Evidence map›Paper›PMID 20444696›Full record

ReviewThe Journal of biological chemistry2010

eEF1A: thinking outside the ribosome.

Maria K Mateyak, Terri Goss Kinzy

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 264 citations in OpenAlex.

  1. Review
  2. RiboScreenBiomedicines · 2026
    Review
  3. Article
  4. Comparative Analysis of the EF-1α Intergenic Region inInternational journal of molecular sciences · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. KAT8-catalyzed lactylation promotes eEF1A2-mediated protein synthesis and colorectal carcinogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

87 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

2 authors at 1 institution in 1 country.

Maria K MateyakDepartment of Molecular Genetics, Microbiology and Immunology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854-5635, USA.
Terri Goss Kinzy
Rutgers, The State University of New Jersey · US

Funding

Regulators of Translation Elongation Factor eEF1AR01GM057483 · NIGMS · WESTERN MICHIGAN UNIVERSITY · PI KINZY, TERRI GOSS · 1998 to 2017
$5.4M
NIGMS NIH HHS GM057483NIGMS NIH HHS R01 GM057483
6 · The paper itself

Abstract

Eukaryotic translation elongation factor 1A (eEF1A) is one of the most abundant protein synthesis factors. eEF1A is responsible for the delivery of all aminoacyl-tRNAs to the ribosome, aside from initiator and selenocysteine tRNAs. In addition to its roles in polypeptide chain elongation, unique cellular and viral activities have been attributed to eEF1A in eukaryotes from yeast to plants and mammals. From preliminary, speculative associations to well characterized biochemical and biological interactions, it is clear that eEF1A, of all the translation factors, has been ascribed the most functions outside of protein synthesis. A mechanistic understanding of these non-canonical functions of eEF1A will shed light on many important biological questions, including viral-host interaction, subcellular organization, and the integration of key cellular pathways.

Indexed as

Protein BiosynthesisActinsActive Transport, Cell NucleusApoptosisCytoskeletonEukaryotic Initiation Factor-1HumansPeptide Elongation FactorsProtein ConformationRibosomesRNA, TransferRNA VirusesSaccharomyces cerevisiaeSelenocysteineActinsEukaryotic Initiation Factor-1eukaryotic peptide initiation factor-1APeptide Elongation FactorsRNA, TransferSelenocysteine

Identifiers

PMID20444696
PMCPMC2898402
OpenAlexW2039869230

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.