Evidence map›Paper›PMID 25029904›Full record

ReviewCritical reviews in biochemistry and molecular biology

The hypusine-containing translation factor eIF5A.

Thomas E Dever, Erik Gutierrez, Byung-Sik Shin

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

95 citing papers in PubMed, 184 citations in OpenAlex.

  1. eIF5A coordinates the transcription and translation of its target genes.Cellular and molecular life sciences : CMLS · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Engineering small peptide secretion inFrontiers in bioengineering and biotechnology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Targeted inhibition of eIF5ACell death & disease · 2023
    Article
  18. Article
  19. Article
  20. Article

35 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

3 authors at 3 institutions in 1 country.

Thomas E DeverLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health , Bethesda, MD , USA and.
Erik Gutierrez
Byung-Sik Shin
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USJohns Hopkins University · USNational Institutes of Health · US

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
Intramural NIH HHS ZIA HD001010
6 · The paper itself

Abstract

In addition to the small and large ribosomal subunits, aminoacyl-tRNAs, and an mRNA, cellular protein synthesis is dependent on translation factors. The eukaryotic translation initiation factor 5A (eIF5A) and its bacterial ortholog elongation factor P (EF-P) were initially characterized based on their ability to stimulate methionyl-puromycin (Met-Pmn) synthesis, a model assay for protein synthesis; however, the function of these factors in cellular protein synthesis has been difficult to resolve. Interestingly, a conserved lysine residue in eIF5A is post-translationally modified to hypusine and the corresponding lysine residue in EF-P from at least some bacteria is modified by the addition of a β-lysine moiety. In this review, we provide a summary of recent data that have identified a novel role for the translation factor eIF5A and its hypusine modification in the elongation phase of protein synthesis and more specifically in stimulating the production of proteins containing runs of consecutive proline residues.

Indexed as

Amino Acid SequenceAnimalsEukaryotic Translation Initiation Factor 5AHumansLysineModels, MolecularMolecular Sequence DataPeptide Elongation FactorsPeptide Initiation FactorsPeptidesRibosomesRNA-Binding ProteinsEukaryotic Translation Initiation Factor 5Afactor EF-PhypusineLysinePeptide Elongation FactorsPeptide Initiation FactorsPeptidespolyprolineRNA-Binding ProteinsDeoxyhypusine hydroxylasedeoxyhypusine synthaseelongation factorpolyprolinetranslation elongation

Identifiers

PMID25029904
PMCPMC4183722
OpenAlexW1970474745

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.