Evidence map›Paper›PMID 21169366›Full record

ArticleThe Journal of biological chemistry2011

NADPH-dependent reductases involved in the detoxification of reactive carbonyls in plants.

Yasuo Yamauchi, Ayaka Hasegawa, Ai Taninaka, Masaharu Mizutani, Yukihiro Sugimoto

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
–field-weighted citation impact
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

70 citing papers in PubMed.

  1. Proteomic and Molecular Biological Analyses of Response Mechanism in Rice (International journal of molecular sciences · 2026
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  10. Roles of Reactive Carbonyl Species (RCS) in Plant Response to Abiotic Stress.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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  12. Review
  13. Enhanced growth rate under elevated COPlant molecular biology · 2022
    Article
  14. Article
  15. Article
  16. Knockout ofMetabolites · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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.

Yasuo YamauchiLaboratory of Functional Phytochemistry, Graduate School of Agricultural Science, Kobe University, Rokkodai 1-1, Nada, Kobe 657-8501, Japan. yamauchi@kobe-u.ac.jp
Ayaka Hasegawa
Ai Taninaka
Masaharu Mizutani
Yukihiro Sugimoto

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reactive carbonyls, especially α,β-unsaturated carbonyls produced through lipid peroxidation, damage biomolecules such as proteins and nucleotides; elimination of these carbonyls is therefore essential for maintaining cellular homeostasis. In this study, we focused on an NADPH-dependent detoxification of reactive carbonyls in plants and explored the enzyme system involved in this detoxification process. Using acrolein (CH(2) = CHCHO) as a model α,β-unsaturated carbonyl, we purified a predominant NADPH-dependent acrolein-reducing enzyme from cucumber leaves, and we identified the enzyme as an alkenal/one oxidoreductase (AOR) catalyzing reduction of an α,β-unsaturated bond. Cloning of cDNA encoding AORs revealed that cucumber contains two distinct AORs, chloroplastic AOR and cytosolic AOR. Homologs of cucumber AORs were found among various plant species, including Arabidopsis, and we confirmed that a homolog of Arabidopsis (At1g23740) also had AOR activity. Phylogenetic analysis showed that these AORs belong to a novel class of AORs. They preferentially reduced α,β-unsaturated ketones rather than α,β-unsaturated aldehydes. Furthermore, we selected candidates of other classes of enzymes involved in NADPH-dependent reduction of carbonyls based on the bioinformatic information, and we found that an aldo-keto reductase (At2g37770) and aldehyde reductases (At1g54870 and At3g04000) were implicated in the reduction of an aldehyde group of saturated aldehydes and methylglyoxal as well as α,β-unsaturated aldehydes in chloroplasts. These results suggest that different classes of NADPH-dependent reductases cooperatively contribute to the detoxification of reactive carbonyls.

Indexed as

AcroleinAlcohol OxidoreductasesAldehyde ReductaseAldehydesAldo-Keto ReductasesArabidopsisArabidopsis ProteinsChloroplastsCucumis sativusLipid PeroxidationMolecular Sequence DataNADPOxidoreductasesPyruvaldehydeSubstrate SpecificityAcroleinAlcohol OxidoreductasesAldehyde ReductaseAldehydesAldo-Keto ReductasesArabidopsis ProteinsAt2g37770 protein, ArabidopsisNADPOxidoreductasesPyruvaldehyde

Identifiers

PMID21169366
PMCPMC3044956

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.