Evidence map›Paper›PMID 15798218›Full record

ArticleMolecular and cellular biology2005

Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo.

Dietrich B Conze, Lori Albert, David A Ferrick, David V Goeddel, Wen-Chen Yeh, Tak Mak, Jonathan D Ashwell

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
6.2field-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

89 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
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  3. Article
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  6. Tumour-associated CD204Neuropathology and applied neurobiology · 2022
    Article
  7. Article
  8. Article
  9. Article
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  11. Targeting the BIR Domains of Inhibitor of Apoptosis (IAP) Proteins in Cancer Treatment.Computational and structural biotechnology journal · 2019
    Review
  12. Getting MAD at MYC.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Review
  14. Article
  15. Review
  16. Modulation of apoptotic response by LAR family phosphatases-cIAP1 signaling during urinary tract morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Review
  19. Article
  20. Poly-ubiquitination in TNFR1-mediated necroptosis.Cellular and molecular life sciences : CMLS · 2016
    Review

29 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

7 authors at 4 institutions in 4 countries.

Dietrich B ConzeLaboratory of Immune Cell Biology, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Building 37, Room 3002, Bethesda, MD 20892, USA.
Lori Albert
David A Ferrick
David V Goeddel
Wen-Chen Yeh
Tak Mak
Jonathan D Ashwell
Ontario Institute for Cancer Research · CANational Institutes of Health · USDiscovery Laboratories (United States) · USUniversity of Tikrit · IQ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inhibitor of apoptosis proteins (IAPs) c-IAP1 and c-IAP2 were identified as part of the tumor necrosis factor receptor 2 (TNFR2) signaling complex and have been implicated as intermediaries in tumor necrosis factor alpha signaling. Like all RING domain-containing IAPs, c-IAP1 and c-IAP2 have ubiquitin protein ligase (E3) activity. To explore the function of c-IAP1 in a physiologic setting, c-IAP1-deficient mice were generated by homologous gene recombination. These animals are viable and have no obvious sensitization to proapoptotic stimuli. Cells from c-IAP1(-/-) mice do, however, express markedly elevated levels of c-IAP2 protein in the absence of increased c-IAP2 mRNA. In contrast to reports implicating c-IAPs in the activation of NF-kappaB, resting and cytokine-induced NF-kappaB activation was not impaired in c-IAP1-deficient cells. Transient transfection studies with wild-type and E3-defective c-IAP1 revealed that c-IAP2 is a direct target for c-IAP1-mediated ubiquitination and subsequent degradation, which are potentiated by the adaptor function of TRAF2. Thus, the c-IAPs represent a pair of TNFR-associated ubiquitin protein ligases in which one regulates the expression of the other by a posttranscriptional and E3-dependent mechanism.

Indexed as

Down-RegulationAnimalsBaculoviral IAP Repeat-Containing 3 ProteinB-LymphocytesInhibitor of Apoptosis ProteinsMiceMice, Mutant StrainsNF-kappa BProteinsRNA, MessengerSequence DeletionSignal TransductionSpleenThymus GlandT-LymphocytesTNF Receptor-Associated Factor 2Baculoviral IAP Repeat-Containing 3 ProteinBirc2 protein, mouseBirc3 protein, mouseInhibitor of Apoptosis ProteinsNF-kappa BProteinsRNA, MessengerTNF Receptor-Associated Factor 2Ubiquitin-Protein Ligases

Identifiers

PMID15798218
PMCPMC1069614
OpenAlexW2149998180

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.