Evidence map›Paper›PMID 19023332›Full record

ReviewCell death and differentiation2009

The enigma of caspase-2: the laymen's view.

G Krumschnabel, B Sohm, F Bock, C Manzl, A Villunger

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.5field-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

62 citing papers in PubMed, 124 citations in OpenAlex.

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  18. Mechanism of caspase-2 activation upon DNA damage.Doklady. Biochemistry and biophysics · 2016
    Article
  19. Review
  20. Article

2 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

5 authors at 1 institution in 1 country.

G KrumschnabelDivision of Developmental Immunology, Biocenter, Innsbruck Medical University, Innsbruck, Austria.
B Sohm
F Bock
C Manzl
A Villunger
Innsbruck Medical University · AT

Funding

Austrian Science Fund FWF Y 212
6 · The paper itself

Abstract

Proteolysis of cellular substrates by caspases (cysteine-dependent aspartate-specific proteases) is one of the hallmarks of apoptotic cell death. Although the activation of apoptotic caspases is considered a 'late-stage' event in apoptosis signaling, past the commitment stage, one caspase family member, caspase-2, splits the cell death community into half - those searching for evidence of an apical initiator function of this molecule and those considering it as an amplifier of the apoptotic caspase cascade, at best, if relevant for apoptosis at all. This review screens past and present biochemical as well as genetic evidence for caspase-2 function in cell death signaling and beyond.

Indexed as

ApoptosisCaspase 2Cell DeathCRADD Signaling Adaptor ProteinDNA DamageSignal TransductionTumor Suppressor Protein p53Caspase 2CRADD Signaling Adaptor ProteinTumor Suppressor Protein p53

Identifiers

PMID19023332
PMCPMC3272397
OpenAlexW1987022495

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.