Structural aspects of protein kinase ASK1 regulation

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11310/17:10372344

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural aspects of protein kinase ASK1 regulation

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Structural aspects of protein kinase ASK1 regulation

Popis výsledku anglicky

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.

Druh

J_SC - Článek v periodiku v databázi SCOPUS

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Advances in Biological Regulation

ISSN

2212-4926

e-ISSN

—

Svazek periodika

66

Číslo periodika v rámci svazku

1 Dec

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

31-36

Kód UT WoS článku

—

EID výsledku v databázi Scopus

2-s2.0-85039855438