ArticleCommunications biology2022
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- α-Synuclein overexpression increases the tropism of pre-formed fibrils and MSA-patient derived seeds towards oligodendroglia.Acta neuropathologica communications · 2026Article
- Molecular profiling of alpha-synuclein pathology and seeding activity in Parkinson's disease.Acta neuropathologica · 2026Article
- Propagation of α-synuclein pathology: models, mechanisms and future goals.Molecular neurodegeneration advances · 2026Review
- Alpha-Synuclein Neurobiology in Parkinson's Disease: A Comprehensive Review of Its Role, Mechanisms, and Therapeutic Perspectives.Brain sciences · 2025Review
- Alpha-synuclein fibril structures cluster into distinct classes.Biophysical journal · 2025Review
- Probing the effect of the disordered flank regions on amyloid fibril growth and proliferation.RSC advances · 2025Article
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- An approach to characterize mechanisms of action of anti-amyloidogenic compounds in vitro and in situ.NPJ Parkinson's disease · 2025Article
- Brain-derived and in vitro-seeded alpha-synuclein fibrils exhibit distinct biophysical profiles.eLife · 2024Article
- α-Synuclein seeding amplification assays for diagnosing synucleinopathies: an innovative tool in clinical implementation.Translational neurodegeneration · 2024Review
- Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.Science advances · 2024Article
- Article
- Are Preformed Fibrils a Model of Parkinson's Disease?Journal of Parkinson's disease · 2024Article
- Early-Onset Parkinson Mutation Remodels Monomer-Fibril Interactions to Allosterically Amplify Synuclein's Amyloid Cascade.JACS Au · 2023Article
- Beyond Strains: Molecular Diversity in Alpha-Synuclein at the Center of Disease Heterogeneity.International journal of molecular sciences · 2023Review
- ⍺-Synuclein Structural Diversity and the Cellular Environment in ⍺-Synuclein Transmission Models and Humans.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023Review
- Synucleins: New Data on Misfolding, Aggregation and Role in Diseases.Biomedicines · 2022Review
- The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils.Nature communications · 2022Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Parkinson's disease (PD) and Multiple System Atrophy (MSA) are progressive and unremitting neurological diseases that are neuropathologically characterized by α-synuclein inclusions. Increasing evidence supports the aggregation of α-synuclein in specific brain areas early in the disease course, followed by the spreading of α-synuclein pathology to multiple brain regions. However, little is known about how the structure of α-synuclein fibrils influence its ability to seed endogenous α-synuclein in recipient cells. Here, we aggregated α-synuclein by seeding with homogenates of PD- and MSA-confirmed brain tissue, determined the resulting α-synuclein fibril structures by cryo-electron microscopy, and characterized their seeding potential in mouse primary oligodendroglial cultures. The combined analysis shows that the two patient material-amplified α-synuclein fibrils share a similar protofilament fold but differ in their inter-protofilament interface and their ability to recruit endogenous α-synuclein. Our study indicates that the quaternary structure of α-synuclein fibrils modulates the seeding of α-synuclein pathology inside recipient cells. It thus provides an important advance in the quest to understand the connection between the structure of α-synuclein fibrils, cellular seeding/spreading, and ultimately the clinical manifestations of different synucleinopathies.
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