Evidence map›Paper›PMID 30989826›Full record

ReviewWiley interdisciplinary reviews. RNA2019

RNA regulation of the antiviral protein 2'-5'-oligoadenylate synthetase.

Samantha L Schwartz, Graeme L Conn

Open access · greenAbstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

82 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Allopatric coevolution: Migratory predators may facilitate mimicry between geographically nonoverlapping species.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. RNase L Regulates Antiviral Responsiveness through Cleavage of XBP1 mRNA.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. iScience · 2025
    Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Review

22 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

2 authors at 1 institution in 1 country.

Samantha L SchwartzDepartment of Biochemistry, Emory University School of Medicine and Graduate Program in Biochemistry, Cell and Developmental Biology (BCDB), Atlanta, Georgia.
Graeme L ConnDepartment of Biochemistry, Emory University School of Medicine and Graduate Program in Biochemistry, Cell and Developmental Biology (BCDB), Atlanta, Georgia.
Emory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
dsRNA regulation of the cytosolic innate immune systemR01AI144067 · NIAID · EMORY UNIVERSITY · PI Graeme L Conn · 2019 to 2026
$3.4M
Regulation of 2'-5'-oligoadenylate synthetase 1 (OAS1) by dsRNAF31AI133950 · NIAID · EMORY UNIVERSITY · PI SCHWARTZ, SAMANTHA LYNNE · 2017 to 2019
$134k
NIAID NIH HHS F31 AI133950NIAID NIH HHS R01 AI144067NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

The innate immune system is a broad collection of critical intra- and extra-cellular processes that limit the infectivity of diverse pathogens. The 2'-5'-oligoadenylate synthetase (OAS) family of enzymes are important sensors of cytosolic double-stranded RNA (dsRNA) that play a critical role in limiting viral infection by activating the latent ribonuclease (RNase L) to halt viral replication and establish an antiviral state. Attesting to the importance of the OAS/RNase L pathway, diverse viruses have developed numerous distinct strategies to evade the effects of OAS activation. How OAS proteins are regulated by viral or cellular RNAs is not fully understood but several recent studies have provided important new insights into the molecular mechanisms of OAS activation by dsRNA. Other studies have revealed unanticipated features of RNA sequence and structure that strongly enhance activation of at least one OAS family member. While these discoveries represent important advances, they also underscore the fact that much remains to be learned about RNA-mediated regulation of the OAS/RNase L pathway. In particular, defining the full complement of RNA molecular signatures that activate OAS is essential to our understanding of how these proteins maximize their protective role against pathogens while still accurately discriminating host molecules to avoid inadvertent activation by cellular RNAs. A more complete knowledge of OAS regulation may also serve as a foundation for the development of novel antiviral therapeutic strategies and lead the way to a deeper understanding of currently unappreciated cellular functions of the OAS/RNase L pathway in the absence of infection. This article is categorized under: RNA in Disease and Development > RNA in Disease RNA Interactions with Proteins and Other Molecules > Protein-RNA Interactions: Functional Implications Translation > Translation Regulation.

Indexed as

Gene Expression Regulation2',5'-Oligoadenylate SynthetaseEndoribonucleasesEnzyme ActivatorsImmunologic FactorsRNA, Double-Stranded2-5A-dependent ribonuclease2',5'-Oligoadenylate SynthetaseEndoribonucleasesEnzyme ActivatorsImmunologic FactorsRNA, Double-Strandeddouble-stranded RNAinnate immunityoligoadenylate synthetase/ribonuclease LRNA structuretranslational regulationvirus

Identifiers

PMID30989826
PMCPMC6585406
OpenAlexW2938019550

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.