Evidence map›Paper›PMID 28484020›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Hsp104 disaggregase at normal levels cures many [

Anton Gorkovskiy, Michael Reidy, Daniel C Masison, Reed B Wickner

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Review
  2. Article
  3. Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025
    Review
  4. Article
  5. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  6. Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023
    Review
  8. Article
  9. Article
  10. Anti-Prion Systems inViruses · 2022
    Review
  11. Review
  12. Review
  13. Review
  14. Antiprion systems in yeast cooperate to cure or prevent the generation of nearly all [Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  16. Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  17. Review
  18. Review
  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.

Anton GorkovskiyLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830.
Michael ReidyLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830.
Daniel C MasisonLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830.
Reed B WicknerLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830 wickner@helix.nih.gov.

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
Genomics Core FacilityZICDK071001 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HANOVER, JOHN A. · 2009 to 2023
$16.6M
Chaperone-amyloid interactionsZIADK024954 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI MASISON, DANIEL · 2009 to 2025
$3.8M
6 · The paper itself

Abstract

Overproduction or deficiency of many chaperones and other cellular components cure the yeast prions [

Indexed as

Amino Acid Transport SystemsHeat-Shock ProteinsHeat-Shock Proteins, SmallHSP40 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAmino Acid Transport SystemsBTN2 protein, S cerevisiaeCUR1 protein, S cerevisiaeHeat-Shock ProteinsHeat-Shock Proteins, SmallHsP104 protein, S cerevisiaeHSP40 Heat-Shock ProteinsHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMolecular ChaperonesPrionsSaccharomyces cerevisiae ProteinsSIS1 protein, S cerevisiaeSTI1 protein, S cerevisiaeVesicular Transport Proteinsantiprion systemprion[PSI+]Sup35p

Identifiers

PMID28484020
PMCPMC5448221

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.