Evidence map›Paper›PMID 11897031›Full record

ReviewGenome biology2002

Plant glutathione transferases.

David P Dixon, Adrian Lapthorn, Robert Edwards

Open access · hybridAbstract readReview
In one paragraph

Review in Genome biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
248citing papers in PubMed, 1 pooled it
6.6field-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

248 citing papers in PubMed, 1 synthesis or guideline pooled it, 823 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Black alder's (Alnus glutinosa L.) defense against polycyclic aromatic hydrocarbons (PAHs).Environmental science and pollution research international · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Phase-Dependent Transcriptional Reprogramming ofInternational journal of molecular sciences · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Identification of thePlants (Basel, Switzerland) · 2025
    Article

188 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

3 authors at 2 institutions in 1 country.

David P DixonSchool of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, UK. Robert.Edwards@durham.ac.uk
Adrian Lapthorn
Robert Edwards
Durham University · GBUniversity of Glasgow · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

summaryThe soluble glutathione transferases (GSTs, EC 2.5.1.18) are encoded by a large and diverse gene family in plants, which can be divided on the basis of sequence identity into the phi, tau, theta, zeta and lambda classes. The theta and zeta GSTs have counterparts in animals but the other classes are plant-specific and form the focus of this article. The genome of Arabidopsis thaliana contains 48 GST genes, with the tau and phi classes being the most numerous. The GST proteins have evolved by gene duplication to perform a range of functional roles using the tripeptide glutathione (GSH) as a cosubstrate or coenzyme. GSTs are predominantly expressed in the cytosol, where their GSH-dependent catalytic functions include the conjugation and resulting detoxification of herbicides, the reduction of organic hydroperoxides formed during oxidative stress and the isomerization of maleylacetoacetate to fumarylacetoacetate, a key step in the catabolism of tyrosine. GSTs also have non-catalytic roles, binding flavonoid natural products in the cytosol prior to their deposition in the vacuole. Recent studies have also implicated GSTs as components of ultraviolet-inducible cell signaling pathways and as potential regulators of apoptosis. Although sequence diversification has produced GSTs with multiple functions, the structure of these proteins has been highly conserved. The GSTs thus represent an excellent example of how protein families can diversify to fulfill multiple functions while conserving form and structure.

Indexed as

ArabidopsisArabidopsis ProteinsGenome, PlantGlutathione TransferaseMultigene FamilyProtein Structure, TertiaryArabidopsis ProteinsGlutathione Transferase

Identifiers

PMID11897031
PMCPMC139027
OpenAlexW1519895850

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.