Evidence map›Paper›PMID 25979826›Full record

ReviewBiochimica et biophysica acta2015

The translation factor eIF5A and human cancer.

Michael B Mathews, John W B Hershey

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
6.9field-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

117 citing papers in PubMed, 198 citations in OpenAlex.

  1. Article
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  8. Polyamine metabolism in prostate cancer.Current opinion in oncology · 2025
    Review
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57 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.

Michael B MathewsDepartment of Medicine, Rutgers New Jersey Medical School, Newark, NJ 07103, USA. Electronic address: mathews@njms.rutgers.edu.
John W B HersheyDepartment of Biochemistry and Molecular Medicine, University of California Davis School of Medicine, Davis, CA 95616, USA. Electronic address: jwhershey@ucdavis.edu.
University of California, Davis · US

Funding

Structured RNAs Binding to Proteins Containing the dsRBDR21HG006339 · NHGRI · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI MATHEWS, MICHAEL B, TIAN, BIN · 2012 to 2013
$436k
NHGRI NIH HHS R21 HG006339NHGRI NIH HHS R21HG006339
6 · The paper itself

Abstract

The eukaryotic initiation factor eIF5A is a translation factor that, unusually, has been assigned functions in both initiation and elongation. Additionally, it is implicated in transcription, mRNA turnover and nucleocytoplasmic transport. Two eIF5A isoforms are generated from distinct but related genes. The major isoform, eIF5A1, is considered constitutive, is abundantly expressed in most cells, and is essential for cell proliferation. The second isoform, eIF5A2, is expressed in few normal tissues but is highly expressed in many cancers and has been designated a candidate oncogene. Elevated expression of either isoform carries unfavorable prognostic implications for several cancers, and both have been advanced as cancer biomarkers. The amino acid hypusine, a presumptively unique eIF5A post-translational modification, is required for most known eIF5A functions and it renders eIF5A susceptible to inhibitors of the modification pathway as therapeutic targets. eIF5A has been shown to regulate a number of gene products specifically, termed the eIF5A regulon, and its role in translating proline-rich sequences has recently been identified. A model is advanced that accommodates eIF5A in both the initiation and elongation phases of translation. We review here the biochemical functions of eIF5A, the relationship of its isoforms with human cancer, and evolving clinical applications. This article is part of a Special Issue entitled: Translation and Cancer.

Indexed as

Gene Expression RegulationPeptide Chain Elongation, TranslationalPeptide Chain Initiation, TranslationalEukaryotic Translation Initiation Factor 5AHumansLysineNeoplasmsOncogene ProteinsPeptide Initiation FactorsProtein IsoformsProtein Processing, Post-TranslationalRNA-Binding ProteinsEukaryotic Translation Initiation Factor 5AhypusineLysineOncogene ProteinsPeptide Initiation FactorsProtein IsoformsRNA-Binding ProteinsCancer therapeuticsEukaryotic initiation factor eIF5AHypusine modificationProtein synthesisTranslational controlTumorigenesis

Identifiers

PMID25979826
PMCPMC4732523
OpenAlexW272899539

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.