Evidence map›Paper›PMID 21454674›Full record

ArticleThe Journal of biological chemistry2011

Molecular basis for transmission barrier and interference between closely related prion proteins in yeast.

Evgenia G Afanasieva, Vitaly V Kushnirov, Mick F Tuite, Michael D Ter-Avanesyan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Nonsense Mutations in the YeastInternational journal of molecular sciences · 2020
    Article
  3. Design of a New [Frontiers in molecular neuroscience · 2019
    Article
  4. Article
  5. Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016
    Review
  6. Article
  7. Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016
    Review
  8. Article
  9. Article
  10. Article
  11. Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Prions in yeast.Genetics · 2012
    Review
  17. Article
  18. 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 at 2 institutions in 2 countries.

Evgenia G AfanasievaCardiology Research Center, Moscow, Russia.
Vitaly V Kushnirov
Mick F Tuite
Michael D Ter-Avanesyan
Institute of Experimental Cardiology · RUUniversity of Kent · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Replicating amyloids, called prions, are responsible for transmissible neurodegenerative diseases in mammals and some heritable phenotypes in fungi. The transmission of prions between species is usually inhibited, being highly sensitive to small differences in amino acid sequence of the prion-forming proteins. To understand the molecular basis of this prion interspecies barrier, we studied the transmission of the [PSI(+)] prion state from Sup35 of Saccharomyces cerevisiae to hybrid Sup35 proteins with prion-forming domains from four other closely related Saccharomyces species. Whereas all the hybrid Sup35 proteins could adopt a prion form in S. cerevisiae, they could not readily acquire the prion form from the [PSI(+)] prion of S. cerevisiae. Expression of the hybrid Sup35 proteins in S. cerevisiae [PSI(+)] cells often resulted in frequent loss of the native [PSI(+)] prion. Furthermore, all hybrid Sup35 proteins showed different patterns of interaction with the native [PSI(+)] prion in terms of co-polymerization, acquisition of the prion state, and induced prion loss, all of which were also dependent on the [PSI(+)] variant. The observed loss of S. cerevisiae [PSI(+)] can be related to inhibition of prion polymerization of S. cerevisiae Sup35 and formation of a non-heritable form of amyloid. We have therefore identified two distinct molecular origins of prion transmission barriers between closely sequence-related prion proteins: first, the inability of heterologous proteins to co-aggregate with host prion polymers, and second, acquisition by these proteins of a non-heritable amyloid fold.

Indexed as

Protein FoldingAmyloidPeptide Termination FactorsPrionsProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityAmyloidPeptide Termination FactorsPrionsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID21454674
PMCPMC3091186
OpenAlexW2144990397

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.