Evidence map›Paper›PMID 15734904›Full record

ArticlePlant physiology2005

Proteomic identification of S-nitrosylated proteins in Arabidopsis.

Christian Lindermayr, Gerhard Saalbach, Jörg Durner

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 228 papers.

0numbers the graph read from it
0cells of the map it votes in
228citing papers in PubMed
19.9field-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

228 citing papers in PubMed, 727 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Linking redox and calcium signaling via thioredoxins.Journal of experimental botany · 2026
    Review
  5. Article
  6. Article
  7. Integration of NO and HPlant communications · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. The Hidden Architects: Nitric Oxide and Redox Dynamics in Plant Stem Cell Homeostasis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

168 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Christian LindermayrInstitute of Biochemical Plant Pathology, GSF-National Research Center for Environment and Health, D-85764 Munich/Neuherberg, Germany.
Gerhard Saalbach
Jörg Durner
Institute of Groundwater Ecology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although nitric oxide (NO) has grown into a key signaling molecule in plants during the last few years, less is known about how NO regulates different events in plants. Analyses of NO-dependent processes in animal systems have demonstrated protein S-nitrosylation of cysteine (Cys) residues to be one of the dominant regulation mechanisms for many animal proteins. For plants, the principle of S-nitrosylation remained to be elucidated. We generated S-nitrosothiols by treating extracts from Arabidopsis (Arabidopsis thaliana) cell suspension cultures with the NO-donor S-nitrosoglutathione. Furthermore, Arabidopsis plants were treated with gaseous NO to analyze whether S-nitrosylation can occur in the specific redox environment of a plant cell in vivo. S-Nitrosylated proteins were detected by a biotin switch method, converting S-nitrosylated Cys to biotinylated Cys. Biotin-labeled proteins were purified and analyzed using nano liquid chromatography in combination with mass spectrometry. We identified 63 proteins from cell cultures and 52 proteins from leaves that represent candidates for S-nitrosylation, including stress-related, redox-related, signaling/regulating, cytoskeleton, and metabolic proteins. Strikingly, many of these proteins have been identified previously as targets of S-nitrosylation in animals. At the enzymatic level, a case study demonstrated NO-dependent reversible inhibition of plant glyceraldehyde-3-phosphate dehydrogenase, suggesting that this enzyme could be affected by S-nitrosylation. The results of this work are the starting point for further investigation to get insight into signaling pathways and other cellular processes regulated by protein S-nitrosylation in plants.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCells, CulturedGlyceraldehyde-3-Phosphate DehydrogenasesMolecular Sequence DataNitric OxidePlant LeavesProteomicsSignal TransductionS-NitrosothiolsArabidopsis ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesNitric OxideS-Nitrosothiols

Identifiers

PMID15734904
PMCPMC1065393
OpenAlexW2086518087

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.