ArticleScientific reports2018
Structural characteristics and membrane interactions of tandem α-synuclein oligomers.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Effects of Site-Specific Glycation on α-Synuclein.ACS chemical biology · 2026Article
- Systematic Comparison of Commercial Uranyl-Alternative Stains for Negative- and Positive-Staining Transmission Electron Microscopy of Organic Specimens.Advanced healthcare materials · 2025Article
- Conformational Selection of α-Synuclein Tetramers at Biological Interfaces.Journal of chemical information and modeling · 2024Article
- Article
- Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease.Nature communications · 2022Article
- Passive Immunization in Alpha-Synuclein Preclinical Animal Models.Biomolecules · 2022Review
- Predictive Modeling of Neurotoxic α-Synuclein Polymorphs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Implementing Complementary Approaches to Shape the Mechanism of α-Synuclein Oligomerization as a Model of Amyloid Aggregation.Molecules (Basel, Switzerland) · 2021Review
- Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation.ACS nano · 2021Article
- Internalization of α-synuclein oligomers into SH-SY5Y cells.Biophysical journal · 2021Article
- Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.Scientific reports · 2020Article
- α-Synuclein-112 Impairs Synaptic Vesicle Recycling Consistent With Its Enhanced Membrane Binding Properties.Frontiers in cell and developmental biology · 2020Article
- From Synaptic Protein to Prion: The Long and Controversial Journey of α-Synuclein.Frontiers in synaptic neuroscience · 2020Review
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Characterizing the inhibition of α-synuclein oligomerization by a pharmacological chaperone that prevents prion formation by the protein PrP.Protein science : a publication of the Protein Society · 2019Article
- Alpha-synuclein structure and Parkinson's disease - lessons and emerging principles.Molecular neurodegeneration · 2019Review
- Baseline concentration of misfolded α-synuclein aggregates in cerebrospinal fluid predicts risk of cognitive decline in Parkinson's disease.Neuropathology and applied neurobiology · 2019Article
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pre-fibrillar oligomers of α-synuclein are thought to be pathogenic molecules leading to neurotoxicity associated with Parkinson's disease and other neurodegenerative disorders. However, small oligomers are difficult to isolate for study. To gain better insight into the properties of small α-synuclein oligomers, we investigated engineered oligomers of specific size (dimers, tetramers, and octamers) linked head-to-tail in tandem, comparing the behavior of the oligomers to monomeric α-synuclein. All oligomeric constructs remained largely disordered in solution, as determined from dynamic light scattering and size-exclusion chromatography. Electron microscopy revealed that each construct could aggregate to form fibrils similar to those formed by monomeric α-synuclein. The interactions with large unilamellar vesicles (LUVs) composed of negatively-charged lipids differed depending on size, with smaller oligomers forming more extensive helical structure as determined by CD spectroscopy. Monitoring the influx of a fluorescence bleaching agent into vesicles showed that larger oligomers were somewhat more effective at degrading vesicular integrity and inducing membrane permeabilization.
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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.