ArticleScientific reports2014
Ultrafast propagation of β-amyloid fibrils in oligomeric cloud.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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
12 citing papers in PubMed.
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- QuICSeedR: an R package for analyzing fluorophore-assisted seed amplification assay data.Bioinformatics (Oxford, England) · 2024Article
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Modulating Nanodroplet Formation En Route to Fibrillization of Amyloid Peptides with Designed Flanking Sequences.Biomacromolecules · 2022Article
- Practical Use of Quartz Crystal Microbalance Monitoring in Cartilage Tissue Engineering.Journal of functional biomaterials · 2022Review
- Direct observation of heterogeneous formation of amyloid spherulites in real-time by super-resolution microscopy.Communications biology · 2022Article
- Single-molecule fluorescence imaging and deep learning reveal highly heterogeneous aggregation of amyloid-β 42.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Application of QCM in Peptide and Protein-Based Drug Product Development.Molecules (Basel, Switzerland) · 2020Review
- Growth-incompetent monomers of human calcitonin lead to a noncanonical direct relationship between peptide concentration and aggregation lag time.The Journal of biological chemistry · 2017Article
- Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry.Scientific reports · 2017Article
- A glass menagerie of low complexity sequences.Current opinion in structural biology · 2016Review
- Measurement of amyloid formation by turbidity assay-seeing through the cloud.Biophysical reviews · 2016Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interaction between monomer peptides and seeds is essential for clarifying the fibrillation mechanism of amyloid β (Aβ) peptides. We monitored the deposition reaction of Aβ(1-40) peptides on immobilized seeds grown from Aβ(1-42), which caused formation of oligomers in the early stage. The deposition reaction and fibrillation procedure were monitored throughout by novel total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM) system. This system allows simultaneous evaluation of the amount of deposited peptides on the surface seeds by QCM and fibril nucleation and elongation by TIRFM. Most fibrils reached other nuclei, forming the fibril network across the nucleus hubs in a short time. We found a fibril-elongation rate two-orders-of-magnitude higher in an oligomeric cloud than reported values, indicating ultrafast transition of oligomers into fibrils.
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Registered trials
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