journal of molecular sciences · 2021Pooled it
- Effect of the recombinant amelogenin peptide TRAP on remineralization of early enamel caries: an in-situ study.BMC oral health · 2025Trial
- Application of Polymers in Advanced Materials for Enamel and Dentine Remineralization.ACS biomaterials science & engineering · 2026Review
- Application of Amorphous Nanomaterials in Dentistry: A Comprehensive Review.Journal of functional biomaterials · 2025Review
- Amyloid-induced mineralization: From biological systems to biomimetic materials.Bioactive materials · 2025Review
- Antimicrobial, remineralization, and infiltration: advanced strategies for interrupting dental caries.Medical review (2021) · 2025Review
- Morphological study of remineralization of the eroded enamel lesions by tyrosine-rich amelogenin peptide.BMC oral health · 2024Article
- A Comparison of the Enamel Remineralisation Potential of Self-Assembling Peptides.International dental journal · 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
- Physicochemical understanding of biomineralization by molecular vibrational spectroscopy: From mechanism to nature.Exploration (Beijing, China) · 2023Review
- Research progress of biomimetic materials in oral medicine.Journal of biological engineering · 2023Review
- Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: AnFrontiers in physiology · 2023Article
- The phosphorylation of serineMatrix biology : journal of the International Society for Matrix Biology · 2022Article
- Advances in biomineralization-inspired materials for hard tissue repair.International journal of oral science · 2021Review
- Advanced non-fluoride approaches to dental enamel remineralization: The next level in enamel repair management.Biomaterials and biosystems · 2021Review
- Effect of Er:YAG Laser Irradiation and Acidulated Phosphate Fluoride Therapy on Re-Mineralization of White Spot Lesions.Journal of dentistry (Shiraz, Iran) · 2021Article
- Biomimetic mineralisation systems for in situ enamel restoration inspired by amelogenesis.Journal of materials science. Materials in medicine · 2021Review
- The Amelogenin-Derived Peptide TVH-19 Promotes Dentinal Tubule Occlusion and Mineralization.Polymers · 2021Article
- Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Amelogenin's capacity to regulate enamel formation is related to its conserved N- and C-terminal domains, its ability to self-assemble, and its ability to stabilize amorphous calcium phosphate (ACP) - a capacity enhanced by amelogenin phosphorylation. This in vitro study provides further insight into amelogenin function, using variations of the Leucine-Rich Amelogenin Peptide (LRAP), an alternative splice product comprised solely of amelogenin's N- and C-terminal domains. Peptide self-assembly was studied by dynamic light-scattering and transmission electron microscopy (TEM). TEM, selected area electron diffraction, and Fourier transform-infrared spectroscopy were also used to determine the effect of phosphorylated and non-phosphorylated LRAP on calcium phosphate formation. Results show that phosphorylated and non-phosphorylated LRAP can self-assemble into chain-like structures in a fashion dependent on the C-terminal domain. Notably, this capacity was enhanced by added calcium and to a much greater degree for phosphorylated LRAP. Furthermore, phosphorylated LRAP was found to stabilize ACP and prevent its transformation to hydroxyapatite (HA), while aligned HA crystals formed in the presence of non-phosphorylated LRAP. The N- and C-terminal amelogenin domains in non-phosphorylated LRAP are, therefore, sufficient to guide ACP transformation into ordered bundles of apatite crystals, making LRAP an excellent candidate for biomimetic approaches for enamel regeneration.
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Registered trials
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.