Walther Haenseler

This paper develops a method to quantitatively analyze the structural states of alpha-synuclein in vitro and in situ, revealing conformational changes in yeast and human neurons.

This study identifies structural and functional differences in alpha-synuclein fibrils from Parkinson's disease, Dementia with Lewy Bodies, and Multiple System Atrophy, linking these differences to disease-specific cellular responses and potential therapeutic targets.

This study systematically identifies structure-specific protein-protein interactions using LiP-MS, demonstrating its application to alpha-synuclein in Parkinson's disease.

This paper introduces a structural proteomic pipeline to study anti-amyloidogenic compounds' mechanisms in vitro and in situ, revealing off-target effects and structural interactions with α-Synuclein.