Evidence map›Paper›PMID 24288182›Full record

ArticleJournal of experimental botany2014

Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation.

Juan C Begara-Morales, Beatriz Sánchez-Calvo, Mounira Chaki, Raquel Valderrama, Capilla Mata-Pérez, Javier López-Jaramillo, María N Padilla, Alfonso Carreras, Francisco J Corpas, Juan B Barroso

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

124 citing papers in PubMed, 328 citations in OpenAlex.

  1. Review
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  6. Integration of NO and HPlant communications · 2026
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64 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

10 authors at 3 institutions in 1 country.

Juan C Begara-MoralesÁrea de Bioquímica y Biología Molecular, Departamento de Biología Experimental, Facultad de Ciencias Experimentales, Ed. B3. Campus Universitario "Las Lagunillas" s/n, Universidad de Jaén, E-23071 Jaén, Spain.
Beatriz Sánchez-Calvo
Mounira Chaki
Raquel Valderrama
Capilla Mata-Pérez
Javier López-Jaramillo
María N Padilla
Alfonso Carreras
Francisco J Corpas
Juan B Barroso
Universidad de Jaén · ESConsejo Superior de Investigaciones Científicas · ESUniversidad de Granada · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications (PTMs) mediated by nitric oxide (NO)-derived molecules have become a new area of research, as they can modulate the function of target proteins. Proteomic data have shown that ascorbate peroxidase (APX) is one of the potential targets of PTMs mediated by NO-derived molecules. Using recombinant pea cytosolic APX, the impact of peroxynitrite (ONOO-) and S-nitrosoglutathione (GSNO), which are known to mediate protein nitration and S-nitrosylation processes, respectively, was analysed. While peroxynitrite inhibits APX activity, GSNO enhances its enzymatic activity. Mass spectrometric analysis of the nitrated APX enabled the determination that Tyr5 and Tyr235 were exclusively nitrated to 3-nitrotyrosine by peroxynitrite. Residue Cys32 was identified by the biotin switch method as S-nitrosylated. The location of these residues on the structure of pea APX reveals that Tyr235 is found at the bottom of the pocket where the haem group is enclosed, whereas Cys32 is at the ascorbate binding site. Pea plants grown under saline (150 mM NaCl) stress showed an enhancement of both APX activity and S-nitrosylated APX, as well as an increase of H2O2, NO, and S-nitrosothiol (SNO) content that can justify the induction of the APX activity. The results provide new insight into the molecular mechanism of the regulation of APX which can be both inactivated by irreversible nitration and activated by reversible S-nitrosylation.

Indexed as

Amino AcidsAmino Acid SequenceAscorbate PeroxidasesChromatography, LiquidCytosolElectrophoresis, Polyacrylamide GelHydrogen PeroxideLipid PeroxidationMass SpectrometryModels, MolecularMolecular Sequence DataNitrosationOxidative StressPeptidesPeroxynitrous AcidPisum sativumAmino AcidsAscorbate PeroxidasesHydrogen PeroxidePeptidesPeroxynitrous AcidPlant ProteinsRecombinant ProteinsS-NitrosoglutathioneSodium ChlorideTyrosineAscorbate peroxidasenitrationnitric oxideperoxynitritereactive nitrogen speciessalinity stress.S-nitrosoglutathioneS-nitrosylation

Identifiers

PMID24288182
PMCPMC3904709
OpenAlexW2102835388

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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.