Evidence map›Paper›PMID 25428993›Full record

ArticleJournal of experimental botany2015

Differential inhibition of Arabidopsis superoxide dismutases by peroxynitrite-mediated tyrosine nitration.

Christian Holzmeister, Frank Gaupels, Arie Geerlof, Hakan Sarioglu, Michael Sattler, Jörg Durner, Christian Lindermayr

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

52 citing papers in PubMed, 129 citations in OpenAlex.

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  12. Functions of NO and HMethods in molecular biology (Clifton, N.J.) · 2023
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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 2 institutions in 1 country.

Christian HolzmeisterInstitute of Biochemical Plant Pathology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany.
Frank GaupelsInstitute of Biochemical Plant Pathology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany.
Arie GeerlofInstitute of Structural Biology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany.
Hakan SariogluDepartment of Protein Science, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany.
Michael SattlerInstitute of Structural Biology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany Munich Center for Integrated Protein Science at Chair of Biomolecular NMR, Department Chemie, Technische Universität München, 85747 Garching, Germany.
Jörg DurnerInstitute of Biochemical Plant Pathology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany Chair of Biochemical Plant Pathology, Technische Universität München, 85354 Freising, Germany.
Christian LindermayrInstitute of Biochemical Plant Pathology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany Lindermayr@helmholtz-muenchen.de.
Helmholtz Zentrum München · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the importance of superoxide dismutases (SODs) in the plant antioxidant defence system little is known about their regulation by post-translational modifications. Here, we investigated the in vitro effects of nitric oxide derivatives on the seven SOD isoforms of Arabidopsis thaliana. S-nitrosoglutathione, which causes S-nitrosylation of cysteine residues, did not influence SOD activities. By contrast, peroxynitrite inhibited the mitochondrial manganese SOD1 (MSD1), peroxisomal copper/zinc SOD3 (CSD3), and chloroplastic iron SOD3 (FSD3), but no other SODs. MSD1 was inhibited by up to 90% but CSD3 and FSD3 only by a maximum of 30%. Down-regulation of these SOD isoforms correlated with tyrosine (Tyr) nitration and both could be prevented by the peroxynitrite scavenger urate. Site-directed mutagenesis revealed that-amongst the 10 Tyr residues present in MSD1-Tyr63 was the main target responsible for nitration and inactivation of the enzyme. Tyr63 is located nearby the active centre at a distance of only 5.26 Å indicating that nitration could affect accessibility of the substrate binding pocket. The corresponding Tyr34 of human manganese SOD is also nitrated, suggesting that this might be an evolutionarily conserved mechanism for regulation of manganese SODs.

Indexed as

Amino Acid SequenceArabidopsisPeroxynitrous AcidPlant ProteinsSequence AlignmentSuperoxide DismutaseTyrosinePeroxynitrous AcidPlant ProteinsSuperoxide DismutaseTyrosineAntioxidant systemnitric oxidenitrosative stresspost-translational modificationsuperoxide dismutasetyrosine nitration.

Identifiers

PMID25428993
PMCPMC4321555
OpenAlexW2108123792

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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.