Wyatt C. Powell

The paper investigates how phosphorylation at specific sites affects tau self-assembly, finding that S396 and S400 phosphorylation promotes aggregation while T403 and S404 phosphorylation suppresses it, with pS400 forming a CTE protofilament structure.

This study investigates how N-linked glycosylation affects Tau propagation and neuronal uptake by analyzing glycan site and structure effects on Tau-polyanion binding and seeding.

The paper develops a high-throughput method to identify fluoroprobes that distinguish between tau fibril polymorphs using paDSF and chemical screening.

This study investigates how AD-specific post-translational modifications affect Tau self-assembly into PHFs, finding that phosphorylation generally inhibits aggregation while acetylation has variable effects.