Evidence map›Paper›PMID 19546244›Full record

ArticleThe Journal of cell biology2009

The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy.

Prajal H Patel, Mauro Costa-Mattioli, Karen L Schulze, Hugo J Bellen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

44 citing papers in PubMed, 75 citations in OpenAlex.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. The hypusine pathway inFrontiers in cellular and infection microbiology · 2025
    Article
  4. Article
  5. Article
  6. Protein modification regulated autophagy inFrontiers in physiology · 2023
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Flexible NADInternational journal of molecular sciences · 2020
    Article
  13. Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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 2 institutions in 2 countries.

Prajal H PatelProgram in Developmental Biology, Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA.
Mauro Costa-Mattioli
Karen L Schulze
Hugo J Bellen
Center for Neurosciences · USInstitute of Developmental Physiology · RU

Funding

UNDERSTANDING FXTAS AMONG MALES WITH THE FMR1 PREMUTATIONP30HD024064 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI TOLIAS, KIMBERLY R · 1988 to 2013
$29.4M
Developmental Biology Training ProgramT32HD055200 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI BELLEN, HUGO J · 2007 to 2011
$1.3M
DEVELOPMENT BIOLOGY TRAINING PROGRAMT32ES007332 · NIEHS · BAYLOR COLLEGE OF MEDICINE · PI BELLEN, HUGO J. · 2000 to 2006
$781k
Howard Hughes Medical InstituteNICHD NIH HHS P30 HD024064NICHD NIH HHS T32 HD055200NIEHS NIH HHS T32 ES007332NIEHS NIH HHS T32 ES07332
6 · The paper itself

Abstract

Hypusination is a unique posttranslational modification by which lysine is transformed into the atypical amino acid hypusine. eIF5A (eukaryotic initiation factor 5A) is the only known protein to contain hypusine. In this study, we describe the identification and characterization of nero, the Drosophila melanogaster deoxyhypusine hydroxylase (DOHH) homologue. nero mutations affect cell and organ size, bromodeoxyuridine incorporation, and autophagy. Knockdown of the hypusination target eIF5A via RNA interference causes phenotypes similar to nero mutations. However, loss of nero appears to cause milder phenotypes than loss of eIF5A. This is partially explained through a potential compensatory mechanism by which nero mutant cells up-regulate eIF5A levels. The failure of eIF5A up-regulation to rescue nero mutant phenotypes suggests that hypusination is required for eIF5A function. Furthermore, expression of enzymatically impaired forms of DOHH fails to rescue nero clones, indicating that hypusination activity is important for nero function. Our data also indicate that nero and eIF5A are required for cell growth and affect autophagy and protein synthesis.

Indexed as

AnimalsAnimals, Genetically ModifiedAutophagyCell CycleCell Growth ProcessesDrosophila melanogasterDrosophila ProteinsEukaryotic Translation Initiation Factor 5AGene Knockdown TechniquesMixed Function OxygenasesPeptide Initiation FactorsPhenotypeProtein Processing, Post-TranslationalRecombinant Fusion ProteinsRNA-Binding ProteinsRNA Interferencedeoxyhypusine hydroxylaseDrosophila ProteinsEukaryotic Translation Initiation Factor 5AMixed Function OxygenasesPeptide Initiation FactorsRecombinant Fusion ProteinsRNA-Binding Proteins

Identifiers

PMID19546244
PMCPMC2712966
OpenAlexW2099522996

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.