Lei Ortigosa-Pascual

This study investigates how phosphorylation levels and the molecular chaperone Bri2 BRICHOS opposingly regulate Tau condensation and aggregation, revealing their roles in tauopathies.

This study designs de novo proteins that selectively inhibit alpha-synuclein aggregation by targeting specific intermediates, with one binder preferentially inhibiting oligomer formation and secondary nucleation.

This study shows that sequence imperfections in synthetic Aβ42 peptides cause differences in aggregation behavior compared to recombinant Aβ42.

This study shows tau proteins from Alzheimer's and CTE folds catalyze Aβ42 aggregation in a fold-specific manner, increasing toxicity and offering new therapeutic insights.

This study uses PICUP to identify transient α-synuclein contacts in different conformational states, revealing state-specific interactions in solution, membrane-bound, and fibril forms.