ReviewActa neuropathologica2022
Consequences of variability in α-synuclein fibril structure on strain biology.
Review in Acta neuropathologica, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- Brain-first and body-first subtypes of Lewy body disease.Nature reviews. Neurology · 2026Review
- A Degron Decoy System Co-opts Pathological Seeding to Enable Clearance of Multimeric α-Synuclein.bioRxiv : the preprint server for biology · 2026Article
- Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.Nature communications · 2025Article
- Co-infection with two α-synuclein strains reveals novel synergistic interactions.Acta neuropathologica · 2025Article
- A novel alpha-synuclein G14R missense variant is associated with atypical neuropathological features.Molecular neurodegeneration · 2025Article
- Co-infection with two α-synuclein strains reveals novel synergistic interactions.bioRxiv : the preprint server for biology · 2025Article
- Rational selection of the monoclonal α-synuclein antibody amlenetug (Lu AF82422) for the treatment of α-synucleinopathies.NPJ Parkinson's disease · 2025Article
- Limitations and Applications of Rodent Models in Tauopathy and Synucleinopathy Research.Journal of neurochemistry · 2025Review
- Precision scalpels for the epigenome: next-gen editing tools in targeted therapies.Frontiers in medicine · 2025Review
- A-synuclein prion strains differentially adapt after passage in mice.PLoS pathogens · 2024Article
- Structurally targeted mutagenesis identifies key residues supporting α-synuclein misfolding in multiple system atrophy.Journal of Parkinson's disease · 2024Article
- Structurally targeted mutagenesis identifies key residues supportingbioRxiv : the preprint server for biology · 2024Article
- Effect of host and strain factors on α-synuclein prion pathogenesis.Trends in neurosciences · 2024Review
- Ligand Profiling as a Diagnostic Tool to Differentiate Patient-Derived α-Synuclein Polymorphs.ACS chemical neuroscience · 2024Article
- Molecular Behavior of α-Synuclein Is Associated with Membrane Transport, Lipid Metabolism, and Ubiquitin-Proteasome Pathways in Lewy Body Disease.International journal of molecular sciences · 2024Article
- Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation.Chemical science · 2024Article
- The molecular spectrum of amyloid-beta (Aβ) in neurodegenerative diseases beyond Alzheimer's disease.Brain pathology (Zurich, Switzerland) · 2024Article
- Are Preformed Fibrils a Model of Parkinson's Disease?Journal of Parkinson's disease · 2024Article
- Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024Review
- Neuronal SNCA transcription during Lewy body formation.Acta neuropathologica communications · 2023Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synucleinopathies are a group of clinically and neuropathologically distinct protein misfolding diseases caused by unique α-synuclein conformations, or strains. While multiple atomic resolution cryo-electron microscopy structures of α-synuclein fibrils are now deposited in Protein Data Bank, significant gaps in the biological consequences arising from each conformation have yet to be unraveled. Mutations in the α-synuclein gene (SNCA), cofactors, and the solvation environment contribute to the formation and maintenance of each disease-causing strain. This review highlights the impact of each of these factors on α-synuclein misfolding and discusses the implications of the resulting structural variability on therapeutic development.
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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.