Evidence map›Paper›PMID 25744296›Full record

ReviewExperimental & molecular medicine2015

Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases.

Un Yung Choi, Ji-Seon Kang, Yune Sahng Hwang, Young-Joon Kim

Abstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 168 papers, 5 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
168citing papers in PubMed, 5 pooled it
–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

168 citing papers in PubMed, 5 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
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  5. Pooled it
  6. Review
  7. Article
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  13. The FunctionalInternational journal of molecular sciences · 2026
    Article
  14. Overexpression ofJournal of clinical medicine · 2026
    Article
  15. Article
  16. Article
  17. Review
  18. Intrinsic OASL expression governs heterogeneity in interferon induction during influenza A virus infection.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Hypomethylation of the HumanArchives of Iranian medicine · 2026
    Article
  20. Article

108 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.

Un Yung ChoiDepartment of Biochemistry, College of Life Science and Technology, Yonsei University, Seoul, Korea.
Ji-Seon KangDepartment of Biochemistry, College of Life Science and Technology, Yonsei University, Seoul, Korea.
Yune Sahng HwangDepartment of Integrated Omics for Biomedical Science, Yonsei University, Seoul, Korea.
Young-Joon Kim1] Department of Biochemistry, College of Life Science and Technology, Yonsei University, Seoul, Korea [2] Department of Integrated Omics for Biomedical Science, Yonsei University, Seoul, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2'-5' oligoadenylate synthase (OAS), is a well-known molecule that regulates the early phase of viral infection by degrading viral RNA in combination with RNase L, resulting in the inhibition of viral replication. In this review, we describe OAS family proteins from a different point of view from that of previous reviews. We discuss not only RNase L-dependent (canonical) and -independent (noncanonical) pathways but also the possibility of the OAS family members as biomarkers for various diseases and clues to non-immunological functions based on recent studies. In particular, we focus on OASL, a member of the OAS family that is relatively less well understood than the other members. We will explain its anti- and pro-viral dual roles as well as the diseases related to single-nucleotide polymorphisms in the corresponding gene.

Indexed as

Disease Susceptibility2',5'-Oligoadenylate SynthetaseAnimalsBiomarkersEndoribonucleasesGenetic Predisposition to DiseaseHumansMultigene FamilyPolymorphism, Single NucleotideSignal Transduction2-5A-dependent ribonuclease2',5'-Oligoadenylate SynthetaseBiomarkersEndoribonucleasesOAS1 protein, humanOAS3 protein, human

Identifiers

PMID25744296
PMCPMC4351405

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.