ArticleBiophysical journal2014
Elucidating the aggregation number of dopamine-induced α-synuclein oligomeric assemblies.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Rethinking Parkinson's disease: could dopamine reduction therapy have clinical utility?Journal of neurology · 2024Review
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- Correction of Systematic Bias in Single Molecule Photobleaching Measurements.Biophysical journal · 2020Article
- Single-molecule photobleaching: Instrumentation and applications.Journal of biosciences · 2018Article
- The number of α-synuclein proteins per vesicle gives insights into its physiological function.Scientific reports · 2016Article
- Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical Guide.International journal of molecular sciences · 2016Review
- The N-terminal residues 43 to 60 form the interface for dopamine mediated α-synuclein dimerisation.PloS one · 2015Article
- Structural insights into amyloid oligomers of the Parkinson disease-related protein α-synuclein.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conventional methods to determine the aggregation number, that is, the number of monomers per oligomer, struggle to yield reliable results for large protein aggregates, such as amyloid oligomers. We have previously demonstrated the use of a combination of single-molecule photobleaching and substoichiometric fluorescent labeling to determine the aggregation number of oligomers of human α-synuclein, implicated in Parkinson's disease. We show here that this approach is capable of accurately resolving mixtures of multiple distinct molecular species present in the same sample of dopamine-induced α-synuclein oligomers, and that we can determine the respective aggregation numbers of each species from a single histogram of bleaching steps. We found two distinct species with aggregation numbers of 15-19 monomers and 34-38 monomers. These results show that this single-molecule approach allows for the systematic study of the aggregation numbers of complex supramolecular assemblies formed under different aggregation conditions.
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