Evidence map›Paper›PMID 17392510›Full record

ArticleMolecular biology of the cell2007

Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.

Dmitry Kryndushkin, Reed B Wickner

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. 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
–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

70 citing papers in PubMed.

  1. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  2. Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Anti-prion systems in yeast.The Journal of biological chemistry · 2019
    Review
  14. Review
  15. Article
  16. Genetics · 2018
    Article
  17. Review
  18. Article
  19. Article
  20. [PSI+] prion propagation is controlled by inositol polyphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article

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

2 authors.

Dmitry KryndushkinLaboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA.
Reed B Wickner

Funding

Curing Prions of YeastZ01DK024948 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WICKNER, REED B. · 2007 to 2008
$641k
Curing Prions of YeastZIADK024948 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WICKNER, REED B. · 2009 to 2009
$214k
Intramural NIH HHS
6 · The paper itself

Abstract

The [URE3] and [PSI(+)] prions are infectious amyloid forms of Ure2p and Sup35p. Several chaperones influence prion propagation: Hsp104p overproduction destabilizes [PSI(+)], whereas [URE3] is sensitive to excess of Ssa1p or Ydj1p. Here, we show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3]. Sse1p and Fes1p are nucleotide exchange factors for Ssa1p. Interestingly, deletion of either SSE1 or FES1 completely blocked [URE3] propagation. In addition, deletion of SSE1 also interfered with [PSI(+)] propagation.

Indexed as

Adenosine TriphosphatasesGlutathione PeroxidaseGuanine Nucleotide Exchange FactorsHSP110 Heat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsIntracellular Signaling Peptides and ProteinsPoint MutationPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesFES1 protein, S cerevisiaeGlutathione PeroxidaseGuanine Nucleotide Exchange FactorsHSP110 Heat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsIntracellular Signaling Peptides and ProteinsPrionsSaccharomyces cerevisiae ProteinsSSA1 protein, S cerevisiaeSSE1 protein, S cerevisiaeURE2 protein, S cerevisiaeYDJ1 protein, S cerevisiae

Identifiers

PMID17392510
PMCPMC1877104

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.