Evidence map›Paper›PMID 19364921›Full record

ArticleThe Journal of cell biology2009

Caspase-2 activation in the absence of PIDDosome formation.

Claudia Manzl, Gerhard Krumschnabel, Florian Bock, Benedicte Sohm, Verena Labi, Florian Baumgartner, Emmanuelle Logette, Jürg Tschopp, Andreas Villunger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

97 citing papers in PubMed, 158 citations in OpenAlex.

  1. Review
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  9. Exploring caspase functions in mouse models.Apoptosis : an international journal on programmed cell death · 2024
    Review
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  16. Induction of apoptosis on ovarian adenocarcinoma cells, A2780 by tricyclohexylphosphanegold (I) mercaptobenzoate derivatives via intrinsic and extrinsic pathways.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
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37 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

9 authors at 2 institutions in 2 countries.

Claudia ManzlDivision of Developmental Immunology, Biocenter, Innsbruck Medical University, A-6020 Innsbruck, Austria.
Gerhard Krumschnabel
Florian Bock
Benedicte Sohm
Verena Labi
Florian Baumgartner
Emmanuelle Logette
Jürg Tschopp
Andreas Villunger
Innsbruck Medical University · ATUniversity of Lausanne · CH

Funding

Austrian Science Fund FWF Y 212
6 · The paper itself

Abstract

PIDD (p53-induced protein with a death domain [DD]), together with the bipartite adapter protein RAIDD (receptor-interacting protein-associated ICH-1/CED-3 homologous protein with a DD), is implicated in the activation of pro-caspase-2 in a high molecular weight complex called the PIDDosome during apoptosis induction after DNA damage. To investigate the role of PIDD in cell death initiation, we generated PIDD-deficient mice. Processing of caspase-2 is readily detected in the absence of PIDDosome formation in primary lymphocytes. Although caspase-2 processing is delayed in simian virus 40-immortalized pidd(-/-) mouse embryonic fibroblasts, it still depends on loss of mitochondrial integrity and effector caspase activation. Consistently, apoptosis occurs normally in all cell types analyzed, suggesting alternative biological roles for caspase-2 after DNA damage. Because loss of either PIDD or its adapter molecule RAIDD did not affect subcellular localization, nuclear translocation, or caspase-2 activation in high molecular weight complexes, we suggest that at least one alternative PIDDosome-independent mechanism of caspase-2 activation exists in mammals in response to DNA damage.

Indexed as

AnimalsApoptosisCarrier ProteinsCaspase 2Cells, CulturedCRADD Signaling Adaptor ProteinCytochromes cDeath Domain Receptor Signaling Adaptor ProteinsDNA DamageEnzyme ActivationFemaleFibroblastsGamma RaysHumansLymphocytesMiceCarrier ProteinsCaspase 2Cradd protein, mouseCRADD Signaling Adaptor ProteinCytochromes cDeath Domain Receptor Signaling Adaptor ProteinsMultiprotein ComplexesPidd1 protein, mouseProtein Precursors

Identifiers

PMID19364921
PMCPMC2700374
OpenAlexW2127072511

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.