Evidence map›Paper›PMID 19690000›Full record

ArticlePlant & cell physiology2009

Resolving the role of plant glutamate dehydrogenase. I. In vivo real time nuclear magnetic resonance spectroscopy experiments.

Soraya Labboun, Thérèse Tercé-Laforgue, Albrecht Roscher, Magali Bedu, Francesco M Restivo, Christos N Velanis, Damianos S Skopelitis, Panagiotis N Moschou, Panagiotis N Moshou, Kalliopi A Roubelakis-Angelakis and 2 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Plant & cell physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
11.0field-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

41 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
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  7. Reversible Parahydrogen Induced Hyperpolarization ofAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. NADH-GOGAT Overexpression Does Not Improve Maize (Plants (Basel, Switzerland) · 2020
    Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Moshou, Panagiotis N [corrected to Moschou, Panagiotis N]
5 · Who and what money

Authors and funding

12 authors at 4 institutions in 3 countries.

Soraya LabbounGénie Enzymatique et Cellulaire, UMR CNRS 6022, UFR des Sciences, Université de Picardie Jules Verne, 33, Rue Saint-Leu, 80039 Amiens cedex, France.
Thérèse Tercé-Laforgue
Albrecht Roscher
Magali Bedu
Francesco M Restivo
Christos N Velanis
Damianos S Skopelitis
Panagiotis N Moschou
Panagiotis N Moshou
Kalliopi A Roubelakis-Angelakis
Akira Suzuki
Bertrand Hirel
Institut Jean-Pierre Bourgin · FRUniversity of Crete · GRCentre National de la Recherche Scientifique · FRUniversity of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In higher plants the glutamate dehydrogenase (GDH) enzyme catalyzes the reversible amination of 2-oxoglutarate to form glutamate, using ammonium as a substrate. For a better understanding of the physiological function of GDH either in ammonium assimilation or in the supply of 2-oxoglutarate, we used transgenic tobacco (Nicotiana tabacum L.) plants overexpressing the two genes encoding the enzyme. An in vivo real time (15)N-nuclear magnetic resonance (NMR) spectroscopy approach allowed the demonstration that, when the two GDH genes were overexpressed individually or simultaneously, the transgenic plant leaves did not synthesize glutamate in the presence of ammonium when glutamine synthetase (GS) was inhibited. In contrast we confirmed that the primary function of GDH is to deaminate Glu. When the two GDH unlabeled substrates ammonium and Glu were provided simultaneously with either [(15)N]Glu or (15)NH(4)(+) respectively, we found that the ammonium released from the deamination of Glu was reassimilated by the enzyme GS, suggesting the occurrence of a futile cycle recycling both ammonium and Glu. Taken together, these results strongly suggest that the GDH enzyme, in conjunction with NADH-GOGAT, contributes to the control of leaf Glu homeostasis, an amino acid that plays a central signaling and metabolic role at the interface of the carbon and nitrogen assimilatory pathways. Thus, in vivo NMR spectroscopy appears to be an attractive technique to follow the flux of metabolites in both normal and genetically modified plants.

Indexed as

Glutamate DehydrogenaseGlutamic AcidMagnetic Resonance SpectroscopyNicotianaNitrogenPlant LeavesPlant ProteinsPlants, Genetically ModifiedQuaternary Ammonium CompoundsGlutamate DehydrogenaseGlutamic AcidNitrogenPlant ProteinsQuaternary Ammonium Compounds

Identifiers

PMID19690000
PMCPMC2759343
OpenAlexW2151890299

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.