Evidence map›Paper›PMID 27532006›Full record

ArticleFrontiers in plant science2016

Comprehensive Analysis of the Membrane Phosphoproteome Regulated by Oligogalacturonides in Arabidopsis thaliana.

Benedetta Mattei, Francesco Spinelli, Daniela Pontiggia, Giulia De Lorenzo

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
11.0field-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

25 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Molecular tipping points in plant cell surface HQuantitative plant biology · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. DIGE-Based Phosphoproteomic Analysis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Review
  9. Article
  10. The plasma membrane-associated CaPlant, cell & environment · 2021
    Article
  11. Review
  12. Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Large-Scale Phosphoproteomic Study ofInternational journal of molecular sciences · 2020
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Benedetta MatteiDipartimento di Biologia e Biotecnologie Charles Darwin, Istituto Pasteur - Fondazione Cenci Bolognetti, Sapienza University of Rome Rome, Italy.
Francesco SpinelliDipartimento di Biologia e Biotecnologie Charles Darwin, Istituto Pasteur - Fondazione Cenci Bolognetti, Sapienza University of Rome Rome, Italy.
Daniela PontiggiaDipartimento di Biologia e Biotecnologie Charles Darwin, Istituto Pasteur - Fondazione Cenci Bolognetti, Sapienza University of Rome Rome, Italy.
Giulia De LorenzoDipartimento di Biologia e Biotecnologie Charles Darwin, Istituto Pasteur - Fondazione Cenci Bolognetti, Sapienza University of Rome Rome, Italy.
Istituto Pasteur · ITSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Early changes in the Arabidopsis thaliana membrane phosphoproteome in response to oligogalacturonides (OGs), a class of plant damage-associated molecular patterns (DAMPs), were analyzed by two complementary proteomic approaches. Differentially phosphorylated sites were determined through phosphopeptide enrichment followed by LC-MS/MS using label-free quantification; differentially phosphorylated proteins were identified by 2D-DIGE combined with phospho-specific fluorescent staining (phospho-DIGE). This large-scale phosphoproteome analysis of early OG-signaling enabled us to determine 100 regulated phosphosites using LC-MS/MS and 46 differential spots corresponding to 34 pdhosphoproteins using phospho-DIGE. Functional classification showed that the OG-responsive phosphoproteins include kinases, phosphatases and receptor-like kinases, heat shock proteins (HSPs), reactive oxygen species (ROS) scavenging enzymes, proteins related to cellular trafficking, transport, defense and signaling as well as novel candidates for a role in immunity, for which elicitor-induced phosphorylation changes have not been shown before. A comparison with previously identified elicitor-regulated phosphosites shows only a very limited overlap, uncovering the immune-related regulation of 70 phosphorylation sites and revealing novel potential players in the regulation of elicitor-dependent immunity.

Indexed as

2DEArabidopsis thalianaDAMPselicitorsimmunityLC-MS/MSoligogalacturonidesphosphoproteomics

Identifiers

PMID27532006
PMCPMC4969306
OpenAlexW2477115718

What OpenQuestion holds

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LicenceCC BY
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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.