The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response
Open accessAbstract
Ubiquitin signaling is a conserved, widespread, and dynamic process in which protein substrates are rapidly modified by ubiquitin to impact protein activity, localization, or stability. To regulate this process, deubiquitinating enzymes (DUBs) counter the signal induced by ubiquitin conjugases and ligases by removing ubiquitin from these substrates. Many DUBs selectively regulate physiological pathways employing conserved mechanisms of ubiquitin bond cleavage. DUB activity is highly regulated in dynamic environments through protein-protein interaction, posttranslational modification, and relocalization. The largest family of DUBs, cysteine proteases, are also sensitive to regulation by oxidative stress, as reactive oxygen species (ROS) directly modify the catalytic cysteine required for their enzymatic activity. Current research has implicated DUB activity in human diseases, including various cancers and neurodegenerative disorders. Due to their selectivity and functional roles, DUBs have become important targets for therapeutic development to treat these conditions. This review will discuss the main classes of DUBs and their regulatory mechanisms with a particular focus on DUB redox regulation and its physiological impact during oxidative stress.
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Citations
Cites
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Cited by
Redox control of the deubiquitinating enzyme Ubp2 regulates translation during stress
Santos, C. M., Cizubu, B. K., Okonkwo, D. A., Chen, C.-Y., Maske, N., Snyder, N. A., Simões, V., Washington, E. J., & Silva, G. M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107870 · Cited by 5
Self-citation
Metadata
- Authors
- Snyder, N. A., & Silva, G. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2021-09
- Volume
- 297
- Issue
- 3
- Pages
- 101077
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W3192387066
- Cited by
- 347
- References
- 19
- FWCI
- 9.33
- Type
- journal article
- Language
- en
- Open access
- gold
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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.
