Evidence map›Paper›PMID 23727016›Full record

ArticleMolecular cell2013

eIF5A promotes translation of polyproline motifs.

Erik Gutierrez, Byung-Sik Shin, Christopher J Woolstenhulme, Joo-Ran Kim, Preeti Saini, Allen R Buskirk, Thomas E Dever

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 338 papers.

0numbers the graph read from it
0cells of the map it votes in
338citing papers in PubMed
18.8field-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

338 citing papers in PubMed, 552 citations in OpenAlex.

  1. Trial
  2. Article
  3. Pyrrolysine supply and demand shapes the translational landscape inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  6. Article
  7. eIF5A and polyamines restrict mRNA levels in response to ribosome stalls.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Ribosome stalling position, spacing, and A-site occupancy impact translation and cotranslational mRNA decay in plants.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. eIF5A coordinates the transcription and translation of its target genes.Cellular and molecular life sciences : CMLS · 2026
    Article
  19. Article
  20. Review

278 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

7 authors at 4 institutions in 2 countries.

Erik GutierrezLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Byung-Sik Shin
Christopher J Woolstenhulme
Joo-Ran Kim
Preeti Saini
Allen R Buskirk
Thomas E Dever
Brigham Young University · USEunice Kennedy Shriver Center · USEunice Kennedy Shriver National Institute of Child Health and Human Development · USGene Therapy Laboratory · FR

Funding

Mechanism and Regulation of Eukaryotic Protein SynthesisZIAHD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 2009 to 2025
$29.4M
Genetic studies on bacterial trans-translationR01GM077633 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI BUSKIRK, ALLEN ROWDON · 2006 to 2010
$1.3M
Intramural NIH HHS ZIA HD001010NIGMS NIH HHS GM77633NIGMS NIH HHS R01 GM077633
6 · The paper itself

Abstract

Translation factor eIF5A, containing the unique amino acid hypusine, was originally shown to stimulate Met-puromycin synthesis, a model assay for peptide bond formation. More recently, eIF5A was shown to promote translation elongation; however, its precise requirement in protein synthesis remains elusive. We use in vivo assays in yeast and in vitro reconstituted translation assays to reveal a specific requirement for eIF5A to promote peptide bond formation between consecutive Pro residues. Addition of eIF5A relieves ribosomal stalling during translation of three consecutive Pro residues in vitro, and loss of eIF5A function impairs translation of polyproline-containing proteins in vivo. Hydroxyl radical probing experiments localized eIF5A near the E site of the ribosome with its hypusine residue adjacent to the acceptor stem of the P site tRNA. Thus, eIF5A, like its bacterial ortholog EFP, is proposed to stimulate the peptidyl transferase activity of the ribosome and facilitate the reactivity of poor substrates like Pro.

Indexed as

Amino Acid MotifsProtein BiosynthesisEukaryotic Translation Initiation Factor 5AModels, BiologicalModels, MolecularPeptide Initiation FactorsPeptidesProtein Structure, TertiaryRibosomesRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEukaryotic Translation Initiation Factor 5APeptide Initiation FactorsPeptidespolyprolineRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID23727016
PMCPMC3744875
OpenAlexW1968202347

What OpenQuestion holds

Textmetadata
LicenceTDM
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.