Evidence map›Paper›PMID 29401259›Full record

ArticleNucleic acids research2018

Structure of a human cap-dependent 48S translation pre-initiation complex.

Boris Eliseev, Lahari Yeramala, Alexander Leitner, Manikandan Karuppasamy, Etienne Raimondeau, Karine Huard, Elena Alkalaeva, Ruedi Aebersold, Christiane Schaffitzel

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

51 citing papers in PubMed, 100 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Male germ cell-specific deletion ofZoological research · 2026
    Article
  7. Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Towards a structurally resolved human protein interaction network.Nature structural & molecular biology · 2023
    Article
  20. Review
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 5 institutions in 4 countries.

Boris EliseevEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Lahari YeramalaEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Alexander LeitnerETH Zürich, Institute of Molecular Systems Biology, Auguste-Piccard-Hof 1, 8093 Zürich, Switzerland.
Manikandan KaruppasamyEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Etienne RaimondeauEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Karine HuardEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
Elena AlkalaevaEngelhardt Institute of Molecular Biology, the Russian Academy of Sciences, 119991 Moscow, Russia.
Ruedi AebersoldETH Zürich, Institute of Molecular Systems Biology, Auguste-Piccard-Hof 1, 8093 Zürich, Switzerland.
Christiane SchaffitzelEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France.
European Molecular Biology Laboratory · FREngelhardt Institute of Molecular Biology · RUETH Zurich · CHUniversity of Bristol · GBUniversity of Zurich · CH

Funding

European Research Council 281331
6 · The paper itself

Abstract

Eukaryotic translation initiation is tightly regulated, requiring a set of conserved initiation factors (eIFs). Translation of a capped mRNA depends on the trimeric eIF4F complex and eIF4B to load the mRNA onto the 43S pre-initiation complex comprising 40S and initiation factors 1, 1A, 2, 3 and 5 as well as initiator-tRNA. Binding of the mRNA is followed by mRNA scanning in the 48S pre-initiation complex, until a start codon is recognised. Here, we use a reconstituted system to prepare human 48S complexes assembled on capped mRNA in the presence of eIF4B and eIF4F. The highly purified h-48S complexes are used for cross-linking/mass spectrometry, revealing the protein interaction network in this complex. We report the electron cryo-microscopy structure of the h-48S complex at 6.3 Å resolution. While the majority of eIF4B and eIF4F appear to be flexible with respect to the ribosome, additional density is detected at the entrance of the 40S mRNA channel which we attribute to the RNA-recognition motif of eIF4B. The eight core subunits of eIF3 are bound at the 40S solvent-exposed side, as well as the subunits eIF3d, eIF3b and eIF3i. elF2 and initiator-tRNA bound to the start codon are present at the 40S intersubunit side. This cryo-EM structure represents a molecular snap-shot revealing the h-48S complex following start codon recognition.

Indexed as

Models, MolecularCryoelectron MicroscopyEukaryotic Initiation Factor-3Eukaryotic Initiation FactorsHumansMass SpectrometryPeptide Chain Initiation, TranslationalRibosomal ProteinsRibosome Subunits, Small, EukaryoticRNA CapsRNA, MessengerRNA, Ribosomal, 18SeIF-4BEukaryotic Initiation Factor-3Eukaryotic Initiation FactorsRibosomal ProteinsRNA CapsRNA, MessengerRNA, Ribosomal, 18S

Identifiers

PMID29401259
PMCPMC5861459
OpenAlexW2793963773

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.