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

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Authors

BERA Krishnendu HRITZ Jozef

Year of publication 2022
Type Appeared in Conference without Proceedings
MU Faculty or unit

Central European Institute of Technology

Citation
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 14-3-3?. 14-3-3? 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 14-3-3? 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
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