Evidence map›Paper›PMID 21467567›Full record

ArticleGenetics2011

Molecular chaperone Hsp104 can promote yeast prion generation.

Dmitry S Kryndushkin, Abbi Engel, Herman Edskes, Reed B Wickner

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  3. Heat Stress Tolerance GeneFrontiers in microbiology · 2021
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Behead and live long or the tale of cathepsin L.Yeast (Chichester, England) · 2018
    Article
  11. Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

4 authors at 2 institutions in 1 country.

Dmitry S KryndushkinLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA.
Abbi Engel
Herman Edskes
Reed B Wickner
National Institutes of Health · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Prions of Yeast and Anti-Prion SystemsZIADK024950 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WICKNER, REED B. · 2009 to 2025
$25.2M
Intramural NIH HHS
6 · The paper itself

Abstract

[URE3] is an amyloid-based prion of Ure2p, a regulator of nitrogen catabolism in Saccharomyces cerevisiae. The Ure2p of the human pathogen Candida albicans can also be a prion in S. cerevisiae. We find that overproduction of the disaggregating chaperone, Hsp104, increases the frequency of de novo [URE3] prion formation by the Ure2p of S. cerevisiae and that of C. albicans. This stimulation is strongly dependent on the presence of the [PIN(+)] prion, known from previous work to enhance [URE3] prion generation. Our data suggest that transient Hsp104 overproduction enhances prion generation through persistent effects on Rnq1 amyloid, as well as during overproduction by disassembly of amorphous Ure2 aggregates (generated during Ure2p overproduction), driving the aggregation toward the amyloid pathway. Overproduction of other major cytosolic chaperones of the Hsp70 and Hsp40 families (Ssa1p, Sse1p, and Ydj1p) inhibit prion formation, whereas another yeast Hsp40, Sis1p, modulates the effects of Hsp104p on both prion induction and prion curing in a prion-specific manner. The same factor may both enhance de novo prion generation and destabilize existing prion variants, suggesting that prion variants may be selected by changes in the chaperone network.

Indexed as

Adenosine TriphosphatasesBlotting, WesternCandida albicansEpigenesis, GeneticGlutathione PeroxidaseHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsModels, GeneticMolecular ChaperonesPeptide Termination FactorsPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransformation, GeneticAdenosine TriphosphatasesGlutathione PeroxidaseHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPeptide Termination FactorsPrionsRNQ1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIS1 protein, S cerevisiaeSSA1 protein, S cerevisiaeSSE1 protein, S cerevisiaeSUP35 protein, S cerevisiaeURE2 protein, S cerevisiaeYDJ1 protein, S cerevisiae

Identifiers

PMID21467567
PMCPMC3122315
OpenAlexW2095787130

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.