Evidence map›Paper›PMID 24382890›Full record

ArticleThe Journal of biological chemistry2014

mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through protein kinase R (PKR) activation requires the N-terminal enabled vasodilator-stimulated protein homology 1 (EVH1) domain.

Jonathan D Dougherty, Lucas C Reineke, Richard E Lloyd

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
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  6. International journal of molecular sciences · 2023
    Article
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  16. Review
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  19. Article
  20. Cytoplasmic RNA Granules and Viral Infection.Annual review of virology · 2014
    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.

Jonathan D DoughertyFrom the Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030.
Lucas C Reineke
Richard E Lloyd
Baylor College of Medicine · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI DAVID R ROWLEY · 2007 to 2026
$73.9M
Tissue Analysis & Molecular Imaging CoreP30DK056338 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI Geoffrey A Preidis · 2001 to 2026
$28.3M
TRANSGENIC MOUSE MODELS TO STUDY OVARIAN FUNCTIONU54HD007495 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI RICHARDS, JOANNE STEWART · 1998 to 2013
$19.9M
Translation Regulation by Enterovirus ProteinaseR01AI050237 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI LLOYD, RICHARD E · 2002 to 2022
$6.9M
GROWTH AND DIFFERENTIATION IN EUKARYOTEST32HD007495 · NICHD · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI KINTNER, CHRISTOPHER ROBERT · 1995 to 2009
$1.6M
Translation Regulation by Enterovirus ProteinaseR56AI050237 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI LLOYD, RICHARD E · 2007 to 2007
$384k
TRANSGENIC ANIMAL--COREP30HD007495 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI GLASSER, STANLEY R · 1985 to 1997
–
NCI NIH HHS CA125123NCI NIH HHS P30 CA125123NCI NIH HHS P30CA1251230NIAID NIH HHS AI50237NIAID NIH HHS R01 AI050237NIAID NIH HHS R56 AI050237NICHD NIH HHS HD007495NICHD NIH HHS P30 HD007495NICHD NIH HHS T32 HD007495NICHD NIH HHS U54 HD007495NIDDK NIH HHS DK56338NIDDK NIH HHS P30 DK056338
6 · The paper itself

Abstract

We have shown previously that poliovirus infection disrupts cytoplasmic P-bodies in infected mammalian cells. During the infectious cycle, poliovirus causes the directed cleavage of Dcp1a and Pan3, coincident with the dispersion of P-bodies. We now show that expression of Dcp1a prior to infection, surprisingly, restricts poliovirus infection. This inhibition of infection was independent of P-body formation because expression of GFP-Dcp1a mutants that cannot enter P-bodies restricted poliovirus infection similar to wild-type GFP-Dcp1a. Expression of wild-type or mutant GFP-Dcp1a induced phosphorylation of eIF2α through the eIF2α kinase protein kinase R (PKR). Activation of PKR required the amino-terminal EVH1 domain of Dcp1a. This PKR-induced translational inhibition appears to be specific to Dcp1a because the expression of other P-body components, Pan2, Pan3, Ccr4, or Caf1, did not result in the inhibition of poliovirus gene expression or induce eIF2α phosphorylation. The translation blockade induced by Dcp1a expression suggests novel signaling linking RNA degradation/decapping and regulation of translation.

Indexed as

AnimalsCell LineeIF-2 KinaseEndoribonucleasesEnzyme ActivationEukaryotic Initiation Factor-2ExoribonucleasesMiceMice, KnockoutMutationPhosphorylationPoliomyelitisPoliovirusProtein BiosynthesisProteinsProtein Structure, TertiaryCcr4 protein, mouseCnot7 protein, mouseeIF-2 KinaseEndoribonucleasesEukaryotic Initiation Factor-2ExoribonucleasesProteinsReceptors, CCR4Repressor ProteinsRibonucleasessmad4-interacting protein SMIF, mouseTrans-ActivatorsMRNA DecayP-bodyPoliovirusPositive-strand RNA VirusesProtein Kinase R (PKR)Translation Regulation

Identifiers

PMID24382890
PMCPMC3924262
OpenAlexW1998246096

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.