Evidence map›Paper›PMID 21593793›Full record

ArticleCell death & disease2011

The propeptide of yeast cathepsin D inhibits programmed necrosis.

D Carmona-Gutiérrez, M A Bauer, J Ring, H Knauer, T Eisenberg, S Büttner, C Ruckenstuhl, A Reisenbichler, C Magnes, G N Rechberger and 6 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. The YeastInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Cellular models of Batten disease.Biochimica et biophysica acta. Molecular basis of disease · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Deletion ofBiotechnology for biofuels · 2019
    Article
  15. Article
  16. Review
  17. 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

16 authors at 4 institutions in 2 countries.

D Carmona-GutiérrezInstitute of Molecular Biosciences, University of Graz, Graz, Austria.
M A Bauer
J Ring
H Knauer
T Eisenberg
S Büttner
C Ruckenstuhl
A Reisenbichler
C Magnes
G N Rechberger
R Birner-Gruenberger
H Jungwirth
K-U Fröhlich
F Sinner
G Kroemer
F Madeo
University of Graz · ATJoanneum Research · ATCentre de Recherche des Cordeliers · FRMedical University of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lysosomal endoprotease cathepsin D (CatD) is an essential player in general protein turnover and specific peptide processing. CatD-deficiency is associated with neurodegenerative diseases, whereas elevated CatD levels correlate with tumor malignancy and cancer cell survival. Here, we show that the CatD ortholog of the budding yeast Saccharomyces cerevisiae (Pep4p) harbors a dual cytoprotective function, composed of an anti-apoptotic part, conferred by its proteolytic capacity, and an anti-necrotic part, which resides in the protein's proteolytically inactive propeptide. Thus, deletion of PEP4 resulted in both apoptotic and necrotic cell death during chronological aging. Conversely, prolonged overexpression of Pep4p extended chronological lifespan specifically through the protein's anti-necrotic function. This function, which triggered histone hypoacetylation, was dependent on polyamine biosynthesis and was exerted via enhanced intracellular levels of putrescine, spermidine and its precursor S-adenosyl-methionine. Altogether, these data discriminate two pro-survival functions of yeast CatD and provide first insight into the physiological regulation of programmed necrosis in yeast.

Indexed as

Aspartic Acid EndopeptidasesSaccharomyces cerevisiae ProteinsAcetylationApoptosisBiogenic PolyaminesCathepsin DCell SurvivalCellular SenescenceGene DeletionGene ExpressionHistonesLysosomesNecrosisPlasmidsProtein EngineeringProtein PrecursorsAspartic Acid EndopeptidasesBiogenic PolyaminesCathepsin DHistonesPEP4 protein, S cerevisiaeProtein PrecursorsSaccharomyces cerevisiae Proteins

Identifiers

PMID21593793
PMCPMC3122122
OpenAlexW1988468826

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.