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Deubiquitinating Enzymes as Cellular Regulators
Abstract
Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26S proteasome. Deubiquitination, reversal of this modification, must also regulate the fate and function of ubiquitin-conjugated proteins. Deubiquitinating enzymes catalyze the removal of ubiquitin from ubiquitin-conjugated substrate proteins as well as from its precursor proteins. Deubiquitinating enzymes occupy the largest family of enzymes in the ubiquitin system, implying their diverse function in regulation of the ubiquitin-mediated pathways. Here we explore the diversity of deubiquitinating enzymes and their emerging roles as cellular regulators.
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Cited by
The ubiquitin-proteasome system
Nandi, D., Tahiliani, P., Kumar, A., & Chandu, D. (2006) · Journal of Biosciences · doi:10.1007/bf02705243 · Cited by 758
Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
Tai, H.-C., & Schuman, E. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2499 · Cited by 532
Lindner, H. A., Fotouhi-Ardakani, N., Lytvyn, V., Lachance, P., Sulea, T., & Ménard, R. (2005) · Journal of Virology · doi:10.1128/jvi.79.24.15199-15208.2005 · Cited by 371
Hu, M., Gu, L., Li, M., Jeffrey, P. D., Gu, W., & Shi, Y. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040027 · Cited by 251
Regulation of T cell development by the deubiquitinating enzyme CYLD
Reiley, W. W., Zhang, M., Jin, W., Losiewicz, M., Donohue, K. B., Norbury, C. C., & Sun, S.-C. (2006) · Nature Immunology · doi:10.1038/ni1315 · Cited by 198
Metadata
- Authors
- Kim, J. H.
- Venue
- Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-07-01
- Volume
- 134
- Issue
- 1
- Pages
- 9-18
- ISSN
- 0021-924X (ISSN-L)
- OpenAlex
- W2162579949
- Cited by
- 162
- References
- 0
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- closed
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