Evidence map›Paper›PMID 24362468›Full record

ReviewNature reviews. Microbiology2014

EF-G and EF4: translocation and back-translocation on the bacterial ribosome.

Hiroshi Yamamoto, Yan Qin, John Achenbach, Chengmin Li, Jaroslaw Kijek, Christian M T Spahn, Knud H Nierhaus

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Review
  3. The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024
    Review
  4. Article
  5. Elongation factor P modulatesProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Function of Cajal Bodies in Nuclear RNA Retention inInternational journal of molecular sciences · 2022
    Article
  8. Article
  9. Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021
    Review
  10. Energetic dependencies dictate folding mechanism in a complex protein.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 4 institutions in 2 countries.

Hiroshi Yamamoto1] Institut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. [2].
Yan Qin1] Laboratory of noncoding RNA, Institute of Biophysics, Chinese Academy of Science; 15 Datun Road, Beijing 100101, China. [2].
John Achenbach1] NOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany. [2].
Chengmin LiLaboratory of noncoding RNA, Institute of Biophysics, Chinese Academy of Science; 15 Datun Road, Beijing 100101, China.
Jaroslaw KijekMax Planck Institut für molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany.
Christian M T SpahnInstitut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Knud H Nierhaus1] Institut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. [2] Max Planck Institut für molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany.
Charité - Universitätsmedizin Berlin · DECzech Academy of Sciences, Institute of Biophysics · CZMax Planck Institute for Molecular Genetics · DENoxxon Pharma (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomes translate the codon sequence of an mRNA into the amino acid sequence of the corresponding protein. One of the most crucial events is the translocation reaction, which involves movement of both the mRNA and the attached tRNAs by one codon length and is catalysed by the GTPase elongation factor G (EF-G). Interestingly, recent studies have identified a structurally related GTPase, EF4, that catalyses movement of the tRNA2-mRNA complex in the opposite direction when the ribosome stalls, which is known as back-translocation. In this Review, we describe recent insights into the mechanistic basis of both translocation and back-translocation.

Indexed as

Bacterial TranslocationModels, MolecularBacteriaBacterial ProteinsBinding SitesGTP PhosphohydrolasesGuanosine TriphosphateHydrolysisPeptide Elongation Factor GProtein BiosynthesisRibosomesRNA, MessengerRNA, TransferBacterial ProteinsGTP PhosphohydrolasesGuanosine TriphosphatePeptide Elongation Factor GRNA, MessengerRNA, Transfer

Identifiers

PMID24362468
OpenAlexW2071993270

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.