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Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5
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SYSNO ASEP 0396044 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5 Author(s) Wald, Tomáš (MBU-M) RID
Osičková, Adriana (MBU-M) RID, ORCID
Šulc, Miroslav (MBU-M) RID, ORCID
Benada, Oldřich (MBU-M) ORCID, RID
Semerádtová, A. (CZ)
Řežábková, Lenka (FGU-C)
Veverka, Václav (UOCHB-X) RID, ORCID
Bednárová, Lucie (UOCHB-X) RID, ORCID
Malý, J. (CZ)
Macek, Pavel (MBU-M)
Šebo, Peter (MBU-M) RID, ORCID
Slabý, Ivan (BTO-N)
Vondrášek, Jiří (UOCHB-X) RID, ORCID
Osička, Radim (MBU-M) RID, ORCIDSource Title Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 288, č. 31 (2013), s. 22333-22345Number of pages 13 s. Language eng - English Country US - United States Keywords Ameloblastin ; Extracellular Matrix Proteins ; Amelogenin Subject RIV CE - Biochemistry Subject RIV - cooperation Institute of Physiology - Biochemistry R&D Projects GAP302/10/0427 GA ČR - Czech Science Foundation (CSF) Institutional support MBU-M - RVO:61388971 ; UOCHB-X - RVO:61388963 ; FGU-C - RVO:67985823 ; BTO-N - RVO:86652036 UT WOS 000330596300015 EID SCOPUS 84881233658 DOI https://doi.org/10.1074/jbc.M113.456012 Annotation Tooth enamel, the hardest tissue in the body, is formed by the evolutionarily highly conserved biomineralization process that is controlled by extracellular matrix proteins. The intrinsically disordered matrix protein ameloblastin (AMBN) is the most abundant nonamelogenin protein of the developing enamel and a key element for correct enamel formation. AMBN was suggested to be a cell adhesion molecule that regulates proliferation and differentiation of ameloblasts. Nevertheless, detailed structural and functional studies on AMBN have been substantially limited by the paucity of the purified nondegraded protein. With this study, we have developed a procedure for production of a highly purified form of recombinant human AMBN in quantities that allowed its structural characterization Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2014
Number of the records: 1