Esther del Cid‐Pellitero

This study shows that USP15 deletion in astrocytes and microglia reduces neuroinflammation and slows synucleinopathy progression in mice, with human data linking USP15 expression to Parkinson's disease risk.

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.

This study identifies how STIP1/HOP interacts with a-Syn to promote toxic oligomer formation in synucleinopathies.

This study identifies WDR44 as a driver of de novo α-synuclein aggregation at the lysosomal membrane, linking early aggregation events to neuronal dysfunction in Parkinson's Disease.

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 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.