Evidence map›Paper›PMID 20442374›Full record

ArticleThe Plant cell2010

A soluble guanylate cyclase mediates negative signaling by ammonium on expression of nitrate reductase in Chlamydomonas.

Amaury de Montaigu, Emanuel Sanz-Luque, Aurora Galván, Emilio Fernández

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
7.0field-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.

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

42 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Review
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  6. Molecular Mechanisms Underlying the Acclimation ofFrontiers in plant science · 2021
    Article
  7. Identification of Partner Proteins of the AlgaeFrontiers in plant science · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Algal photosynthesis converts nitric oxide into nitrous oxide.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
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  15. Review
  16. Article
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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 1 institution in 1 country.

Amaury de MontaiguDepartamento de Bioquímica y Biología Molecular, Universidad de Córdoba, Córdoba, Spain.
Emanuel Sanz-Luque
Aurora Galván
Emilio Fernández
University of Córdoba · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrate assimilation in plants and related organisms is a highly regulated and conserved pathway in which the enzyme nitrate reductase (NR) occupies a central position. Although some progress has been made in understanding the regulation of the protein, transcriptional regulation of the NR gene (NIA1) is poorly understood. This work describes a mechanism for the ammonium-mediated repression of NIA1. We report the characterization of a mutant defective in the repression of NIA1 and NR in response to ammonium and show that a gene (CYG56) coding for a nitric oxide (NO)-dependent guanylate cyclase (GC) was interrupted in this mutant. NO donors, cGMP analogs, a phosphodiesterase inhibitor isobutylmethylxanthine (IBMX), and a calcium ionophore (A23187) repress the expression of NIA1 in Chlamydomonas reinhardtii wild-type cells and also repress the expression of other ammonium-sensitive genes. In addition, the GC inhibitors LY83,583 (6-anilino-5,8-quinolinedione) and ODQ (1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one) release cells from ammonium repression. Intracellular NO and cGMP levels were increased in the presence of ammonium in wild-type cells. In the cyg56 mutant, NIA1 transcription was less sensitive to NO donors and A23187, but responded like the wild type to IBMX. Results presented here suggest that CYG56 participates in ammonium-mediated NIA1 repression through a pathway that involves NO, cGMP, and calcium and that similar mechanisms might be occurring in plants.

Indexed as

AminoquinolinesArabidopsisArabidopsis ProteinsCalciumChlamydomonas reinhardtiiCyclic GMPCyclic N-OxidesGene Expression Regulation, EnzymologicGuanylate CyclaseImidazolesModels, BiologicalMolecular Sequence DataMutationNG-Nitroarginine Methyl EsterNitrate ReductaseNitric Oxide1H-(1,2,4)oxadiazolo(4,3-a)quinoxalin-1-one2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide6-anilino-5,8-quinolinedioneAminoquinolinesArabidopsis ProteinsCalciumCyclic GMPCyclic N-OxidesGuanylate CyclaseImidazolesNG-Nitroarginine Methyl EsterNitrate ReductaseNitric OxideNitrogenOxadiazolesQuaternary Ammonium CompoundsQuinoxalinesReceptors, Cytoplasmic and NuclearSoluble Guanylyl Cyclase

Identifiers

PMID20442374
PMCPMC2899865
OpenAlexW2118847772

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.