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
—