Evidence map›Paper›PMID 28808124›Full record

ArticleRNA (New York, N.Y.)2017

Rapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machinery.

Jesse Donovan, Sneha Rath, David Kolet-Mandrikov, Alexei Korennykh

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
4.6field-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

113 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. tRNA modifications in viral replication.The Journal of biological chemistry · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. RNase L Regulates Antiviral Responsiveness through Cleavage of XBP1 mRNA.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. iScience · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

53 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 1 institution in 1 country.

Jesse DonovanDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Sneha RathDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
David Kolet-MandrikovDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Alexei KorennykhDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA akorenny@princeton.edu.
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Structure and Function of Kinase Family Receptors Regulating TranslationR01GM110161 · NIGMS · PRINCETON UNIVERSITY · PI KORENNYKH, ALEXEI · 2014 to 2022
$2.5M
Beyond infection: Innate immune receptors as an emerging brake on metastasisF99CA212468 · NCI · PRINCETON UNIVERSITY · PI RATH, SNEHA PRAKASH · 2016 to 2017
$89k
NCI NIH HHS F99 CA212468NIGMS NIH HHS R01 GM110161NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Mammalian cells respond to double-stranded RNA (dsRNA) by activating a translation-inhibiting endoribonuclease, RNase L. Consensus in the field indicates that RNase L arrests protein synthesis by degrading ribosomal RNAs (rRNAs) and messenger RNAs (mRNAs). However, here we provide evidence for a different and far more efficient mechanism. By sequencing abundant RNA fragments generated by RNase L in human cells, we identify site-specific cleavage of two groups of noncoding RNAs: Y-RNAs, whose function is poorly understood, and cytosolic tRNAs, which are essential for translation. Quantitative analysis of human RNA cleavage versus nascent protein synthesis in lung carcinoma cells shows that RNase L stops global translation when tRNAs, as well as rRNAs and mRNAs, are still intact. Therefore, RNase L does not have to degrade the translation machinery to stop protein synthesis. Our data point to a rapid mechanism that transforms a subtle RNA cleavage into a cell-wide translation arrest.

Indexed as

Protein BiosynthesisBinding SitesCell LineConsensus SequenceEndoribonucleasesHeLa CellsHumansModels, BiologicalRNA CleavageRNA, Double-StrandedRNA Processing, Post-TranscriptionalRNA, Small UntranslatedRNA StabilityRNA, Transfer2-5A-dependent ribonucleaseEndoribonucleasesRNA, Double-StrandedRNA, Small UntranslatedRNA, TransferRNase LsignalingtranslationtRNAY-RNA

Identifiers

PMID28808124
PMCPMC5648034
OpenAlexW2747389445

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.