Evidence map›Paper›PMID 26554337›Full record

ArticleChemico-biological interactions2015

Benzene oxide is a substrate for glutathione S-transferases.

Adam T Zarth, Sharon E Murphy, Stephen S Hecht

Open access · greenAbstract read
In one paragraph

Article in Chemico-biological interactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Characterization of Cytosolic GlutathioneDrug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  6. Review
  7. Article
  8. A Predictive Model Assessing Genetic Susceptibility Risk at Workplace.International journal of environmental research and public health · 2019
    Article
  9. Article
  10. 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

3 authors at 2 institutions in 1 country.

Adam T ZarthMasonic Cancer Center, University of Minnesota, Minneapolis, MN, USA; Medicinal Chemistry Graduate Program, University of Minnesota, Minneapolis, MN, USA. Electronic address: zarth002@umn.edu.
Sharon E MurphyMasonic Cancer Center, University of Minnesota, Minneapolis, MN, USA; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, USA.
Stephen S HechtMasonic Cancer Center, University of Minnesota, Minneapolis, MN, USA; Medicinal Chemistry Graduate Program, University of Minnesota, Minneapolis, MN, USA.
University of Minnesota · USUniversity of Minnesota Medical Center · US

Funding

Women's CancerP30CA077598 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI Douglas Yee · 1998 to 2026
$100.4M
Untargeted Adductomics to Characterize Ethnic Differences in the Exposome of SmokersP01CA138338 · NCI · UNIVERSITY OF MINNESOTA · PI NATALIA Y TRETYAKOVA · 2010 to 2026
$33.4M
NCI NIH HHS CA-138338NCI NIH HHS P01 CA138338NCI NIH HHS P30 CA077598
6 · The paper itself

Abstract

Benzene is a known human carcinogen which must be activated to benzene oxide (BO) to exert its carcinogenic potential. BO can be detoxified in vivo by reaction with glutathione and excretion in the urine as S-phenylmercapturic acid. This process may be catalyzed by glutathione S-transferases (GSTs), but kinetic data for this reaction have not been published. Therefore, we incubated GSTA1, GSTT1, GSTM1, and GSTP1 with glutathione and BO and quantified the formation of S-phenylglutathione. Kinetic parameters were determined for GSTT1 and GSTP1. At 37 °C, the putative Km and Vmax values for GSTT1 were 420 μM and 450 fmol/s, respectively, while those for GSTP1 were 3600 μM and 3100 fmol/s. GSTA1 and GSTM1 did not exhibit sufficient activity for determination of kinetic parameters. We conclude that GSTT1 is a critical enzyme in the detoxification of BO and that GSTP1 may also play an important role, while GSTA1 and GSTM1 seem to be less important.

Indexed as

BiocatalysisCyclohexanesGlutathioneGlutathione TransferaseHumansProtein Bindingbenzene oxideCyclohexanesGlutathioneGlutathione TransferaseBenzene oxideDetoxificationGlutathione S-transferaseGSTP1GSTT1Kinetics

Identifiers

PMID26554337
PMCPMC4695229
OpenAlexW2174438116

What OpenQuestion holds

Textmetadata
LicenceTDM
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.