ArticleProtein engineering, design & selection : PEDS2012
Identification of beta-amyloid-binding sites on transthyretin.
Article in Protein engineering, design & selection : PEDS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 68 citations in OpenAlex.
- Unravelling the myriad physiologic roles of transthyretin: critical considerations for treating transthyretin amyloidosis.Annals of medicine · 2025Review
- Article
- New Hybrid Compounds Incorporating Natural Products as Multifunctional Agents against Alzheimer's Disease.Pharmaceutics · 2023Article
- Amyloid Disassembly: What Can We Learn from Chaperones?Biomedicines · 2022Review
- Endogenous Human Proteins Interfering with Amyloid Formation.Biomolecules · 2022Review
- Salivary Proteomics Identifies Transthyretin as a Biomarker of Early Dementia Conversion.Journal of Alzheimer's disease reports · 2022Article
- Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.Science advances · 2021Article
- Extracellular protein components of amyloid plaques and their roles in Alzheimer's disease pathology.Molecular neurodegeneration · 2021Review
- The interaction of zinc with the multi-functional plasma thyroid hormone distributor protein, transthyretin: evolutionary and cross-species comparative aspects.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021Review
- The inhibition of cellular toxicity of amyloid-β by dissociated transthyretin.The Journal of biological chemistry · 2020Article
- The Positive Side of the Alzheimer's Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1.Molecules (Basel, Switzerland) · 2020Review
- Undiscovered Roles for Transthyretin: From a Transporter Protein to a New Therapeutic Target for Alzheimer's Disease.International journal of molecular sciences · 2020Review
- ROSETTA-informed design of structurally stabilized cyclic anti-amyloid peptides.Protein engineering, design & selection : PEDS · 2019Article
- Copper mediated amyloid-β binding to Transthyretin.Scientific reports · 2018Article
- Retinol-Binding Protein Interferes with Transthyretin-Mediated β-Amyloid Aggregation Inhibition.Biochemistry · 2018Article
- Transthyretin Mimetics as Anti-β-Amyloid Agents: A Comparison of Peptide and Protein Approaches.ChemMedChem · 2018Article
- Peptides as Potential Therapeutics for Alzheimer's Disease.Molecules (Basel, Switzerland) · 2018Review
- Role of Prenatal Hypoxia in Brain Development, Cognitive Functions, and Neurodegeneration.Frontiers in neuroscience · 2018Review
- Transthyretin stability is critical in assisting beta amyloid clearance- Relevance of transthyretin stabilization in Alzheimer's disease.CNS neuroscience & therapeutics · 2017Article
- Cerebrospinal Fluid Proteins as Regulators of Beta-amyloid Aggregation and Toxicity.Israel journal of chemistry · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Transthyretin (TTR) binds to the Alzheimer-related peptide beta-amyloid (Aβ), and may protect against Aβ-induced neurotoxicity. In this work, the specific domains on TTR involved with binding to Aβ were probed. An array was constructed of peptides derived from overlapping sequences from TTR. Strong binding of Aβ to TIAALLSPYSYS (residues 106-117) was detected, corresponding to strand G on the inner β-sheet of TTR. Aβ bound weakly to four contiguous peptides spanning residues 59-83, which includes strand E through the E/F helix and loop. To further pinpoint specific residues on TTR involved with Aβ binding, nine alanine mutants were generated: I68A, I73A, K76A, L82A, I84A, S85A, L17A, T106A and L110A. Aβ binding was significantly inhibited only in L82A and L110A, indicating that Aβ binding to TTR is mediated through these bulky hydrophobic leucines. Aβ binding to L17A and S85A was significantly higher than to wild-type TTR. Enhancement of binding in L17A is postulated to arise from reduced steric restriction to the interior L110 site, since these two residues are adjacent in the native protein. The S85A mutation caused a reduction in TTR tetramer stability; increased Aβ binding is postulated to be a direct consequence of the reduced quaternary stability.
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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.