Sonia Donzelli

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

This study reports the atomic structure of mouse α-synuclein fibrils and shows they differ structurally and functionally from human fibrils linked to Parkinson's and MSA.

Post-fibrillization nitration of alpha-synuclein abolishes its seeding activity and pathology formation in primary neurons and in vivo

This study shows that nitration of alpha-synuclein after fibrillization reduces its seeding activity and pathology formation in neurons and in vivo.

Neighbouring modifications interfere with the detection of phosphorylated alpha-synuclein at Serine 129: Revisiting the specificity of pS129 antibodies

The paper shows that neighboring post-translational modifications affect the detection of phosphorylated alpha-synuclein at Serine 129 by existing antibodies.

A novel mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein fibrils and recapitulates its pathological diversity

The paper investigates the effects of the E83Q mutation on alpha-synuclein aggregation and toxicity, finding it accelerates fibrillization and enhances pathological features in neuronal models.

Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the unfolded protein response (UPR) in models of neurodegeneration

This study shows that forcing dimerization between ATF6f and XBP1s enhances UPR activity, reducing protein aggregation in neurodegenerative disease models.

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of α-synuclein monomers, oligomers and fibrils: towards improving experimental reproducibility in α-synuclein research

This paper introduces a centrifugation-based filtration protocol to isolate and quantify α-synuclein monomers, oligomers, and fibrils to improve experimental reproducibility in Parkinson's research.