ArticleMembranes2017
Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets.
Article in Membranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 57 citations in OpenAlex.
- Lipid Composition Drives Mutant Huntingtin Dimerization and Membrane Association: Insights from Computational Simulations.Molecules (Basel, Switzerland) · 2026Article
- Concentration Effects in Peptide-Lipid Bilayer Interactions: A Coarse-Grained Molecular Dynamics Study.The journal of physical chemistry. B · 2026Article
- Amyloid β-Cholesterol Interplay: Removal of Cholesterol From the Membranes to Catalyze Aggregation and Amyloid Pathology.Journal of neurochemistry · 2026Article
- Nucleation dynamics in amyloid-beta dimerization revealed by single-molecule fingerprinting.Cell reports. Physical science · 2025Article
- The Amyloid Assembly of the Bacterial Hfq Is Lipid-Driven and Lipid-Specific.International journal of molecular sciences · 2024Article
- Availability of iron ions impacts physicochemical properties and proteome of outer membrane vesicles released by Neisseria gonorrhoeae.Scientific reports · 2023Article
- Lipid-induced polymorphic amyloid fibril formation by α-synuclein.Protein science : a publication of the Protein Society · 2023Article
- Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers.Biophysical chemistry · 2023Article
- Ganglioside-Enriched Phospholipid Vesicles Induce Cooperative Aβ Oligomerization and Membrane Disruption.Biochemistry · 2022Article
- Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation.Molecules (Basel, Switzerland) · 2022Review
- Electrografting a Hybrid Bilayer Membrane via Diazonium Chemistry for Electrochemical Impedance Spectroscopy of Amyloid-β Aggregation.Micromachines · 2022Article
- Semax, a Synthetic Regulatory Peptide, Affects Copper-Induced Abeta Aggregation and Amyloid Formation in Artificial Membrane Models.ACS chemical neuroscience · 2022Article
- Cations Regulate Membrane Attachment and Functionality of DNA Nanostructures.Journal of the American Chemical Society · 2021Article
- Physical mechanisms of amyloid nucleation on fluid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Tert-butyl-(4-hydroxy-3-((3-(2-methylpiperidin-yl)propyl)carbamoyl)phenyl)carbamate Has Moderated Protective Activity in Astrocytes Stimulated with Amyloid Beta 1-42 and in a Scopolamine Model.Molecules (Basel, Switzerland) · 2020Article
- Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.Scientific reports · 2020Article
- The Amphipathic GM1 Molecule Stabilizes Amyloid Aggregates, Preventing their Cytotoxicity.Biophysical journal · 2020Article
- Amyloid B-Protein Aggregation at Physiologically Relevant Concentrations. A Critical Role of Membranes.Alzheimer's research & therapy open access · 2020Article
- Effect of lipid saturation on amyloid-beta peptide partitioning and aggregation in neuronal membranes: molecular dynamics simulations.European biophysics journal : EBJ · 2019Article
- Nanodisc-Forming Scaffold Protein Promoted Retardation of Amyloid-Beta Aggregation.Journal of molecular biology · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid- β aggregates play a causative role in Alzheimer's disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- β peptides to nucleate and form well-ordered cross- β sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- β protein, A β 25 - 35 , with the hydrophobicity, fluidity, and charge density of a lipid bilayer. We summarize recent biophysical studies of model membranes and relate these to the process of aggregation in physiological systems.
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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.