Evidence map›Paper›PMID 11707395›Full record

ArticleThe EMBO journal2001

Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion.

S M Uptain, G J Sawicki, B Caughey, S Lindquist

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

70 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Michler's hydrol blue elucidates structural differences in prion strains.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Article
  14. The role of prion strain diversity in the development of successful therapeutic treatments.Progress in molecular biology and translational science · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Translational Control by Prion-like Proteins.Trends in cell biology · 2018
    Review
  19. Review
  20. The life of [PSI].Current genetics · 2018
    Review

10 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

4 authors at 1 institution in 1 country.

S M UptainHoward Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA.
G J Sawicki
B Caughey
S Lindquist
Howard Hughes Medical Institute · US

Funding

BIOCHEMISTRY OF SCRAPIE PATHOGENESISZ01AI000580 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI CAUGHEY, BYRON · 1990 to 2008
$4.8M
YEAST PRION DYNAMICS AND CHAPERONE INTERACTIONSR01GM057840 · NIGMS · UNIVERSITY OF CHICAGO · PI ARNSDORF, MORTON F · 2000 to 2003
$1.1M
NIGMS NIH HHS GM57840NIGMS NIH HHS R01 GM057840
6 · The paper itself

Abstract

Yeast prions are protein-based genetic elements that produce phenotypes through self-perpetuating changes in protein conformation. For the prion [PSI(+)] this protein is Sup35, which is comprised of a prion-determining region (NM) fused to a translational termination region. [PSI(+)] strains (variants) with different heritable translational termination defects (weak or strong) can exist in the same genetic background. [PSI(+)] variants are reminiscent of mammalian prion strains, which can be passaged in the same mouse strain yet have different disease latencies and brain pathologies. We found that [PSI(+)] variants contain different ratios of Sup35 in the prion and non-prion state that correlate with different translation termination efficiencies. Indeed, the partially purified prion form of Sup35 from a strong [PSI(+)] variant converted purified NM much more efficiently than that of several weak variants. However, this difference was lost in a second round of conversion in vitro. Thus, [PSI(+)] variants result from differences in the efficiency of prion-mediated conversion, and the maintenance of [PSI(+)] variants involves more than nucleated conformational conversion (templating) to NM alone.

Indexed as

Saccharomyces cerevisiae ProteinsBrainCell NucleusDose-Response Relationship, DrugFungal ProteinsImmunoblottingLyasesPeptide Termination FactorsPhenotypePrionsProtein BiosynthesisProtein ConformationRecombinant Fusion ProteinsRecombinant ProteinsSpectroscopy, Fourier Transform InfraredTime FactorsFungal ProteinsLyasesPeptide Termination FactorsPrionsRecombinant Fusion ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID11707395
PMCPMC125732
OpenAlexW1980941432

What OpenQuestion holds

Textmetadata
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.