ArticleActa neuropathologica communications2018
Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methods.
Article in Acta neuropathologica communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.
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65 citing papers in PubMed, 1 synthesis or guideline pooled it, 109 citations in OpenAlex.
- Biofluid Detection of Pathological α-Synuclein in the Prodromal Phase of Synucleinopathies.Journal of Parkinson's disease · 2024Pooled it
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- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Unraveling the Mystery of Hemoglobin in Hypoxia-Accelerated Neurodegenerative Diseases.Biomolecules · 2025Review
- Distinct tau filament folds in human MAPT mutants P301L and P301T.Nature structural & molecular biology · 2025Article
- Tau filaments with the Alzheimer fold in human MAPT mutants V337M and R406W.Nature structural & molecular biology · 2025Article
- Rational selection of the monoclonal α-synuclein antibody amlenetug (Lu AF82422) for the treatment of α-synucleinopathies.NPJ Parkinson's disease · 2025Article
- Novel Poly-Arginine Peptide R18D Reduces α-Synuclein Aggregation and Uptake of α-Synuclein Seeds in Cortical Neurons.Biomedicines · 2025Article
- Identification and In Vitro and In Vivo Characterization of KAC-50.1 as a Potential α-Synuclein PET Radioligand.ACS chemical neuroscience · 2024Article
- TMEM106B amyloid filaments in the Biondi bodies of ependymal cells.Acta neuropathologica · 2024Article
- In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils.bioRxiv : the preprint server for biology · 2024Article
- A skin-specific α-Synuclein seeding amplification assay for diagnosing Parkinson's disease.NPJ Parkinson's disease · 2024Article
- Rational design of structure-based vaccines targeting misfolded alpha-synuclein conformers of Parkinson's disease and related disorders.Bioengineering & translational medicine · 2024Article
- Tau filaments with the chronic traumatic encephalopathy fold in a case of vacuolar tauopathy with VCP mutation D395G.Acta neuropathologica · 2024Article
- Tau filaments with the Alzheimer fold in cases withbioRxiv : the preprint server for biology · 2024Article
- The potential of phosphorylated α-synuclein as a biomarker for the diagnosis and monitoring of multiple system atrophy.CNS neuroscience & therapeutics · 2024Review
- Ultrastructures of α-Synuclein Filaments in Synucleinopathy Brains and Experimental Models.Journal of movement disorders · 2024Article
5 more citing papers are in PubMed but not listed here.
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5 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The concept that abnormal protein aggregates show prion-like propagation between cells has been considered to explain the onset and progression of many neurodegenerative diseases. Indeed, both synthetic amyloid-like fibrils and pathogenic proteins extracted from patients' brains induce self-templated amplification and cell-to-cell transmission in vitro and in vivo. However, it is unclear whether exposure to exogenous prion-like proteins can potentially cause these diseases in humans. Here, we investigated in detail the prion-like seeding activities of several kinds of pathogenic α-synuclein (α-syn), including synthetic fibrils and detergent-insoluble fractions extracted from brains of patients with α-synucleinopathies. Exposure to synthetic α-syn fibrils at concentrations above 100 pg/mL caused seeded aggregation of α-syn in SH-SY5Y cells, and seeded aggregation was also observed in C57BL/6 J mice after intracerebral inoculation of at least 0.1 μg/animal. α-Syn aggregates extracted from brains of multiple system atrophy (MSA) patients showed higher seeding activity than those extracted from patients with dementia with Lewy bodies (DLB), and their potency was similar to that of synthetic α-syn fibrils. We also examined the effects of various methods that have been reported to inactivate abnormal prion proteins (PrP
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