ArticleJournal of molecular biology2020
Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1-42).
Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Hydration water dynamics in amyloid-β aggregates using deuterium and oxygen-17 solid-state NMR spectroscopy.The Journal of chemical physics · 2026Article
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- The concentric β-barrel hypothesis for amyloids: Models of soluble and transmembrane amyloid-β42 oligomers and channels composed of identical subunits and GM1 gangliosides.bioRxiv : the preprint server for biology · 2026Article
- Asparagine Deamidation Attenuates Toxicity, Aggregation, and Microglial Responses of Alzheimer's Amyloid-β.ACS chemical neuroscience · 2025Article
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Structural convergence and membrane interactions of AβCommunications chemistry · 2025Article
- Aggregation dynamics of a 150 kDa Aβ42 oligomer: Insights from cryo electron microscopy and multimodal analysis.Computational and structural biotechnology journal · 2024Article
- Heterotypic Seeding Generates Mixed Amyloid Polymorphs.Small science · 2024Article
- Aggregation Dynamics of a 150 kDa Aβ42 Oligomer: Insights from Cryo Electron Microscopy and Multimodal Analysis.bioRxiv : the preprint server for biology · 2024Article
- Parallel β-Sheet Structure and Structural Heterogeneity Detected within Q11 Self-Assembling Peptide Nanofibers.The journal of physical chemistry. B · 2024Article
- A common pathway for detergent-assisted oligomerization of Aβ42.Communications biology · 2023Article
- On-Pathway Oligomer of Human Islet Amyloid Polypeptide Induced and Stabilized by Mechanical Rotation during Magic Angle Spinning Nuclear Magnetic Resonance.The journal of physical chemistry letters · 2023Article
- On-Pathway Oligomer of Human Islet Amyloid Polypeptide Induced and Stabilized by Mechanical Rotation During MAS NMR.bioRxiv : the preprint server for biology · 2023Article
- Oligomerization by co-assembly of β-amyloid and α-synuclein.Frontiers in molecular biosciences · 2023Review
- Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer's Disease.Molecules (Basel, Switzerland) · 2022Review
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- The amyloid concentric β-barrel hypothesis: Models of amyloid beta 42 oligomers and annular protofibrils.Proteins · 2022Article
- Lipid membranes induce structural conversion from amyloid oligomers to fibrils.Biochemical and biophysical research communications · 2021Article
- Aβ receptors specifically recognize molecular features displayed by fibril ends and neurotoxic oligomers.Nature communications · 2021Article
- Glucosamine and Its Analogues as Modulators of Amyloid-β Toxicity.ACS medicinal chemistry letters · 2021Article
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Authors and funding
10 authors.
Funding
Abstract
We present solid-state NMR measurements of β-strand secondary structure and inter-strand organization within a 150-kDa oligomeric aggregate of the 42-residue variant of the Alzheimer's amyloid-β peptide (Aβ(1-42)). We build upon our previous report of a β-strand spanned by residues 30-42, which arranges into an antiparallel β-sheet. New results presented here indicate that there is a second β-strand formed by residues 11-24. Contrary to expectations, NMR data indicate that this second β-strand is organized into a parallel β-sheet despite the co-existence of an antiparallel β-sheet in the same structure. In addition, the in-register parallel β-sheet commonly observed for amyloid fibril structure does not apply to residues 11-24 in the 150-kDa oligomer. Rather, we present evidence for an inter-strand registry shift of three residues that likely alternate in direction between adjacent molecules along the β-sheet. We corroborated this unexpected scheme for β-strand organization using multiple two-dimensional NMR and
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