Evidence map›Paper›PMID 35939694›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

dsRNA-induced condensation of antiviral proteins modulates PKR activity.

Giulia A Corbet, James M Burke, Gaia R Bublitz, Jian Wei Tay, Roy Parker

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.3field-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

51 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Nonsense-mediated decay controls a negative feedback loop in innate immune sensing.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  18. Article
  19. Article
  20. Review
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

5 authors at 2 institutions in 1 country.

Giulia A CorbetDepartment of Biochemistry, University of Colorado, Boulder, CO 80309.
James M BurkeDepartment of Biochemistry, University of Colorado, Boulder, CO 80309.
Gaia R BublitzDepartment of Biochemistry, University of Colorado, Boulder, CO 80309.
Jian Wei TayBioFrontiers Institute, Boulder, CO 80309.
Roy ParkerDepartment of Biochemistry, University of Colorado, Boulder, CO 80309.ORCID 0000-0002-8412-4152
University of Colorado Boulder · USHoward Hughes Medical Institute · US

Funding

Stress Granules in Yeast and MammalsR01GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 1991 to 2021
$3.3M
mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
Determining the specificity and biological functions of widespread host mRNA degradation by RNase LF32AI145112 · NIAID · UNIVERSITY OF COLORADO · PI BURKE, JAMES M · 2019 to 2021
$200k
Howard Hughes Medical InstituteNIAID NIH HHS F32 AI145112NIGMS NIH HHS R01 GM045443NIGMS NIH HHS R37 GM045443
6 · The paper itself

Abstract

Mammalian cells respond to dsRNA in multiple manners. One key response to dsRNA is the activation of PKR, an eIF2α kinase, which triggers translational arrest and the formation of stress granules. However, the process of PKR activation in cells is not fully understood. In response to increased endogenous or exogenous dsRNA, we observed that PKR forms novel cytosolic condensates, referred to as dsRNA-induced foci (dRIFs). dRIFs contain dsRNA, form in proportion to dsRNA, and are enhanced by longer dsRNAs. dRIFs enrich several other dsRNA-binding proteins, including ADAR1, Stau1, NLRP1, and PACT. Strikingly, dRIFs correlate with and form before translation repression by PKR and localize to regions of cells where PKR activation is initiated. We hypothesize that dRIF formation is a mechanism that cells use to enhance the sensitivity of PKR activation in response to low levels of dsRNA or to overcome viral inhibitors of PKR activation.

Indexed as

eIF-2 KinaseRNA, Double-StrandedRNA, ViralVirus DiseasesEnzyme ActivationHumansImmunity, InnatePhosphorylationProtein BiosynthesisRNA-Binding ProteinsStress GranuleseIF-2 KinaseRNA-Binding ProteinsRNA, Double-StrandedRNA, ViralcondensatedsRNAPKR

Identifiers

PMID35939694
PMCPMC9388085
OpenAlexW4290725198

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.