Evidence map›Paper›PMID 9255563›Full record

ReviewEnvironmental health perspectives1997

The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics.

J Seidegård, G Ekström

Open access · diamondAbstract readReview
In one paragraph

Review in Environmental health perspectives, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 2 pooled it
2.3field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 2 syntheses or guidelines pooled it, 184 citations in OpenAlex.

  1. Pooled it
  2. Phase I and II enzyme polymorphisms as risk factors for Barrett's esophagus and esophageal adenocarcinoma: a systematic review and meta-analysis.Diseases of the esophagus : official journal of the International Society for Diseases of the Esophagus · 2009
    Pooled it
  3. Trial
  4. Article
  5. Article
  6. Article
  7. Structural and Mechanistic Insights into C-S Bond Formation in Gliotoxin.Angewandte Chemie (International ed. in English) · 2021
    Article
  8. The Metabolic Rainbow: Deep Learning Phase I Metabolism in Five Colors.Journal of chemical information and modeling · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Oxidative Stress from Environmental Exposures.Current opinion in toxicology · 2018
    Article
  13. Article
  14. Article
  15. Missing link between microRNA and prostate cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Review
  16. Review
  17. Article
  18. 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

2 authors.

J SeidegårdHuman Pharmacology at Astra Draco AB, Lund, Sweden. janeric.seidegard@clraco.se.astra.com
G Ekström

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human glutathione transferases (GSTs) are a multigene family of enzymes that are involved in the metabolism of a wide range of electrophilic compounds of both exogenous and endogenous origin. GSTs are generally recognized as detoxifying enzymes by catalyzing the conjugation of these compounds with glutathione, but they may also be involved in activation of some carcinogens. The memmalian GSTs can be differentiated into four classes of cytosolic enzymes and two membrane bound enzymes. Human epoxide hydrolases (EHs) catalyze the addition of water to epoxides to form the corresponding dihydrodiol. The enzymatic hydration is essentially irreversible and produces mainly metabolites of lower reactivity that can be conjugated and excreted. The reaction of EHs is therefore generally regarded as detoxifying. The mammalian EHs can be distinguished by their physical and enzymatic properties. Microsomal EH (mEH) exhibits a broad substrate specificity, while the soluble EH (sEH) is an enzyme with a "complementary" substrate specificity to mEH. Cholesterol EH and leukotriene A4 hydrolase are two EHs with very limited substrate specificity. The activities of either GSTs or EHs expressed in vivo exhibit a relatively large interindividual variation, which might be explained by induction, inhibition, or genetic factors. These variations in levels or activities of individual isoenzymes are of importance with respect to an individual's susceptibility to genotoxic effects. This article gives a general overview of GSTs and EHs, discussing the modulation of activities, determination of these enzymes ex vivo, and the polymorphic expression of some isoenzymes.

Indexed as

Epoxide HydrolasesGlutathione TransferaseHumansPolymorphism, GeneticXenobioticsEpoxide HydrolasesGlutathione TransferaseXenobiotics

Identifiers

PMID9255563
PMCPMC1470052
OpenAlexW1980662668

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.