Evidence map›Paper›PMID 21597462›Full record

ReviewCell death and differentiation2011

Metacaspases.

L Tsiatsiani, F Van Breusegem, P Gallois, A Zavialov, E Lam, P V Bozhkov

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
10.9field-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

166 citing papers in PubMed, 316 citations in OpenAlex.

  1. Article
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  14. An inclusive assessment of apoptosis mechanisms inCurrent research in parasitology & vector-borne diseases · 2025
    Review
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  19. Article
  20. Roles of CgEde1 and CgMca in Development and Virulence ofInternational journal of molecular sciences · 2024
    Article

106 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

6 authors at 5 institutions in 4 countries.

L TsiatsianiDepartment of Plant Systems Biology, VIB, Ghent, Belgium.
F Van Breusegem
P Gallois
A Zavialov
E Lam
P V Bozhkov
Swedish University of Agricultural Sciences · SEGhent University · BERutgers, The State University of New Jersey · USUniversity of Manchester · GBVIB-UGent Center for Plant Systems Biology · BE

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Metacaspases are cysteine-dependent proteases found in protozoa, fungi and plants and are distantly related to metazoan caspases. Although metacaspases share structural properties with those of caspases, they lack Asp specificity and cleave their targets after Arg or Lys residues. Studies performed over the past 10 years have demonstrated that metacaspases are multifunctional proteases essential for normal physiology of non-metazoan organisms. This article provides a comprehensive overview of the metacaspase function and molecular regulation during programmed cell death, stress and cell proliferation, as well as an analysis of the first metacaspase-mediated proteolytic pathway. To prevent further misapplication of caspase-specific molecular probes for measuring and inhibiting metacaspase activity, we provide a list of probes suitable for metacaspases.

Indexed as

AnimalsApoptosisCaspasesFungal ProteinsHumansIsoenzymesModels, MolecularPlant ProteinsProtein ConformationProtozoan ProteinsCaspasesFungal ProteinsIsoenzymesPlant ProteinsProtozoan Proteins

Identifiers

PMID21597462
PMCPMC3172103
OpenAlexW4232254803

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.