Michel Goedert, MD, PhD

Goedert and colleagues showed that the intracellular filamentous amyloid inclusions of most neurodegenerative diseases are made of either tau protein or alpha-synuclein. In 2017, they reported the cryo-EM structures of a human brain amyloid, the Alzheimer tau fold (in collaboration with the Scheres group from the MRC Laboratory of Molecular Biology). Since then, they have solved the structures of tau, alpha-synuclein, amyloid-beta and TMEM106B filaments from the brains of individuals with many neurodegenerative diseases, establishing that each sporadic tauopathy and synucleinopathy is characterised by a specific filament fold and providing neuropathological descriptions of disease at the atomic level. They must now develop methods for forming the human disease filament folds under experimental conditions. For tau, they already formed Alzheimer and chronic traumatic encephalopathy folds from recombinant proteins and established the formation of transient intermediate filaments as part of the assembly process.