The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Invited Commentary Potential Contribution of the Glutathione S-Transferase Supergene Family to Resistance to Oxidative Stress
Abstract
The glutathione S-transferase (GST) supergene family comprises gene families that encode isoenzymes that are widely expressed in mammalian tissue cytosols and membranes. Both cytosolic (particularly the isoenzymes encoded by the alpha, mu and theta gene families) and microsomal GST catalyse the conjugation of reduced glutathione (GSH) with a wide variety of electrophiles which include known carcinogens as well as various compounds that are products of oxidative stress including oxidised DNA and lipid. Indeed, several lines of evidence suggest certain of these isoenzymes play a pivotal role in protecting cells from the consequences of such stress. An assessment of the importance of these GST in humans is presently difficult however, because the number of alpha and theta class genes is not known and, the catalytic preferences of even identified isoforms is not always clear.
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
Cites
The American Journal of Physiology
(1899) · The American Naturalist · doi:10.1086/277182 · Cited by 5,654
Free Radicals in Biology and Medicine
Land, E. T. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,854
Oxidative stress: oxidants and antioxidants
Sies, H. (1997) · Experimental Physiology · doi:10.1113/expphysiol.1997.sp004024 · Cited by 4,566
Schreck, R., Rieber, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,816
DNA damage by oxygen‐derived species Its mechanism and measurement in mammalian systems
Halliwell, B., & Aruoma, O. I. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80347-6 · Cited by 1,537
Rushmore, T. H., Morton, M. R., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99004-6 · Cited by 1,464
Pemble, S., Schroeder, K. R., Spencer, S. R., Meyer, D. J., Hallier, E., Bolt, H. M., Ketterer, B., & Taylor, J. B. (1994) · Biochemical Journal · doi:10.1042/bj3000271 · Cited by 1,296
Oxidative Stress: Oxidants and Antioxidants.
Haddock, P. (1992) · Cardiovascular Research · doi:10.1093/cvr/26.8.816a · Cited by 1,185
The Journal of Laboratory and Clinical Medicine
(2004) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(04)00026-5 · Cited by 1,156
American Journal of Human Genetics
(2005) · Encyclopedia of Statistical Sciences · doi:10.1002/0471667196.ess7082.pub2 · Cited by 874
Cited by
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,624
Greer, E. L., Oskoui, P. R., Banko, M. R., Maniar, J. M., Gygi, M. P., Gygi, S. P., & Brunet, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705325200 · Cited by 818
Mazzone, P., Tierney, W., Hossain, M., Puvenna, V., Janigro, D., & Cucullo, L. (2010) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph7124111 · Cited by 183
Gawryluk, J. W., Wang, J.-F., Andreazza, A. C., Shao, L., Yatham, L. N., & Young, L. T. (2011) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145711000617 · Cited by 99
Fiander, H. (2000) · Cancer Letters · doi:10.1016/s0304-3835(00)00368-2 · Cited by 97
Metadata
- Authors
- Hayes, J. D., & Strange, R. C.
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 1995-01
- Volume
- 22
- Issue
- 3
- Pages
- 193-207
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W1973063537
- Cited by
- 395
- References
- 57
- FWCI
- 2.84
- Type
- journal article
- Language
- en
- Open access
- closed
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: Invited Commentary Potential Contribution of the Glutathione S-Transferase Supergene Family to Resistance to Oxidative Stress. https://app.cochat.ai/papers/10.3109/10715769509147539
- The paper
- Hayes, J. D., & Strange, R. C. (1995). Invited Commentary Potential Contribution of the Glutathione S-Transferase Supergene Family to Resistance to Oxidative Stress. Free Radical Research. https://doi.org/10.3109/10715769509147539
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.
