Michel Goedert

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.

This study shows that primary neurons can propagate Alzheimer's disease paired helical filaments and that tau filament folds determine inclusion morphologies.

This study demonstrates that tau filaments from Alzheimer's and corticobasal degeneration patients can seed the formation of structurally identical mouse tau filaments, supporting the prion-like transmission hypothesis.

This study shows that reduced microtubule polyglutamylation causes neuronal dysfunction and worsens Tau-induced neurodegeneration in mice.

This study reports cryo-EM structures of tau filaments from MAPT mutants, showing how specific mutations alter the Pick fold structure and enable reconstitution of variants.

This study identifies twelve phosphomimetic mutations in tau that induce the formation of paired helical filaments in vitro, mimicking Alzheimer's disease structures.

The paper reports the structures of α-synuclein filaments from individuals with Parkinson's disease and dementia, revealing differences in dimerisation and twist reversal between pathogenic and non-pathogenic variants.

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 the structures of tau filaments in individuals with MAPT mutations V337M and R406W using cryo-EM, finding the Alzheimer fold in all cases and a new triple filament assembly.

The paper reports that tau filaments in vacuolar tauopathy with VCP mutation D395G have the CTE fold, similar to environmentally induced diseases.

The paper determines cryo-EM structures of Aβ40 filaments from Alzheimer's and cerebral amyloid angiopathy samples, revealing structural differences at higher resolution.

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 tau filaments formed in SH-SY5Y cells seeded with brain extracts from Alzheimer's and corticobasal degeneration cases, showing some structural templating.

The paper uses cryo-EM to study tau filaments from Alzheimer's and CTE cases with and without flortaucipir, finding binding only in CTE Type I filaments.

The paper reports the presence of abundant Aβ fibrils in aqueous extracts from Alzheimer's disease brains, with structures identical to those in amyloid plaques.

This study shows that tau filaments in subacute sclerosing panencephalitis and chronic traumatic encephalopathy have identical structural features.

This study uses cryo-EM to show that tau filaments in ALS/PDC share the CTE fold, suggesting environmental causes for the disease.

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 identifies a SNCA mutation causing juvenile-onset synucleinopathy and describes the structural features of α-synuclein filaments associated with the disease.

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.

This study reports in vitro assembly of recombinant tau into filaments structurally similar to those in Alzheimer's disease and chronic traumatic encephalopathy using cryo-EM.

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.

Cryo-EM structures sort four-repeat tauopathies into three-layered (PSP, GGT, LNT) and four-layered (CBD, AGD, ARTAG, MAPT intron 10 mutations) tau folds, grounding a hierarchical structure-based classification.

This study tracks tau fibrillogenesis and microglial phagocytosis of neurons in a living tauopathy model, showing that microglia engulf tangle-bearing neurons and that TSPO ligands can reduce this process.

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.

This paper reports the structure of tau filaments in corticobasal degeneration using cryo-EM, revealing a novel four-layered fold distinct from other tauopathies.

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