ArticleThe Journal of biological chemistry2015
Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their Metabolites.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- Machine Learning-Based Prediction of Transthyretin-Binding Activity and Its Application to Screening Food-Derived Compounds for ATTR Amyloidosis.Pharmaceuticals (Basel, Switzerland) · 2026Article
- A Preliminary Analysis of the Influence of Elderberry Juice Consumption on Thyroid Metabolism in Mice and Humans Fed High-Fat Diets.Nutrients · 2025Article
- Optimization of the Search for Neuroprotectors among Bioflavonoids.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Review
- Inhibitors of Transthyretin Amyloidosis: How to Rank Drug Candidates Using X-ray Crystallography Data.Molecules (Basel, Switzerland) · 2024Article
- 3-O-Methyltolcapone and Its Lipophilic Analogues Are Potent Inhibitors of Transthyretin Amyloidogenesis with High Permeability and Low Toxicity.International journal of molecular sciences · 2023Article
- Gut microbial metabolites of dietary polyphenols and their potential role in human health and diseases.Journal of physiology and biochemistry · 2023Review
- Transthyretin Binding Mode Dichotomy of FluorescentACS chemical neuroscience · 2023Article
- Mechanistic Insights of Polyphenolic Compounds from Rosemary Bound to Their Protein Targets Obtained by Molecular Dynamics Simulations and Free-Energy Calculations.Foods (Basel, Switzerland) · 2023Article
- Anticancer Therapeutic Strategies Targeting p53 Aggregation.International journal of molecular sciences · 2022Review
- The Transthyretin/Oleuropein Aglycone Complex: A New Tool against TTR Amyloidosis.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Chemo-Preventive Action of Resveratrol: Suppression of p53-A Molecular Targeting Approach.Molecules (Basel, Switzerland) · 2021Review
- Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021Review
- Natural compounds as inhibitors of transthyretin amyloidosis and neuroprotective agents: analysis of structural data for future drug design.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Structural Stabilization of Human Transthyretin byBiomolecules · 2019Article
- Uncovering the Neuroprotective Mechanisms of Curcumin on Transthyretin Amyloidosis.International journal of molecular sciences · 2019Review
- Inhibition of protein misfolding and aggregation by natural phenolic compounds.Cellular and molecular life sciences : CMLS · 2018Review
- Resveratrol prevents p53 aggregationOncotarget · 2018Article
- Polypharmacology or Promiscuity? Structural Interactions of Resveratrol With Its Bandwagon of Targets.Frontiers in pharmacology · 2018Review
- Cancer Chemoprevention by Resveratrol: The p53 Tumor Suppressor Protein as a Promising Molecular Target.Molecules (Basel, Switzerland) · 2017Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transthyretin (TTR) is an amyloidogenic protein, the amyloidogenic potential of which is enhanced by a number of specific point mutations. The ability to inhibit TTR fibrillogenesis is known for several classes of compounds, including natural polyphenols, which protect the native state of TTR by specifically interacting with its thyroxine binding sites. Comparative analyses of the interaction and of the ability to protect the TTR native state for polyphenols, both stilbenoids and flavonoids, and some of their main metabolites have been carried out. A main finding of this investigation was the highly preferential binding of resveratrol and thyroxine, both characterized by negative binding cooperativity, to distinct sites in TTR, consistent with the data of x-ray analysis of TTR in complex with both ligands. Although revealing the ability of the two thyroxine binding sites of TTR to discriminate between different ligands, this feature has allowed us to evaluate the interactions of polyphenols with both resveratrol and thyroxine preferential binding sites, by using resveratrol and radiolabeled T4 as probes. Among flavonoids, genistein and apigenin were able to effectively displace resveratrol from its preferential binding site, whereas genistein also showed the ability to interact, albeit weakly, with the preferential thyroxine binding site. Several glucuronidated polyphenol metabolites did not exhibit significant competition for resveratrol and thyroxine preferential binding sites and lacked the ability to stabilize TTR. However, resveratrol-3-O-sulfate was able to significantly protect the protein native state. A rationale for the in vitro properties found for polyphenol metabolites was provided by x-ray analysis of their complexes with TTR.
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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.