Evidence map›Paper›PMID 16452152›Full record

ArticleGenetics2006

De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.

Kyung-Won Park, Ji-Sook Hahn, Qing Fan, Dennis J Thiele, Liming Li

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Analysis of [SWIMolecular microbiology · 2017
    Article
  5. De novo [PSIScientific reports · 2017
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Prions in yeast.Genetics · 2012
    Review
  14. Article
  15. Article
  16. Article
  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

5 authors at 3 institutions in 2 countries.

Kyung-Won ParkDepartment of Molecular Pharmacology and Biological Chemistry, Northwestern University Institute of Neuroscience, Feinberg School of Medicine, Chicago, Illinois 60611, USA.
Ji-Sook Hahn
Qing Fan
Dennis J Thiele
Liming Li
Northwestern University · USDuke Medical Center · USSeoul National University · KR

Funding

HEAT SHOCK TRANSCRIPTION FACTOR FUNCTION AND REGULATIONR01GM059911 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI THIELE, DENNIS J. · 1999 to 2007
$2.2M
NIGMS NIH HHS GM59911NIGMS NIH HHS R01 GM059911
6 · The paper itself

Abstract

Yeast prions are non-Mendelian genetic elements that are conferred by altered and self-propagating protein conformations. Such a protein conformation-based transmission is similar to that of PrP(Sc), the infectious protein responsible for prion diseases. Despite recent progress in understanding the molecular nature and epigenetic transmission of prions, the underlying mechanisms governing prion conformational switch and determining prion "strains" are not understood. We report here that the evolutionarily conserved heat-shock transcription factor (HSF) strongly influences yeast prion formation and strain determination. An hsf1 mutant lacking the amino-terminal activation domain inhibits the yeast prion [PSI+] formation whereas a mutant lacking the carboxyl-terminal activation domain promotes [PSI+] formation. Moreover, specific [PSI+] strains are preferentially formed in these mutants, demonstrating the importance of genetic makeup in determining de novo appearance of prion strains. Although these hsf1 mutants preferentially support the formation of certain [PSI+] strains, they are capable of receiving and faithfully propagating nonpreferable strains, suggesting that prion initiation and propagation are distinct processes requiring different cellular components. Our findings establish the importance of HSF in prion initiation and strain determination and imply a similar regulatory role of mammalian HSFs in the complex etiology of prion disease.

Indexed as

Gene Expression Regulation, FungalAllelesHeat-Shock ProteinsPolyglutamic AcidPrionsProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionTranscription FactorsHeat-Shock ProteinsHsP104 protein, S cerevisiaePolyglutamic AcidPrionsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID16452152
PMCPMC1461444
OpenAlexW2122142406

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.