Manuel Schweighauser

Cortical organoids from healthy human iPSCs, seeded with Alzheimer brain tau, form three-repeat tau filaments that cryo-EM shows are identical to Alzheimer paired helical filaments and need endogenous tau.

The paper reports cryo-EM structures of tau filaments from individuals with P301L and P301T MAPT mutations, revealing distinct filament folds associated with FTDP-17.

The paper determines cryo-EM structures of Tau filaments from transgenic mice models and identifies differences compared to human Tau filaments.

The paper reports cryo-EM structures of amyloid-beta filaments with the Arctic mutation from human and mouse brains, revealing structural differences and conformational changes.

The paper reports cryo-EM structures of α-synuclein filaments from Parkinson's disease, PD dementia, and dementia with Lewy bodies, showing they are composed of a single protofilament distinct from those in multiple system atrophy.

This study identifies age-dependent formation of TMEM106B amyloid filaments in human brains using cryo-EM, showing they appear in older individuals but not younger ones.

Cryo-EM shows brain-derived Aβ42 filaments adopt two related S-shaped protofilament folds: Type I dominates sporadic Alzheimer's, Type II familial Alzheimer's, other disorders and App^NL-F knock-in mice.

This study determines the structure of α-synuclein filaments in multiple system atrophy using cryo-EM, revealing distinct filament types and conformers that differ from in vitro assemblies.

The paper determines the structure of tau filaments in Alzheimer's disease cases and finds they adopt a common fold across individuals.