Evidence map›Paper›PMID 23706745›Full record

ArticleCell2013

Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29.

Yaser Hashem, Amedee des Georges, Vidya Dhote, Robert Langlois, Hstau Y Liao, Robert A Grassucci, Christopher U T Hellen, Tatyana V Pestova, Joachim Frank

Abstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.

0numbers the graph read from it
0cells of the map it votes in
144citing papers in PubMed
–field-weighted citation impact
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

144 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. A ribosomal kinetic checkpoint governs selective mRNA recruitment.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Purification and characterization of recombinant human translation initiation factor eIF3.Protein science : a publication of the Protein Society · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  14. Life science alliance · 2024
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

84 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.

Yaser HashemDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Amedee des Georges
Vidya Dhote
Robert Langlois
Hstau Y Liao
Robert A Grassucci
Christopher U T Hellen
Tatyana V Pestova
Joachim Frank

Funding

STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
SCANNING PROCESS IN EUKARYOTIC TRANSLATIONR01GM059660 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI PESTOVA, TATYANA V · 1999 to 2016
$4.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM059660NIGMS NIH HHS R01 GM29169NIGMS NIH HHS R01 GM59660
6 · The paper itself

Abstract

Eukaryotic translation initiation begins with assembly of a 43S preinitiation complex. First, methionylated initiator methionine transfer RNA (Met-tRNAi(Met)), eukaryotic initiation factor (eIF) 2, and guanosine triphosphate form a ternary complex (TC). The TC, eIF3, eIF1, and eIF1A cooperatively bind to the 40S subunit, yielding the 43S preinitiation complex, which is ready to attach to messenger RNA (mRNA) and start scanning to the initiation codon. Scanning on structured mRNAs additionally requires DHX29, a DExH-box protein that also binds directly to the 40S subunit. Here, we present a cryo-electron microscopy structure of the mammalian DHX29-bound 43S complex at 11.6 Å resolution. It reveals that eIF2 interacts with the 40S subunit via its α subunit and supports Met-tRNAi(Met) in an unexpected P/I orientation (eP/I). The structural core of eIF3 resides on the back of the 40S subunit, establishing two principal points of contact, whereas DHX29 binds around helix 16. The structure provides insights into eukaryote-specific aspects of translation, including the mechanism of action of DHX29.

Indexed as

Peptide Chain Initiation, TranslationalAnimalsBase SequenceCell-Free SystemCryoelectron MicroscopyEukaryotic Initiation Factor-2HumansMammalsModels, MolecularMolecular Sequence DataRabbitsRibonucleoproteinsRNA HelicasesRNA, RibosomalRNA, Ribosomal, 18SEukaryotic Initiation Factor-2RibonucleoproteinsRNA HelicasesRNA, RibosomalRNA, Ribosomal, 18S

Identifiers

PMID23706745
PMCPMC3730827

What OpenQuestion holds

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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.