ArticleThe Journal of biological chemistry2020
α-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.
- Alpha-Synuclein Strain Variability in Body-First and Brain-First Synucleinopathies.Frontiers in aging neuroscience · 2022Pooled it
- Divalent and Trivalent Metallic Ions Differentially Affect Alpha-Synuclein Aggregation.ACS chemical neuroscience · 2025Article
- Article
- Research models to study lewy body dementia.Molecular neurodegeneration · 2025Review
- Is There a Place for Lewy Bodies before and beyond Alpha-Synuclein Accumulation? Provocative Issues in Need of Solid Explanations.International journal of molecular sciences · 2024Review
- Ultrastructures of α-Synuclein Filaments in Synucleinopathy Brains and Experimental Models.Journal of movement disorders · 2024Article
- Experimental Animal Models of Prodromal Parkinson's Disease.Journal of Parkinson's disease · 2024Review
- α-Synuclein Strains and Their Relevance to Parkinson's Disease, Multiple System Atrophy, and Dementia with Lewy Bodies.International journal of molecular sciences · 2023Review
- The G51D SNCA mutation generates a slowly progressive α-synuclein strain in early-onset Parkinson's disease.Acta neuropathologica communications · 2023Article
- New SNCA mutation and structures of α-synuclein filaments from juvenile-onset synucleinopathy.Acta neuropathologica · 2023Article
- Multiple system atrophy: α-Synuclein strains at the neuron-oligodendrocyte crossroad.Molecular neurodegeneration · 2022Review
- Quantum-dot-labeled synuclein seed assay identifies drugs modulating the experimental prion-like transmission.Communications biology · 2022Article
- Karyopherin abnormalities in neurodegenerative proteinopathies.Brain : a journal of neurology · 2021Review
- Assembly of α-synuclein and neurodegeneration in the central nervous system of heterozygous M83 mice following the peripheral administration of α-synuclein seeds.Acta neuropathologica communications · 2021Article
- Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers.Chembiochem : a European journal of chemical biology · 2021Article
- Microglial inclusions and neurofilament light chain release follow neuronal α-synuclein lesions in long-term brain slice cultures.Molecular neurodegeneration · 2021Article
- Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells.Communications biology · 2021Article
- Robust α-synuclein pathology in select brainstem neuronal populations is a potential instigator of multiple system atrophy.Acta neuropathologica communications · 2021Article
- Seeded assembly in vitro does not replicate the structures of α-synuclein filaments from multiple system atrophy.FEBS open bio · 2021Article
- Prominent microglial inclusions in transgenic mouse models of α-synucleinopathy that are distinct from neuronal lesions.Acta neuropathologica communications · 2020Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Assembled α-synuclein in nerve cells and glial cells is the defining pathological feature of neurodegenerative diseases called synucleinopathies. Seeds of α-synuclein can induce the assembly of monomeric protein. Here, we used sucrose gradient centrifugation and transiently transfected HEK 293T cells to identify the species of α-synuclein from the brains of homozygous, symptomatic mice transgenic for human mutant A53T α-synuclein (line M83) that seed aggregation. The most potent fractions contained Sarkosyl-insoluble assemblies enriched in filaments. We also analyzed six cases of idiopathic Parkinson's disease (PD), one case of familial PD, and six cases of multiple system atrophy (MSA) for their ability to induce α-synuclein aggregation. The MSA samples were more potent than those of idiopathic PD in seeding aggregation. We found that following sucrose gradient centrifugation, the most seed-competent fractions from PD and MSA brains are those that contain Sarkosyl-insoluble α-synuclein. The fractions differed between PD and MSA, consistent with the presence of distinct conformers of assembled α-synuclein in these different samples. We conclude that α-synuclein filaments are the main driving force for amplification and propagation of pathology in synucleinopathies.
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