Ulf Dettmer

This study identifies WDR44 as a driver of de novo α-synuclein aggregation at the lysosomal membrane, linking early aggregation events to neuronal dysfunction in Parkinson's Disease.

This study shows lipid droplets promote alpha-synuclein phase separation, leading to mitochondrial toxicity and neurodegeneration in Parkinson's disease.

The paper develops an assay to compare protein levels and toxicity of alpha-synuclein variants, finding that the S129A mutant does not affect acute expression or toxicity.

The paper identifies genes regulating alpha-synuclein homeostasis and shows their differential expression correlates with increased rare risk variant burden in Parkinson's disease.

This paper investigates the role of alpha-synuclein in lipid regulation at MAM domains in synucleinopathies, showing disease-specific lipid alterations and Syn's impact on phosphatidylserine metabolism.

This paper develops an iPSC platform to rapidly generate alpha-synuclein inclusions and investigates their formation, subtypes, and molecular interactions.