ArticleScientific reports2014
Effects of several quinones on insulin aggregation.
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 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 147 citations in OpenAlex.
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- Searching potential GSK-3β inhibitors from marine sources using atomistic simulations.Molecular diversity · 2026Article
- High-Throughput Screening of Amyloid Inhibitors via Covalent-Labeling Mass Spectrometry.Analytical chemistry · 2025Article
- Insights into the Sources, Structure, and Action Mechanisms of Quinones on Diabetes: A Review.Molecules (Basel, Switzerland) · 2025Review
- Examining the role of antioxidant supplementation in mitigating oxidative stress markers in Alzheimer's disease: a comprehensive review.Inflammopharmacology · 2025Review
- Genetic, phytochemical and morphological identification and genetic diversity of selected Moringa species.Scientific reports · 2024Article
- β-synuclein regulates the phase transitions and amyloid conversion of α-synuclein.Nature communications · 2024Article
- Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions.International journal of molecular sciences · 2024Article
- Synthesis of a highly thermostable insulin by phenylalanine conjugation at B29 Lysine.Communications chemistry · 2024Article
- Clues to the Design of Aggregation-Resistant Insulin from Proline Scanning of Highly Amyloidogenic Peptides Derived from the N-Terminal Segment of the A-Chain.Molecular pharmaceutics · 2024Article
- Treatment Effects of Natural Products on Inflammatory Bowel Disease In Vivo and Their Mechanisms: Based on Animal Experiments.Nutrients · 2023Review
- Amyloid Disassembly: What Can We Learn from Chaperones?Biomedicines · 2022Review
- Catechol-containing compounds are a broad class of protein aggregation inhibitors: Redox state is a key determinant of the inhibitory activities.Pharmacological research · 2022Article
- Article
- Molecular Aspects of Insulin Aggregation and Various Therapeutic Interventions.ACS bio & med chem Au · 2022Review
- Antioxidants in Alzheimer's Disease: Current Therapeutic Significance and Future Prospects.Biology · 2022Review
- UV Resonance Raman explores protein structural modification upon fibrillation and ligand interaction.Biophysical journal · 2021Article
- Marine derivatives preventRoyal Society open science · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding and aggregation are associated with more than twenty diseases, such as neurodegenerative diseases and metabolic diseases. The amyloid oligomers and fibrils may induce cell membrane disruption and lead to cell apoptosis. A great number of studies have focused on discovery of amyloid inhibitors which may prevent or treat amyloidosis diseases. Polyphenols have been extensively studied as a class of amyloid inhibitors, with several polyphenols under clinical trials as anti-neurodegenerative drugs. As oxidative intermediates of natural polyphenols, quinones widely exist in medicinal plants or food. In this study, we used insulin as an amyloid model to test the anti-amyloid effects of four simple quinones and four natural anthraquinone derivatives from rhubarb, a traditional herbal medicine used for treating Alzheimer's disease. Our results demonstrated that all eight quinones show inhibitory effects to different extent on insulin oligomerization, especially for 1,4-benzoquinone and 1,4-naphthoquinone. Significantly attenuated oligomerization, reduced amount of amyloid fibrils and reduced hemolysis levels were found after quinones treatments, indicating quinones may inhibit insulin from forming toxic oligomeric species. The results suggest a potential action of native anthraquinone derivatives in preventing protein misfolding diseases, the quinone skeleton may thus be further explored for designing effective anti-amyloidosis compounds.
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