Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5

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Abstract

Background: Ameloblastin plays a key role in the complex biomineralization process that forms tooth enamel, the hardest tissue of the body. Results: Ameloblastin self-associates into ribbon-like supramolecular structures via a short segment encoded by exon 5. Conclusion: Ameloblastin self-association may be essential for correct structural organization and mineralization of the enamel in vivo. Significance: The results provide molecular insight into biology of tooth enamel formation. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Wald, T., Osickova, A., Sulc, M., Benada, O., Semeradtova, A., Rezabkova, L., … Osicka, R. (2013). Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5. Journal of Biological Chemistry, 288(31), 22333–22345. https://doi.org/10.1074/jbc.M113.456012

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