Evidence map›Paper›PMID 29101251›Full record

ArticleThe Journal of experimental medicine2017

The methyltransferase NSD3 promotes antiviral innate immunity via direct lysine methylation of IRF3.

Chunmei Wang, Qinlan Wang, Xiaoqing Xu, Bin Xie, Yong Zhao, Nan Li, Xuetao Cao

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Many faces of mammalian NSD methyltransferases.Cellular & molecular biology letters · 2026
    Review
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  5. Review
  6. Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Chunmei WangDepartment of Immunology and Center for Immunotherapy, Institute of Basic Medical Sciences, Peking Union Medical College, Chinese Academy of Medical Sciences, Beijing, China.
Qinlan WangInstitute of Immunology, Zhejiang University School of Medicine, Hangzhou, China.
Xiaoqing XuDepartment of Immunology and Center for Immunotherapy, Institute of Basic Medical Sciences, Peking Union Medical College, Chinese Academy of Medical Sciences, Beijing, China.
Bin XieInstitute of Immunology, Zhejiang University School of Medicine, Hangzhou, China.
Yong ZhaoDepartment of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY.
Nan LiNational Key Laboratory of Medical Immunology and Institute of Immunology, Second Military Medical University, Shanghai, China linan@immunol.org.ORCID http://orcid.org/0000-0003-1179-0063
Xuetao CaoDepartment of Immunology and Center for Immunotherapy, Institute of Basic Medical Sciences, Peking Union Medical College, Chinese Academy of Medical Sciences, Beijing, China caoxt@immunol.org.ORCID http://orcid.org/0000-0001-9677-7647
Second Military Medical University · CNZhejiang University · CNChinese Academy of Medical Sciences & Peking Union Medical College · CNIcahn School of Medicine at Mount Sinai · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine methylation is an important posttranslational modification, implicated in various biological pathological conditions. The transcription factor interferon regulatory factor 3 (IRF3) is essential for antiviral innate immunity, yet the mechanism for methylation control of IRF3 activation remains unclear. In this paper, we discovered monomethylation of IRF3 at K366 is critical for IRF3 transcription activity in antiviral innate immunity. By mass spectrometry analysis of IRF3-associated proteins, we identified nuclear receptor-binding SET domain 3 (NSD3) as the lysine methyltransferase that directly binds to the IRF3 C-terminal region through its PWWP1 domain and methylates IRF3 at K366 via its SET domain. Deficiency of NSD3 impairs the antiviral innate immune response in vivo

Indexed as

Immunity, InnateAnimalsCell NucleusHEK293 CellsHistone-Lysine N-MethyltransferaseHumansInterferon Regulatory Factor-3LysineMacrophagesMethylationMice, Inbred C57BLNuclear ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein BindingTranscription, GeneticHistone-Lysine N-MethyltransferaseInterferon Regulatory Factor-3LysineNuclear ProteinsPhosphoprotein PhosphatasesWHSC1L1 protein, mouse

Identifiers

PMID29101251
PMCPMC5716042
OpenAlexW2767449381

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.