ArticleProteins2010
Models of membrane-bound Alzheimer's Abeta peptide assemblies.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 71 citations in OpenAlex.
- The concentric β-barrel hypothesis for amyloids: Models of soluble and transmembrane amyloid-β42 oligomers and channels composed of identical subunits and GM1 gangliosides.bioRxiv : the preprint server for biology · 2026Article
- The structure of tyrosine-10 favors ionic conductance of Alzheimer's disease-associated full-length amyloid-β channels.Nature communications · 2024Article
- The amyloid concentric β-barrel hypothesis: Models of amyloid beta 42 oligomers and annular protofibrils.Proteins · 2022Article
- Article
- An Alzheimer's Disease Mechanism Based on Early Pathology, Anatomy, Vascular-Induced Flow, and Migration of Maximum Flow Stress Energy Location with Increasing Vascular Disease.Journal of Alzheimer's disease : JAD · 2022Article
- Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer's Disease Development.Molecules (Basel, Switzerland) · 2021Review
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Shear-Induced Amyloid Aggregation in the Brain: V. Are Alzheimer's and Other Amyloid Diseases Initiated in the Lower Brain and Brainstem by Cerebrospinal Fluid Flow Stresses?Journal of Alzheimer's disease : JAD · 2021Article
- Progress toward Alzheimer's disease treatment: Leveraging the Achilles' heel of Aβ oligomers?Protein science : a publication of the Protein Society · 2020Review
- The Interaction between Amyloid Prefibrillar Oligomers of Salmon Calcitonin and a Lipid-Raft Model: Molecular Mechanisms Leading to Membrane Damage, CaBiomolecules · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Calcitonin native prefibrillar oligomers but not monomers induce membrane damage that triggers NMDA-mediated CaScientific reports · 2019Article
- Concentration-dependent effects of mercury and lead on Aβ42: possible implications for Alzheimer's disease.European biophysics journal : EBJ · 2019Article
- Structure of amyloid βScientific reports · 2019Article
- Alzheimer's amyloid-beta intermediates generated using polymer-nanodiscs.Chemical communications (Cambridge, England) · 2018Article
- Modulation of Alzheimer's amyloid β peptide oligomerization and toxicity by extracellular Hsp70.Cell stress & chaperones · 2018Article
- Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Biophysical reviews · 2017Review
- Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein.Scientific reports · 2016Article
- Comparative modeling of hypothetical amyloid pores based on cylindrin.Journal of molecular modeling · 2015Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Although it is clear that amyloid beta (Aβ) peptides play a pivotal role in the development of Alzheimer's disease, the precise molecular model of action remains unclear. Aβ peptide forms assemble both in aqueous solution and in lipid membranes. It has been proposed that deleterious effects occur when the peptides interact with membranes, possibly by forming Ca(2+) permeant ion channels. In the accompanying manuscript, we propose models in which the C-terminus third of six Aβ42 peptides forms a six-stranded β-barrel in highly toxic soluble oligomers. Here we extend this hypothesis to membrane-bound assemblies. In these Aβ models, the hydrophobic β-barrel of a hexamer may either reside on the surface of the bilayer, or span the bilayer. Transmembrane pores are proposed to form between several hexamers. Once the β-barrels of six hexamers have spanned the bilayer, they may merge to form a more stable 36-stranded β-barrel. We favor models in which parallel β-barrels formed by N-terminus segments comprise the lining of the pores. These types of models explain why the channels are selective for cations and how metal ions, such as Zn(2+) , synthetic peptides that contain histidines, and some small organic cations may block channels or inhibit formation of channels. Our models were developed to be consistent with microscopy studies of Aβ assemblies in membranes, one of which is presented here for the first time.
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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.