Evidence map›Paper›PMID 9372964›Full record

ArticleMolecular and cellular biology1997

ch-IAP1, a member of the inhibitor-of-apoptosis protein family, is a mediator of the antiapoptotic activity of the v-Rel oncoprotein.

M You, P T Ku, R Hrdlicková, H R Bose

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 179 citations in OpenAlex.

  1. Article
  2. Article
  3. Targeting the BIR Domains of Inhibitor of Apoptosis (IAP) Proteins in Cancer Treatment.Computational and structural biotechnology journal · 2019
    Review
  4. Article
  5. Oncotarget · 2017
    Article
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  7. Review
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  16. Proteasome inhibition and allogeneic hematopoietic stem cell transplantation: a review.Biology of blood and marrow transplantation : journal of the American Society for Blood and Marrow Transplantation · 2009
    Review
  17. Article
  18. Article
  19. Article
  20. Article

3 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

4 authors at 1 institution in 1 country.

M YouDepartment of Microbiology and Institute for Cellular and Molecular Biology, The University of Texas at Austin, 78712-1095, USA.
P T Ku
R Hrdlicková
H R Bose
The University of Texas at Austin · US

Funding

NCI NIH HHS CA331921NIA NIH HHS AG05707
6 · The paper itself

Abstract

The oncoprotein v-Rel, a member of the Rel/NF-kappaB family of transcription factors, induces neoplasias and inhibits apoptosis. To identify differentially regulated cellular genes and to evaluate their relevance to transformation and apoptosis in v-Rel-transformed cells, mRNA differential display has been used. One of the recovered cDNAs corresponds to a gene that was highly expressed in v-Rel-transformed fibroblasts. Analysis of the isolated full-length cDNA of a chicken inhibitor-of-apoptosis protein (ch-IAP1) revealed that it encodes a 68-kDa protein that is highly homologous to members of the IAP family, such as human c-LAP1. Like other IAPs, ch-IAP1 contains the N-terminal baculovirus IAP repeats and C-terminal RING finger motifs. Northern blot analysis identified a 3.3-kb ch-IAP1 transcript expressed at relatively high levels in the spleen, thymus, bursa, intestine, and lungs. Expression of v-Rel in fibroblasts, a B-cell line, and spleen cells up-regulated the expression of ch-IAP1. In contrast, ch-IAP1 expression levels were low in chicken cell lines transformed by several other unrelated tumor viruses. ch-IAP1 was expressed predominantly in the cytoplasm of the v-Rel-transformed cells. ch-IAP1 suppressed mammalian cell apoptosis induced by the overexpression of the interleukin-1-converting enzyme. Expression of exogenous ch-IAP1 in temperature-sensitive v-Rel transformed spleen cells inhibited apoptosis of these cells at the nonpermissive temperature. Collectively, these results suggest that ch-IAP1 is induced during the v-Rel-mediated transformation process and functions as a suppressor of apoptosis in v-Rel-transformed cells.

Indexed as

Amino Acid SequenceAnimalsApoptosisBase SequenceCaspase 1Cell Line, TransformedChickensCysteine EndopeptidasesDNA, ComplementaryDNA PrimersGene ExpressionHumansInhibitor of Apoptosis ProteinsMolecular Sequence DataOncogene Proteins v-relPolymerase Chain ReactionBIRC2 protein, humanCaspase 1Cysteine EndopeptidasesDNA, ComplementaryDNA PrimersInhibitor of Apoptosis ProteinsOncogene Proteins v-relProteinsRetroviridae Proteins, OncogenicRNA, MessengerUbiquitin-Protein Ligases

Identifiers

PMID9372964
PMCPMC232589
OpenAlexW2097961822

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.