Abstract

Aggregation of microtuble-associated protein Tau is a hallmark of several neurological disorders collectively termed as Tauopathies. Fluorescent tagging is a powerful tool for studying Tau aggregation in vitro. Conventionally, cysteine residues of Tau are used to label the protein fluorescently. However, the full-length Tau isoform contains two cysteine (Cys) residues at positions 291 and 322 in the microtubule binding region, which may play a crucial role in Tau aggregation by forming intra-sheet disulfide bonds.

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