Florent Laferrière

This study shows synthetic alpha-synuclein fibrils can replicate in mice, causing MSA-like pathology and forming glial cytoplasmic inclusions.

The paper compares aggregated alpha-synuclein in Parkinson's disease and multiple system atrophy brains to determine their proteomic composition and potential cross-seeding mechanisms.

The paper develops a human iPSC-derived neural model to study TDP-43 pathology, identifying NPTX2 misregulation as a key factor in ALS/FTLD neurotoxicity.

Stealth α-synuclein fibrils escape ThT detection, outcompete visible polymorphs, and spread neurodegeneratively in vivo.

The paper uses machine learning to identify neurodegeneration signatures in non-human primates caused by patient-derived α-synuclein structures, showing that small aggregates are as toxic as larger fibrils.

The paper shows that structurally diverse PrPSc assemblies complement each other to cross species barriers, supporting the quasi-species concept in prions.