Evidence map›Paper›PMID 19417105›Full record

ArticleGenes & development2009

Structural insights into eRF3 and stop codon recognition by eRF1.

Zhihong Cheng, Kazuki Saito, Andrey V Pisarev, Miki Wada, Vera P Pisareva, Tatyana V Pestova, Michal Gajda, Adam Round, Chunguang Kong, Mengkiat Lim and 4 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing 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

90 citing papers in PubMed, 164 citations in OpenAlex.

  1. Article
  2. RNAViruses · 2026
    Review
  3. RiboScreenBiomedicines · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Prion-Dependent Lethality ofInternational journal of molecular sciences · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Translation Phases in Eukaryotes.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  20. Article

30 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

14 authors at 8 institutions in 5 countries.

Zhihong ChengCancer and Developmental Cell Biology Division, Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research (A*STAR), Singapore, Singapore.
Kazuki Saito
Andrey V Pisarev
Miki Wada
Vera P Pisareva
Tatyana V Pestova
Michal Gajda
Adam Round
Chunguang Kong
Mengkiat Lim
Yoshikazu Nakamura
Dmitri I Svergun
Koichi Ito
Haiwei Song
Tokyo University of Science · JPAgency for Science, Technology and Research · SGEuropean Molecular Biology Laboratory · DEInstitute of Molecular and Cell Biology · SGState University of New York · USJapan Science and Technology Agency · JPRussian Academy of Sciences · RUSUNY Downstate Health Sciences University · US

Funding

THE MECHANISMS OF EUKARYOTIC TRANSLATION TERMINATION AND RIBOSOMAL RECYCLINGR01GM080623 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI PESTOVA, TATYANA V · 2007 to 2015
$2.7M
NIGMS NIH HHS R01 GM080623NIGMS NIH HHS R01 GM 80623
6 · The paper itself

Abstract

Eukaryotic translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act cooperatively to ensure efficient stop codon recognition and fast polypeptide release. The crystal structures of human and Schizosaccharomyces pombe full-length eRF1 in complex with eRF3 lacking the GTPase domain revealed details of the interaction between these two factors and marked conformational changes in eRF1 that occur upon binding to eRF3, leading eRF1 to resemble a tRNA molecule. Small-angle X-ray scattering analysis of the eRF1/eRF3/GTP complex suggested that eRF1's M domain contacts eRF3's GTPase domain. Consistently, mutation of Arg192, which is predicted to come in close contact with the switch regions of eRF3, revealed its important role for eRF1's stimulatory effect on eRF3's GTPase activity. An ATP molecule used as a crystallization additive was bound in eRF1's putative decoding area. Mutational analysis of the ATP-binding site shed light on the mechanism of stop codon recognition by eRF1.

Indexed as

Models, MolecularSchizosaccharomycesAdenosine TriphosphateCodon, TerminatorGene OrderGTP PhosphohydrolasesHumansMutationPeptide Termination FactorsProtein BindingProtein BiosynthesisProtein Structure, QuaternaryProtein Structure, TertiaryReproducibility of ResultsRibosomesScattering, Small AngleAdenosine TriphosphateCodon, TerminatorETF1 protein, humanGTP Phosphohydrolasespeptide-chain-release factor 3Peptide Termination FactorsSchizosaccharomyces pombe Proteins

Identifiers

PMID19417105
PMCPMC2682955
OpenAlexW2132650893

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.