ArticleBiophysical journal2012
Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formation.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.
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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
147 citing papers in PubMed, 358 citations in OpenAlex.
- Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026Review
- Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- Effect of Tau Fragment and Membrane Interactions on Membrane Permeabilization and Peptide Aggregation.Membranes · 2025Article
- Serotonergic Regulation in Alzheimer's Disease.International journal of molecular sciences · 2025Review
- Quantitative Analysis of the Influence of Trehalose on Amyloid-β Binding to Membranes by Localized Surface Plasmon Resonance Spectroscopy.ACS omega · 2025Article
- Plant-Based Inhibitors of Protein Aggregation.Biomolecules · 2025Review
- Amyloid beta (Aβ) fibrillation kinetics and its impact on membrane polarity.Journal of bioenergetics and biomembranes · 2025Article
- Modulation of Lipid Dynamics in the β-Amyloid Aggregates Induced Membrane Fragmentation.The journal of physical chemistry. B · 2024Article
- LL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases.Biomolecules · 2024Review
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Delineating the Role of GxxxG Motif in Amyloidogenesis: A New Perspective in Targeting Amyloid-Beta Mediated AD Pathogenesis.ACS bio & med chem Au · 2024Review
- Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles.Physical chemistry chemical physics : PCCP · 2024Article
- Possible Role of Fibrinaloid Microclots in Postural Orthostatic Tachycardia Syndrome (POTS): Focus on Long COVID.Journal of personalized medicine · 2024Article
- Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction-the trigger for PANoptosis in neurons.Frontiers in aging neuroscience · 2024Review
- Changes in hippocampal volume, synaptic plasticity and amylin sensitivity in an animal model of type 2 diabetes are associated with increased vulnerability to amyloid-beta in advancing age.Frontiers in aging neuroscience · 2024Article
- A β-barrel-like tetramer formed by a β-hairpin derived from Aβ.Chemical science · 2023Article
- Extracellular high molecular weight α-synuclein oligomers induce cell death by disrupting the plasma membrane.NPJ Parkinson's disease · 2023Article
- Lipid rafts and human diseases: why we need to target gangliosides.FEBS open bio · 2023Review
- Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers.Biophysical chemistry · 2023Article
87 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Disruption of cell membranes by Aβ is believed to be one of the key components of Aβ toxicity. However, the mechanism by which this occurs is not fully understood. Here, we demonstrate that membrane disruption by Aβ occurs by a two-step process, with the initial formation of ion-selective pores followed by nonspecific fragmentation of the lipid membrane during amyloid fiber formation. Immediately after the addition of freshly dissolved Aβ(1-40), defects form on the membrane that share many of the properties of Aβ channels originally reported from single-channel electrical recording, such as cation selectivity and the ability to be blockaded by zinc. By contrast, subsequent amyloid fiber formation on the surface of the membrane fragments the membrane in a way that is not cation selective and cannot be stopped by zinc ions. Moreover, we observed that the presence of ganglioside enhances both the initial pore formation and the fiber-dependent membrane fragmentation process. Whereas pore formation by freshly dissolved Aβ(1-40) is weakly observed in the absence of gangliosides, fiber-dependent membrane fragmentation can only be observed in their presence. These results provide insights into the toxicity of Aβ and may aid in the design of specific compounds to alleviate the neurodegeneration of Alzheimer's disease.
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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.