ArticleBiochemistry2018
Retinol-Binding Protein Interferes with Transthyretin-Mediated β-Amyloid Aggregation Inhibition.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Levels and instability of transthyretin and correlations with core biomarkers in Alzheimer's disease.Scientific reports · 2026Article
- Transthyretin as a therapeutic target: the future of disease-modifying therapies for Alzheimer's disease.Molecular biology reports · 2025Review
- From Molecular to Radionuclide and Pharmacological Aspects in Transthyretin Cardiac Amyloidosis.International journal of molecular sciences · 2024Review
- Circulating adipokines and MRI markers of brain aging in middle-aged adults from the community.Journal of Alzheimer's disease : JAD · 2024Article
- Association of Dietary Retinol Intake and Serum Neurofilament Light Chain Levels: Results from NHANES 2013-2014.Nutrients · 2024Article
- New Hybrid Compounds Incorporating Natural Products as Multifunctional Agents against Alzheimer's Disease.Pharmaceutics · 2023Article
- Serum transthyretin and risk of cognitive decline and dementia: 22-year longitudinal study.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2021Article
- Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
β-Amyloid (Aβ) aggregation is causally linked to Alzheimer's disease. On the basis of in vitro and transgenic animal studies, transthyretin (TTR) is hypothesized to provide neuroprotection against Aβ toxicity by binding to Aβ and inhibiting its aggregation. TTR is a homotetrameric protein that circulates in blood and cerebrospinal fluid; its normal physiological role is as a carrier for thyroxine and retinol-binding protein (RBP). RBP forms a complex with retinol, and the holoprotein (hRBP) binds with high affinity to TTR. In this study, the role of TTR ligands in TTR-mediated inhibition of Aβ aggregation was investigated. hRBP strongly reduced the ability of TTR to inhibit Aβ aggregation. The effect was not due to competition between Aβ and hRBP for binding to TTR, as Aβ bound equally well to TTR-hRBP complexes and TTR. hRBP is known to stabilize the TTR tetrameric structure. We show that Aβ partially destabilizes TTR and that hRBP counteracts this destabilization. Taken together, our results support a mechanism wherein TTR-mediated inhibition of Aβ aggregation requires not only TTR-Aβ binding but also destabilization of TTR quaternary structure.
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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.