ArticleeLife2020
Structural rearrangement of amyloid-β upon inhibitor binding suppresses formation of Alzheimer's disease related oligomers.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 31 citations in OpenAlex.
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Analysis of amyloid beta oligomers by cyclic ion mobility-mass spectrometry.Analytical and bioanalytical chemistry · 2026Article
- N-Terminal Protein Binding and Disorder-to-Order Transition by a Synthetic Receptor.Biochemistry · 2025Article
- Highly prevalent geriatric medications and their effect on β-amyloid fibril formation.BMC neurology · 2024Article
- Advances in mass spectrometry to unravel the structure and function of protein condensates.Nature protocols · 2023Review
- Disrupting Dimeric β-Amyloid by Electric Fields.ACS physical chemistry Au · 2023Article
- A novel peptide derived from vascular endothelial growth factor prevents amyloid beta aggregation and toxicity.Aging cell · 2023Article
- A Hairpin Motif in the Amyloid-β Peptide Is Important for Formation of Disease-Related Oligomers.Journal of the American Chemical Society · 2023Article
- Mass spectrometric insights into protein aggregation.Essays in biochemistry · 2023Review
- A Novel Strategy for Alzheimer's Disease Based on the Regulatory Effect of Amyloid-β on Gut Flora.Journal of Alzheimer's disease : JAD · 2023Review
- A Small Molecule Stabilizes the Disordered Native State of the Alzheimer's Aβ Peptide.ACS chemical neuroscience · 2022Article
- Cell-Penetrating Peptides with Unexpected Anti-Amyloid Properties.Pharmaceutics · 2022Review
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Using mass spectrometry-based methods to understand amyloid formation and inhibition of alpha-synuclein and amyloid beta.Mass spectrometry reviewsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The formation of oligomers of the amyloid-β peptide plays a key role in the onset of Alzheimer's disease. We describe herein the investigation of disease-relevant small amyloid-β oligomers by mass spectrometry and ion mobility spectrometry, revealing functionally relevant structural attributes. In particular, we can show that amyloid-β oligomers develop in two distinct arrangements leading to either neurotoxic oligomers and fibrils or non-toxic amorphous aggregates. Comprehending the key-attributes responsible for those pathways on a molecular level is a pre-requisite to specifically target the peptide's tertiary structure with the aim to promote the emergence of non-toxic aggregates. Here, we show for two fibril inhibiting ligands, an ionic molecular tweezer and a hydrophobic peptide that despite their different interaction mechanisms, the suppression of the fibril pathway can be deduced from the disappearance of the corresponding structure of the first amyloid-β oligomers.
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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.