0396044 - MBÚ 2014 RIV US eng J - Journal Article
Wald, Tomáš - Osičková, Adriana - Šulc, Miroslav - Benada, Oldřich - Semerádtová, A. - Řežábková, Lenka - Veverka, Václav - Bednárová, Lucie - Malý, J. - Macek, Pavel - Šebo, Peter - Slabý, Ivan - Vondrášek, Jiří - Osička, Radim
Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5.
Journal of Biological Chemistry. Roč. 288, č. 31 (2013), s. 22333-22345. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR GAP302/10/0427
Institutional support: RVO:61388971 ; RVO:61388963 ; RVO:67985823 ; RVO:86652036
Keywords : Ameloblastin * Extracellular Matrix Proteins * Amelogenin
Subject RIV: CE - Biochemistry; CE - Biochemistry (FGU-C)
Impact factor: 4.600, year: 2013 ; AIS: 1.84, rok: 2013
DOI: https://doi.org/10.1074/jbc.M113.456012

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
Permanent Link: http://hdl.handle.net/11104/0230280