ArticleChemphyschem : a European journal of chemical physics and physical chemistry2017
Direct Visualization of Model Membrane Remodeling by α-Synuclein Fibrillization.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 19 citations in OpenAlex.
- Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces.Nature communications · 2023Article
- Methods to mechanically perturb and characterize GUV-based minimal cell models.Computational and structural biotechnology journal · 2023Review
- Neurons and Glia Interplay in α-Synucleinopathies.International journal of molecular sciences · 2021Review
- Physical mechanisms of amyloid nucleation on fluid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Preparation of Monodisperse Giant Unilamellar Anchored Vesicles Using Micropatterned Hydrogel Substrates.ACS omega · 2019Article
- Direct Visualization of Model Membrane Remodeling by α-Synuclein Fibrillization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of α-synuclein (αS) with membranes is thought to be critical in the etiology of Parkinson's disease. Besides oligomeric αS aggregates that possibly form membrane pores, the aggregation of αS into amyloid fibrils has been reported to disrupt membranes. The mechanism by which aggregation affects the integrity of membranes is, however, unknown. Here, we show that whereas mature αS fibrils only weakly adhere to POPC/POPG giant unilamellar vesicles (GUVs), fibrillization of αS on the membrane results in large-scale membrane remodeling. Fibrils that grow on the vesicle surface stiffen the membrane and make the initially spherical membrane become polyhedral. Additionally, membrane-attached fibrils extract lipids. The lipid extraction and membrane remodeling of growing fibrils can consume the complete bilayer surface and results in loss of vesicle content. These observations suggest that there are several mechanisms by which growing fibrils can disrupt membrane function.
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Registered trials
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.