ArticleACS chemical neuroscience2020
Real-Time Characterization of Cell Membrane Disruption by α-Synuclein Oligomers in Live SH-SY5Y Neuroblastoma Cells.
Article in ACS chemical neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins.Science advances · 2025Article
- Single-Molecule Insight Into α-Synuclein Fibril Structure and Mechanics Modulated by Chemical Compounds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Emerging targets of α-synuclein spreading in α-synucleinopathies: a review of mechanistic pathways and interventions.Molecular neurodegeneration · 2025Review
- Scanning ion conductance microscopy reveals differential effect of PMAnalytical and bioanalytical chemistry · 2023Article
- Observation of α-Synuclein Preformed Fibrils Interacting with SH-SY5Y Neuroblastoma Cell Membranes Using Scanning Ion Conductance Microscopy.ACS chemical neuroscience · 2022Article
- Article
- Scanning Ion Conductance Microscopy.Chemical reviews · 2021Review
- Scanning Ion Conductance Microscopy Study Reveals the Disruption of the Integrity of the Human Cell Membrane Structure by Oxidative DNA Damage.ACS applied bio materials · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Aggregation of the natively unfolded protein α-synuclein (α-Syn) has been widely correlated to the neuronal death associated with Parkinson's disease. Mutations and protein overaccumulation can promote the aggregation of α-Syn into oligomers and fibrils. Recent work has suggested that α-Syn oligomers can permeabilize the neuronal membrane, promoting calcium influx and cell death. However, the mechanism of this permeabilization is still uncertain and has yet to be characterized in live cells. This work uses scanning ion conductance microscopy (SICM) to image, in real time and without using chemical probes, the topographies of live SH-SY5Y neuroblastoma cells after exposure to α-Syn oligomers. Substantial morphological changes were observed, with micrometer-scale hills and troughs observed at lower α-Syn concentrations (1.00 μM) and large, transient pores observed at higher α-Syn concentrations (6.0 μM). These findings suggest that α-Syn oligomers may permeabilize the neuronal membrane by destabilizing the lipid bilayer and opening transient pores.
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Registered trials
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