The DOI matches its Crossref record; 206 of the 206 references it cites were found in a registry or an index.
Glutathione-Related Enzymes and Proteins: A Review
Open accessAbstract
The tripeptide glutathione is found in all eukaryotic cells, and due to the compartmentalization of biochemical processes, its synthesis takes place exclusively in the cytosol. At the same time, its functions depend on its transport to/from organelles and interorgan transport, in which the liver plays a central role. Glutathione is determined as a marker of the redox state in many diseases, aging processes, and cell death resulting from its properties and reactivity. It also uses other enzymes and proteins, which enables it to engage and regulate various cell functions. This paper approximates the role of these systems in redox and detoxification reactions such as conjugation reactions of glutathione-S-transferases, glyoxylases, reduction of peroxides through thiol peroxidases (glutathione peroxidases, peroxiredoxins) and thiol–disulfide exchange reactions catalyzed by glutaredoxins.
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Cites
Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
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Glutathione: overview of its protective roles, measurement, and biosynthesis
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Structure, mechanism and regulation of peroxiredoxins
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Regulation of glutathione synthesis
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The importance of glutathione in human disease
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Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
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Cited by
Balogun, O., Shao, D., Carson, M., King, T., Kosar, K., Zhang, R., Zeng, G., Cornuet, P., Goel, C., Lee, E., et al. (2024) · Hepatology Communications · doi:10.1097/hc9.0000000000000485 · Cited by 6
Metadata
- Authors
- Vašková, J., Kočan, L., Vaško, L., & Perjési, P.
- Venue
- Molecules
- Publisher
- MDPI AG
- Published
- 2023-02-02
- Volume
- 28
- Issue
- 3
- Pages
- 1447
- ISSN
- 1420-3049 (ISSN-L)
- OpenAlex
- W4319160463
- Cited by
- 355
- References
- 206
- FWCI
- 26.52
- Type
- journal article
- Language
- en
- Open access
- gold
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