Evidence map›Paper›PMID 29425039›Full record

ArticleJournal of the American Chemical Society2018

E22G Pathogenic Mutation of β-Amyloid (Aβ) Enhances Misfolding of Aβ40 by Unexpected Prion-like Cross Talk between Aβ42 and Aβ40.

Brian K Yoo, Yiling Xiao, Dan McElheny, Yoshitaka Ishii

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024
    Article
  7. Heterotypic Seeding Generates Mixed Amyloid Polymorphs.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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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

4 authors at 2 institutions in 2 countries.

Brian K YooDepartment of Chemistry, University of Illinois at Chicago , Chicago, Illinois 60607, United States.
Yiling XiaoDepartment of Chemistry, University of Illinois at Chicago , Chicago, Illinois 60607, United States.
Dan McElhenyDepartment of Chemistry, University of Illinois at Chicago , Chicago, Illinois 60607, United States.
Yoshitaka IshiiDepartment of Chemistry, University of Illinois at Chicago , Chicago, Illinois 60607, United States.ORCID 0000-0002-7724-6469
University of Illinois Chicago · USTokyo Institute of Technology · JP

Funding

Alzheimer's Brain-Seeded Abeta FibrilsR01AG048793 · NIA · UNIVERSITY OF CHICAGO · PI MEREDITH, STEPHEN C. · 2015 to 2019
$2.1M
Structures and Propagation of Pathologically Relevant Amyloids in Alzheimer's.U01GM098033 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ISHII, YOSHITAKA · 2016 to 2020
$1.3M
Structures and Toxicity of Amyloid Protein Assemblies in Alzheimer'sR01GM098033 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ISHII, YOSHITAKA · 2011 to 2014
$1.1M
Molecular Structures and Kinetics of Amyloid Intermediates by Solid-State NMRR01AG028490 · NIA · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ISHII, YOSHITAKA · 2006 to 2009
$1.1M
NIA NIH HHS R01 AG028490NIA NIH HHS R01 AG048793NIGMS NIH HHS R01 GM098033NIGMS NIH HHS U01 GM098033
6 · The paper itself

Abstract

Cross-seeding of misfolded amyloid proteins is postulated to induce cross-species infection of prion diseases. In sporadic Alzheimer's disease (AD), misfolding of 42-residue β-amyloid (Aβ) is widely considered to trigger amyloid plaque deposition. Despite increasing evidence that misfolded Aβ mimics prions, interactions of misfolded 42-residue Aβ42 with more abundant 40-residue Aβ40 in AD are elusive. This study presents in vitro evidence that a heterozygous E22G pathogenic ("Arctic") mutation of Aβ40 can enhance misfolding of Aβ via cross-seeding from wild-type (WT) Aβ42 fibril. Thioflavin T (ThT) fluorescence analysis suggested that misfolding of E22G Aβ40 was enhanced by adding 5% (w/w) WT Aβ42 fibril as "seed", whereas WT Aβ40 was unaffected by Aβ42 fibril seed.

Indexed as

MutationProtein FoldingAmyloid beta-PeptidesBenzothiazolesFluorescent DyesPeptide FragmentsPrionsThiazolesAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)BenzothiazolesFluorescent DyesPeptide FragmentsPrionsThiazolesthioflavin T

Identifiers

PMID29425039
PMCPMC6408951
OpenAlexW2789004830

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.