Tom Scheidt

This study shows phosphorylation of TDP-43's low-complexity domain shifts its self-assembly from macrophase separation to micellization, potentially protecting against pathological aggregation.

This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.

This study shows that PEG affects phase-separated droplets differently depending on the protein, accelerating Nup98 maturation but stabilizing BSA droplets.

This study shows that small heat shock proteins inhibit FUS and TDP-43 nano-cluster formation and target aggregation interfaces, highlighting their role in preventing neurodegenerative protein aggregation.