Evidence map›Paper›PMID 25601439›Full record

ArticleMolecular microbiology2015

Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.

Victoria A Doronina, Gemma L Staniforth, Shaun H Speldewinde, Mick F Tuite, Chris M Grant

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Causative Links between Protein Aggregation and Oxidative Stress: A Review.International journal of molecular sciences · 2019
    Review
  8. The three faces of Sup35.Yeast (Chichester, England) · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Spontaneous mutations inMicrobial cell (Graz, Austria) · 2018
    Article
  13. What Is Our Current Understanding of PrPPathogens (Basel, Switzerland) · 2017
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

Victoria A DoroninaFaculty of Life Sciences, University of Manchester, The Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.
Gemma L Staniforth
Shaun H Speldewinde
Mick F Tuite
Chris M Grant
University of Manchester · GBUniversity of Kent · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J000183/1Biotechnology and Biological Sciences Research Council BB/J000191/1Wellcome Trust
6 · The paper itself

Abstract

Prions are self-perpetuating amyloid protein aggregates which underlie various neurodegenerative diseases in mammals and heritable traits in yeast. The molecular basis of how yeast and mammalian prions form spontaneously into infectious amyloid-like structures is poorly understood. We have explored the hypothesis that oxidative stress is a general trigger for prion formation using the yeast [PSI(+)] prion, which is the altered conformation of the Sup35 translation termination factor. We show that the frequency of [PSI(+)] prion formation is elevated under conditions of oxidative stress and in mutants lacking key antioxidants. We detect increased oxidation of Sup35 methionine residues in antioxidant mutants and show that overexpression of methionine sulphoxide reductase abrogates both the oxidation of Sup35 and its conversion to the [PSI(+)] prion. [PSI(+)] prion formation is particularly elevated in a mutant lacking the Sod1 Cu,Zn-superoxide dismutase. We have used fluorescence microscopy to show that the de novo appearance of [PSI(+)] is both rapid and increased in frequency in this mutant. Finally, electron microscopy analysis of native Sup35 reveals that similar fibrillar structures are formed in both the wild-type and antioxidant mutants. Together, our data indicate that oxidative stress is a general trigger of [PSI(+) formation, which can be alleviated by antioxidant defenses.

Indexed as

Oxidative StressMicroscopy, ElectronMicroscopy, FluorescenceMutationOxidation-ReductionPeptide Termination FactorsProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuperoxide DismutasePeptide Termination FactorsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeSuperoxide Dismutase

Identifiers

PMID25601439
PMCPMC4407919
OpenAlexW1487810255

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.