ArticleBiochemistry2010
Characterization of the interaction of β-amyloid with transthyretin monomers and tetramers.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 85 citations in OpenAlex.
- Levels and instability of transthyretin and correlations with core biomarkers in Alzheimer's disease.Scientific reports · 2026Article
- βProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- The antibody-peptide fusion protein, AT-02, is an effective opsonin with pan-amyloid reactivity.npj drug discovery · 2025Article
- Transthyretin as a therapeutic target: the future of disease-modifying therapies for Alzheimer's disease.Molecular biology reports · 2025Review
- Tetrameric Transthyretin as a Protective Factor Against Alzheimer's Disease.Molecular neurobiology · 2025Review
- Cationic Surface Charge Engineering of Recombinant Transthyretin Remarkably Increases the Inhibitory Potency Against Amyloid β-Protein Fibrillogenesis.Molecules (Basel, Switzerland) · 2024Article
- Pathology of Amyloid-β (Aβ) Peptide Peripheral Clearance in Alzheimer's Disease.International journal of molecular sciences · 2024Review
- A three-dimensional valve-on-chip microphysiological system implicates cell cycle progression, cholesterol metabolism and protein homeostasis in early calcific aortic valve disease progression.Acta biomaterialia · 2024Article
- Approaches for Increasing Cerebral Efflux of Amyloid-β in Experimental Systems.Journal of Alzheimer's disease : JAD · 2024Review
- New Hybrid Compounds Incorporating Natural Products as Multifunctional Agents against Alzheimer's Disease.Pharmaceutics · 2023Article
- The Role of Traditional Chinese Medicine Natural Products in β-Amyloid Deposition and Tau Protein Hyperphosphorylation in Alzheimer's Disease.Drug design, development and therapy · 2023Review
- Amyloid Disassembly: What Can We Learn from Chaperones?Biomedicines · 2022Review
- Endogenous Human Proteins Interfering with Amyloid Formation.Biomolecules · 2022Review
- The potential neuroprotective effect of allicin and melatonin in acrylamide-induced brain damage in rats.Environmental science and pollution research international · 2021Article
- Neuroprotection in early stages of Alzheimer's disease is promoted by transthyretin angiogenic properties.Alzheimer's research & therapy · 2021Article
- Interaction of amyloid beta with humanin and acetylcholinesterase is modulated by ATP.FEBS open bio · 2020Article
- The Function of Transthyretin Complexes with Metallothionein in Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Transthyretin Stabilization: An Emerging Strategy for the Treatment of Alzheimer's Disease?International journal of molecular sciences · 2020Review
- Epigenetic profiling of Italian patients identified methylation sites associated with hereditary transthyretin amyloidosis.Clinical epigenetics · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
β-Amyloid (Aβ) is the main protein component of the amyloid plaques associated with Alzheimer's disease. Transthyretin (TTR) is a homotetramer that circulates in both blood and cerebrospinal fluid. Wild-type (wt) TTR amyloid deposits are linked to senile systemic amyloidosis, a common disease of aging, while several TTR mutants are linked to familial amyloid polyneuropathy. Several recent studies provide support for the hypothesis that these two amyloidogenic proteins interact, and that this interaction is biologically relevant. For example, upregulation of TTR expression in Tg2576 mice was linked to protection from the toxic effects of Aβ deposition [Stein, T. D., and Johnson, J. A. (2002) J. Neurosci. 22, 7380-7388]. We examined the interaction of Aβ with wt TTR as well as two mutants: F87M/L110M, engineered to be a stable monomer, and T119M, a naturally occurring mutant with a tetrameric stability higher than that of the wild type. On the basis of enzyme-linked immunoassays as well as cross-linking experiments, we conclude that Aβ monomers bind more to TTR monomers than to TTR tetramers. The data further suggest that TTR tetramers interact preferably with Aβ aggregates rather than Aβ monomers. Through tandem mass spectrometry analysis of cross-linked TTR-Aβ fragments, we identified the A strand, in the inner β-sheet of TTR, as well as the EF helix, as regions of TTR that are involved with Aβ association. Light scattering and electron microscopy studies demonstrate that the outcome of the TTR-Aβ interaction strongly depends on TTR quaternary structure. While TTR tetramers may modestly enhance aggregation, TTR monomers decidedly arrest Aβ aggregate growth. These data provide important new insights into the nature of TTR-Aβ interactions. Such interactions may regulate TTR-mediated protection against Aβ toxicity.
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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.