Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 496

The DOI matches its Crossref record.

Zeta, a novel class of glutathione transferases in a range of species from plants to humans

Open access
BOARD, G. Philip, BAKER, T. Rohan, CHELVANAYAGAM, Gareth, JERMIIN, S. Lars·1997·Biochemical Journal

Abstract

Sequence alignment and phylogenetic analysis has identified a new subgroup of glutathione S-transferase (GST)-like proteins from a range of species extending from plants to humans. This group has been termed the Zeta class. An atomic model of the N-terminal domain suggests that the members of the Zeta class have a similar structure to that of other GSTs, binding glutathione in a similar orientation in the G site. Recombinant human GSTZ1-1 has been expressed in Escherichia coli and characterized. The protein is a dimer composed of 24.2 kDa subunits and has minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole. Although low in comparison with other GSTs, GSTZ1-1 has glutathione peroxidase activity with t-butyl and cumene hydroperoxides. The members of the Zeta class have been conserved over a long evolutionary period, suggesting that they might have a role in the metabolism of a compound that is common in many living cells.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1042/bj3280929

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cited by

See all 496

Metadata

Authors
BOARD, G. P., BAKER, T. R., CHELVANAYAGAM, G., & JERMIIN, S. L.
Venue
Biochemical Journal
Published
1997-12-15
Volume
328
Issue
3
Pages
929-935
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W11118004
Cited by
496
References
0
FWCI
9.68
Type
journal article
Language
en
Open access
bronze

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Zeta, a novel class of glutathione transferases in a range of species from plants to humans. https://app.cochat.ai/papers/10.1042/bj3280929
The paper
BOARD, G. P., BAKER, T. R., CHELVANAYAGAM, G., & JERMIIN, S. L. (1997). Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochemical Journal. https://doi.org/10.1042/bj3280929

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.