Evidence map›Paper›PMID 21378116›Full record

ArticleJournal of experimental botany2011

In vivo protein tyrosine nitration in Arabidopsis thaliana.

Jorge Lozano-Juste, Rosa Colom-Moreno, José León

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 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
6.7field-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

70 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Integration of NO and HPlant communications · 2026
    Review
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  19. Redox Components: Key Regulators of Epigenetic Modifications in Plants.International journal of molecular sciences · 2020
    Review
  20. Review

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

3 authors at 2 institutions in 1 country.

Jorge Lozano-JusteInstituto de Biología Molecular y Celular de Plantas, CSIC-Universidad Politécnica de Valencia, CPI Ed. 8E, Camino de Vera s/n, 46022 Valencia, Spain.
Rosa Colom-Moreno
José León
Universitat Politècnica de València · ESInstituto de Biología Molecular y Celular de Plantas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitration of tyrosine (Y) residues of proteins is a low abundant post-translational modification that modulates protein function or fate in animal systems. However, very little is known about the in vivo prevalence of this modification and its corresponding targets in plants. Immunoprecipitation, based on an anti-3-nitroY antibody, was performed to pull-down potential in vivo targets of Y nitration in the Arabidopsis thaliana proteome. Further shotgun liquid chromatography-mass spectrometry (LC-MS/MS) proteomic analysis of the immunoprecipitated proteins allowed the identification of 127 proteins. Around 35% of them corresponded to homologues of proteins that have been previously reported to be Y nitrated in other non-plant organisms. Some of the putative in vivo Y-nitrated proteins were further confirmed by western blot with specific antibodies. Furthermore, MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis of protein spots, separated by two-dimensional electrophoresis from immunoprecipitated proteins, led to the identification of seven nitrated peptides corresponding to six different proteins. However, in vivo nitration sites among putative targets could not be identified by MS/MS. Nevertheless, an MS/MS spectrum with 3-aminoY318 instead of the expected 3-nitroY was found for cytosolic glyceraldehyde-3-phosphate dehydrogenase. Reduction of nitroY to aminoY during MS-based proteomic analysis together with the in vivo low abundance of these modifications made the identification of nitration sites difficult. In turn, in vitro nitration of methionine synthase, which was also found in the shotgun proteomic screening, allowed unequivocal identification of a nitration site at Y287.

Indexed as

5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseArabidopsisArabidopsis ProteinsBlotting, WesternChromatography, LiquidElectrophoresis, Gel, Two-DimensionalImmunoprecipitationNitratesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryTyrosine5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseArabidopsis ProteinsNitratesTyrosine

Identifiers

PMID21378116
PMCPMC3130175
OpenAlexW2166632201

What OpenQuestion holds

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LicenceCC BY-NC
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.