Evidence map›Paper›PMID 11060042›Full record

ArticleThe EMBO journal2000

Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms.

C Giglione, A Serero, M Pierre, B Boisson, T Meinnel

Open access · greenAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
7.6field-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

72 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
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  6. Review
  7. Article
  8. Multi-Omics Analysis Revealed thePlants (Basel, Switzerland) · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. The Potential Role of the Methionine Aminopeptidase GeneInternational journal of molecular sciences · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Maternally inherited peptides as strain-specific chemosignals.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Review
  18. Expedient on-resin synthesis of peptidic benzimidazoles.Bioorganic & medicinal chemistry letters · 2018
    Article
  19. Article
  20. Article

12 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

5 authors at 1 institution in 1 country.

C GiglioneInstitut des Sciences Végétales, UPR40, Centre National de la Recherche Scientifique, Bâtiment 23, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette Cedex, France.
A Serero
M Pierre
B Boisson
T Meinnel
Institut des Sciences du Végétal · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N-terminal protein processing pathway is an essential mechanism found in all organisms. However, it is widely believed that deformylase, a key enzyme involved in this process in bacteria, does not exist in eukaryotes, thus making it a target for antibacterial agents such as actinonin. In an attempt to define this process in higher eukaryotes we have used Arabidopsis thaliana as a model organism. Two deformylase cDNAs, the first identified in any eukaryotic system, and six distinct methionine aminopeptidase cDNAs were cloned. The corresponding proteins were characterized in vivo and in vitro. Methionine aminopeptidases were found in the cytoplasm and in the organelles, while deformylases were localized in the organelles only. Our work shows that higher plants have a much more complex machinery for methionine removal than previously suspected. We were also able to identify deformylase homologues from several animals and clone the corresponding cDNA from human cells. Our data provide the first evidence that lower and higher eukaryotes, as well as bacteria, share a similar N-terminal protein processing machinery, indicating universality of this system.

Indexed as

AmidohydrolasesProtein Processing, Post-TranslationalAmino Acid SequenceAminopeptidasesAnimalsArabidopsisCell CompartmentationCloning, MolecularDNA, ComplementaryDNA, PlantDrosophilaEscherichia coliEukaryotic CellsGene ExpressionGenes, PlantHumansAmidohydrolasesAminopeptidasesDNA, ComplementaryDNA, PlantMethionyl Aminopeptidasespeptide deformylasePlant Proteins

Identifiers

PMID11060042
PMCPMC305796
OpenAlexW2042397530

What OpenQuestion holds

Textmetadata
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.