ArticleActa neuropathologica2026
Biochemical signatures of skin α-synuclein in synucleinopathies revealed by RT-QuIC assay end-product analysis.
Article in Acta neuropathologica, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Distinct alpha-synuclein seeding in post-mortem skin of Lewy body disease and multiple system atrophy.Acta neuropathologica · 2026Article
- A multimodal biomarker strategy to enhance diagnostic precision in neurodegenerative parkinsonism.Nature medicine · 2026Article
- Molecular profiling of alpha-synuclein pathology and seeding activity in Parkinson's disease.Acta neuropathologica · 2026Article
- Skin-Based α-Synuclein Deposits Detection Across the Prodromal Continuum of Synucleinopathies: Updated Evidence and Perspectives.Biomolecules · 2026Review
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6 authors.
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Abstract
Synucleinopathies, including Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA), share pathological accumulation of misfolded α-synuclein (αSyn) in the brain and overlapping clinical features, complicating accurate diagnosis with current methods. In this study, we utilized a real-time quaking-induced conversion (RT-QuIC) assay to demonstrate that autopsied skin samples from PD, DLB, and MSA patients (but not non-synucleinopathy controls) seed aggregation of recombinant αSyn. While RT-QuIC generated similarly positive fluorescence kinetic curves across synucleinopathies, biochemical and morphological analyses of RT-QuIC end products revealed distinct properties in the resulting αSyn aggregates. Notably, αSyn aggregates from DLB samples exhibited the highest resistance to proteinase K digestion, whereas MSA-derived aggregates showed the least aggregated bands on Western blots. Transmission electron microscopy revealed significant differences in length, width, and volume of skin αSyn fibrils of RT-QuIC end products from different synucleinopathies. These findings provide critical insights into disease-specific αSyn structural characteristics and suggest new strategies to improve diagnostic discrimination.
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