ArticleProceedings of the National Academy of Sciences of the United States of America2016
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 422 papers.
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Who cites it
422 citing papers in PubMed.
- Brain-seeded 42-residue Amyloid-β Fibrils That Resemble Fibrils Directly Extracted From Alzheimer's Disease Brain Tissue.Journal of molecular biology · 2026Article
- Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.Biophysical journal · 2026Article
- Co-sedimentation is the key to the structural investigation of wild-type FAT10.Journal of biomolecular NMR · 2026Article
- A small molecule modulating heterogeneous amyloid-β isoforms improves cognitive and pathological outcomes in acute and 5XFAD Alzheimer's disease models.Alzheimer's research & therapy · 2026Article
- Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.bioRxiv : the preprint server for biology · 2026Article
- Massively parallel quantification of mutational impact on IAPP amyloid formation.Nature communications · 2026Article
- YIAD-0501 directly dissociates aggregates of full-length and N-terminal pyroglutamate-modified forms of Aβ.Alzheimer's research & therapy · 2026Article
- Differentiating Alzheimer's Aβ Isoforms Coaggregated in Cerebrospinal Fluid via Single-Particle Imaging.ACS chemical neuroscience · 2026Article
- Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation.Methods in enzymology · 2026Review
- Aducanumab binding to AβProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.The journal of physical chemistry letters · 2025Article
- Orexin-A and Circadian Disruption in Alzheimer's Disease: Implications for Amyloid-Beta Pathology.Molecular neurobiology · 2025Article
- Structural reconstruction of individual filaments in AβCommunications chemistry · 2025Article
- Aducanumab Binding to AβbioRxiv : the preprint server for biology · 2025Article
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- Computational study of conformational interconversion of an amyloid β double layer system.RSC advances · 2025Article
- The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Diamond rotors for high magic angle spinning frequencies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Small-Molecule Inhibitors of Amyloid Beta: Insights from Molecular Dynamics-Part B: Natural Compounds.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
362 more citing papers are in PubMed but not listed here.
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9 authors.
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Abstract
Amyloid-β (Aβ) is present in humans as a 39- to 42-amino acid residue metabolic product of the amyloid precursor protein. Although the two predominant forms, Aβ(1-40) and Aβ(1-42), differ in only two residues, they display different biophysical, biological, and clinical behavior. Aβ(1-42) is the more neurotoxic species, aggregates much faster, and dominates in senile plaque of Alzheimer's disease (AD) patients. Although small Aβ oligomers are believed to be the neurotoxic species, Aβ amyloid fibrils are, because of their presence in plaques, a pathological hallmark of AD and appear to play an important role in disease progression through cell-to-cell transmissibility. Here, we solved the 3D structure of a disease-relevant Aβ(1-42) fibril polymorph, combining data from solid-state NMR spectroscopy and mass-per-length measurements from EM. The 3D structure is composed of two molecules per fibril layer, with residues 15-42 forming a double-horseshoe-like cross-β-sheet entity with maximally buried hydrophobic side chains. Residues 1-14 are partially ordered and in a β-strand conformation, but do not display unambiguous distance restraints to the remainder of the core structure.
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