Evidence map›Paper›PMID 38778761›Full record

ReviewBiochemical Society transactions2024

A closer look at mammalian antiviral condensates.

J Monty Watkins, James M Burke

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. 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
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. The Unusual Role of Ribonuclease L in Innate Immunity.Wiley interdisciplinary reviews. RNA
    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

2 authors.

J Monty WatkinsDepartment of Molecular Medicine, The Herbert Wertheim University of Florida Scripps Institute for Biomedical Innovation and Technology, Jupiter, FL, U.S.A.ORCID 0000-0002-3552-5734
James M BurkeDepartment of Molecular Medicine, The Herbert Wertheim University of Florida Scripps Institute for Biomedical Innovation and Technology, Jupiter, FL, U.S.A.ORCID 0000-0002-5525-3641

Funding

Understanding the OAS/RNase L pathway during pathogenic viral infectionsR35GM151249 · NIGMS · UNIVERSITY OF FLORIDA · PI James M Burke · 2023 to 2026
$1.9M
NIGMS NIH HHS R35 GM151249
6 · The paper itself

Abstract

Several biomolecular condensates assemble in mammalian cells in response to viral infection. The most studied of these are stress granules (SGs), which have been proposed to promote antiviral innate immune signaling pathways, including the RLR-MAVS, the protein kinase R (PKR), and the OAS-RNase L pathways. However, recent studies have demonstrated that SGs either negatively regulate or do not impact antiviral signaling. Instead, the SG-nucleating protein, G3BP1, may function to perturb viral RNA biology by condensing viral RNA into viral-aggregated RNA condensates, thus explaining why viruses often antagonize G3BP1 or hijack its RNA condensing function. However, a recently identified condensate, termed double-stranded RNA-induced foci, promotes the activation of the PKR and OAS-RNase L antiviral pathways. In addition, SG-like condensates known as an RNase L-induced bodies (RLBs) have been observed during many viral infections, including SARS-CoV-2 and several flaviviruses. RLBs may function in promoting decay of cellular and viral RNA, as well as promoting ribosome-associated signaling pathways. Herein, we review these recent advances in the field of antiviral biomolecular condensates, and we provide perspective on the role of canonical SGs and G3BP1 during the antiviral response.

Indexed as

RNA HelicasesRNA Recognition Motif ProteinsRNA, ViralStress GranulesAnimalsBiomolecular CondensatesCOVID-19DNA HelicaseseIF-2 KinaseEndoribonucleasesHumansImmunity, InnatePoly-ADP-Ribose Binding ProteinsSARS-CoV-2Signal TransductionVirus Diseases2-5A-dependent ribonucleaseDNA HelicaseseIF-2 KinaseEndoribonucleasesG3BP1 protein, humanPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsRNA, ViralcondensateG3BP1PKRRNARNase Lstress granules

Identifiers

PMID38778761
PMCPMC11234502

What OpenQuestion holds

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Registered trials

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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.