ArticleBiophysical journal2009
Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
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Who cites it
39 citing papers in PubMed, 93 citations in OpenAlex.
- Key questions for the future of amyloid research in dementia: a framework for integrating complex datasets.Molecular psychiatry · 2025Review
- Review
- Multiscale Models for Fibril Formation: Rare Events Methods, Microkinetic Models, and Population Balances.Life (Basel, Switzerland) · 2021Article
- Alzheimer's Disease "Non-amyloidogenic" p3 Peptide Revisited: A Case for Amyloid-α.ACS chemical neuroscience · 2020Article
- Amyloid Evolution: Antiparallel Replaced by Parallel.Biophysical journal · 2020Article
- Atomic resolution map of the soluble amyloid beta assembly toxic surfaces.Chemical science · 2019Article
- Surveying the Energy Landscapes of Aβ Fibril Polymorphism.The journal of physical chemistry. B · 2018Article
- Molecular Recognition between Aβ-Specific Single-Domain Antibody and Aβ Misfolded Aggregates.Antibodies (Basel, Switzerland) · 2018Article
- Understanding the roles of mutations in the amyloid precursor protein in Alzheimer disease.Molecular psychiatry · 2018Review
- Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid β (Aβ) peptides in the monomer and protofibril states.The Journal of biological chemistry · 2017Article
- Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts.ACS chemical neuroscience · 2017Article
- Influence of Hyperglycemic Conditions on Self-Association of the Alzheimer's Amyloid β (AβACS omega · 2017Article
- Human Neuronal Calcium Sensor-1 Protein Avoids Histidine Residues To Decrease pH Sensitivity.The journal of physical chemistry. B · 2017Article
- Polymorphism of fibrillar structures depending on the size of assembled AβScientific reports · 2016Article
- Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer's Disease Immunotherapy.Drugs & aging · 2016Review
- Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways.PLoS computational biology · 2015Article
- Nucleation of polymorphic amyloid fibrils.Biophysical journal · 2015Article
- Stability of Iowa mutant and wild type Aβ-peptide aggregates.The Journal of chemical physics · 2014Article
- A fibril-like assembly of oligomers of a peptide derived from β-amyloid.Journal of the American Chemical Society · 2014Article
- Polymorphism of oligomers of a peptide from β-amyloid.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Abeta(17-42) (so-called p3) amyloid is detected in vivo in the brains of individuals with Alzheimer's disease or Down's syndrome. We investigated the polymorphism of Abeta(17-42) oligomers based on experimental data from steady-state NMR measurements, electron microscopy, two-dimensional hydrogen exchange, and mutational studies, using all-atom molecular-dynamics simulation with explicit solvent. We assessed the structural stability and the populations. Our results suggest that conformational differences in the U-turn of Abeta(17-42) lead to polymorphism in beta-sheet registration and retention of an ordered beta-strand organization at the termini. Further, although the parallel Abeta(17-42) oligomer organization is the most stable of the conformers investigated here, different antiparallel Abeta(17-42) organizations are also stable and compete with the parallel architectures, presenting a polymorphic population. In this study we propose that 1), the U-turn conformation is the primary factor leading to polymorphism in the assembly of Abeta(17-42) oligomers, and is also coupled to oligomer growth; and 2), both parallel Abeta(17-42) oligomers and an assembly of Abeta(17-42) oligomers that includes both parallel and antiparallel organizations contribute to amyloid fibril formation. Finally, since a U-turn motif generally appears in amyloids formed by full proteins or long fragments, and since to date these have been shown to exist only in parallel architectures, our results apply to a broad range of oligomers and fibrils.
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Registered trials
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