Evidence map›Paper›PMID 28373280›Full record

ArticleThe Journal of biological chemistry2017

Heat shock protein 104 (Hsp104)-mediated curing of [

Xiaohong Zhao, Ramon Rodriguez, Rebecca E Silberman, Joseph M Ahearn, Sheela Saidha, Kaelyn C Cummins, Evan Eisenberg, Lois E Greene

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. 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
2.1field-weighted citation impact, top 12% 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, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021
    Review
  12. Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Review
  15. Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019
    Review
  16. Article
  17. Article
  18. Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.International journal of molecular sciences · 2019
    Article
  19. Review
  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

8 authors at 2 institutions in 1 country.

Xiaohong ZhaoFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Ramon RodriguezFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Rebecca E SilbermanFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Joseph M AhearnFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Sheela SaidhaFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Kaelyn C CumminsFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Evan EisenbergFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301.
Lois E GreeneFrom the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301 greenel@helix.nih.gov.
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Role of molecular chaperones in protein folding diseasesZIAHL000516 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI GREENE, LOIS · 2009 to 2022
$19.6M
6 · The paper itself

Abstract

Prions arise from proteins that have two possible conformations: properly folded and non-infectious or misfolded and infectious. The [

Indexed as

Adenosine TriphosphatasesCandida albicansGenetic Complementation TestHeat-Shock ProteinsPeptide Termination FactorsPrionsProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesAdenosine TriphosphatasesHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP104 protein, S pombePeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeamyloidHsp104molecular chaperoneprionprotein foldingyeast

Identifiers

PMID28373280
PMCPMC5448092
OpenAlexW2604251699

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.