Evidence map›Paper›PMID 19997760›Full record

ReviewAmino acids2010

Functional significance of eIF5A and its hypusine modification in eukaryotes.

M H Park, K Nishimura, C F Zanelli, S R Valentini

Registry-linked trialOpen access · greenAbstract readReview
In one paragraph

Review in Amino acids, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT05594563 (TArgeting Type 1 Diabetes Using POLyamines), which is not on this map. Cited by 181 papers.

0numbers the graph read from it
0cells of the map it votes in
181citing papers in PubMed
6.5field-weighted citation impact, top 3% 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.

NCT05594563 phase2active not recruitingnot on this mapstarted 2023, after this paper: background citation

TArgeting Type 1 Diabetes Using POLyamines (TADPOL): A Randomized, Double-Masked, Placebo-Controlled Phase 2 Study to Evaluate the Efficacy and Safety of Difluoromethylornithine (DFMO) to Preserve Insulin Production in Type 1 Diabetes

TypeinterventionalSponsorEmily K. SimsRan2023 to 2027Enrolled74ConditionsType 1 DiabetesArmsDFMO, Placebo
3 · Its place in the literature

Who cites it

181 citing papers in PubMed, 346 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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  12. Article
  13. Effect of Temperature on Polyamine Oxidase Genes inInternational journal of molecular sciences · 2025
    Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Article
  20. Article

121 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

4 authors at 3 institutions in 2 countries.

M H ParkOral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bldg 30, Room 211, Bethesda, MD 20892-4340, USA. mhpark@nih.gov
K Nishimura
C F Zanelli
S R Valentini
Universidade Estadual Paulista (Unesp) · BRNational Institute of Dental and Craniofacial Research · USNational Institutes of Health · US

Funding

The Post-translational Synthesis of Hypusine In eIF5A and roles of eIF5A and polyamines in cell growth and animal developmentZIADE000608 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI PARK, MYUNG HEE · 2009 to 2021
$12.3M
Intramural NIH HHS ZIA DE000608
6 · The paper itself

Abstract

The unusual basic amino acid, hypusine [N(epsilon)-(4-amino-2-hydroxybutyl)-lysine], is a modified lysine with the addition of the 4-aminobutyl moiety from the polyamine spermidine. This naturally occurring amino acid is a product of a unique posttranslational modification that occurs in only one cellular protein, eukaryotic translation initiation factor 5A (eIF5A, eIF-5A). Hypusine is synthesized exclusively in this protein by two sequential enzymatic steps involving deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). The deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, and eIF5A, DHS and DOHH are highly conserved suggesting a vital cellular function of eIF5A. Gene disruption and mutation studies in yeast and higher eukaryotes have provided valuable information on the essential nature of eIF5A and the deoxyhypusine/hypusine modification in cell growth and in protein synthesis. In view of the extraordinary specificity and functional significance of hypusine-containing eIF5A in mammalian cell proliferation, eIF5A and the hypusine biosynthetic enzymes are novel potential targets for intervention in aberrant cell proliferation.

Indexed as

AnimalsBacteriaBacterial ProteinsEukaryotaEukaryotic Translation Initiation Factor 5AFungal ProteinsFungiHumansLysinePeptide Initiation FactorsProtein Structure, SecondaryRNA-Binding ProteinsBacterial ProteinsEukaryotic Translation Initiation Factor 5AFungal ProteinshypusineLysinePeptide Initiation FactorsRNA-Binding Proteins

Identifiers

PMID19997760
PMCPMC2829442
OpenAlexW2083119952

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

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.