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OPTIMIZATION OF EXPRESSSION AND PURIFICATION OF FRAGMENT FROM TAU PROTEIN
Authors | |
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Year of publication | 2020 |
Type | Conference abstract |
MU Faculty or unit | |
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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