Evidence map›Paper›PMID 23706307›Full record

ArticleVirology2013

RNA-dependent protein kinase PKR and the Z-DNA binding orthologue PKZ differ in their capacity to mediate initiation factor eIF2α-dependent inhibition of protein synthesis and virus-induced stress granule formation.

Nora Taghavi, Charles E Samuel

Abstract read
In one paragraph

Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Z-DNA and Z-RNA: Methods-Past and Future.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Article
  6. Review
  7. Protein Synthesis and Translational Control: A Historical Perspective.Cold Spring Harbor perspectives in biology · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. 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

2 authors at 1 institution in 1 country.

Nora TaghaviDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, California 93106, USA.
Charles E Samuel
University of California, Santa Barbara · US

Funding

INTERFERON ACTION AND PROTEIN PHOSPHORYLATIONR01AI020611 · NIAID · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI SAMUEL, CHARLES E · 1985 to 2014
$3.4M
MECHANISM OF INTERFERON ACTIONR01AI012520 · NIAID · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI SAMUEL, CHARLES E · 1985 to 2009
$3.1M
MECHANISM OF INTERFERON ACTIONR37AI012520 · NIAID · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI SAMUEL, CHARLES E. · 1989 to 1998
–
NIAID NIH HHS AI-12520NIAID NIH HHS AI-20611NIAID NIH HHS R01 AI012520NIAID NIH HHS R01 AI020611NIAID NIH HHS R37 AI012520
6 · The paper itself

Abstract

Protein kinase R (PKR), a regulator of translation in mammalian cells, possesses two ds-RNA binding domains responsible for kinase activation. Protein kinase Z (PKZ), a PKR-like kinase present in fish, possesses two Z-DNA binding domains. A complementation strategy with cells stably deficient in PKR was used to compare the functions of PKR and PKZ. We found reporter expression was inhibited by wildtype (WT) PKR but not by either catalytic (K296R) or RNA-binding (K64E) mutants. PKZ, like PKR, more potently inhibited 5' cap-dependent compared to IRES-dependent reporter expression. However, in contrast to PKR-expressing cells, phosphorylation of initiation factor eIF2α was not detectably increased in PKZ-expressing cells. Furthermore, virus-induced stress granule formation was observed in PKR-deficient cells complemented with WT PKR but not K296R mutant PKR or WT PKZ. These results suggest that PKR and PKZ function by distinguishable mechanisms to modulate host responses including protein synthesis inhibition and stress granule formation.

Indexed as

Protein BiosynthesisAnimalsCytoplasmic GranulesDNA-Activated Protein KinaseeIF-2 KinaseEukaryotic Initiation Factor-2Genetic Complementation TestHeLa CellsHumansMeasles virusVirus ReplicationZebrafishDNA-Activated Protein KinaseeIF-2 KinaseEukaryotic Initiation Factor-2

Identifiers

PMID23706307
PMCPMC3700635
OpenAlexW2066756921

What OpenQuestion holds

Textmetadata
LicenceTDM
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.