Evidence map›Paper›PMID 29453282›Full record

ArticleThe Journal of biological chemistry2018

Eukaryotic translation elongation factor 2 (eEF2) catalyzes reverse translocation of the eukaryotic ribosome.

Denis Susorov, Nikita Zakharov, Ekaterina Shuvalova, Alexander Ivanov, Tatiana Egorova, Alexey Shuvalov, Ivan N Shatsky, Elena Alkalaeva

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
    Article
  2. Targeting elongation factor 2 inFrontiers in insect science · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Translation inhibition efficacy does not determine thebioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Translational andrology and urology · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

8 authors.

Denis SusorovFrom the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Nikita Zakharovthe Department of Biological and Medical Physics, Moscow Institute of Physics and Technology, Dolgoprudny, Russia 141700.
Ekaterina ShuvalovaFrom the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Alexander IvanovFrom the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Tatiana EgorovaFrom the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Alexey ShuvalovFrom the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Ivan N Shatskythe Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
Elena AlkalaevaFrom the Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia, alkalaeva@eimb.ru.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During protein synthesis, a ribosome moves along the mRNA template and, using aminoacyl-tRNAs, decodes the template nucleotide triplets to assemble a protein amino acid sequence. This movement is accompanied by shifting of mRNA-tRNA complexes within the ribosome in a process called translocation. In living cells, this process proceeds in a unidirectional manner, bringing the ribosome to the 3' end of mRNA, and is catalyzed by the GTPase translation elongation factor 2 (EF-G in prokaryotes and eEF2 in eukaryotes). Interestingly, the possibility of spontaneous backward translocation has been shown

Indexed as

AnimalsEscherichia coliEukaryotaEukaryotic CellsGuanosine TriphosphateHumansModels, MolecularPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2Peptide Elongation Factor GPeptide Elongation FactorsProtein BindingProtein BiosynthesisRabbitsRecombinant ProteinsRibosomesGuanosine TriphosphatePeptide Elongation Factor 2Peptide Elongation Factor GPeptide Elongation FactorsRecombinant ProteinsRNA, MessengerRNA, TransferRNA, Transfer, Amino AcylADP-ribosylationribosomeribosome functiontranslation elongation factortranslocation

Identifiers

PMID29453282
PMCPMC5892567

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.