Evidence map›Paper›PMID 12655297›Full record

ReviewCell death and differentiation2003

Many cuts to ruin: a comprehensive update of caspase substrates.

U Fischer, R U Jänicke, K Schulze-Osthoff

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 324 papers.

0numbers the graph read from it
0cells of the map it votes in
324citing papers in PubMed
31.1field-weighted citation impact, top 1% 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

324 citing papers in PubMed, 1,014 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Tissue turnover and rejuvenation through mechanics.Frontiers in cell and developmental biology · 2026
    Review
  7. Frontiers in cell and developmental biology · 2026
    Article
  8. Review
  9. Article
  10. Review
  11. DR5 is a restriction factor for human herpesviruses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Exploring caspase functions in mouse models.Apoptosis : an international journal on programmed cell death · 2024
    Review
  18. Article
  19. Article
  20. Article

264 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

U FischerInstitute of Molecular Medicine, University of Düsseldorf, Germany.
R U Jänicke
K Schulze-Osthoff
Heinrich Heine University Düsseldorf · DEHochschule Düsseldorf University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apoptotic cell death is executed by the caspase-mediated cleavage of various vital proteins. Elucidating the consequences of this endoproteolytic cleavage is crucial for our understanding of cell death and other biological processes. Many caspase substrates are just cleaved as bystanders, because they happen to contain a caspase cleavage site in their sequence. Several targets, however, have a discrete function in propagation of the cell death process. Many structural and regulatory proteins are inactivated by caspases, while other substrates can be activated. In most cases, the consequences of this gain-of-function are poorly understood. Caspase substrates can regulate the key morphological changes in apoptosis. Several caspase substrates also act as transducers and amplifiers that determine the apoptotic threshold and cell fate. This review summarizes the known caspase substrates comprising a bewildering list of more than 280 different proteins. We highlight some recent aspects inferred by the cleavage of certain proteins in apoptosis. We also discuss emerging themes of caspase cleavage in other forms of cell death and, in particular, in apparently unrelated processes, such as cell cycle regulation and cellular differentiation.

Indexed as

AnimalsApoptosisBinding SitesCaspasesEukaryotic CellsHumansProteinsSignal TransductionCaspasesProteins

Identifiers

PMID12655297
PMCPMC7091709
OpenAlexW2142911981

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.