ArticleJournal of the American Chemical Society2016
Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 408 papers.
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Who cites it
408 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
- High-frequency dynamic nuclear polarization in rotating solids.Science advances · 2026Review
- Hydration water dynamics in amyloid-β aggregates using deuterium and oxygen-17 solid-state NMR spectroscopy.The Journal of chemical physics · 2026Article
- Co-sedimentation is the key to the structural investigation of wild-type FAT10.Journal of biomolecular NMR · 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
- Self-Assembly of Peptides and Biomolecular Systems Into Functional Nanomaterials.Journal of peptide science : an official publication of the European Peptide Society · 2026Review
- The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomers.Physical chemistry chemical physics : PCCP · 2026Article
- Epigallocatechin Gallate as a State-Dependent Modulator of Amyloid-Biomolecules · 2026Review
- SEC Purified Monomeric Aβ42 Produces Reproducible and Reliable Aggregation Measurements.bioRxiv : the preprint server for biology · 2026Article
- The temperature dependence of amyloidProceedings of the National Academy of Sciences of the United States of America · 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
- Zooming into Disease at the Nanoscale: High-Speed Atomic Force Microscopy in Biomedical Discovery.ACS nano · 2026Review
- Structural defects in amyloid-β fibrils drive secondary nucleation.Nature communications · 2026Article
- Novel 1,4-Diazepane derivatives as amyloid-beta (Aβ) aggregation inhibitors.Frontiers in chemistry · 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
- Structural reconstruction of individual filaments in AβCommunications chemistry · 2025Article
348 more citing papers are in PubMed but not listed here.
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11 authors.
Funding
Abstract
Amyloid-β (Aβ) is a 39-42 residue protein produced by the cleavage of the amyloid precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that are a hallmark of Alzheimer's disease (AD). The most prominent forms of Aβ are Aβ1-40 and Aβ1-42, which differ by two amino acids (I and A) at the C-terminus. However, Aβ42 is more neurotoxic and essential to the etiology of AD. Here, we present an atomic resolution structure of a monomorphic form of AβM01-42 amyloid fibrils derived from over 500 (13)C-(13)C, (13)C-(15)N distance and backbone angle structural constraints obtained from high field magic angle spinning NMR spectra. The structure (PDB ID: 5KK3 ) shows that the fibril core consists of a dimer of Aβ42 molecules, each containing four β-strands in a S-shaped amyloid fold, and arranged in a manner that generates two hydrophobic cores that are capped at the end of the chain by a salt bridge. The outer surface of the monomers presents hydrophilic side chains to the solvent. The interface between the monomers of the dimer shows clear contacts between M35 of one molecule and L17 and Q15 of the second. Intermolecular (13)C-(15)N constraints demonstrate that the amyloid fibrils are parallel in register. The RMSD of the backbone structure (Q15-A42) is 0.71 ± 0.12 Å and of all heavy atoms is 1.07 ± 0.08 Å. The structure provides a point of departure for the design of drugs that bind to the fibril surface and therefore interfere with secondary nucleation and for other therapeutic approaches to mitigate Aβ42 aggregation.
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