Evidence map›Paper›PMID 19164897›Full record

ReviewPrion

Prion stability.

Brian S Cox, Lee J Byrne, Mick F Tuite

Open access · bronzeAbstract readReview
In one paragraph

Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Behead and live long or the tale of cathepsin L.Yeast (Chichester, England) · 2018
    Article
  6. Review
  7. Article
  8. Article
  9. Prions in yeast.Genetics · 2012
    Review
  10. Review
  11. Article
  12. Article
  13. Use of yeast as a system to study amyloid toxicity.Methods (San Diego, Calif.) · 2011
    Article
  14. Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  15. Review
  16. Hsp104 and prion propagation.Protein and peptide letters · 2009
    Review
  17. Review
  18. 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

3 authors at 1 institution in 1 country.

Brian S CoxDepartment of Biosciences, University of Kent, Canterbury, Kent, UK.
Lee J Byrne
Mick F Tuite
University of Kent · GB

Funding

Biotechnology and Biological Sciences Research Council E18382
6 · The paper itself

Abstract

The rate of spontaneous change from psi(-) to the psi(+) condition, determined in yeast by states of the Sup35p protein, is briefly discussed together with the conditions necessary for such change to occur. Conditions that promote and which affect the rate of induction of psi(+) in Sup35p and of other prion-forming proteins to their respective prion forms are also discussed. These include the influence of the amount of non-prion protein, the presence of other prions, the activity of chaperones, and brief descriptions of the role of native sequences in the proteins and how alteration of sequences in prion-forming proteins influences the rate of induction of [prion(+)] and amyloid forms. The second part of this article discusses the conditions which affect the reversion of psi(+) to psi-, including factors which affect the copy-number of prion "seeds" or propagons and their partition. The principal factor discussed is the activity of the chaperone Hsp104, but the existence of other factors, such protein sequence and of other, less well-studied agents is touched upon and comparisons are made, as appropriate, with studies with other yeast prions. We conclude with a discussion of models of maintenance, in particular that of Tanaka et al. published in Nature (2006), which provides much insight into the phenotypic and genetic parameters of the numerous "variants" of prions increasingly being described in the literature.

Indexed as

AmyloidHeat-Shock ProteinsPeptide Termination FactorsPrionsProtein StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidHeat-Shock ProteinsHsP104 protein, S cerevisiaePeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID19164897
PMCPMC2634590
OpenAlexW4206218714

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.