Evidence map›Paper›PMID 23150880›Full record

ArticleScience signaling2012

Single amino acid substitutions confer the antiviral activity of the TRAF3 adaptor protein onto TRAF5.

Peng Zhang, Anna Reichardt, Huanhuan Liang, Roghiyh Aliyari, David Cheng, Yaya Wang, Feng Xu, Genhong Cheng, Yingfang Liu

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. TRAF6 coiled-coil domain mediates its trimerization.bioRxiv : the preprint server for biology · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Rv3722c PromotesFrontiers in cellular and infection microbiology · 2021
    Article
  7. Comparison of Target Recognition by TRAF1 and TRAF2.International journal of molecular sciences · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Molecular basis for unique specificity of human TRAF4 for platelets GPIbβ and GPVI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

9 authors at 1 institution in 1 country.

Peng ZhangState Key Laboratory of Biomacromolecules, CAS Key Laboratory of Infection and Immunity, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
Anna Reichardt
Huanhuan Liang
Roghiyh Aliyari
David Cheng
Yaya Wang
Feng Xu
Genhong Cheng
Yingfang Liu
University of California, Los Angeles · US

Funding

Viral Mediated Type I Interferon InductionR01AI069120 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHENG, GENHONG · 2006 to 2021
$6.0M
Mechanisms of Biodefense By Toll-Like ReceptorsR01AI056154 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHENG, GENHONG · 2004 to 2014
$3.7M
Regulation of Type 2 NF-kappaB Activation and InflammationR01GM078607 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHENG, GENHONG · 2008 to 2011
$1.1M
NIAID NIH HHS R01 AI056154NIAID NIH HHS R01 AI069120NIAID NIH HHS R01AI069120NIGMS NIH HHS R01 GM078607NIGMS NIH HHS R01GM078607
6 · The paper itself

Abstract

The TRAF [tumor necrosis factor receptor-associated factor] family of cytoplasmic adaptor proteins link cell-surface receptors to intracellular signaling pathways that regulate innate and adaptive immune responses. In response to activation of RIG-I (retinoic acid-inducible gene I), a component of a pattern recognition receptor that detects viruses, TRAF3 binds to the adaptor protein Cardif [caspase activation and recruitment domain (CARD) adaptor-inducing interferon-β (IFN-β)], leading to induction of type I IFNs. We report the crystal structures of the TRAF domain of TRAF5 and that of TRAF3 bound to a peptide from the TRAF-interacting motif of Cardif. By comparing these structures, we identified two residues located near the Cardif binding pocket in TRAF3 (Tyr(440) and Phe(473)) that potentially contributed to Cardif recognition. In vitro and cellular experiments showed that forms of TRAF5 with mutation of the corresponding residues to those of TRAF3 had TRAF3-like antiviral activity. Our results provide a structural basis for the critical role of TRAF3 in activating RIG-I-mediated IFN production.

Indexed as

Antiviral AgentsTNF Receptor-Associated Factor 3TNF Receptor-Associated Factor 5Adaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SubstitutionAnimalsCrystallography, X-RayDEAD Box Protein 58DEAD-box RNA HelicasesInterferonsMiceProtein Structure, TertiaryAdaptor Proteins, Signal TransducingAntiviral AgentsDdx58 protein, mouseDEAD Box Protein 58DEAD-box RNA HelicasesInterferonsMAVS protein, mouseTNF Receptor-Associated Factor 3TNF Receptor-Associated Factor 5

Identifiers

PMID23150880
PMCPMC4114212
OpenAlexW2103074558

What OpenQuestion holds

Textmetadata
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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.