ReviewActa neuropathologica2021
Evidence of distinct α-synuclein strains underlying disease heterogeneity.
Review in Acta neuropathologica, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
57 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 citations in OpenAlex.
- Alpha-Synuclein Strain Variability in Body-First and Brain-First Synucleinopathies.Frontiers in aging neuroscience · 2022Pooled it
- α-Synuclein strain homogeneity in multiple system atrophy subtypes.Brain pathology (Zurich, Switzerland) · 2026Article
- Adaptation of α-synuclein fibrils following multiple system atrophy transmission to mice.bioRxiv : the preprint server for biology · 2026Article
- Transcriptional dysregulation in the cerebellum triggered by oligodendroglial α-synucleinopathy: insights from a transgenic mouse into the early disease mechanisms of MSA.Journal of neural transmission (Vienna, Austria : 1996) · 2026Article
- Seed amplification of MSA alpha-synuclein aggregates preserves the biological and structural properties of brain-derived aggregates.Nature communications · 2025Article
- Structural polymorphism of α-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation.The EMBO journal · 2025Article
- Novel in situ seeding immunodetection assay uncovers neuronal-driven alpha-synuclein seeding in Parkinson's disease.NPJ Parkinson's disease · 2025Article
- Evidence of a novel α-synuclein strain isolated from a Parkinson's disease with dementia patient sample.Acta neuropathologica communications · 2025Article
- Age-dependent progression from clearance to vulnerability in the early response of periventricular microglia to α-synuclein toxic species.Molecular neurodegeneration · 2025Article
- Review
- α-Synuclein seeding amplification assays for diagnosing synucleinopathies: an innovative tool in clinical implementation.Translational neurodegeneration · 2024Review
- In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging.International journal of molecular sciences · 2024Article
- Structurally targeted mutagenesis identifies key residues supporting α-synuclein misfolding in multiple system atrophy.Journal of Parkinson's disease · 2024Article
- Single-Molecule Fingerprinting Reveals Different Growth Mechanisms in Seed Amplification Assays for Different Polymorphs of α-Synuclein Fibrils.ACS chemical neuroscience · 2024Article
- Current insights and assumptions on α-synuclein in Lewy body disease.Acta neuropathologica · 2024Review
- Structurally targeted mutagenesis identifies key residues supportingbioRxiv : the preprint server for biology · 2024Article
- Ligand Profiling as a Diagnostic Tool to Differentiate Patient-Derived α-Synuclein Polymorphs.ACS chemical neuroscience · 2024Article
- Nonintuitive Immunogenicity and Plasticity of Alpha-Synuclein Conformers: A Paradigm for Smart Delivery of Neuro-Immunotherapeutics.Pharmaceutics · 2024Review
- Tracing TMEM106B fibril deposition in aging and Parkinson's disease with dementia brains.Life medicine · 2024Article
- Are Preformed Fibrils a Model of Parkinson's Disease?Journal of Parkinson's disease · 2024Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synucleinopathies are a group of neurodegenerative disorders caused by the misfolding and self-templating of the protein α-synuclein, or the formation of α-synuclein prions. Each disorder differs by age of onset, presenting clinical symptoms, α-synuclein inclusion morphology, and neuropathological distribution. Explaining this disease-specific variability, the strain hypothesis postulates that each prion disease is encoded by a distinct conformation of the misfolded protein, and therefore, each synucleinopathy is caused by a unique α-synuclein structure. This review discusses the current data supporting the role of α-synuclein strains in disease heterogeneity. Several in vitro and in vivo models exist for evaluating strain behavior, however, as the focus of this article is to compare strains across synucleinopathy patients, our discussion predominantly focuses on the two models most commonly used for this purpose: the α-syn140*A53T-YFP cell line and the TgM83
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.