ArticleACS chemical neuroscience2014
Transthyretin-derived peptides as β-amyloid inhibitors.
Article in ACS chemical neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- Aggregation Limiting Cell-Penetrating Peptides Derived from Protein Signal Sequences.International journal of molecular sciences · 2023Article
- Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly.Nature communications · 2022Article
- Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.Science advances · 2021Article
- The inhibition of cellular toxicity of amyloid-β by dissociated transthyretin.The Journal of biological chemistry · 2020Article
- Rodent Models of Amyloid-Beta Feature of Alzheimer's Disease: Development and Potential Treatment Implications.Aging and disease · 2020Review
- Mixed Phospholipid Vesicles Catalytically Inhibit and Reverse Amyloid Fibril Formation.The journal of physical chemistry letters · 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
- Peptide-Based Molecular Strategies To Interfere with Protein Misfolding, Aggregation, and Cell Degeneration.Angewandte Chemie (International ed. in English) · 2020Review
- ROSETTA-informed design of structurally stabilized cyclic anti-amyloid peptides.Protein engineering, design & selection : PEDS · 2019Article
- Retinol-Binding Protein Interferes with Transthyretin-Mediated β-Amyloid Aggregation Inhibition.Biochemistry · 2018Article
- Multicomponent peptide assemblies.Chemical Society reviews · 2018Review
- Transthyretin Mimetics as Anti-β-Amyloid Agents: A Comparison of Peptide and Protein Approaches.ChemMedChem · 2018Article
- Cerebrospinal Fluid Proteins as Regulators of Beta-amyloid Aggregation and Toxicity.Israel journal of chemistry · 2017Article
- TANGO-Inspired Design of Anti-Amyloid Cyclic Peptides.ACS chemical neuroscience · 2016Article
- Transthyretin variants with improved inhibition of β-amyloid aggregation.Protein engineering, design & selection : PEDS · 2016Article
- A Cyclic Peptide Mimic of the β-Amyloid Binding Domain on Transthyretin.ACS chemical neuroscience · 2015Article
- Effects of polyamino acids and polyelectrolytes on amyloid β fibril formation.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Self-association of β-amyloid (Aβ) into soluble oligomers and fibrillar aggregates is associated with Alzheimer's disease pathology, motivating the search for compounds that selectively bind to and inhibit Aβ oligomerization and/or neurotoxicity. Numerous small-molecule inhibitors of Aβ aggregation or toxicity have been reported in the literature. However, because of their greater size and complexity, peptides and peptidomimetics may afford improved specificity and affinity as Aβ aggregation modulators compared to small molecules. Two divergent strategies have been employed in the search for peptides that bind Aβ: (i) using recognition domains corresponding to sequences in Aβ itself (such as KLVFF) and (ii) screening random peptide-based libraries. In this study, we propose a third strategy, specifically, designing peptides that mimic binding domains of Aβ-binding proteins. Transthyretin, a plasma transport protein that is also relatively abundant in cerebrospinal fluid, has been shown to bind to Aβ, inhibit aggregation, and reduce its toxicity. Previously, we identified strand G of transthyretin as a specific Aβ binding domain. In this work we further explore and define the necessary features of this binding domain. We demonstrate that peptides derived from transthyretin bind Aβ and inhibit its toxicity. We also show that, although both transthyretin and transthyretin-derived peptides bind Aβ and inhibit toxicity, they differ significantly in their effect on Aβ aggregation.
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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.