ReviewPhysical chemistry chemical physics : PCCP2013
Alzheimer's disease: which type of amyloid-preventing drug agents to employ?
Review in Physical chemistry chemical physics : PCCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed.
- Amyloid β 1-42 Can Form Ion Channels as Small as Gramicidin in Model Lipid Membranes.Membranes · 2025Article
- Ras, RhoA, and vascular pharmacology in neurodevelopment and aging.Neurochemistry international · 2024Review
- Lipid rafts and human diseases: why we need to target gangliosides.FEBS open bio · 2023Review
- AmyP53, a Therapeutic Peptide Candidate for the Treatment of Alzheimer's and Parkinson's Disease: Safety, Stability, Pharmacokinetics Parameters and Nose-to Brain Delivery.International journal of molecular sciences · 2022Article
- Patients with Alzheimer's disease have an increased removal rate of soluble beta-amyloid-42.PloS one · 2022Article
- Gene Therapy Strategy for Alzheimer's and Parkinson's Diseases Aimed at Preventing the Formation of Neurotoxic Oligomers in SH-SY5Y Cells.International journal of molecular sciences · 2021Article
- Membrane-dependent amyloid aggregation of human BAX α9 (173-192).Protein science : a publication of the Protein Society · 2021Article
- Progress toward Alzheimer's disease treatment: Leveraging the Achilles' heel of Aβ oligomers?Protein science : a publication of the Protein Society · 2020Review
- Article
- Anthoxanthin Polyphenols Attenuate Aβ Oligomer-induced Neuronal Responses Associated with Alzheimer's Disease.CNS neuroscience & therapeutics · 2017Article
- Small molecule NPT-440-1 inhibits ionic flux through AβNanomedicine : nanotechnology, biology, and medicine · 2016Article
- Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein.Scientific reports · 2016Article
- Amyloid-β peptides in interaction with raft-mime model membranes: a neutron reflectivity insight.Scientific reports · 2016Article
- Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Coupling of Zinc-Binding and Secondary Structure in Nonfibrillar Aβ40 Peptide Oligomerization.Journal of chemical information and modeling · 2015Article
- Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.Acta neuropathologica · 2015Review
- Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Chemical Society reviews · 2014Review
- Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Chemical Society reviews · 2014Review
- Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Biochemistry · 2014Article
- Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) pores.The journal of physical chemistry. B · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The current paradigm in the amyloid hypothesis brands small β-amyloid (Aβ) oligomers as the toxic species in Alzheimer's disease (AD). These oligomers are fibril-like; contain β-sheet structure, and present exposed hydrophobic surface. Oligomers with this motif are capable of penetrating the cell membrane, gathering to form toxic ion channels. Current agents suppressing precursor Aβ cleavage have only met partial success; and to date, those targeting the peptides and their assemblies in the aqueous environment of the extracellular space largely fail in clinical trials. One possible reason is failure to reach membrane-embedded targets of disease-'infected' cells. Here we provide an overview, point to the need to account for the lipid environment when aiming to prevent the formation of toxic channels, and propose a combination therapy to target the species spectrum.
Indexed as
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.