Luc Bousset

Synthetic alpha-synuclein fibrils replicate in mice causing MSA-like pathology

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

Perilipin 4 repetitive region forms amyloid fibrils promoted by a genetic expansion found in myopathy patients

This study shows that a genetic expansion in PLIN4 repeats leads to amyloid fibril formation, contributing to myopathy.

C9orf72-derived poly-GA DPRs undergo endocytic uptake in iNPC-derived astrocytes and spread to motor neurons

This study shows poly-GA DPRs are taken up by astrocytes via endocytosis, spread to motor neurons, and cause axonal swellings through lysosomal dysfunction.

Quantitative study of alpha-synuclein prion-like spreading in fully oriented reconstructed neural networks reveals non-synaptic dissemination of seeding aggregates

This study uses a novel microfluidic system to investigate how alpha-synuclein aggregates spread between neurons, finding that synaptic connectivity does not significantly affect transfer efficiency.

Cryo-EM structure of alpha-synuclein fibrils amplified by PMCA from PD and MSA patient brains

Three fibril polymorphs, amplified from Parkinson's and multiple system atrophy brain homogenate by PMCA, adopt folds unlike any published alpha-synuclein arrangement; their disease relevance is untested.

Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species

This study shows that the Hsp70 disaggregation machinery disassembles Tau fibrils, generating small seeding-competent Tau species that can drive aggregation.

Two new polymorphic structures of alpha-synuclein solved by cryo-electron microscopy

The paper reports two new polymorphic structures of alpha-synuclein fibrils solved by cryo-EM, showing distinct structural features and interactions compared to previous structures.

LRRK2 modifies α-syn pathology and spread in mouse models and human neurons

This study shows that LRRK2 modifies α-syn aggregation and spread in both mouse and human models, suggesting potential therapeutic targets for Parkinson's disease.