The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Glutathione transferases in bacteria
Open accessAbstract
Bacterial glutathione transferases (GSTs) are part of a superfamily of enzymes that play a key role in cellular detoxification. GSTs are widely distributed in prokaryotes and are grouped into several classes. Bacterial GSTs are implicated in a variety of distinct processes such as the biodegradation of xenobiotics, protection against chemical and oxidative stresses and antimicrobial drug resistance. In addition to their role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic processes such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol. This review article summarizes the current status of knowledge regarding the functional and structural properties of bacterial GSTs.
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Cites
Fahey, R. C. (2001) · Annual Review of Microbiology · doi:10.1146/annurev.micro.55.1.333 · Cited by 266
Cited by
Allocati, N., Masulli, M., Di Ilio, C., & Federici, L. (2018) · Oncogenesis · doi:10.1038/s41389-017-0025-3 · Cited by 625
Self-citationChemistry and Redox Biology of Mycothiol
Reyes, A. M., Pedre, B., De Armas, M. I., Tossounian, M.-A., Radi, R., Messens, J., & Trujillo, M. (2018) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7074 · Cited by 64
Metadata
- Authors
- Allocati, N., Federici, L., Masulli, M., & Di Ilio, C.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2008-12-12
- Volume
- 276
- Issue
- 1
- Pages
- 58-75
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1801547473
- Cited by
- 365
- References
- 1
- FWCI
- 5.58
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Allocati, N., Federici, L., Masulli, M., & Di Ilio, C. (2009). Glutathione transferases in bacteria. The FEBS Journal. https://doi.org/10.1111/j.1742-4658.2008.06743.x
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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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