Dorothee Dormann

This study shows that kinase-phosphatase cycles drive self-sustained oscillations in TDP-43 condensates through differential recruitment and slow redistribution of enzymes.

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

This paper introduces programmable DNA-based protonuclei to study protein phase separation, showing that environmental factors significantly influence FUS behavior.

This study investigates how TDP-43 phase separation affects its protein interactome and regulation of alternative splicing, showing PS-dependent interactions with RNA regulators.

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 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 SRSF5 is critical for paraspeckle assembly and dynamics, with stress-induced changes and compensatory effects on TDP-43 and NEAT1.

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

The paper uses molecular simulations to study how phosphorylation by CK1δ affects TDP-43 condensates and aggregation, finding that phosphorylation patterns depend on sequence and charge rather than position.

This study identifies PUN motifs in yeast Loc1p that cooperate to catalyze RNA folding and drive phase separation, suggesting a role in RNA and DNA-related processes across species.

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.

The paper develops a method to purify phase-separated FUS droplets and shows that LLPS alters FUS interactome composition, linking it to chromatin remodeling and mitochondrial function in ALS.