Evidence map›Paper›PMID 25395337›Full record

ArticleAngewandte Chemie (International ed. in English)2015

Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.

Anne K Schütz, Toni Vagt, Matthias Huber, Oxana Y Ovchinnikova, Riccardo Cadalbert, Joseph Wall, Peter Güntert, Anja Böckmann, Rudi Glockshuber, Beat H Meier

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

157 citing papers in PubMed.

  1. Article
  2. Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Modulation of AβJournal of chemical information and modeling · 2025
    Article
  8. Article
  9. Diamond rotors for high magic angle spinning frequencies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  15. Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025
    Article
  16. Membrane-assisted Aβ40 aggregation pathways.Cell reports. Physical science · 2025
    Article
  17. Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024
    Article
  18. Review
  19. Membrane-assisted Aβ40 aggregation pathways.bioRxiv : the preprint server for biology · 2024
    Article
  20. Article

97 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Anne K SchützPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093 Zurich (Switzerland).
Toni Vagt
Matthias Huber
Oxana Y Ovchinnikova
Riccardo Cadalbert
Joseph Wall
Peter Güntert
Anja Böckmann
Rudi Glockshuber
Beat H Meier

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints.

Indexed as

Alzheimer DiseaseAmino Acid SequenceAmyloid beta-PeptidesHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsAlzheimer's diseaseamyloidssolid-state NMR spectroscopystructure elucidation

Identifiers

PMID25395337
PMCPMC4502972

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.