Evidence map›Paper›PMID 24019145›Full record

ArticleMolecular & cellular proteomics : MCP2013

New Arabidopsis thaliana cytochrome c partners: a look into the elusive role of cytochrome c in programmed cell death in plants.

Jonathan Martínez-Fábregas, Irene Díaz-Moreno, Katiuska González-Arzola, Simon Janocha, José A Navarro, Manuel Hervás, Rita Bernhardt, Antonio Díaz-Quintana, Miguel Á De la Rosa

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 62 citations in OpenAlex.

  1. Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. CytochromePlants (Basel, Switzerland) · 2021
    Article
  10. Article
  11. Post-Translational Modifications of CytochromeInternational journal of molecular sciences · 2020
    Review
  12. Review
  13. Article
  14. Review
  15. Oxidative stress is tightly regulated by cytochromeProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Review
  18. Structural basis of mitochondrial dysfunction in response to cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017
    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

9 authors at 4 institutions in 2 countries.

Jonathan Martínez-FábregasInstituto de Bioquímica Vegetal y Fotosíntesis (IBVF), Centro de Investigaciones Científicas Isla de la Cartuja (cicCartuja), Universidad de Sevilla-Consejo Superior de Investigaciones Científicas (CSIC), Seville, 41092, Spain;
Irene Díaz-Moreno
Katiuska González-Arzola
Simon Janocha
José A Navarro
Manuel Hervás
Rita Bernhardt
Antonio Díaz-Quintana
Miguel Á De la Rosa
Instituto de Bioquímica Vegetal y Fotosíntesis · ESCentro de Investigaciones Científicas Isla de la Cartuja · ESConsejo Superior de Investigaciones Científicas · ESSaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Programmed cell death is an event displayed by many different organisms along the evolutionary scale. In plants, programmed cell death is necessary for development and the hypersensitive response to stress or pathogenic infection. A common feature in programmed cell death across organisms is the translocation of cytochrome c from mitochondria to the cytosol. To better understand the role of cytochrome c in the onset of programmed cell death in plants, a proteomic approach was developed based on affinity chromatography and using Arabidopsis thaliana cytochrome c as bait. Using this approach, ten putative new cytochrome c partners were identified. Of these putative partners and as indicated by bimolecular fluorescence complementation, nine of them bind the heme protein in plant protoplasts and human cells as a heterologous system. The in vitro interaction between cytochrome c and such soluble cytochrome c-targets was further corroborated using surface plasmon resonance. Taken together, the results obtained in the study indicate that Arabidopsis thaliana cytochrome c interacts with several distinct proteins involved in protein folding, translational regulation, cell death, oxidative stress, DNA damage, energetic metabolism, and mRNA metabolism. Interestingly, some of these novel Arabidopsis thaliana cytochrome c-targets are closely related to those for Homo sapiens cytochrome c (Martínez-Fábregas et al., unpublished). These results indicate that the evolutionarily well-conserved cytosolic cytochrome c, appearing in organisms from plants to mammals, interacts with a wide range of targets on programmed cell death. The data have been deposited to the ProteomeXchange with identifier PXD000280.

Indexed as

Gene Expression Regulation, PlantApoptosisArabidopsisArabidopsis ProteinsChromatography, AffinityCytochromes cCytosolEnergy MetabolismEvolution, MolecularHEK293 CellsHumansMass SpectrometryMitochondriaMolecular Sequence AnnotationOxidative StressProtein BindingArabidopsis ProteinsCytochromes cRNA, Messenger

Identifiers

PMID24019145
PMCPMC3861715
OpenAlexW2134403950

What OpenQuestion holds

Textmetadata
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.