Saskia Hutten

This study shows how different domains of TDP-43 interact to control phase separation and condensate dynamics through simulations and experiments.

This study shows that the disordered NLS-region of TDP-43 is essential for its self-assembly across multiple scales, with a minimal mutation preserving condensation while others reduce it.

This study shows how FUS's RNA-binding and condensation properties shape its function in nuclear organization and DNA damage response through distinct and synergistic mechanisms.

The paper investigates how sequence context of RG/RGG motifs influences condensate formation, transportin-1 binding, and chaperoning using bioinformatics and experimental analysis.

This study uses microscopy to show that FUS condensates form clusters with high density and exhibit dynamic structural changes over time.

This study shows that TDP-43 and Tau directly interact, promoting co-condensation but reducing Tau fibril formation and seeding.

This study identifies FUS's role in muscle differentiation and structure through phase separation-mediated recruitment of ETV5 and MEF2, showing its dysfunction in FUS-ALS.

This study shows that PURA syndrome mutations disrupt PURA's structure and P-body association, explaining full penetrance of the disease.