Evidence map›Paper›PMID 20495349›Full record

ArticlePrion

The effects of amino acid composition on yeast prion formation and prion domain interactions.

Eric D Ross, James A Toombs

Abstract read
In one paragraph

Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
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  6. Review
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  13. Review
  14. What makes a protein sequence a prion?PLoS computational biology · 2015
    Article
  15. Article
  16. Article
  17. Ion-specific effects on prion nucleation and strain formation.The Journal of biological chemistry · 2013
    Article
  18. Article
  19. De novo design of synthetic prion domains.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

2 authors.

Eric D RossDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA. eric.ross@colostate.edu
James A Toombs

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast prions provide a powerful model system for examining prion formation and propagation in vivo. Yeast prion formation is driven primarily by amino acid composition, not by primary amino acid sequence. However, although yeast prion domains are consistently glutamine/asparagine-rich, they otherwise vary significantly in their compositions. Therefore, elucidating the exact compositional requirements for yeast prion formation has proven challenging. We have developed an in vivo method that allows for estimation of the prion propensity of each amino acid within the context of a yeast prion domain.(1) Using these values, we are able to predict the prion-propensity of various glutamine/asparagine-rich yeast domains. These results provide insight into the basis for yeast prion formation, and may aid in the discovery of additional novel prion domains. Additionally, we examined whether amino acid composition could drive interactions between heterologous glutamine/asparagine-rich proteins.(2) Although inefficient interactions between yeast prion domains have previously been observed, we found that one prion protein, Ure2, is able to interact with compositionally similar domains with unprecedented efficiency. This observation, combined with the growing number of yeast prions, suggests that a broad network of interactions between heterologous glutamine/asparagine-rich proteins may affect yeast prion formation.

Indexed as

Amino AcidsAsparagineComputational BiologyFungal ProteinsGlutamineGlutathione PeroxidasePrionsProtein Interaction Domains and MotifsSaccharomyces cerevisiae ProteinsAmino AcidsAsparagineFungal ProteinsGlutamineGlutathione PeroxidasePrionsSaccharomyces cerevisiae ProteinsURE2 protein, S cerevisiae

Identifiers

PMID20495349
PMCPMC2933052

What OpenQuestion holds

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Registered trials

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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.