OPTIMIZATION OF EXPRESSSION AND PURIFICATION OF FRAGMENT FROM TAU PROTEIN

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Authors

PLEŠINGROVÁ Klára GAŠPARIK Norbert HRITZ Jozef

Year of publication 2020
Type Conference abstract
MU Faculty or unit

Central European Institute of Technology

Citation
Description Tau protein is abundant in the central nervous system, where it stabilizes microtubules by binding to the interface between tubulin sub-units [1,2]. Hyperphosphorylation of Tau leads to aggregation of protein and disruption of normal function of the neurons. These disorders can cause neurodegenerative diseases such as Alzheimer’s disease or Parkinson’s disease [3,4]. This work is focused on a short fragment from Tau protein, which has a key role in microtubule binding [2].
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