Evidence map›Paper›PMID 23766293›Full record

ArticleNucleic acids research2013

Two RNA-binding motifs in eIF3 direct HCV IRES-dependent translation.

Chaomin Sun, Jordi Querol-Audí, Stefanie A Mortimer, Ernesto Arias-Palomo, Jennifer A Doudna, Eva Nogales, Jamie H D Cate

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

61 citing papers in PubMed, 82 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Purification and characterization of recombinant human translation initiation factor eIF3.Protein science : a publication of the Protein Society · 2026
    Article
  5. Article
  6. Structural insights into the role of eIF3 in translation mediated by the HCV IRES.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. A highly efficient human cell-free translation system.bioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Review
  19. Review
  20. Article

1 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

7 authors at 1 institution in 1 country.

Chaomin SunDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA, Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA and Department of Chemistry, University of California, Berkeley, CA 94720, USA.
Jordi Querol-Audí
Stefanie A Mortimer
Ernesto Arias-Palomo
Jennifer A Doudna
Eva Nogales
Jamie H D Cate
Lawrence Berkeley National Laboratory · US

Funding

PROJECT 3P50GM102706 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CATE, JAMIE H · 2012 to 2016
$9.5M
HCV IRES Control of Human Translational InitiationR56AI095687 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI DOUDNA, JENNIFER A · 2011 to 2011
$627k
NIAID NIH HHS R56-AI095687NIGMS NIH HHS P50-GM102706
6 · The paper itself

Abstract

The initiation of protein synthesis plays an essential regulatory role in human biology. At the center of the initiation pathway, the 13-subunit eukaryotic translation initiation factor 3 (eIF3) controls access of other initiation factors and mRNA to the ribosome by unknown mechanisms. Using electron microscopy (EM), bioinformatics and biochemical experiments, we identify two highly conserved RNA-binding motifs in eIF3 that direct translation initiation from the hepatitis C virus internal ribosome entry site (HCV IRES) RNA. Mutations in the RNA-binding motif of subunit eIF3a weaken eIF3 binding to the HCV IRES and the 40S ribosomal subunit, thereby suppressing eIF2-dependent recognition of the start codon. Mutations in the eIF3c RNA-binding motif also reduce 40S ribosomal subunit binding to eIF3, and inhibit eIF5B-dependent steps downstream of start codon recognition. These results provide the first connection between the structure of the central translation initiation factor eIF3 and recognition of the HCV genomic RNA start codon, molecular interactions that likely extend to the human transcriptome.

Indexed as

Protein BiosynthesisBinding SitesCodon, InitiatorEukaryotic Initiation Factor-3Helix-Loop-Helix MotifsHepacivirusHumansMultiprotein ComplexesMutationProtein BindingProtein Interaction MappingRibosomesRibosome Subunits, Small, EukaryoticRNA, ViralCodon, InitiatorEIF3A protein, humanEukaryotic Initiation Factor-3Multiprotein ComplexesRNA, Viral

Identifiers

PMID23766293
PMCPMC3753635
OpenAlexW2086421374

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.