Evidence map›Paper›PMID 19279195›Full record

ArticlePlant physiology2009

Physiological roles of glutathione s-transferases in soybean root nodules.

David A Dalton, Chris Boniface, Zachary Turner, Amy Lindahl, Hyeon Jeong Kim, Laura Jelinek, Manjula Govindarajulu, Richard E Finger, Christopher G Taylor

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

51 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Triacontanol Boosts Soybean Nodulation viaPlants (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. International journal of molecular sciences · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Meta-QTLs, ortho-MQTLs and candidate genes for nitrogen use efficiency and root system architecture in bread wheat (Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  13. Article
  14. Article
  15. Unstable Relationship BetweenFrontiers in plant science · 2021
    Article
  16. Article
  17. Assessment of oxidative stress response genes inBiotechnology reports (Amsterdam, Netherlands) · 2020
    Article
  18. Antagonistic Potential of Novel EndophyticPlants (Basel, Switzerland) · 2020
    Article
  19. Article
  20. Review
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 2 institutions in 1 country.

David A DaltonBiology Department, Reed College, Portland, Oregon 97202, USA. david.dalton@reed.edu
Chris Boniface
Zachary Turner
Amy Lindahl
Hyeon Jeong Kim
Laura Jelinek
Manjula Govindarajulu
Richard E Finger
Christopher G Taylor
Reed College · USDonald Danforth Plant Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutathione S-transferases (GSTs) are ubiquitous enzymes that catalyze the conjugation of toxic xenobiotics and oxidatively produced compounds to reduced glutathione, which facilitates their metabolism, sequestration, or removal. We report here that soybean (Glycine max) root nodules contain at least 14 forms of GST, with GST9 being most prevalent, as measured by both real-time reverse transcription-polymerase chain reaction and identification of peptides in glutathione-affinity purified extracts. GST8 was prevalent in stems and uninfected roots, whereas GST2/10 prevailed in leaves. Purified, recombinant GSTs were shown to have wide-ranging kinetic properties, suggesting that the suite of GSTs could provide physiological flexibility to deal with numerous stresses. Levels of GST9 increased with aging, suggesting a role related to senescence. RNA interference studies of nodules on composite plants showed that a down-regulation of GST9 led to a decrease in nitrogenase (acetylene reduction) activity and an increase in oxidatively damaged proteins. These findings indicate that GSTs are abundant in nodules and likely function to provide antioxidant defenses that are critical to support nitrogen fixation.

Indexed as

AcetyleneDown-RegulationGlutathione TransferaseGlycine maxKineticsNitrogenaseOxidation-ReductionPlant ProteinsRNA InterferenceRoot Nodules, PlantAcetyleneGlutathione TransferaseNitrogenasePlant Proteins

Identifiers

PMID19279195
PMCPMC2675717
OpenAlexW1972892843

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.