Evidence map›Paper›PMID 10880459›Full record

ArticleThe EMBO journal2000

Adenovirus-specific translation by displacement of kinase Mnk1 from cap-initiation complex eIF4F.

R Cuesta, Q Xi, R J Schneider

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

58 citing papers in PubMed, 112 citations in OpenAlex.

  1. Trial
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  8. Phosphorylation and Signal Transduction Pathways in Translational Control.Cold Spring Harbor perspectives in biology · 2019
    Review
  9. Article
  10. Review
  11. Article
  12. Developing anti-neoplastic biotherapeutics against eIF4F.Cellular and molecular life sciences : CMLS · 2017
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Tinkering with translation: protein synthesis in virus-infected cells.Cold Spring Harbor perspectives in biology · 2013
    Review
  19. Review
  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

3 authors at 1 institution in 1 country.

R CuestaDepartment of Microbiology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Q Xi
R J Schneider
New York University · US

Funding

TRANSLATIONAL REGULATION OF ADENOVIRUS GENE EXPRESSIONR01CA042357 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SCHNEIDER, ROBERT · 1986 to 2004
$1.6M
NCI NIH HHS CA 42357NCI NIH HHS R01 CA042357
6 · The paper itself

Abstract

Translation of cellular mRNAs involves formation of a cap-binding translation initiation complex known as eIF4F, containing phosphorylated cap-binding protein eIF4E, eIF4E kinase Mnk1, eIF4A, poly(A)-binding protein and eIF4G. Adenovirus is shown to prevent cellular translation by displacing Mnk1 from eIF4F, thereby blocking phosphorylation of eIF4E. Over expression of an eIF4E mutant that cannot be phosphorylated by Mnk1 impairs translation of cellular but not viral late mRNAs. Adenovirus 100k protein is shown to bind the C-terminus of eIF4G in vivo and in vitro, the same region bound by Mnk1. In vivo, 100k protein displaces Mnk1 from eIF4G during adenovirus infection, or in transfected cells. Purified 100k protein also evicts Mnk1 from isolated eIF4F complexes in vitro. A mutant adenovirus with a temperature-sensitive 100k protein that cannot inhibit cellular protein synthesis at restrictive temperature no longer blocks Mnk1 binding to eIF4G, or phosphorylation of eIF4E. We describe a mechanism whereby adenovirus selectively inhibits the translation of cellular but not viral mRNAs by displacement of Mnk1 from eIF4G and inhibition of eIF4E phosphorylation.

Indexed as

AdenoviridaeAdenoviridae InfectionsBase SequenceCell LineDNA PrimersEukaryotic Initiation Factor-4FHumansIntracellular Signaling Peptides and ProteinsPeptide Initiation FactorsProtein BindingProtein BiosynthesisProtein Serine-Threonine KinasesRecombinant Fusion ProteinsDNA PrimersEukaryotic Initiation Factor-4FIntracellular Signaling Peptides and ProteinsMKNK1 protein, humanPeptide Initiation FactorsProtein Serine-Threonine KinasesRecombinant Fusion Proteins

Identifiers

PMID10880459
PMCPMC313943
OpenAlexW2034289420

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.