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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191606" target="_blank" >RIV/00216208:11310/13:10191606 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/13:00396044 RIV/67985823:_____/13:00396044 RIV/61388971:_____/13:00396044 RIV/61388963:_____/13:00396044 RIV/44555601:13440/13:43885015

  • Result on the web

    <a href="http://dx.doi.org/10.1074/jbc.M113.456012" target="_blank" >http://dx.doi.org/10.1074/jbc.M113.456012</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M113.456012" target="_blank" >10.1074/jbc.M113.456012</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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 non-degraded protein. Here we developed a procedure for production of a highly purified form of recombinant human AMBN in quantities that allowed its structural characterization. Using size-exclusion chromatography, analytical ultracentrifugation, transmission electron and atomic-force microscopy techniques, we show that AMBN self-associates into ribbon-like supramolecular structures with an average

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    288

  • Issue of the periodical within the volume

    31

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    13

  • Pages from-to

    22333-22345

  • UT code for WoS article

    000330596300015

  • EID of the result in the Scopus database