Evidence map›Paper›PMID 14970392›Full record

ArticleRNA (New York, N.Y.)2004

Translation of cellular inhibitor of apoptosis protein 1 (c-IAP1) mRNA is IRES mediated and regulated during cell stress.

Marc E Van Eden, Marshall P Byrd, Kyle W Sherrill, Richard E Lloyd

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Targeting RNA helicases in cancer: The translation trap.Biochimica et biophysica acta. Reviews on cancer · 2017
    Review
  5. Article
  6. Review
  7. A researcher's guide to the galaxy of IRESs.Cellular and molecular life sciences : CMLS · 2017
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Evasion of apoptosis as a cellular stress response in cancer.International journal of cell biology · 2010
    Article
  18. Up-regulation of a cellular protein at the translational level by a retrovirus.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. Article
  20. Article
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.

Marc E Van EdenDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030-3498, USA.
Marshall P Byrd
Kyle W Sherrill
Richard E Lloyd
Baylor College of Medicine · US

Funding

Translation Regulation by Enterovirus ProteinaseR01AI050237 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI LLOYD, RICHARD E · 2002 to 2022
$6.9M
RESEARCH TRAINING PROGRAM IN MOLECULAR VIROLOGYT32AI007471 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI RAMIG, ROBERT FRANKLIN · 1996 to 2010
$2.6M
MECHANISMS OF TRANSLATION CONTROL DURING APOPTOSISR01GM059803 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LLOYD, RICHARD E · 1999 to 2007
$2.2M
Translation Regulation by Enterovirus ProteinaseR56AI050237 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI LLOYD, RICHARD E · 2007 to 2007
$384k
NIAID NIH HHS AI50237NIAID NIH HHS R01 AI050237NIAID NIH HHS R56 AI050237NIAID NIH HHS T32 AI007471NIAID NIH HHS T32 AI07471NIGMS NIH HHS GM59803NIGMS NIH HHS R01 GM059803
6 · The paper itself

Abstract

Cellular inhibitor of apoptosis protein 1 (c-IAP1) can regulate apoptosis through its interaction with downstream TNF receptor effectors (TRAF1 and TRAF2), by binding to and inhibiting certain caspases, and by controlling the levels of specific proapoptotic stimuli (e.g., Smac/DIABLO) within the cell. Studies involving the expression of c-IAP1 mRNA and protein in cells and tissues have provided evidence suggesting c-IAP1 expression may be posttranscriptionally controlled. Because the 5'-UTR of c-IAP1 mRNA is unusually long, contains multiple upstream AUG codons, and has the potential to form thermodynamically stable secondary structures, we investigated the possibility it contained an internal ribosome entry site (IRES) that may regulate its expression. In the present study, the c-IAP1 5'-UTR exhibited IRES activity when dicistronic RNA constructs were translated in rabbit reticulocyte lysate (RRL) and in transiently transfected cells. IRES-mediated translation was similar to that exhibited by the hepatitis C virus IRES but varied significantly in RRL and in HeLa, HepG2, and 293T cells, indicating the c-IAP1 IRES was system and cell type specific. IRES-mediated translation was maintained in mono- and dicistronic constructs in which the UTR was inserted downstream from a stable hairpin that prevented cap-dependent ribosome scanning. In cells, the presence or absence of a methylated cap did not significantly affect the translation of polyadenylated, monocistronic RNAs containing the c-IAP1 5'-UTR. IRES-mediated translation was stimulated in transfected cells treated with low doses of pro-apoptotic stimuli (i.e., etoposide and sodium arsenite) that inhibited endogenous cellular translation.

Indexed as

Base SequenceHeLa CellsHumansInhibitor of Apoptosis ProteinsMolecular Sequence DataProteinsReticulocytesRNA, MessengerTransfectionUbiquitin-Protein LigasesBIRC2 protein, humanInhibitor of Apoptosis ProteinsProteinsRNA, MessengerUbiquitin-Protein Ligases

Identifiers

PMID14970392
PMCPMC1370942
OpenAlexW2140857141

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.