ArticleNature2013
Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.
What it found
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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.
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.
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Who cites it
154 citing papers in PubMed, 223 citations in OpenAlex.
- Trial
- The capping arms race: evolutionary interplay between IFIT proteins and viral molecular mimicry.Molecular biology reports · 2026Review
- Review
- The promoting roles of GLP1R and GIPR in stemness maintenance and multiple lineage-specific differentiation of PDLSCs.Cellular & molecular biology letters · 2026Article
- Novel trinucleotide mRNA capping reagents: improved synthetic route and efficient cotranscriptional incorporation in mRNA.RNA (New York, N.Y.) · 2026Article
- The 5' Cap Epitranscriptome and Beyond: Natural and Engineered 5' Cap Modifications for Optimizing mRNA Therapeutics and Functional Studies.ChemMedChem · 2026Review
- Hepatitis B Virus Nucleocapsid Assembly.Journal of molecular biology · 2025Review
- The IFIT2-IFIT3 antiviral complex targets short 5' untranslated regions on viral mRNAs for translation inhibition.Nature microbiology · 2025Article
- Transcriptomic Analysis of MGF360-4L Mediated Regulation in African Swine Fever Virus-Infected Porcine Alveolar Macrophages.Animals : an open access journal from MDPI · 2025Article
- O-GlcNAc transferase plays dual antiviral roles by integrating innate immunity and lipid metabolism.Nature communications · 2025Article
- The Role of Chemical Modifications in the Genome of Negative-Sense RNA Viruses on the Innate Immune Response.Viruses · 2025Review
- In vitro characterization of the antiviral activity of Bat Interferon-Induced protein with tetratricopeptide repeats 5 (bat IFIT5) against bat-associated rabies virus.Journal of neurovirology · 2025Article
- A poxvirus ankyrin protein LSDV012 inhibits IFIT1 in a host-species-specific manner by compromising its RNA binding ability.PLoS pathogens · 2025Article
- RNA sensing at the crossroads of autoimmunity and autoinflammation.RNA (New York, N.Y.) · 2025Review
- Short 5' UTRs serve as a marker for viral mRNA translation inhibition by the IFIT2-IFIT3 antiviral complex.bioRxiv : the preprint server for biology · 2025Article
- 5' terminal nucleotide determines the immunogenicity of IVT RNAs.Nucleic acids research · 2025Article
- An MST-based assay reveals new binding preferences of IFIT1 for canonically and noncanonically capped RNAs.RNA (New York, N.Y.) · 2025Article
- Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024Review
- Antiviral Effects of Avian Interferon-Stimulated Genes.Animals : an open access journal from MDPI · 2024Review
- Downregulation of the mThe Journal of biological chemistry · 2024Article
94 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Interferon-induced proteins with tetratricopeptide repeats (IFITs) are innate immune effector molecules that are thought to confer antiviral defence through disruption of protein-protein interactions in the host translation-initiation machinery. However, it was recently discovered that IFITs can directly recognize viral RNA bearing a 5'-triphosphate group (PPP-RNA), which is a molecular signature that distinguishes it from host RNA. Here we report crystal structures of human IFIT5, its complex with PPP-RNAs, and an amino-terminal fragment of IFIT1. The structures reveal a new helical domain that houses a positively charged cavity designed to specifically engage only single-stranded PPP-RNA, thus distinguishing it from the canonical cytosolic sensor of double-stranded viral PPP-RNA, retinoic acid-inducible gene I (RIG-I, also known as DDX58). Mutational analysis, proteolysis and gel-shift assays reveal that PPP-RNA is bound in a non-sequence-specific manner and requires a 5'-overhang of approximately three nucleotides. Abrogation of PPP-RNA binding in IFIT1 and IFIT5 was found to cause a defect in the antiviral response by human embryonic kidney cells. These results demonstrate the mechanism by which IFIT proteins selectively recognize viral RNA, and lend insight into their downstream effector function.
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What OpenQuestion holds
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.