P. M. Wydorski

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.

This paper identifies an aromatic-rich motif in DNAJB8 that mediates oligomerization and shows that disrupting this motif affects oligomerization but not substrate activity.

This study identifies how SARS-CoV-2 PLpro selectively binds human ISG15 and K48-linked di-ubiquitin through dual domain recognition, revealing potential drug targets.

This study identifies DnaJC7's interaction with tau's beta-turn element to inhibit amyloid formation, suggesting a mechanism for tau aggregation regulation.