The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F20%3A00535581" target="_blank" >RIV/67985823:_____/20:00535581 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/20:10420692
Result on the web
<a href="https://www.mdpi.com/1422-0067/21/22/8824" target="_blank" >https://www.mdpi.com/1422-0067/21/22/8824</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms21228824" target="_blank" >10.3390/ijms21228824</a>
Alternative languages
Result language
angličtina
Original language name
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
Original language description
Phosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation often leads to disease. Moreover, the functions of many kinases are regulated through protein–protein interactions, which in turn are mediated by phosphorylated motifs and often involve associations with the scaffolding and chaperon protein 14-3-3. Therefore, the aim of this review article is to provide an overview of the state of the art on 14-3-3-mediated kinase regulation, focusing on the most recent mechanistic insights into these important protein–protein interactions and discussing in detail both their structural aspects and functional consequences.
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
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
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
1422-0067
e-ISSN
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Volume of the periodical
21
Issue of the periodical within the volume
22
Country of publishing house
CH - SWITZERLAND
Number of pages
16
Pages from-to
8824
UT code for WoS article
000594952500001
EID of the result in the Scopus database
2-s2.0-85096514011