Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F20%3A00536820" target="_blank" >RIV/86652036:_____/20:00536820 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11130/20:10418465 RIV/00216208:11310/20:10418465 RIV/60461373:22330/20:43921042
Result on the web
<a href="https://doi.org/10.3390/ijms21239293" target="_blank" >https://doi.org/10.3390/ijms21239293</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms21239293" target="_blank" >10.3390/ijms21239293</a>
Alternative languages
Result language
angličtina
Original language name
Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties
Original language description
Ameloblastin (Ambn) as an intrinsically disordered protein (IDP) stands for an important role in the formation of enamel—the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two isoforms: full-length isoform I (AMBN ISO I) and isoform II (AMBN ISO II), which is about 15 amino acid residues shorter than AMBN ISO I. The significant feature of AMBN—its oligomerization ability—is enabled due to a specific sequence encoded by exon 5 present at the N-terminal part in both known isoforms. In this study, we characterized AMBN ISO I and AMBN ISO II by biochemical and biophysical methods to determine their common features and differences. We confirmed that both AMBN ISO I and AMBN ISO II form oligomers in in vitro conditions. Due to an important role of AMBN in biomineralization, we further addressed the calcium (Ca2+)-binding properties of AMBN ISO I and ISO II. The binding properties of AMBN to Ca2+ may explain the role of AMBN in biomineralization and more generally in Ca2+ homeostasis processes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LM2018127" target="_blank" >LM2018127: Czech Infrastructure for Integrative Structural Biology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1661-6596
e-ISSN
—
Volume of the periodical
21
Issue of the periodical within the volume
23
Country of publishing house
CH - SWITZERLAND
Number of pages
17
Pages from-to
9293
UT code for WoS article
000597881700001
EID of the result in the Scopus database
2-s2.0-85097403944