Evidence map›Paper›PMID 21246257›Full record

ArticlePlant molecular biology2011

Overproduction of a rice aldo-keto reductase increases oxidative and heat stress tolerance by malondialdehyde and methylglyoxal detoxification.

Zoltán Turóczy, Petra Kis, Katalin Török, Mátyás Cserháti, Agnes Lendvai, Dénes Dudits, Gábor V Horváth

Abstract read
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In one paragraph

Article in Plant molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.6field-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

59 citing papers in PubMed, 157 citations in OpenAlex.

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  12. Genome-Wide Identification and Characterization ofInternational journal of molecular sciences · 2023
    Article
  13. Pyramiding of transcription factor,Frontiers in plant science · 2023
    Article
  14. Article
  15. Review
  16. Antioxidants (Basel, Switzerland) · 2022
    Article
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  18. Review
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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

7 authors at 3 institutions in 1 country.

Zoltán TuróczyInstitute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, 6726, Szeged, Hungary.
Petra Kis
Katalin Török
Mátyás Cserháti
Agnes Lendvai
Dénes Dudits
Gábor V Horváth
Hungarian Academy of Sciences · HUInstitute of Plant Biology · HUHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The accumulation of toxic compounds generated by the interaction between reactive oxygen species and polyunsaturated fatty acids of membrane lipids can significantly damage plant cells. A plethora of enzymes act on these reactive carbonyls, reducing their toxicity. Based on the chromosomal localization and on their homology with other stress-induced aldo-keto reductases (AKRs) we have selected three rice AKR genes. The transcription level of OsAKR1 was greatly induced by abscisic acid and various stress treatments; the other two AKR genes tested were moderately stress-inducible. The OsAKR1 recombinant protein exhibited a high nicotinamide adenine dinucleotide phosphate-dependent catalytic activity to reduce toxic aldehydes including glycolysis-derived methylglyoxal (MG) and lipid peroxidation-originated malondialdehyde (MDA). The function of this enzyme in MG detoxification was demonstrated in vivo in E. coli and in transgenic plants overproducing the OsAKR1 protein. Heterologous synthesis of the OsAKR1 enzyme in transgenic tobacco plants resulted in increased tolerance against oxidative stress generated by methylviologen (MV) and improved resistance to high temperature. In these plants lower levels of MDA were detected both following MV and heat treatment due to the activity of the OsAKR1 enzyme. The transgenic tobaccos also exhibited higher AKR activity and accumulated less MG in their leaves than the wild type plants; both in the presence and absence of heat stress. These results support the positive role of OsAKR1 in abiotic stress-related reactive aldehyde detoxification pathways and its use for improvement of stress tolerance in plants.

Indexed as

AcclimatizationAlcohol OxidoreductasesAldehyde ReductaseAldo-Keto ReductasesEscherichia coliGenes, PlantHot TemperatureMalondialdehydeMembrane LipidsNicotianaOryzaOxidative StressPhylogenyPlants, Genetically ModifiedPyruvaldehydeRecombinant Fusion ProteinsAlcohol OxidoreductasesAldehyde ReductaseAldo-Keto ReductasesMalondialdehydeMembrane LipidsPyruvaldehydeRecombinant Fusion Proteins

Identifiers

PMID21246257
OpenAlexW2060742338

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.