Johannes Burtscher

The paper develops and validates an expanded antibody panel to capture diverse alpha-synuclein conformations and modifications in Lewy body diseases.

This study shows that nitration of alpha-synuclein after fibrillization reduces its seeding activity and pathology formation in neurons and in vivo.

The paper examines the biochemical composition, interactome, and ultrastructural properties of nuclear and cytoplasmic Htt inclusions in mammalian cells and neurons.

This study shows that early α-synuclein pathology in a mouse model does not cause mitochondrial respiration deficits in the striatum and amygdala, even under corticosterone-induced hyperactivity.

This study develops a neuronal model of Lewy body formation and shows that the process of Lewy body maturation, not just fibrillization, drives neurodegeneration in synucleinopathies.

Calpain-1/2 cleavage of the alpha-synuclein C-terminus after fibril formation is reported to drive seeding, aggregation and the maturation of Lewy-body-like inclusions in primary neurons.

This study shows that chronic corticosterone worsens alpha-synuclein pathology and neurodegeneration in a mouse model of Parkinson's disease.