Dailu Chen

This study shows that tau aggregation can be reduced by modifying sequences near the PGGG β-turn motif, while maintaining microtubule binding, offering therapeutic insights for neurodegenerative diseases.

The paper shows that seed-competent tau monomer (Ms) forms before insoluble fibrils in PS19 tauopathy mice, initiating pathology in a phosphorylation-independent manner.

The paper investigates how local structure in tau protein modulates aggregation propensity and how mutations disrupt this structure to trigger amyloid formation.

The paper identifies inert and seed-competent tau monomers, showing structural differences that influence aggregation potential.