The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Glutathione transferases: a structural perspective
Abstract
The glutathione transferases (GSTs) are one of the most important families of detoxifying enzymes in nature. The classic activity of the GSTs is conjugation of compounds with electrophilic centers to the tripeptide glutathione (GSH), but many other activities are now associated with GSTs, including steroid and leukotriene biosynthesis, peroxide degradation, double-bond cis-trans isomerization, dehydroascorbate reduction, Michael addition, and noncatalytic "ligandin" activity (ligand binding and transport). Since the first GST structure was determined in 1991, there has been an explosion in structural data across GSTs of all three families: the cytosolic GSTs, the mitochondrial GSTs, and the membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG family). In this review, the major insights into GST structure and function will be discussed.
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Hayes, J. D., Flanagan, J. U., & Jowsey, I. R. (2005) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095857 · Cited by 3,544
Regulation of JNK signaling by GSTp
Adler, V. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1321 · Cited by 1,116
Jakobsson, P.-J., Thorén, S., Morgenstern, R., & Samuelsson, B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7220 · Cited by 996
Glutathione-Associated Enzymes In Anticancer Drug Resistance
Tew, K. D. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3143 · Cited by 856
Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases
Board, P. G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L. S., Schulte, G. K., Danley, D. E., Hoth, L. R., Griffor, M. C., Kamath, A. V., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001706200 · Cited by 722
The Identity of Glutathione S -Transferase B with Ligandin, a Major Binding Protein of Liver
Habig, W. H., Pabst, M. J., Fleischner, G., Gatmaitan, Z., Arias, I. M., & Jakoby, W. B. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.10.3879 · Cited by 539
Sinning, I., Kleywegt, G. J., Cowan, S. W., Reinemer, P., Dirr, H. W., Huber, R., Gilliland, G. L., Armstrong, R. N., Ji, X., Board, P. G., et al. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1376 · Cited by 446
Laborde, E. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2010.80 · Cited by 409
Glutathione transferases in bacteria
Allocati, N., Federici, L., Masulli, M., & Di Ilio, C. (2009) · The FEBS Journal · doi:10.1111/j.1742-4658.2008.06743.x · Cited by 365
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Cited by
Allocati, N., Masulli, M., Di Ilio, C., & Federici, L. (2018) · Oncogenesis · doi:10.1038/s41389-017-0025-3 · Cited by 625
Glutathione and glutathione-dependent enzymes: From biochemistry to gerontology and successful aging
Lapenna, D. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102066 · Cited by 239
Regulation of antioxidant defense and glyoxalase systems in cyanobacteria
Rai, R., Singh, S., Rai, K. K., Raj, A., Sriwastaw, S., & Rai, L. C. (2021) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2021.09.037 · Cited by 51
Oakley, A. J. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.12.072 · Cited by 3
Self-citation
Metadata
- Authors
- Oakley, A.
- Venue
- Drug Metabolism Reviews
- Publisher
- Informa UK Limited
- Published
- 2011-03-23
- Volume
- 43
- Issue
- 2
- Pages
- 138-151
- ISSN
- 0360-2532 (ISSN-L)
- 1097-9883
- OpenAlex
- W1977138583
- Cited by
- 403
- References
- 54
- FWCI
- 7.52
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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