ArticleInternational journal of Alzheimer's disease2011
Membrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.
Article in International journal of Alzheimer's disease, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 80 citations in OpenAlex.
- Efficient removal of Ni, Al, and As from water using Micrococcus yunnanensis: batch experiments and explainable machine learning.Biodegradation · 2026Article
- Azilsartan prevents central modulation of BDNF and PPARγ in Alzheimer's pathology through amyloidogenic and inflammatory pathways: experimental and computational evidence.Inflammopharmacology · 2026Article
- Cellular and molecular outcomes of Pseudomonas putida KT2440 exposure to aluminium.Folia microbiologica · 2025Article
- Extracellular vesicles from hiPSC-derived NSCs protect human neurons against Aβ-42 oligomers induced neurodegeneration, mitochondrial dysfunction and tau phosphorylation.Stem cell research & therapy · 2025Article
- Lipid rafts and human diseases: why we need to target gangliosides.FEBS open bio · 2023Review
- Review
- A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents.ACS chemical neuroscience · 2022Article
- Structural and mechanistic insights into amyloid-β and α-synuclein fibril formation and polyphenol inhibitor efficacy in phospholipid bilayers.The FEBS journal · 2022Article
- Reversing Aβ Fibrillation and Inhibiting Aβ Primary Neuronal Cell Toxicity Using Amphiphilic Polyphenylene Dendrons.Advanced healthcare materials · 2022Article
- Mind the Gap: Mitochondria and the Endoplasmic Reticulum in Neurodegenerative Diseases.Biomedicines · 2021Review
- Neurometals in the Pathogenesis of Prion Diseases.International journal of molecular sciences · 2021Review
- Prediction of Transmembrane Regions, Cholesterol, and Ganglioside Binding Sites in Amyloid-Forming Proteins Indicate Potential for Amyloid Pore Formation.Frontiers in molecular neuroscience · 2021Article
- Quantifying the dose-dependent impact of intracellular amyloid beta in a mathematical model of calcium regulation in xenopus oocyte.PloS one · 2021Article
- Catechol-Type Flavonoids from the Branches ofMolecules (Basel, Switzerland) · 2020Article
- Amyloids: Regulators of Metal Homeostasis in the Synapse.Molecules (Basel, Switzerland) · 2020Review
- Review of Current Strategies for Delivering Alzheimer's Disease Drugs across the Blood-Brain Barrier.International journal of molecular sciences · 2019Review
- Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation.International journal of molecular sciences · 2018Review
- A novel dynamic multicellular co-culture system for studying individual blood-brain barrier cell types in brain diseases and cytotoxicity testing.Scientific reports · 2018Article
- Zinc, Carnosine, and Neurodegenerative Diseases.Nutrients · 2018Review
- Amyloid β-42 induces neuronal apoptosis by targeting mitochondria.Molecular medicine reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligomerization, conformational changes, and the consequent neurodegeneration of Alzheimer's β-amyloid protein (AβP) play crucial roles in the pathogenesis of Alzheimer's disease (AD). Mounting evidence suggests that oligomeric AβPs cause the disruption of calcium homeostasis, eventually leading to neuronal death. We have demonstrated that oligomeric AβPs directly incorporate into neuronal membranes, form cation-sensitive ion channels ("amyloid channels"), and cause the disruption of calcium homeostasis via the amyloid channels. Other disease-related amyloidogenic proteins, such as prion protein in prion diseases or α-synuclein in dementia with Lewy bodies, exhibit similarities in the incorporation into membranes and the formation of calcium-permeable channels. Here, based on our experimental results and those of numerous other studies, we review the current understanding of the direct binding of AβP into membrane surfaces and the formation of calcium-permeable channels. The implication of composition of membrane lipids and the possible development of new drugs by influencing membrane properties and attenuating amyloid channels for the treatment and prevention of AD is also discussed.
Identifiers
What OpenQuestion holds
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.