Evidence map›Paper›PMID 25192423›Full record

ArticlePloS one2014

S-nitroso-proteome in poplar leaves in response to acute ozone stress.

Elisa Vanzo, Andrea Ghirardo, Juliane Merl-Pham, Christian Lindermayr, Werner Heller, Stefanie M Hauck, Jörg Durner, Jörg-Peter Schnitzler

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
9.3field-weighted citation impact, top 3% 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

13 citing papers in PubMed, 49 citations in OpenAlex.

  1. Integration of NO and HPlant communications · 2026
    Review
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  5. Quantitative Proteome Profiling of aFrontiers in plant science · 2021
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  6. Review
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  8. Article
  9. Article
  10. Article
  11. TheFrontiers in bioengineering and biotechnology · 2016
    Article
  12. Article
  13. Article
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

8 authors at 1 institution in 1 country.

Elisa VanzoResearch Unit Environmental Simulation, Institute for Biochemical Plant Pathology, Helmholtz Zentrum München, Neuherberg, Germany.
Andrea GhirardoResearch Unit Environmental Simulation, Institute for Biochemical Plant Pathology, Helmholtz Zentrum München, Neuherberg, Germany.
Juliane Merl-PhamResearch Unit Protein Science, Helmholtz Zentrum München, Neuherberg, Germany.
Christian LindermayrInstitute for Biochemical Plant Pathology, Helmholtz Zentrum München, Neuherberg, Germany.
Werner HellerInstitute for Biochemical Plant Pathology, Helmholtz Zentrum München, Neuherberg, Germany.
Stefanie M HauckResearch Unit Protein Science, Helmholtz Zentrum München, Neuherberg, Germany.
Jörg DurnerInstitute for Biochemical Plant Pathology, Helmholtz Zentrum München, Neuherberg, Germany.
Jörg-Peter SchnitzlerResearch Unit Environmental Simulation, Institute for Biochemical Plant Pathology, Helmholtz Zentrum München, Neuherberg, Germany.
Helmholtz Zentrum München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein S-nitrosylation, the covalent binding of nitric oxide (NO) to protein cysteine residues, is one of the main mechanisms of NO signaling in plant and animal cells. Using a combination of the biotin switch assay and label-free LC-MS/MS analysis, we revealed the S-nitroso-proteome of the woody model plant Populus x canescens. Under normal conditions, constitutively S-nitrosylated proteins in poplar leaves and calli comprise all aspects of primary and secondary metabolism. Acute ozone fumigation was applied to elicit ROS-mediated changes of the S-nitroso-proteome. This treatment changed the total nitrite and nitrosothiol contents of poplar leaves and affected the homeostasis of 32 S-nitrosylated proteins. Multivariate data analysis revealed that ozone exposure negatively affected the S-nitrosylation status of leaf proteins: 23 proteins were de-nitrosylated and 9 proteins had increased S-nitrosylation content compared to the control. Phenylalanine ammonia-lyase 2 (log2[ozone/control] = -3.6) and caffeic acid O-methyltransferase (-3.4), key enzymes catalyzing important steps in the phenylpropanoid and subsequent lignin biosynthetic pathways, respectively, were de-nitrosylated upon ozone stress. Measuring the in vivo and in vitro phenylalanine ammonia-lyase activity indicated that the increase of the phenylalanine ammonia-lyase activity in response to acute ozone is partly regulated by de-nitrosylation, which might favor a higher metabolic flux through the phenylpropanoid pathway within minutes after ozone exposure.

Indexed as

Metabolic Networks and PathwaysMethyltransferasesNitric OxideNitroso CompoundsOzonePhenylalanine Ammonia-LyasePlant LeavesPlant ProteinsPopulusProtein Processing, Post-TranslationalProteomeS-NitrosothiolsStress, PhysiologicalTime Factorscaffeate O-methyltransferaseMethyltransferasesNitric OxideNitroso CompoundsOzonePhenylalanine Ammonia-LyasePlant ProteinsProteomeS-Nitrosothiols

Identifiers

PMID25192423
PMCPMC4156402
OpenAlexW1970420299

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.