The DOI matches its Crossref record.
Glutathione S-transferases, structure, regulation, and therapeutic implications
Open accessAbstract
The glutathione S-transferases (GSTs)' are a family of enzymes that catalyze the nucleophilic addition of the thiol of reduced glutathione to a variety of electrophiles (1-9). In addition, the GSTs bind with varying affinities a variety of hydrophobic compounds such as heme, bilirubin, polycyclic aromatic hydrocarbons, and dexamethasone (1-9). It is now generally accepted that the GSTs are encoded by at least five different gene families (9-12). Four of the gene families encode the cytosolic GSTs whereas the fifth en-codes a microsomal form of the enzyme (13, 14). In this review, we have focused on three GST research areas: 1) structure-function analysis of GSTs; 2) regulation of GST expression; and 3) GSTs as therapeutic targets in disease. Since our review will not be com-prehensive, we would like to direct the reader to several excellent recent reviews focusing on various aspects of GSTs (4,8,9).
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.
Integrity signals
Registry
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.
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
Nrf2:INrf2 (Keap1) signaling in oxidative stress
Kaspar, J. W., Niture, S. K., & Jaiswal, A. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.035 · Cited by 1,648
Nrf2 signaling in coordinated activation of antioxidant gene expression
Jaiswal, A. K. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.074 · Cited by 1,254
Tomarev, S. I., & Piatigorsky, J. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00449.x · Cited by 146
IKEDA, H., NISHI, S., & SAKAI, M. (2004) · Biochemical Journal · doi:10.1042/bj20031948 · Cited by 136
Presence and induction of the enzyme NAD(P)H: Quinone oxidoreductase 1 in the central nervous system
Stringer, J. L., Gaikwad, A., Gonzales, B. N., Long, D. J., Marks, L. M., & Jaiswal, A. K. (2004) · Journal of Comparative Neurology · doi:10.1002/cne.20048 · Cited by 41
Metadata
- Authors
- Rushmore, T. H., & Pickett, C. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 268
- Issue
- 16
- Pages
- 11475-11478
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1486158855
- Cited by
- 405
- References
- 0
- FWCI
- 8.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: Glutathione S-transferases, structure, regulation, and therapeutic implications. https://app.cochat.ai/papers/10.1016/s0021-9258(19)50219-8
- The paper
- Rushmore, T. H., & Pickett, C. B. (1993). Glutathione S-transferases, structure, regulation, and therapeutic implications. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)50219-8
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.