Evidence map›Paper›PMID 24034249›Full record

ArticleCell2013

Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue.

Jun-Xia Lu, Wei Qiang, Wai-Ming Yau, Charles D Schwieters, Stephen C Meredith, Robert Tycko

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 589 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
589citing papers in PubMed, 1 pooled it
56.4field-weighted citation impact, top 1% of its field
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

589 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,108 citations in OpenAlex.

  1. Pooled it
  2. Article
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  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Preclinical evaluation of [EJNMMI research · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.bioRxiv : the preprint server for biology · 2026
    Article
  14. From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  15. Review
  16. Review
  17. Article
  18. Decoding the mechanisms of amyloid-β in synaptic toxicity.Journal of Alzheimer's disease : JAD · 2026
    Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Jun-Xia LuLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Wei Qiang
Wai-Ming Yau
Charles D Schwieters
Stephen C Meredith
Robert Tycko
National Institutes of Health · USNational Institute of Diabetes and Digestive and Kidney Diseases · USUniversity of Chicago · US

Funding

Structural Studies of Alzheimer's beta-Amyloid FibrilsZIADK029061 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$8.4M
Structural Heterogeneity and Covalent Changes in Beta Amyloid FibrilsR01NS042852 · NINDS · UNIVERSITY OF CHICAGO · PI MEREDITH, STEPHEN C. · 2003 to 2010
$2.4M
Intramural NIH HHS ZIA DK029061NINDS NIH HHS R01 NS042852
6 · The paper itself

Abstract

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here, we investigate structures of human brain-derived Aβ fibrils, using seeded fibril growth from brain extract and data from solid-state nuclear magnetic resonance and electron microscopy. Experiments on tissue from two Alzheimer's disease (AD) patients with distinct clinical histories showed a single predominant 40 residue Aβ (Aβ40) fibril structure in each patient; however, the structures were different from one another. A molecular structural model developed for Aβ40 fibrils from one patient reveals features that distinguish in-vivo- from in-vitro-produced fibrils. The data suggest that fibrils in the brain may spread from a single nucleation site, that structural variations may correlate with variations in AD, and that structure-specific amyloid imaging agents may be an important future goal.

Indexed as

AgedAlzheimer DiseaseAmyloidAmyloid beta-PeptidesBrainFemaleHumansModels, BiologicalAmyloidAmyloid beta-Peptides

Identifiers

PMID24034249
PMCPMC3814033
OpenAlexW2081855136

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.