ArticleScientific reports2016
Structural and functional properties of prefibrillar α-synuclein oligomers.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 141 citations in OpenAlex.
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- Gene delivery of SUMO1-derived peptide rescues neuronal degeneration and motor deficits in a mouse model of Parkinson's disease.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Abundant non-inclusion α-synuclein pathology in Lewy body-negative LRRK2-mutant cases.Acta neuropathologica · 2025Article
- Detection of non-native species formed during fibrillization of the myocilin olfactomedin domain.Protein science : a publication of the Protein Society · 2025Article
- Elucidation of cytotoxicity of α-Synuclein fibrils on immune cells.Biochimica et biophysica acta. Proteins and proteomics · 2025Article
- MJF-14 proximity ligation assay detects early non-inclusion alpha-synuclein pathology with enhanced specificity and sensitivity.NPJ Parkinson's disease · 2024Article
- Elucidation of molecular mechanisms by which amyloid βBiochimica et biophysica acta. Molecular and cell biology of lipids · 2024Article
- Interaction between α-Synuclein and Bioactive Lipids: Neurodegeneration, Disease Biomarkers and Emerging Therapies.Metabolites · 2024Review
- Macrophages and Natural Killers Degrade α-Synuclein Aggregates.Molecular pharmaceutics · 2024Article
- Thrombomodulin reduces α-synuclein generation and ameliorates neuropathology in a mouse model of Parkinson's disease.Cell death discovery · 2024Article
- Phospholipids and Cholesterol Determine Molecular Mechanisms of Cytotoxicity of α-Synuclein Oligomers and Fibrils.ACS chemical neuroscience · 2024Article
- Conformational dynamics of α-synuclein and study of its intramolecular forces in the presence of selected compounds.Scientific reports · 2023Article
- Synapses do not facilitate prion-like transfer of alpha-synuclein: a quantitative study in reconstructed unidirectional neural networks.Cellular and molecular life sciences : CMLS · 2023Article
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.ACS nano · 2023Article
- AAV-mediated expression of a new conformational anti-aggregated α-synuclein antibody prolongs survival in a genetic model of α-synucleinopathies.NPJ Parkinson's disease · 2023Article
- Nanoscale imaging of individual amyloid aggregates extracted from brains of Alzheimer and Parkinson patients reveals presence of lipids in α-synuclein but not in amyloid βProtein science : a publication of the Protein Society · 2023Article
- The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation.International journal of molecular sciences · 2023Review
- Development of fluorophores for the detection of oligomeric aggregates of amyloidogenic proteins found in neurodegenerative diseases.Frontiers in chemistry · 2023Review
- Detrimental effects of soluble α-synuclein oligomers at excitatory glutamatergic synapses.Frontiers in aging neuroscience · 2023Article
17 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The deposition of fibrillar alpha-synuclein (α-syn) within inclusions (Lewy bodies and Lewy neurites) in neurons and glial cells is a hallmark of synucleinopathies. α-syn populates a variety of assemblies ranging from prefibrillar oligomeric species to fibrils whose specific contribution to neurodegeneration is still unclear. Here, we compare the specific structural and biological properties of distinct soluble prefibrillar α-syn oligomers formed either spontaneously or in the presence of dopamine and glutaraldehyde. We show that both on-fibrillar assembly pathway and distinct dopamine-mediated and glutaraldehyde-cross-linked α-syn oligomers are only slightly effective in perturbing cell membrane integrity and inducing cytotoxicity, while mature fibrils exhibit the highest toxicity. In contrast to low-molecular weight and unstable oligomers, large stable α-syn oligomers seed the aggregation of soluble α-syn within reporter cells although to a lesser extent than mature α-syn fibrils. These oligomers appear elongated in shape. Our findings suggest that α-syn oligomers represent a continuum of species ranging from unstable low molecular weight particles to mature fibrils via stable elongated oligomers composed of more than 15 α-syn monomers that possess seeding capacity.
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