ArticleACS nano2018
Quantifying Co-Oligomer Formation by α-Synuclein.
Article in ACS nano, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Imaging nanoscopic co-assemblies of α-synuclein and Tau in human samples.Nature communications · 2026Article
- In Vivo Seeding of Amyloid-β Protein and Implications in Modeling Alzheimer's Disease Pathology.Biomolecules · 2025Review
- Precision Medicine in Neurodegenerative Diseases: Genomic Approaches to Target Amyloid-β, Tau, and Alpha-Synuclein Pathways.Current genomics · 2025Review
- Unraveling the interplay of β-amyloid pathology and Parkinson's disease progression: Insights from autopsy-confirmed patients.Heliyon · 2024Article
- Morphometric and Nanomechanical Screening of Peripheral Blood Cells with Atomic Force Microscopy for Label-Free Assessment of Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2023Review
- α-Synuclein Aggregation Is Triggered by Oligomeric Amyloid-β 42 via Heterogeneous Primary Nucleation.Journal of the American Chemical Society · 2023Article
- Thermodynamic Signatures of Blood Plasma Proteome in Neurodegenerative Pathologies.International journal of molecular sciences · 2023Article
- Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Morphometry and Stiffness of Red Blood Cells-Signatures of Neurodegenerative Diseases and Aging.International journal of molecular sciences · 2021Article
- Red Blood Cells' Thermodynamic Behavior in Neurodegenerative Pathologies and Aging.Biomolecules · 2021Article
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers.PloS one · 2021Article
- The Role of α-Synuclein Oligomers in Parkinson's Disease.International journal of molecular sciences · 2020Review
- Stochastic master equation for early protein aggregation in the transthyretin amyloid disease.Scientific reports · 2020Article
- Kinetic diversity of amyloid oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Anti-aggregation Effects of Phenolic Compounds on α-synuclein.Molecules (Basel, Switzerland) · 2020Review
- Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation.Chemical science · 2020Article
- Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer's disease neurons.Brain communications · 2020Article
- Imaging individual protein aggregates to follow aggregation and determine the role of aggregates in neurodegenerative disease.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small oligomers of the protein α-synuclein (αS) are highly cytotoxic species associated with Parkinson's disease (PD). In addition, αS can form co-aggregates with its mutational variants and with other proteins such as amyloid-β (Aβ) and tau, which are implicated in Alzheimer's disease. The processes of self-oligomerization and co-oligomerization of αS are, however, challenging to study quantitatively. Here, we have utilized single-molecule techniques to measure the equilibrium populations of oligomers formed in vitro by mixtures of wild-type αS with its mutational variants and with Aβ40, Aβ42, and a fragment of tau. Using a statistical mechanical model, we find that co-oligomer formation is generally more favorable than self-oligomer formation at equilibrium. Furthermore, self-oligomers more potently disrupt lipid membranes than do co-oligomers. However, this difference is sometimes outweighed by the greater formation propensity of co-oligomers when multiple proteins coexist. Our results suggest that co-oligomer formation may be important in PD and related neurodegenerative diseases.
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Registered trials
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