ArticlePeerJ2015
Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives.
Article in PeerJ, 2015. 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
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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
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Who cites it
23 citing papers in PubMed, 51 citations in OpenAlex.
- Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related α-Synuclein.Biomacromolecules · 2025Article
- Development of an efficient expression system for human chaperone BiP in Pichia pastoris: production optimization and functional validation.Microbial cell factories · 2025Article
- Imidazo[2,1-ACS chemical neuroscience · 2024Article
- Prion Seeding Activity in Plant Tissues Detected by RT-QuIC.Pathogens (Basel, Switzerland) · 2024Article
- Formation of amyloid fibrils by the regulatory 14-3-3Open biology · 2024Article
- A Multilevel Study of Eupatorin and Scutellarein as Anti-Amyloid Agents in Alzheimer's Disease.Biomedicines · 2023Article
- The Major Components of Cerebrospinal Fluid Dictate the Characteristics of Inhibitors against Amyloid-Beta Aggregation.International journal of molecular sciences · 2023Article
- Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties.Antioxidants (Basel, Switzerland) · 2022Article
- Exploring the Formation of Polymers with Anti-Amyloid Properties within the 2'3'-Dihydroxyflavone Autoxidation Process.Antioxidants (Basel, Switzerland) · 2022Article
- Article
- Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.International journal of molecular sciences · 2021Article
- S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.International journal of molecular sciences · 2021Article
- Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation.PeerJ · 2021Article
- Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases.Frontiers in neuroscience · 2021Review
- Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics.Biomacromolecules · 2020Article
- Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity.International journal of molecular sciences · 2020Article
- Merging the Multi-Target Effects of Phytochemicals in Neurodegeneration: From Oxidative Stress to Protein Aggregation and Inflammation.Antioxidants (Basel, Switzerland) · 2020Review
- Targeting α-synuclein for PD Therapeutics: A Pursuit on All Fronts.Biomolecules · 2020Review
- Nutraceuticals: An integrative approach to starve Parkinson's disease.Brain, behavior, & immunity - health · 2020Review
- The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG.Biomolecules · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A range of diseases is associated with amyloid fibril formation. Despite different proteins being responsible for each disease, all of them share similar features including beta-sheet-rich secondary structure and fibril-like protein aggregates. A number of proteins can form amyloid-like fibrils in vitro, resembling structural features of disease-related amyloids. Given these generic structural properties of amyloid and amyloid-like fibrils, generic inhibitors of fibril formation would be of interest for treatment of amyloid diseases. Recently, we identified five outstanding inhibitors of insulin amyloid-like fibril formation among the pool of 265 commercially available flavone derivatives. Here we report testing of these five compounds and of epi-gallocatechine-3-gallate (EGCG) on aggregation of alpha-synuclein and beta-amyloid. We used a Thioflavin T (ThT) fluorescence assay, relying on halftimes of aggregation as the measure of inhibition. This method avoids large numbers of false positive results. Our data indicate that four of the five flavones and EGCG inhibit alpha-synuclein aggregation in a concentration-dependent manner. However none of these derivatives were able to increase halftimes of aggregation of beta-amyloid.
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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.