Evidence map›Paper›PMID 27352624›Full record

ReviewCold Spring Harbor perspectives in biology2016

The HET-S/s Prion Motif in the Control of Programmed Cell Death.

Roland Riek, Sven J Saupe

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2016. 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
–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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  5. Article
  6. Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Proliferation and dissemination of killer meiotic drive loci.Current opinion in genetics & development · 2023
    Review
  12. Review
  13. Review
  14. Molecular Mechanisms and Evolutionary Consequences of Spore Killers in Ascomycetes.Microbiology and molecular biology reviews : MMBR · 2021
    Review
  15. Article
  16. Article
  17. Review
  18. Structural and molecular basis of cross-seeding barriers in amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. TheeLife · 2020
    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 at 2 institutions in 2 countries.

Roland RiekLaboratory of Physical Chemistry, ETH Zürich, 8093 Zürich, Switzerland.
Sven J SaupeInstitut de Biochimie et de Génétique Cellulaire UMR 5095, CNRS - Université de Bordeaux, 33077 Bordeaux, France.
ETH Zurich · CHUniversité de Bordeaux · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The [Het-s] prion of the fungus Podospora anserina is a well-studied model system to elucidate the action of prions and beyond. The [Het-s] prion works as an activation trigger of a cell death execution protein termed HET-S. Amyloid transconformation of the prion-forming region of HET-S induces activation of its pore-forming cell death execution HeLo domain. The prion motif functions in a signal transduction process by which a nucleotide-binding oligomerization domain (NOD)-like receptor termed NWD2 controls the HET-S cell death effector. This prion motif thus corresponds to a functional amyloid motif, allowing a conformational crosstalk between homologous motif domains in signal transduction processes that appears to be widespread from the fungal to the mammalian animal kingdoms. This review aims to establish a structure-activity relationship of the HET-S/s prion system and sets it in the context of its wider biological significance.

Indexed as

ApoptosisFungal ProteinsPodosporaPrionsSignal TransductionStructure-Activity RelationshipFungal ProteinsHET-S protein, Podospora anserinaPrions

Identifiers

PMID27352624
PMCPMC5008070
OpenAlexW2475319226

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.