Evidence map›Paper›PMID 18798523›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2008

Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.

Reed B Wickner, Frank Shewmaker, Dmitry Kryndushkin, Herman K Edskes

Open access · greenAbstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Anti-prion systems in yeast.The Journal of biological chemistry · 2019
    Review
  10. Review
  11. Review
  12. Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. Article
  15. Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  16. Article
  17. 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
  18. Review
  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

4 authors at 2 institutions in 1 country.

Reed B WicknerLaboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA. wickner@helix.nih.gov
Frank Shewmaker
Dmitry Kryndushkin
Herman K Edskes
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Prions of Yeast and Anti-Prion SystemsZIADK024950 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WICKNER, REED B. · 2009 to 2025
$25.2M
Structure of Prion AmyloidsZIADK024949 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WICKNER, REED B. · 2009 to 2009
$285k
Intramural NIH HHS ZIA DK024950
6 · The paper itself

Abstract

Most prions (infectious proteins) are self-propagating amyloids (filamentous protein multimers), and have been found in both mammals and fungal species. The prions [URE3] and [PSI+] of yeast are disease agents of Saccharomyces cerevisiae while [Het-s] of Podospora anserina may serve a normal cellular function. The parallel in-register beta-sheet structure shown by prion amyloids makes possible a templating action at the end of filaments which explains the faithful transmission of variant differences in these molecules. This property of self-reproduction, in turn, allows these proteins to act as de facto genes, encoding heritable information.

Indexed as

AmyloidGlutathione PeroxidasePeptide Termination FactorsPodosporaPrionsProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidGlutathione PeroxidasePeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeURE2 protein, S cerevisiae

Identifiers

PMID18798523
PMCPMC3086512
OpenAlexW2135893969

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.