Evidence map›Paper›PMID 20501910›Full record

ArticleThe Plant cell2010

Identification of the 2-hydroxyglutarate and isovaleryl-CoA dehydrogenases as alternative electron donors linking lysine catabolism to the electron transport chain of Arabidopsis mitochondria.

Wagner L Araújo, Kimitsune Ishizaki, Adriano Nunes-Nesi, Tony R Larson, Takayuki Tohge, Ina Krahnert, Sandra Witt, Toshihiro Obata, Nicolas Schauer, Ian A Graham and 2 more

Open access · hybridAbstract 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 178 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
178citing papers in PubMed, 1 pooled it
7.8field-weighted citation impact, top 2% 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

178 citing papers in PubMed, 1 synthesis or guideline pooled it, 324 citations in OpenAlex.

  1. Pooled it
  2. HPlant cell reports · 2026
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  19. Coenzyme Q inMarine drugs · 2023
    Article
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118 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

12 authors at 5 institutions in 3 countries.

Wagner L AraújoMax Planck Institut für Molekulare Pflanzenphysiologie, Golm, Germany.
Kimitsune Ishizaki
Adriano Nunes-Nesi
Tony R Larson
Takayuki Tohge
Ina Krahnert
Sandra Witt
Toshihiro Obata
Nicolas Schauer
Ian A Graham
Christopher J Leaver
Alisdair R Fernie
Max Planck Institute of Molecular Plant Physiology · DEMax Planck Society · DEUniversity of York · GBKyoto University · JPUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The process of dark-induced senescence in plants is relatively poorly understood, but a functional electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO) complex, which supports respiration during carbon starvation, has recently been identified. Here, we studied the responses of Arabidopsis thaliana mutants deficient in the expression of isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase to extended darkness and other environmental stresses. Evaluations of the mutant phenotypes following carbon starvation induced by extended darkness identify similarities to those exhibited by mutants of the ETF/ETFQO complex. Metabolic profiling and isotope tracer experimentation revealed that isovaleryl-CoA dehydrogenase is involved in degradation of the branched-chain amino acids, phytol, and Lys, while 2-hydroxyglutarate dehydrogenase is involved exclusively in Lys degradation. These results suggest that isovaleryl-CoA dehydrogenase is the more critical for alternative respiration and that a series of enzymes, including 2-hydroxyglutarate dehydrogenase, plays a role in Lys degradation. Both physiological and metabolic phenotypes of the isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase mutants were not as severe as those observed for mutants of the ETF/ETFQO complex, indicating some functional redundancy of the enzymes within the process. Our results aid in the elucidation of the pathway of plant Lys catabolism and demonstrate that both isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an ETF/ETFQO-mediated route.

Indexed as

ElectronsAcyl Coenzyme AAlcohol OxidoreductasesArabidopsisCarbohydrate MetabolismDarknessDNA, BacterialElectron TransportGas Chromatography-Mass SpectrometryIsotope LabelingIsovaleryl-CoA DehydrogenaseLeucineLysineMetabolomeMitochondriaModels, Biological2-hydroxyglutarate dehydrogenaseAcyl Coenzyme AAlcohol OxidoreductasesDNA, BacterialIsovaleryl-CoA DehydrogenaseLeucineLysinePhytolT-DNA

Identifiers

PMID20501910
PMCPMC2899879
OpenAlexW2100999167

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.