ArticleInternational journal of molecular sciences2020
Characterization of AMBN I and II Isoforms and Study of Their Ca
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Antimicrobial peptides derived from human ameloblastin targeting biofilms.BMC oral health · 2025Article
- Oligomerization Function of the Native Exon 5 Sequence of Ameloblastin Fused with Calmodulin.ACS omega · 2025Article
- Expression ofInternational journal of molecular sciences · 2025Article
- Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
- Novel Ameloblastin Variants, Contrasting Amelogenesis Imperfecta Phenotypes.Journal of dental research · 2024Article
- Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin-Amelogenin Interactions.ACS biomaterials science & engineering · 2023Article
- The Dynamic Interactions of a Multitargeting Domain in Ameloblastin Protein with Amelogenin and Membrane.International journal of molecular sciences · 2023Article
- Early evolution of enamel matrix proteins is reflected by pleiotropy of physiological functions.Scientific reports · 2023Article
- Revisiting ameloblastin; addressing the EMT-ECM axis above and beyond oral biology.Frontiers in cell and developmental biology · 2023Article
- Biomineralization of Enamel and Dentin Mediated by Matrix Proteins.Journal of dental research · 2021Review
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Authors and funding
14 authors at 5 institutions in 2 countries.
Funding
Abstract
Ameloblastin (Ambn) as an intrinsically disordered protein (IDP) stands for an important role in the formation of enamel-the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two isoforms: full-length isoform I (AMBN ISO I) and isoform II (AMBN ISO II), which is about 15 amino acid residues shorter than AMBN ISO I. The significant feature of AMBN-its oligomerization ability-is enabled due to a specific sequence encoded by exon 5 present at the N-terminal part in both known isoforms. In this study, we characterized AMBN ISO I and AMBN ISO II by biochemical and biophysical methods to determine their common features and differences. We confirmed that both AMBN ISO I and AMBN ISO II form oligomers in in vitro conditions. Due to an important role of AMBN in biomineralization, we further addressed the calcium (Ca
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