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@proceedings{1875183,
author = {Bera, Krishnendu and Hritz, Jozef},
booktitle = {CEITEC PhD Conference},
keywords = {Phosphorylation; Tau210-240 Peptide},
language = {eng},
title = {Impact of Phosphorylation for Tau210-240 Peptide and Interaction of Small Molecules and 14-3-3ζ Protein Studies Using Computational Methods},
url = {https://www.ceitec.eu/ceitec-phd-conference-2022/a4145},
year = {2022}
}
TY - CONF
ID - 1875183
AU - Bera, Krishnendu - Hritz, Jozef
PY - 2022
TI - Impact of Phosphorylation for Tau210-240 Peptide and Interaction of Small Molecules and 14-3-3ζ Protein Studies Using Computational Methods
KW - Phosphorylation
KW - Tau210-240 Peptide
UR - https://www.ceitec.eu/ceitec-phd-conference-2022/a4145
N2 - The conformational dynamics of intrinsically disordered proteins (IDPs) regulated by post-translational modifications such as phosphorylation is challenging to elucidate. A well-known IDP Tau is found hyper-phosphorylated in Alzheimer’s disease (AD) in humans [1]. The proline-rich motif of Tau210-240 peptide directly interacts with proteins such as 14-3-3ζ. 14-3-3ζ is one of the crucial protein in the human brain and bind to a multiarray of proteins. It has a significant impact on forming and deforming neurofibrillary tangles, and it was shown that the 14-3-3ζ monomer has strong anti-aggregation properties [2]. It was shown that monomerization of 14-3-3z can be induced by phosphorylation of Ser58 at the dimeric interface
ER -
BERA, Krishnendu a Jozef HRITZ. Impact of Phosphorylation for Tau210-240 Peptide and Interaction of Small Molecules and 14-3-3ζ Protein Studies Using Computational Methods. In \textit{CEITEC PhD Conference}. 2022.
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