ArticleInternational journal of molecular sciences2022
A Palette of Fluorescent A
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 14 citations in OpenAlex.
- Selective Reversal of Cu-Amyloid Aggregation Monitored in Real Time by Fluorescence Anisotropy: Ni-Bme-Dach vs EDTA Benchmarks.ACS omega · 2026Article
- Lipid-induced condensate formation from the Alzheimer's Aβ peptide triggers amyloid aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Design of amyloidogenic peptide traps.Nature chemical biology · 2024Article
- The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.ACS chemical neuroscience · 2024Article
- Ganglioside Micelles Affect Amyloid β Aggregation by Coassembly.ACS chemical neuroscience · 2023Article
- Direct observation of secondary nucleation along the fibril surface of the amyloidProceedings of the National Academy of Sciences of the United States of America · 2023Article
- An aggregation inhibitor specific to oligomeric intermediates of Aβ42 derived from phage display libraries of stable, small proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Fluorescence-based single molecule techniques provide important tools towards understanding the molecular mechanism of complex neurodegenerative diseases. This requires efficient covalent attachment of fluorophores. Here we create a series of cysteine mutants (S8C, Y10C, S26C, V40C, and A42C) of Aβ42, involved in Alzheimer's disease, based on exposed positions in the fibril structure and label them with the Alexa-fluorophores using maleimide chemistry. Direct stochastic optical reconstruction microscopy imaging shows that all the labelled mutants form fibrils that can be detected by virtue of Alexa fluorescence. Aggregation assays and cryo-electron micrographs establish that the careful choice of labelling position minimizes the perturbation of the aggregation process and fibril structure. Peptides labelled at the N-terminal region, S8C and Y10C, form fibrils independently and with wild-type. Peptides labelled at the fibril core surface, S26C, V40C and A42C, form fibrils only in mixture with wild-type peptide. This can be understood on the basis of a recent fibril model, in which S26, V40 and A42 are surface exposed in two out of four monomers per fibril plane. We provide a palette of fluorescently labelled Aβ42 peptides that can be used to gain understanding of the complex mechanisms of Aβ42 self-assembly and help to develop a more targeted approach to cure the disease.
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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.