ArticleACS chemical neuroscience2021
Probing the Structure of Toxic Amyloid-β Oligomers with Electron Spin Resonance and Molecular Modeling.
Article in ACS chemical neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The Effect of CuACS chemical neuroscience · 2026Article
- Evaluating the Role of N-Acetyl-L-Tryptophan in the Aβ 1-42-Induced Neuroinflammation and Cognitive Decline in Alzheimer's Disease.Molecular neurobiology · 2024Article
- Exploring the AβFrontiers in molecular biosciences · 2024Article
- Amyloid-International journal of molecular sciences · 2023Article
- Location of the cross-β structure in prion fibrils: A search by seeding and electron spin resonance spectroscopy.Protein science : a publication of the Protein Society · 2022Article
- Amyloid β Dodecamer Disrupts the Neuronal Membrane More Strongly than the Mature Fibril: Understanding the Role of Oligomers in Neurotoxicity.The journal of physical chemistry. B · 2022Article
- The amyloid concentric β-barrel hypothesis: Models of amyloid beta 42 oligomers and annular protofibrils.Proteins · 2022Article
- Mechanistic Understanding from Molecular Dynamics in Pharmaceutical Research 2: Lipid Membrane in Drug Design.Pharmaceuticals (Basel, Switzerland) · 2021Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural models of the toxic species involved in the development of Alzheimer's disease are of utmost importance to understand the molecular mechanism and to describe early biomarkers of the disease. Among toxic species, soluble oligomers of amyloid-β (Aβ) peptides are particularly important, because they are responsible for spreading cell damages over brain regions, thus rapidly impairing brain functions. In this work we obtain structural information on a carefully prepared Aβ(1-42) sample, representing a toxic state for cell cultures, by combining electron spin resonance spectroscopy and computational models. We exploited the binding of Cu
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