Cell-to-cell transmission of α-synuclein (α-Syn) aggregates is a key event in Parkinson’s disease (PD) pathogenesis, yet the neuronal surface factors that govern uptake of pathogenic α-Syn fibrils remain undefined. We developed a flow cytometry-based CRISPR activation screen for modifiers of α-Syn preformed fibril (PFF...
Sandesh Neupane, Lea Šustić, Lorenzo Maraio et al.· bioRxiv· 0 citations
It is demonstrated that αSyn-specific CAR iTregs can selectively exert potent local immunomodulatory effects, establishing a promising antigen-specific cellular immunotherapy platform for PD and other synucleinopathies.
Alice Calderoni, Melania Nannoni, Giorgia Ruffini et al.· bioRxiv· 0 citations
Synucleinopathies are a group of neurodegenerative disorders characterized by the misfolding, aggregation, and accumulation of α-synuclein (α-syn) into oligomeric assemblies and amyloid inclusions. Alongside neurons, glial cells can internalize pathological α-syn and play a major role in its degradation. Despite...
Lea Šustić, Elena de Cecco, Sandesh Neupane et al.· Cell Communication and Signa...· 1 citation
In both models, the CIAP-resistant interactome largely overlapped with the broader PS129 interactome, suggesting that seeded aggregation primarily affects existing PS129 interactions rather than directing the formation of new pathological ones.
Solji G. Choi, Atousa Bahrami, Jayda B. Duvernay et al.· bioRxiv· 1 citation
Interestingly, amplified material from MSA brains induced significantly more oligodendroglial pSyn aggregates than amplified material from PD brains, and mice injected with the fibril polymorph, showed mild changes in microglial reactivity.
Anne-Line Strange Laursen, K. Willén, Alexis Fenyi et al.· Neurobiology of Disease· 0 citations
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