ArticleScientific reports2016
Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence.
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 20 papers.
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Who cites it
20 citing papers in PubMed.
- Direct observation and quantification of single nanocondensates of the low complexity domain of TDP-43.Nature communications · 2026Article
- Neuropathology of Lewy body dementia: Lewy-related pathology, α-synuclein oligomers, and comorbid pathologies.Molecular neurodegeneration · 2025Review
- Dynamic PRC1-CBX8 stabilizes a porous structure of chromatin condensates.Nature structural & molecular biology · 2025Article
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.ACS nano · 2023Article
- A dominant-negative SOX18 mutant disrupts multiple regulatory layers essential to transcription factor activity.Nucleic acids research · 2021Article
- Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein.Communications biology · 2021Article
- Potent inhibitors of toxic alpha-synuclein identified via cellular time-resolved FRET biosensors.NPJ Parkinson's disease · 2021Article
- Single-Molecule Counting Coupled to Rapid Amplification Enables Detection of α-Synuclein Aggregates in Cerebrospinal Fluid of Parkinson's Disease Patients.Angewandte Chemie (International ed. in English) · 2021Article
- MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography.Nature communications · 2021Article
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- Viral M45 and necroptosis-associated proteins form heteromeric amyloid assemblies.EMBO reports · 2019Article
- Review
- Lipids asFrontiers in neuroscience · 2019Review
- Pathological mutations differentially affect the self-assembly and polymerisation of the innate immune system signalling adaptor molecule MyD88.BMC biology · 2018Article
- Quantifying Co-Oligomer Formation by α-Synuclein.ACS nano · 2018Article
- Structure of a PSI-LHCI-cyt bProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Pre-aggregation kinetics and intermediates of α-synuclein monitored by the ESIPT probe 7MFE.European biophysics journal : EBJ · 2018Article
- Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein.International journal of molecular sciences · 2018Article
- A Split-Luciferase Reporter Recognizing GFP and mCherry Tags to Facilitate Studies of Protein-Protein Interactions.International journal of molecular sciences · 2017Article
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
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13 authors.
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Abstract
Protein aggregation is a hallmark of many neurodegenerative diseases, notably Alzheimer's and Parkinson's disease. Parkinson's disease is characterized by the presence of Lewy bodies, abnormal aggregates mainly composed of α-synuclein. Moreover, cases of familial Parkinson's disease have been linked to mutations in α-synuclein. In this study, we compared the behavior of wild-type (WT) α-synuclein and five of its pathological mutants (A30P, E46K, H50Q, G51D and A53T). To this end, single-molecule fluorescence detection was coupled to cell-free protein expression to measure precisely the oligomerization of proteins without purification, denaturation or labelling steps. In these conditions, we could detect the formation of oligomeric and pre-fibrillar species at very short time scale and low micromolar concentrations. The pathogenic mutants surprisingly segregated into two classes: one group forming large aggregates and fibrils while the other tending to form mostly oligomers. Strikingly, co-expression experiments reveal that members from the different groups do not generally interact with each other, both at the fibril and monomer levels. Together, this data paints a completely different picture of α-synuclein aggregation, with two possible pathways leading to the development of fibrils.
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