Structural aspects of protein kinase ASK1 regulation

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F17%3A00487591" target="_blank" >RIV/67985823:_____/17:00487591 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/17:10372344
Result on the web
<a href="http://dx.doi.org/10.1016/j.jbior.2017.10.002" target="_blank" >http://dx.doi.org/10.1016/j.jbior.2017.10.002</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jbior.2017.10.002" target="_blank" >10.1016/j.jbior.2017.10.002</a>

Result language
angličtina
Original language name
Structural aspects of protein kinase ASK1 regulation
Original language description
Apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5), a member of the mitogen-activated protein kinase kinase kinase (MAP3K) family, activates the p38 mitogen-activated protein kinase and the c-Jun N-terminal kinase (JNK) signaling cascades in response to various stressors. ASK1 activity is tightly regulated through phosphorylation and interaction with various binding partners. However, the mechanistic details underlying the ASK1 regulation are still not fully understood. This review focuses on recent advances in structural studies of protein kinase ASK1 and on the insights they provide into its mechanism of regulation. In addition, we also discuss protein–protein interactions between ASK1 and its binding partners thioredoxin (TRX) and 14-3-3 protein.
Czech name
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Czech description
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Type
J<sub>SC</sub> - Article in a specialist periodical, which is included in the SCOPUS database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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