The complex understanding of Annexin A1 phosphorylation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F14%3A43897524" target="_blank" >RIV/60461373:22330/14:43897524 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S089865681300301X" target="_blank" >http://www.sciencedirect.com/science/article/pii/S089865681300301X</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.cellsig.2013.09.020" target="_blank" >10.1016/j.cellsig.2013.09.020</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The complex understanding of Annexin A1 phosphorylation

Popis výsledku v původním jazyce

Annexin A1 (ANXA1) is the first characterized member of the annexins superfamily. It binds the cellular membrane phospholipids in Ca2+ regulated manner. Annexin A1 has been found in several tissues and many physiological roles as hormones secretion, vesiculation, inflammatory response, apoptosis and differentiation have been shown. Its subcellular localization and binding with many partner proteins are altered accordingly with its physiological role. The Annexin A1 membrane localization is crucial for binding to receptors, suggesting a paracrine and juxtacrine extracellular action. Annexin A1 is subjected to several post-translational modifications. In particular the protein is phosphorylated on several residues both on the N-terminal functional domainand on the C-terminus core. Different kinases have been identified as responsible for the phosphotylation status of selective residues. The specific change in the phosphorylation status on the different sites alters ANXA1 localization, b

Název v anglickém jazyce

The complex understanding of Annexin A1 phosphorylation

Popis výsledku anglicky

Annexin A1 (ANXA1) is the first characterized member of the annexins superfamily. It binds the cellular membrane phospholipids in Ca2+ regulated manner. Annexin A1 has been found in several tissues and many physiological roles as hormones secretion, vesiculation, inflammatory response, apoptosis and differentiation have been shown. Its subcellular localization and binding with many partner proteins are altered accordingly with its physiological role. The Annexin A1 membrane localization is crucial for binding to receptors, suggesting a paracrine and juxtacrine extracellular action. Annexin A1 is subjected to several post-translational modifications. In particular the protein is phosphorylated on several residues both on the N-terminal functional domainand on the C-terminus core. Different kinases have been identified as responsible for the phosphotylation status of selective residues. The specific change in the phosphorylation status on the different sites alters ANXA1 localization, b

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

—

Návaznosti

O - Projekt operacniho programu

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Cellular Signalling

ISSN

0898-6568

e-ISSN

—

Svazek periodika

26

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

173-178

Kód UT WoS článku

000330817600018

EID výsledku v databázi Scopus

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