ArticleFrontiers in chemistry2020
Reproducibility Problems of Amyloid-β Self-Assembly and How to Deal With Them.
Article in Frontiers in chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed.
- SEC Purified Monomeric Aβ42 Produces Reproducible and Reliable Aggregation Measurements.bioRxiv : the preprint server for biology · 2026Article
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Secondary Nucleation of Aβ Revealed by Single-Molecule and Computational Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Hybrid Nanoparticle-Hydrogel Systems for Drug Delivery Depots and Other Biomedical Applications.ACS nano · 2024Review
- APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-βAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Differential Effects of Lipid Bilayers on αPSM Peptide Functional Amyloid Formation.International journal of molecular sciences · 2023Article
- Oxidative Damages on the Alzheimer's Related-Aβ Peptide Alters Its Ability to Assemble.Antioxidants (Basel, Switzerland) · 2023Article
- Simple, Reliable Protocol for High-Yield Solubilization of Seedless Amyloid-β Monomer.ACS chemical neuroscience · 2023Article
- Review
- Nanoscale Infrared Spectroscopy Identifies Structural Heterogeneity in Individual Amyloid Fibrils and Prefibrillar Aggregates.The journal of physical chemistry. B · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The self-assembly of peptides and proteins into amyloid fibrils and other aggregates are linked to several diseases. One of the most studied cases is the peptide amyloid-β (Aβ), found self-assembled in Alzheimer's disease patients' brains. In test tubes, assays with chemically synthesized or recombinant Aβ are widely investigated to understand the aggregation process and to find modulators, which could be of therapeutic interest. Experience over more than a decade in our laboratory through discussions with colleagues, expertly studying the literature, and as reviewers revealed to us the widely encountered difficulty to control the aggregation and obtain reproducible results in the test tube. However, this issue is scarcely reported and discussed in the publications, which we think hampers strongly the progress in this field and can deceive newcomers. Here, we describe the difficulty and potential reasons to obtain reproducible aggregation data and propose some guidelines for working with it.
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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.