Evidence map›Paper›PMID 23584025›Full record

ArticleInternational journal of molecular sciences2013

A differential redox regulation of the pathways metabolizing glyceraldehyde-3-phosphate tunes the production of reducing power in the cytosol of plant cells.

Claudia V Piattoni, Sergio A Guerrero, Alberto A Iglesias

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 40 citations in OpenAlex.

  1. Genomes of NBMC genomics · 2026
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  2. Review
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  5. Silicon enhances plant resistance toFrontiers in plant science · 2022
    Article
  6. Article
  7. Article
  8. A cytosolic oxidation-reduction cycle in plant leaves.Journal of experimental botany · 2021
    Article
  9. Proteomic Investigation ofInternational journal of molecular sciences · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
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

3 authors at 2 institutions in 1 country.

Claudia V PiattoniInstituto de Agrobiotecnología del Litoral (IAL, CONICET-UNL), FBCB, Paraje "El Pozo", CC 242, Santa Fe S3000ZAA, Argentina. iglesias@fbcb.unl.edu.ar.
Sergio A Guerrero
Alberto A Iglesias
National University of the Littoral · ARInstituto de Agrobiotecnología del Litoral · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adaptation to aerobic life leads organisms to sense reactive oxygen species and use the signal for coordination of the entire metabolism. Glycolysis in plants is a particular network where specific steps, like oxidation of glyceraldehydes-3-phosphate (Ga3P), are critical in order for it to function. The triose-phosphate can be converted into 3-phosphoglycerate through the phosphorylating Ga3P dehydrogenase (Ga3PDHase, EC 1.2.1.12) producing ATP and NADH, or via the non-phosphorylating enzyme (np-Ga3PDHase; EC 1.2.1.9) generating NADPH. In this work we found redox regulation to be a posttranslational mechanism allowing the fine-tuning of the triose-phosphate fate. Both enzymes were inactivated after oxidation by reactive oxygen and nitrogen species. Kinetic studies determined that Ga3PDHase is marked (63-fold) more sensitive to oxidants than np-Ga3PDHase. Thioredoxin-h reverted the oxidation of both enzymes (although with differences between them), suggesting a physiological redox regulation. The results support a metabolic scenario where the cytosolic triose-phosphate dehydrogenases are regulated under changeable redox conditions. This would allow coordinate production of NADPH or ATP through glycolysis, with oxidative signals triggering reducing power synthesis in the cytosol. The NADPH increment would favor antioxidant responses to cope with the oxidative situation, while the thioredoxin system would positively feedback NADPH production by maintaining np-Ga3PDHase at its reduced active state.

Indexed as

CytosolGlyceraldehyde 3-PhosphateGlyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisKineticsMetabolic Networks and PathwaysOxidation-ReductionPlant CellsPlant ProteinsProtein Processing, Post-TranslationalRecombinant ProteinsTriticumGlyceraldehyde 3-PhosphateGlyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Plant ProteinsRecombinant Proteins

Identifiers

PMID23584025
PMCPMC3645732
OpenAlexW2074657895

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.