The complex understanding of Annexin A1 phosphorylation
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
The complex understanding of Annexin A1 phosphorylation
Original language description
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
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
—
Result continuities
Project
—
Continuities
O - Projekt operacniho programu
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Cellular Signalling
ISSN
0898-6568
e-ISSN
—
Volume of the periodical
26
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
173-178
UT code for WoS article
000330817600018
EID of the result in the Scopus database
—