ArticleInternational journal of molecular sciences2019
Aggregation States of A
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Arsenic Promotes Intracellular AβBiological trace element research · 2026Article
- Plasma and cerebrospinal fluid biomarkers in aged dogs with cognitive decline.BMC veterinary research · 2025Article
- Investigating the Impact of NMDA Receptor Organization and Biological Sex in the APPswe/PS1dE9 Mouse Model of Alzheimer's Disease.International journal of molecular sciences · 2025Article
- A Practical Guide to All-Atom and Coarse-Grained Molecular Dynamics Simulations Using Amber and Gromacs: A Case Study of Disulfide-Bond Impact on the Intrinsically Disordered Amyloid Beta.International journal of molecular sciences · 2024Article
- Exploring Structural Insights of Aβ42 and α-Synuclein Monomers and Heterodimer: A Comparative Study Using Implicit and Explicit Solvent Simulations.The journal of physical chemistry. B · 2024Article
- Alzheimer's disease linked Aβ42 exerts product feedback inhibition on γ-secretase impairing downstream cell signaling.bioRxiv : the preprint server for biology · 2024Article
- A novel mouse model for N-terminal truncated Aβ2-x generation through meprin β overexpression in astrocytes.Cellular and molecular life sciences : CMLS · 2024Article
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- Effect of Bacterial Amyloid Protein Phenol-Soluble Modulin Alpha 3 on the Aggregation of Amyloid Beta Protein Associated with Alzheimer's Disease.Biomimetics (Basel, Switzerland) · 2023Article
- Overview on the Polyphenol Avenanthramide in Oats (Nutrients · 2023Review
- Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023Review
- S100B Expression Plays a Crucial Role in Cytotoxicity, Reactive Oxygen Species Generation and Nitric Oxide Synthase Activation Induced by Amyloid β-Protein in an Astrocytoma Cell Line.International journal of molecular sciences · 2023Article
- Solid-phase synthesis and pathological evaluation of pyroglutamate amyloid-βScientific reports · 2023Article
- The Physical Chemistry and Chemical Physics (PCCP) Section of theInternational journal of molecular sciences · 2021Article
- Amyloid β 42 fibril structure based on small-angle scattering.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Zinc Binding to NAP-Type Neuroprotective Peptides: Nuclear Magnetic Resonance Studies and Molecular Modeling.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Multi-Target Drug Candidates for Multifactorial Alzheimer's Disease: AChE and NMDAR as Molecular Targets.Molecular neurobiology · 2021Review
- On the Cluster Formation of α-Synuclein Fibrils.Frontiers in molecular biosciences · 2021Article
- Disclosing the Interaction of Gold Nanoparticles with Aβ(1-40) Monomers through Replica Exchange Molecular Dynamics Simulations.International journal of molecular sciences · 2020Article
- Cognitive Training as a Potential Activator of Hippocampal Neurogenesis in the Rat Model of Sporadic Alzheimer's Disease.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation states of amyloid beta peptides for amyloid beta A β 1 - 40 to A β 1 - 42 and A β p 3 - 42 are investigated through small angle neutron scattering (SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer's disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomers and fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radius of gyration of the order of 10 Å, while the oligomers and fibrils display differences in size and aggregation ability, with A β p 3 - 42 showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloid peptide and indeed to the development of the associated disease.
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Registered trials
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