Impact of Phosphorylation for Tau210-240 Peptide and Interaction of Small Molecules and 14-3-3ζ Protein Studies Using Computational Methods

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00126277" target="_blank" >RIV/00216224:14740/22:00126277 - isvavai.cz</a>
Result on the web
<a href="https://www.ceitec.eu/ceitec-phd-conference-2022/a4145" target="_blank" >https://www.ceitec.eu/ceitec-phd-conference-2022/a4145</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Impact of Phosphorylation for Tau210-240 Peptide and Interaction of Small Molecules and 14-3-3ζ Protein Studies Using Computational Methods
Original language description
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
Czech name
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Czech description
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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