Evidence map›Paper›PMID 25326326›Full record

ArticleNucleic acids research2014

Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.

Thibaut Crepin, Vyacheslav F Shalak, Anna D Yaremchuk, Dmytro O Vlasenko, Andrew McCarthy, Boris S Negrutskii, Michail A Tukalo, Anna V El'skaya

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 55 citations in OpenAlex.

  1. RNAViruses · 2026
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  6. Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.bioRxiv : the preprint server for biology · 2025
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  12. Glycosylating Effectors ofBiomolecules · 2022
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  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 at 4 institutions in 2 countries.

Thibaut CrepinUniversity of Grenoble Alpes, UVHCI, F-38000 Grenoble, France CNRS, UVHCI, F-38000 Grenoble, France Unit for Virus Host-Cell Interactions, University of Grenoble Alpes-EMBL-CNRS, 71 avenue des Martyrs, 38042 France.
Vyacheslav F ShalakState Key laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine.
Anna D YaremchukState Key laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine European Molecular Biology Laboratory, Grenoble Outstation, 71 avenue des Martyrs, 38042 France.
Dmytro O VlasenkoState Key laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine.
Andrew McCarthyUnit for Virus Host-Cell Interactions, University of Grenoble Alpes-EMBL-CNRS, 71 avenue des Martyrs, 38042 France European Molecular Biology Laboratory, Grenoble Outstation, 71 avenue des Martyrs, 38042 France.
Boris S NegrutskiiState Key laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine negrutskii@imbg.org.ua.
Michail A TukaloState Key laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine.
Anna V El'skayaState Key laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo str., Kiev 03680, Ukraine anna.elskaya@yahoo.com.
Institute of Molecular Biology and Genetics · UACentre National de la Recherche Scientifique · FREuropean Molecular Biology Laboratory · FRUniversité Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. eEF1A*GTP establishes a complex with the aminoacyl-tRNA in the A site of the 80S ribosome. Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. The structures of both the 'GTP'- and 'GDP'-bound conformations of eEF1A are unknown. Thus, the eEF1A-related ribosomal mechanisms were anticipated only by analogy with the bacterial homolog EF-Tu. Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis.

Indexed as

AnimalsCrystallography, X-RayGuanosine DiphosphateGuanosine TriphosphateMagnesiumModels, MolecularPeptide Elongation Factor 1Protein BindingProtein ConformationProtein IsoformsRabbitsGuanosine DiphosphateGuanosine TriphosphateMagnesiumPeptide Elongation Factor 1Protein Isoforms

Identifiers

PMID25326326
PMCPMC4227793
OpenAlexW2132307548

What OpenQuestion holds

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LicenceCC BY-NC
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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.