ReviewThe Yale journal of biology and medicine2018
The Role of α-sheet in Amyloid Oligomer Aggregation and Toxicity.
Review in The Yale journal of biology and medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- Capillary serum-based spectroscopic signature for multiple sclerosis: A novel diagnostic perspective.Practical laboratory medicine · 2026Article
- Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Designed De Novo α-Sheet Peptides Destabilize Bacterial Biofilms and Increase the Susceptibility ofInternational journal of molecular sciences · 2024Article
- Performance of SOBA-AD blood test in discriminating Alzheimer's disease patients from cognitively unimpaired controls in two independent cohorts.Scientific reports · 2024Article
- Human islet amyloid polypeptide-induced β-cell cytotoxicity is linked to formation of α-sheet structure.Protein science : a publication of the Protein Society · 2024Article
- Designed α-sheet peptides disrupt uropathogenic E. coli biofilms rendering bacteria susceptible to antibiotics and immune cells.Scientific reports · 2023Article
- The role of α-sheet structure in amyloidogenesis: characterization and implications.Open biology · 2022Review
- Review
- From Quantum Mechanics, Classical Mechanics, and Bioinformatics to Artificial Intelligence Studies in Neurodegenerative Diseases.Methods in molecular biology (Clifton, N.J.) · 2022Article
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
- Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.International journal of molecular sciences · 2021Review
- Aggregation Mechanism of Alzheimer's Amyloid β-Peptide Mediated by α-Strand/α-Sheet Structure.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A major barrier to developing effective treatments and diagnostics for amyloid diseases is the inability of traditional protein structure characterization methods to elucidate the structure of the toxic oligomers that form during amyloidogenesis. Some years ago, our lab "discovered" a novel protein secondary structure in molecular dynamics simulations of multiple unrelated amyloid proteins, which we call α-sheet. We hypothesize that α-sheet plays an important role in amyloid aggregation and oligomer toxicity. De novo monomeric α-sheet peptides designed to be complementary to the structure observed in simulations inhibit amyloid aggregation and toxicity and specifically bind to the toxic oligomeric species in a variety of unrelated mammalian and bacterial amyloid systems associated with a range of diseases. Furthermore, spectroscopic analysis of α-sheet structure, including nuclear magnetic resonance (NMR), circular dichroism (CD), and Fourier-transform infrared spectroscopy (FTIR), correspond well to values predicted for α-sheet. These α-sheet designs are now being tested for their ability to detect and neutralize toxic oligomers in animals and in patient samples, demonstrating the potential of this nonstandard secondary structure as a target for therapeutic and diagnostic agents for amyloid diseases.
Indexed as
Identifiers
30258312PMC6153628What OpenQuestion holds
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.