ArticleJournal of molecular modeling2021
Destabilization of the Alzheimer's amyloid-β peptide by a proline-rich β-sheet breaker peptide: a molecular dynamics simulation study.
Article in Journal of molecular modeling, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Amyloid-reoriented enzyme catalysis.Nature communications · 2025Article
- Role of Copper and Zinc Ions in the Hydrolytic Degradation of Neurodegeneration-Related Peptides.Molecules (Basel, Switzerland) · 2025Article
- Inhibitory Effects of Gliadin Hydrolysates on BACE1 Expression and APP Processing to Prevent Aβ Aggregation.International journal of molecular sciences · 2024Article
- Small Molecule Decoys of Aggregation for Elimination of Aβ-Peptide Toxicity.ACS chemical neuroscience · 2023Article
- Consecutive Aromatic Residues Are Required for Improved Efficacy of β-Sheet Breakers.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The amyloid-β peptide exists in the form of fibrils in the plaques found in the brains of patients with Alzheimer's disease. One of the therapeutic strategies is the design of molecules which can destabilize these fibrils. We present a designed peptide KLVFFP
Indexed as
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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.