Evidence map›Paper›PMID 24591715›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2014

Putative role of the malate valve enzyme NADP-malate dehydrogenase in H2O2 signalling in Arabidopsis.

Eiri Heyno, Gilles Innocenti, Stéphane D Lemaire, Emmanuelle Issakidis-Bourguet, Anja Krieger-Liszkay

Open access · bronzeAbstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 54 citations in OpenAlex.

  1. Pooled it
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  7. Redox regulation of NADP-malate dehydrogenase is vital for land plants under fluctuating light environment.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
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  14. Malate valves: old shuttles with new perspectives.Plant biology (Stuttgart, Germany) · 2019
    Review
  15. Article
  16. Moonlighting NADThe Plant cell · 2018
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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

5 authors at 4 institutions in 1 country.

Eiri HeynoCommissariat à l'Energie Atomique (CEA) Saclay, iBiTec-S, CNRS UMR 8221, Service de Bioénergétique, Biologie Structurale et Mécanisme, , 91191 Gif-sur-Yvette Cedex, France.
Gilles Innocenti
Stéphane D Lemaire
Emmanuelle Issakidis-Bourguet
Anja Krieger-Liszkay
CEA Paris-Saclay · FRInstitut des Sciences des Plantes de Paris Saclay · FRSorbonne Université · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In photosynthetic organisms, sudden changes in light intensity perturb the photosynthetic electron flow and lead to an increased production of reactive oxygen species. At the same time, thioredoxins can sense the redox state of the chloroplast. According to our hypothesis, thioredoxins and related thiol reactive molecules downregulate the activity of H2O2-detoxifying enzymes, and thereby allow a transient oxidative burst that triggers the expression of H2O2 responsive genes. It has been shown recently that upon light stress, catalase activity was reversibly inhibited in Chlamydomonas reinhardtii in correlation with a transient increase in the level of H2O2. Here, it is shown that Arabidopsis thaliana mutants lacking the NADP-malate dehydrogenase have lost the reversible inactivation of catalase activity and the increase in H2O2 levels when exposed to high light. The mutants were slightly affected in growth and accumulated higher levels of NADPH in the chloroplast than the wild-type. We propose that the malate valve plays an essential role in the regulation of catalase activity and the accumulation of a H2O2 signal by transmitting the redox state of the chloroplast to other cell compartments.

Indexed as

ArabidopsisCatalaseChloroplastsDNA PrimersElectron Spin Resonance SpectroscopyElectrophoresis, Polyacrylamide GelFluorescenceHydrogen PeroxideImmunoblottingMalate Dehydrogenase (NADP+)Models, BiologicalPhotosynthesisPlant ExtractsPlant LeavesReactive Oxygen SpeciesSignal TransductionCatalaseDNA PrimersHydrogen PeroxideMalate Dehydrogenase (NADP+)Plant ExtractsReactive Oxygen SpeciesThioredoxinscatalaselight stressmalate valvereactive oxygen species

Identifiers

PMID24591715
PMCPMC3949393
OpenAlexW2119399666

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.