Valerie A. Perez

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 identifies amino acids critical for tau strain propagation by analyzing their role in amyloid templating across different tauopathies.

This study identifies DnaJC7 as a specific regulator of tau seeding through its interaction with Hsp70, showing that its protective activity depends on the J domain and substrate binding site.

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