Evidence map›Paper›PMID 28251928›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Structure of human IFIT1 with capped RNA reveals adaptable mRNA binding and mechanisms for sensing N1 and N2 ribose 2'-O methylations.

Yazan M Abbas, Beatrice Theres Laudenbach, Saúl Martínez-Montero, Regina Cencic, Matthias Habjan, Andreas Pichlmair, Masad J Damha, Jerry Pelletier, Bhushan Nagar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

88 citing papers in PubMed, 127 citations in OpenAlex.

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  14. RNA chemistry and therapeutics.Nature reviews. Drug discovery · 2025
    Review
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  18. Sequence Diversity in the 3' Untranslated Region of Alphavirus Modulates IFIT2-Dependent Restriction in a Cell Type-Dependent Manner.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2025
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28 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

9 authors at 3 institutions in 2 countries.

Yazan M AbbasDepartment of Biochemistry and Groupe de Recherche Axe sur la Structure des Proteines, McGill University, Montreal, QC, Canada H3G 0B1.ORCID 0000-0001-5625-1034
Beatrice Theres LaudenbachInnate Immunity Laboratory, Max-Planck Institute of Biochemistry, 82152 Martinsried/Munich, Germany.
Saúl Martínez-MonteroDepartment of Chemistry, McGill University, Montreal, QC, Canada H3A 0B8.
Regina CencicDepartment of Biochemistry, McGill University, Montreal, QC, Canada H3G 1Y6.
Matthias HabjanInnate Immunity Laboratory, Max-Planck Institute of Biochemistry, 82152 Martinsried/Munich, Germany.
Andreas PichlmairInnate Immunity Laboratory, Max-Planck Institute of Biochemistry, 82152 Martinsried/Munich, Germany.
Masad J DamhaDepartment of Chemistry, McGill University, Montreal, QC, Canada H3A 0B8.
Jerry PelletierDepartment of Biochemistry, McGill University, Montreal, QC, Canada H3G 1Y6.
Bhushan NagarDepartment of Biochemistry and Groupe de Recherche Axe sur la Structure des Proteines, McGill University, Montreal, QC, Canada H3G 0B1; bhushan.nagar@mcgill.ca.
McGill University · CAMax Planck Institute of Biochemistry · DEOccupational Cancer Research Centre · CA

Funding

CIHR MOP-115126CIHR MOP-133535European Research Council 311339
6 · The paper itself

Abstract

IFIT1 (IFN-induced protein with tetratricopeptide repeats-1) is an effector of the host innate immune antiviral response that prevents propagation of virus infection by selectively inhibiting translation of viral mRNA. It relies on its ability to compete with the translation initiation factor eIF4F to specifically recognize foreign capped mRNAs, while remaining inactive against host mRNAs marked by ribose 2'-O methylation at the first cap-proximal nucleotide (N1). We report here several crystal structures of RNA-bound human IFIT1, including a 1.6-Å complex with capped RNA. IFIT1 forms a water-filled, positively charged RNA-binding tunnel with a separate hydrophobic extension that unexpectedly engages the cap in multiple conformations (

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsBase SequenceBinding SitesCarrier ProteinsHumansMethylationMiceModels, MolecularMolecular ConformationNucleic Acid ConformationPosition-Specific Scoring MatricesProtein BindingProtein BiosynthesisRNA-Binding ProteinsAdaptor Proteins, Signal TransducingCarrier ProteinsIFIT1 protein, humanRNA-Binding ProteinsRNA CapsRNA, MessengerRNA, Viral2′-O methylationIFIT1 crystal structureinnate immunitymRNA cap recognitionself vs. nonself

Identifiers

PMID28251928
PMCPMC5358387
OpenAlexW2594378769

What OpenQuestion holds

Textmetadata
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.