Evidence map›Paper›PMID 17172357›Full record

ArticleThe Plant cell2006

The coactivator function of Arabidopsis NPR1 requires the core of its BTB/POZ domain and the oxidation of C-terminal cysteines.

Amanda Rochon, Patrick Boyle, Tracy Wignes, Pierre R Fobert, Charles Després

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
14.5field-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

124 citing papers in PubMed, 299 citations in OpenAlex.

  1. Mediator subunit MED19 modulates elf18-inducedPlant signaling & behavior · 2026
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  10. Cellular energy sensor SnRK1 suppresses salicylic acid-dependent and -independent defenses and bacterial resistance inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
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  13. Metabolomic Profiling Identifies Key Metabolites and Defense Pathways inInternational journal of molecular sciences · 2025
    Article
  14. Review
  15. Article
  16. Review
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  18. Review
  19. Article
  20. NPR1 promotes blue light-induced plant photomorphogenesis by ubiquitinating and degrading PIF4.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

64 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

5 authors at 3 institutions in 1 country.

Amanda RochonDepartment of Biological Sciences, Brock University, St. Catharines, Ontario, Canada L2S 3A1.
Patrick Boyle
Tracy Wignes
Pierre R Fobert
Charles Després
Brock University · CANational Research Council Canada · CAPlant Biotechnology Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import. The interaction of nucleus-localized NPR1 with TGA transcription factors results in the activation of defense genes, including the SAR marker PATHOGENESIS-RELATED-1 (PR-1), and the deployment of SAR. Little is known about how TGA factors or NPR1 regulate transcription or whether a TGA-NPR1 complex forms on DNA. We show that TGA2 and NPR1 are recruited to PR-1 independently of each other and of SA treatment. Consistent with the result that a triple knockout in TGA2/5/6 derepresses PR-1, in vivo plant transcription assays revealed that TGA2 is not an autonomous transcription activator but is a transcriptional repressor in both untreated and SA-treated cells. However, after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain (residues 80 to 91) and the oxidation of NPR1 Cys-521 and Cys-529. These Cys residues are found in a new type of transactivation domain that we term Cys-oxidized. These data further our understanding of the mechanism by which TGA2 and NPR1 activate Arabidopsis PR-1.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsCysteineGene Expression Regulation, PlantModels, GeneticMolecular Sequence DataNuclear ProteinsOxidation-ReductionPlant ProteinsPromoter Regions, GeneticProtein Structure, TertiaryProtein TransportRNA, MessengerSalicylic AcidAHBP-1b protein, ArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsCysteineNPR1 protein, ArabidopsisNuclear Proteinspathogenesis-related proteins, plantPlant ProteinsRNA, MessengerSalicylic Acid

Identifiers

PMID17172357
PMCPMC1785396
OpenAlexW2162702318

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.