Evidence map›Paper›PMID 21810907›Full record

ArticleDisease models & mechanisms2011

Development and validation of a yeast high-throughput screen for inhibitors of Aβ₄₂ oligomerization.

Sei-Kyoung Park, Scott D Pegan, Andrew D Mesecar, Lisa M Jungbauer, Mary Jo LaDu, Susan W Liebman

Open access · goldAbstract readValidation Study
In one paragraph

Article in Disease models & mechanisms, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Pathway swapping: Toward modular engineering of essential cellular processes.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
  18. Inhibition of AβMicrobial cell (Graz, Austria) · 2016
    Article
  19. Review
  20. Article
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

6 authors at 3 institutions in 1 country.

Sei-Kyoung ParkLaboratory for Molecular Biology, Department of Biological Sciences, University of Illinois, Chicago, IL 60607, USA.
Scott D Pegan
Andrew D Mesecar
Lisa M Jungbauer
Mary Jo LaDu
Susan W Liebman
University of Illinois Chicago · USPurdue University West Lafayette · USUniversity of Denver · US

Funding

TRANSGENIC MOUSE COREP01AG030128 · NIA · UNIVERSITY OF ILLINOIS AT CHICAGO · PI WEEBER, EDWIN JOHN · 2009 to 2013
$9.4M
A screen for molecules that inhibit formation of A-beta oligomers in yeastR21AG028818 · NIA · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LIEBMAN, SUSAN W. · 2006 to 2007
$345k
NIA NIH HHS P01 AG030128NIA NIH HHS R21 AG02881NIA NIH HHS R21 AG028818
6 · The paper itself

Abstract

Recent reports point to small soluble oligomers, rather than insoluble fibrils, of amyloid β (Aβ), as the primary toxic species in Alzheimer's disease. Previously, we developed a low-throughput assay in yeast that is capable of detecting small Aβ(42) oligomer formation. Specifically, Aβ(42) fused to the functional release factor domain of yeast translational termination factor, Sup35p, formed sodium dodecyl sulfate (SDS)-stable low-n oligomers in living yeast, which impaired release factor activity. As a result, the assay for oligomer formation uses yeast growth to indicate restored release factor activity and presumably reduced oligomer formation. We now describe our translation of this assay into a high-throughput screen (HTS) for anti-oligomeric compounds. By doing so, we also identified two presumptive anti-oligomeric compounds from a sub-library of 12,800 drug-like small molecules. Subsequent biochemical analysis confirmed their anti-oligomeric activity, suggesting that this form of HTS is an efficient, sensitive and cost-effective approach to identify new inhibitors of Aβ(42) oligomerization.

Indexed as

PolymerizationAmyloid beta-PeptidesDrug Evaluation, PreclinicalElectrophoresis, Polyacrylamide GelHigh-Throughput Screening AssaysModels, BiologicalPeptide FragmentsPilot ProjectsProtein Structure, QuaternaryProtein Structure, TertiaryReproducibility of ResultsSaccharomyces cerevisiaeAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide Fragments

Identifiers

PMID21810907
PMCPMC3209651
OpenAlexW2158582460

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.