Wen Luo

This study shows that pS129 accumulation in M83 mice leads to structural atrophy, reduced functional connectivity, and hypoactivation in somatosensory areas.

This study identifies plasma protein biomarkers and mechanistic pathways in Parkinson's disease using deep proteomics and functional genomics.

This study tracks how striatal α-synuclein seeding affects brain networks and cognitive flexibility in marmosets, showing multi-scale reorganization and impaired cognitive flexibility.

This paper develops an automated assay to quantify synuclein aggregate formation in human dopaminergic neurons using pS129-syn as a marker, showing dose- and time-dependent increases with PFFs and genetic factors affecting aggregate formation.

This study shows that N-terminal acetylation of α-synuclein reduces aggregation, uptake, seeding, and toxicity in Parkinson's disease models.

The paper describes a high-content imaging assay to screen small molecules that reduce cellular uptake of α-synuclein preformed fibrils in hiPSC-derived cells, identifying compounds that effectively lower intracellular PFF load.

This study shows that Parkin is essential for neuronal differentiation and survival, and small molecule Parkin agonists like FB231 protect dopaminergic neurons in Parkinson's disease models.

This study compares four methods of purifying α-synuclein for seed amplification assays, finding that osmotic shock-purified monomer has the lowest aggregation propensity and best inter-batch reproducibility.

This study investigates how alpha-synuclein propagation affects brain atrophy and motor deficits across different genotypes and inoculation sites in mice.

The paper investigates sex differences in aSyn pathology progression in M83 mice using MRI and behavioral analysis, finding female resilience to neurodegeneration despite earlier motor symptom onset in males.

This study investigates the role of cathepsin B in Parkinson's disease by analyzing genetic variants and manipulating catB function in cell models to assess its impact on lysosomal activity and alpha-synuclein clearance.

The paper shows that combining α-synuclein fibrils with immune challenges causes Lewy body-like inclusions in human dopaminergic neurons, while cortical neurons do not form such inclusions.

This study identifies β-neurexins as presynaptic proteins that bind to α-synuclein preformed fibrils, impairing presynaptic organization and contributing to synucleinopathy pathology.

This study shows that genetic inactivation of USP19 reduces a-synuclein ubiquitination and Lewy body-like aggregate accumulation in a mouse model of Parkinson's disease.

This study identifies neuroanatomical and cognitive biomarkers of alpha-synuclein propagation in a mouse model, showing early cognitive deficits and brain atrophy linked to prion-like spread of misfolded alpha-synuclein.