Evidence map›Paper›PMID 11751580›Full record

ArticleEMBO reports2002

The [URE3] phenotype: evidence for a soluble prion in yeast.

Eric Fernandez-Bellot, Elisabeth Guillemet, Frederique Ness, Agnes Baudin-Baillieu, Leslie Ripaud, Mick Tuite, Christophe Cullin

Abstract read
In one paragraph

Article in EMBO reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Prions in yeast.Genetics · 2012
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+].Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  12. Article
  13. Amyloid aggregates of the HET-s prion protein are infectious.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

7 authors.

Eric Fernandez-BellotCentre de Génétique Moléculaire, 91190 Gif-sur-Yvette, France.
Elisabeth Guillemet
Frederique Ness
Agnes Baudin-Baillieu
Leslie Ripaud
Mick Tuite
Christophe Cullin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explaining the prion propagation of the phenotypes [PSI+] and [URE3], respectively. Here, we demonstrate that the propagation of [URE3] cannot simply be the consequence of generating large aggregates of Ure2p, because such aggregation can be found in some conditions that are not related to the prion state of Ure2p. A comparison of [PSI+] and [URE3] aggregation demonstrates differences between these two prion mechanisms. Our findings lead us to propose a new unifying model for yeast prion propagation.

Indexed as

Amino Acid SequenceGlutathione PeroxidaseMolecular Sequence DataPhenotypePrionsProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityGlutathione PeroxidasePrionsProtein IsoformsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsURE2 protein, S cerevisiae

Identifiers

PMID11751580
PMCPMC1083930

What OpenQuestion holds

Textmetadata
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Registered trials

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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.