Other formats:
BibTeX
LaTeX
RIS
@proceedings{1710376,
author = {Louša, Petr and Trošanová, Zuzana and Kozeleková, Aneta and Brom, Tomáš and Gašparik, Norbert and Weisová, Veronika and Žoldák, G. and Hritz, Jozef},
booktitle = {XX. Workshop of Biophysical Chemists and Electrochemists.},
language = {eng},
isbn = {978-80-210-9655-4},
title = {HOW PHOSPHORYLATION IMPACTS 14-3-3ζ DIMERIZATION},
url = {https://www.sci.muni.cz/labifel/files/soubory/sbornik_2020.pdf},
year = {2020}
}
TY - CONF
ID - 1710376
AU - Louša, Petr - Trošanová, Zuzana - Kozeleková, Aneta - Brom, Tomáš - Gašparik, Norbert - Weisová, Veronika - Žoldák, G. - Hritz, Jozef
PY - 2020
TI - HOW PHOSPHORYLATION IMPACTS 14-3-3ζ DIMERIZATION
SN - 9788021096554
UR - https://www.sci.muni.cz/labifel/files/soubory/sbornik_2020.pdf
N2 - The 14-3-3 proteins represent a large group of dimeric proteins. Specifically, the 14-3-3 family consists of 7 isoforms, that can create many homo- and heterodimeric forms, not even accounting for the possibility of changing the oligomerization properties by posttranslational modifications such as phosphorylation. The functions of 14-3-3 are very often dependent on its oligomeric state. Therefore, the parameters of oligomerization are very interesting in order to correctly understand the regulation and behavior of 14-3-3 itself.
ER -
LOUŠA, Petr, Zuzana TROŠANOVÁ, Aneta KOZELEKOVÁ, Tomáš BROM, Norbert GAŠPARIK, Veronika WEISOVÁ, G. ŽOLDÁK and Jozef HRITZ. HOW PHOSPHORYLATION IMPACTS 14-3-3ζ DIMERIZATION. In \textit{XX. Workshop of Biophysical Chemists and Electrochemists.}. 2020. ISBN~978-80-210-9655-4.
|
