Evidence map›Paper›PMID 20444092›Full record

ArticleMolecular microbiology2010

Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission.

Buxin Chen, Kathryn L Bruce, Gary P Newnam, Stefka Gyoneva, Andrey V Romanyuk, Yury O Chernoff

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Anti-Prion Systems inViruses · 2022
    Review
  4. Article
  5. How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020
    Review
  6. Article
  7. Article
  8. Review
  9. Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Review
  16. Article
  17. Ion-specific effects on prion nucleation and strain formation.The Journal of biological chemistry · 2013
    Article
  18. Article
  19. 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

6 authors at 1 institution in 1 country.

Buxin ChenSchool of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, 310 Ferst Drive, Atlanta, GA 30332-0230, USA.
Kathryn L Bruce
Gary P Newnam
Stefka Gyoneva
Andrey V Romanyuk
Yury O Chernoff
Georgia Institute of Technology · US

Funding

GENETIC STUDY OF THE YEAST PRION INTERACTING PROTEINSR01GM058763 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI CHERNOFF, YURY O · 1999 to 2010
$2.6M
NIGMS NIH HHS R01 GM058763NIGMS NIH HHS R01GM58763
6 · The paper itself

Abstract

Self-perpetuating amyloid-based protein isoforms (prions) transmit neurodegenerative diseases in mammals and phenotypic traits in yeast. Although mechanisms that control species specificity of prion transmission are poorly understood, studies of closely related orthologues of yeast prion protein Sup35 demonstrate that cross-species prion transmission is modulated by both genetic (specific sequence elements) and epigenetic (prion variants, or 'strains') factors. Depending on the prion variant, the species barrier could be controlled at the level of either heterologous co-aggregation or conversion of the aggregate-associated heterologous protein into a prion polymer. Sequence divergence influences cross-species transmission of different prion variants in opposing ways. The ability of a heterologous prion domain to either faithfully reproduce or irreversibly switch the variant-specific prion patterns depends on both sequence divergence and the prion variant. Sequence variations within different modules of prion domains contribute to transmission barriers in different cross-species combinations. Individual amino acid substitutions within short amyloidogenic stretches drastically alter patterns of cross-species prion conversion, implicating these stretches as major determinants of species specificity.

Indexed as

Gene Expression Regulation, FungalGene Transfer, HorizontalPolymorphism, GeneticAmino Acid SequenceAmyloidMolecular Sequence DataPeptide Termination FactorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentAmyloidPeptide Termination FactorsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID20444092
PMCPMC3025758
OpenAlexW2118785256

What OpenQuestion holds

Textmetadata
LicenceTDM
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.