Evidence map›Paper›PMID 37751211›Full record

ReviewJournal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research2023

The Many Faces of Oligoadenylate Synthetases.

Saumendra N Sarkar, Munesh K Harioudh, Lulu Shao, Joseph Perez, Arundhati Ghosh

Open access · greenAbstract readReview
In one paragraph

Review in Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Hypomethylation of the HumanArchives of Iranian medicine · 2026
    Article
  6. Review
  7. The strategies and advances of mRNA translation booster.Asian journal of pharmaceutical sciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Understanding the impact ofFrontiers in molecular biosciences · 2024
    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 1 institution in 1 country.

Saumendra N SarkarCancer Virology Program, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.ORCID 0000-0002-2850-6121
Munesh K HarioudhCancer Virology Program, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Lulu ShaoCancer Virology Program, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Joseph PerezCancer Virology Program, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Arundhati GhoshCancer Virology Program, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
University of Pittsburgh · US

Funding

Innate Immune Regulation of Zika Virus InfectionR01AI145296 · NIAID · UNIVERSITY OF WASHINGTON · PI COYNE, CAROLYN B, DIAMOND, MICHAEL S · 2019 to 2023
$4.1M
A new mechanism of antiviral activity of 2’-5’ Oligoadenylate Synthetase 1R01AI150214 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DIAMOND, MICHAEL S, SARKAR, SAUMENDRA N · 2020 to 2024
$2.6M
New roles of IFN-inducible OAS proteins in innate immune defense against bacterial infectionsR01AI176333 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Vijay Rathinam, Saumendra N Sarkar · 2023 to 2026
$2.5M
Differential modulation of RIG-I and cGAS signaling by OASL and its role in antiviral response.R01AI118896 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SARKAR, SAUMENDRA N · 2015 to 2019
$2.1M
NIAID NIH HHS R01 AI118896NIAID NIH HHS R01 AI145296NIAID NIH HHS R01 AI150214NIAID NIH HHS R01 AI176333
6 · The paper itself

Abstract

2'-5' Oligoadenylate synthetases (OAS) are interferon-stimulated genes that are most well-known to protect hosts from viral infections. They are evolutionarily related to an ancient family of Nucleotidyltransferases, which are primarily involved in pathogen-sensing and innate immune response. Classical function of OAS proteins involves double-stranded RNA-stimulated polymerization of adenosine triphosphate in 2'-5' oligoadenylates (2-5A), which can activate the latent RNase (RNase L) to degrade RNA. However, accumulated evidence over the years have suggested alternative mode of antiviral function of several OAS family proteins. Furthermore, recent studies have connected some OAS proteins with wider function beyond viral infection. Here, we review some of the canonical and noncanonical functions of OAS proteins and their mechanisms.

Indexed as

RNA, Double-StrandedVirus Diseases2',5'-Oligoadenylate SynthetaseAdenine NucleotidesEndoribonucleasesHumansInterferonsOligoribonucleotides2',5'-oligoadenylate2',5'-Oligoadenylate SynthetaseAdenine NucleotidesEndoribonucleasesInterferonsOligoribonucleotidesRNA, Double-Strandedantiviral mechanisminterferoninterferon-stimulated genesoligoadenylate synthetaseWest Nile virus

Identifiers

PMID37751211
PMCPMC10654648
OpenAlexW4387033404

What Socratic holds

Textmetadata
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 Socratic graph.