ArticleThe Biochemical journal2013
Crystal structure of the TRIM25 B30.2 (PRYSPRY) domain: a key component of antiviral signalling.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it.
- To TRIM the Immunity: From Innate to Adaptive Immunity.Frontiers in immunology · 2020Pooled it
- Swine TRIM25 inhibits vesicular stomatitis virus replication by activation of type I IFN signaling pathway and binding vRNA.Journal of veterinary science · 2026Article
- Single-cell profiling reveals context-dependent immune regulation shared by sepsis and systemic lupus erythematosus.Frontiers in immunology · 2026Article
- TRIM21 modulates stability of pro-survival non-coding RNA vtRNA1-1 in human hepatocellular carcinoma cells.PLoS genetics · 2025Article
- TRIM25, TRIM28 and TRIM59 and Their Protein Partners in Cancer Signaling Crosstalk: Potential Novel Therapeutic Targets for Cancer.Current issues in molecular biology · 2024Review
- Article
- Structural Investigations of Interactions between the Influenza a Virus NS1 and Host Cellular Proteins.Viruses · 2023Review
- TRIM25 and ZAP target the Ebola virus ribonucleoprotein complex to mediate interferon-induced restriction.PLoS pathogens · 2022Article
- Recurrent expansions of B30.2-associated immune receptor families in fish.Immunogenetics · 2022Article
- Review
- Article
- Competitive binding of E3 ligases TRIM26 and WWP2 controls SOX2 in glioblastoma.Nature communications · 2021Article
- A Comparative Perspective on Functionally-Related, Intracellular Calcium Channels: The Insect Ryanodine and Inositol 1,4,5-Trisphosphate Receptors.Biomolecules · 2021Review
- Targeting TRIM Proteins: A Quest towards Drugging an Emerging Protein Class.Chembiochem : a European journal of chemical biology · 2021Review
- Regulatory effects of chicken TRIM25 on the replication of ALV-A and the MDA5-mediated type I interferon response.Veterinary research · 2020Article
- Crystal structure of the SPRY domain of human SPSB2 in the apo state.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Article
- Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition.Nature communications · 2018Article
- Conserved structural and functional aspects of the tripartite motif gene family point towards therapeutic applications in multiple diseases.Pharmacology & therapeutics · 2018Review
- Identification of a second binding site on the TRIM25 B30.2 domain.The Biochemical journal · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
TRIM (tripartite motif) proteins primarily function as ubiquitin E3 ligases that regulate the innate immune response to infection. TRIM25 [also known as Efp (oestrogen-responsive finger protein)] has been implicated in the regulation of oestrogen receptor α signalling and in the regulation of innate immune signalling via RIG-I (retinoic acid-inducible gene-I). RIG-I senses cytosolic viral RNA and is subsequently ubiquitinated by TRIM25 at its N-terminal CARDs (caspase recruitment domains), leading to type I interferon production. The interaction with RIG-I is dependent on the TRIM25 B30.2 domain, a protein-interaction domain composed of the PRY and SPRY tandem sequence motifs. In the present study we describe the 1.8 Å crystal structure of the TRIM25 B30.2 domain, which exhibits a typical B30.2/SPRY domain fold comprising two N-terminal α-helices, thirteen β-strands arranged into two β-sheets and loop regions of varying lengths. A comparison with other B30.2/SPRY structures and an analysis of the loop regions identified a putative binding pocket, which is likely to be involved in binding target proteins. This was supported by mutagenesis and functional analyses, which identified two key residues (Asp(488) and Trp(621)) in the TRIM25 B30.2 domain as being critical for binding to the RIG-I CARDs.
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Registered trials
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.