Evidence map›Paper›PMID 31494035›Full record

ArticleMolecular cell2019

RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs.

James M Burke, Stephanie L Moon, Tyler Matheny, Roy Parker

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
6.3field-weighted citation impact, top 2% 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

115 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
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  7. Article
  8. Review
  9. Article
  10. SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Review
  12. Article
  13. Article
  14. RNase L Regulates Antiviral Responsiveness through Cleavage of XBP1 mRNA.bioRxiv : the preprint server for biology · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

55 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

James M BurkeDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Stephanie L MoonDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Tyler MathenyDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Roy ParkerDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA; Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA. Electronic address: roy.parker@colorado.edu.
University of Colorado Boulder · USHoward Hughes Medical Institute · US

Funding

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
NIAID NIH HHS F32 AI145112
6 · The paper itself

Abstract

In response to foreign and endogenous double-stranded RNA (dsRNA), protein kinase R (PKR) and ribonuclease L (RNase L) reprogram translation in mammalian cells. PKR inhibits translation initiation through eIF2α phosphorylation, which triggers stress granule (SG) formation and promotes translation of stress responsive mRNAs. The mechanisms of RNase L-driven translation repression, its contribution to SG assembly, and its regulation of dsRNA stress-induced mRNAs are unknown. We demonstrate that RNase L drives translational shut-off in response to dsRNA by promoting widespread turnover of mRNAs. This alters stress granule assembly and reprograms translation by allowing translation of mRNAs resistant to RNase L degradation, including numerous antiviral mRNAs such as interferon (IFN)-β. Individual cells differentially activate dsRNA responses revealing variation that can affect cellular outcomes. This identifies bulk mRNA degradation and the resistance of antiviral mRNAs as the mechanism by which RNase L reprograms translation in response to dsRNA.

Indexed as

Cellular ReprogrammingProtein BiosynthesisA549 CellseIF-2 KinaseEndoribonucleasesHEK293 CellsHumansInterferon-betaRNA, Double-StrandedRNA, MessengerRNA Stability2-5A-dependent ribonucleaseeIF-2 KinaseEndoribonucleasesInterferon-betaRNA, Double-StrandedRNA, MessengerdsRNAeIF2ainnate immune responseinterferonmRNA degradationmRNA metabolismPABPC1PKRRNase Lstress granule

Identifiers

PMID31494035
PMCPMC6754297
OpenAlexW2971561550

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.