ArticleNature structural & molecular biology2015
Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 383 papers.
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Who cites it
383 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
- Use of high-affinity scFv antibody NUsc1 for isolation and sensitive detection of Alzheimer's-associated amyloid beta oligomers.The Journal of biological chemistry · 2026Article
- Co-sedimentation is the key to the structural investigation of wild-type FAT10.Journal of biomolecular NMR · 2026Article
- Strategic physicochemical tuning: amphiphilic polymers as molecular regulators of amyloid aggregation and cytotoxicity.Chemical science · 2026Article
- Temperature-Dependent Dynamics of Aβ42 and α-Synuclein Monomers and Early Oligomerization of Aβ42: Shared Residues Mediate Intra- and Intermolecular β-Sheets.ACS chemical neuroscience · 2026Article
- Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.bioRxiv : the preprint server for biology · 2026Article
- Higher Magnetic Field NMR Renders Resolution Enhancement on Ganglioside GD3 Catalyzed AβbioRxiv : the preprint server for biology · 2026Article
- Massively parallel quantification of mutational impact on IAPP amyloid formation.Nature communications · 2026Article
- Identification of TMED10 as A Regulator for Neuronal Exocytosis of Amyloid Beta 42.Neuroscience bulletin · 2026Article
- Naringenin as a dual-target modulator of RAGE-NF-κB signaling and Aβ fibrillization in Alzheimer's disease: integrated computational and experimental analyses.Frontiers in pharmacology · 2026Article
- Exploring the Impact of Curcumin and Carbon Nanotubes on Beta-amyloid Peptide Dimer: Insights from Molecular Dynamics Simulation and Density Functional Theory Methods.Current pharmaceutical biotechnology · 2026Article
- Fucoxanthin attenuates carbonyl stress and neuroinflammation by modulating MGO/RAGE/NF-κB axis in Aβ-induced models.Frontiers in pharmacology · 2026Article
- Identification of potent high-affinity secondary nucleation inhibitors of Aβ42 aggregation from an ultra-large chemical library using deep docking.Molecular systems biology · 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
- Inhibition of amyloid-beta aggregation by phenyl butyric acid analogs and bile acids: a comprehensive in silico study.Molecular diversity · 2025Article
- High-dimensional solid-state NMR facilitated by transverse-mixing optimal control.Research square · 2025Article
- Aducanumab Binding to AβbioRxiv : the preprint server for biology · 2025Article
- Computational study of conformational interconversion of an amyloid β double layer system.RSC advances · 2025Article
323 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
Abstract
Increasing evidence has suggested that formation and propagation of misfolded aggregates of 42-residue human amyloid β (Aβ(1-42)), rather than of the more abundant Aβ(1-40), provokes the Alzheimer's disease cascade. However, structural details of misfolded Aβ(1-42) have remained elusive. Here we present the atomic model of an Aβ(1-42) amyloid fibril, from solid-state NMR (ssNMR) data. It displays triple parallel-β-sheet segments that differ from reported structures of Aβ(1-40) fibrils. Remarkably, Aβ(1-40) is incompatible with the triple-β-motif, because seeding with Aβ(1-42) fibrils does not promote conversion of monomeric Aβ(1-40) into fibrils via cross-replication. ssNMR experiments suggest that C-terminal Ala42, absent in Aβ(1-40), forms a salt bridge with Lys28 to create a self-recognition molecular switch that excludes Aβ(1-40). The results provide insight into the Aβ(1-42)-selective self-replicating amyloid-propagation machinery in early-stage Alzheimer's disease.
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