The DOI matches its Crossref record; 296 of the 296 references it cites were found in a registry or an index.
Deubiquitylases From Genes to Organism
Abstract
Ubiquitylation is a major posttranslational modification that controls most complex aspects of cell physiology. It is reversed through the action of a large family of deubiquitylating enzymes (DUBs) that are emerging as attractive therapeutic targets for a number of disease conditions. Here, we provide a comprehensive analysis of the complement of human DUBs, indicating structural motifs, typical cellular copy numbers, and tissue expression profiles. We discuss the means by which specificity is achieved and how DUB activity may be regulated. Generically DUB catalytic activity may be used to 1) maintain free ubiquitin levels, 2) rescue proteins from ubiquitin-mediated degradation, and 3) control the dynamics of ubiquitin-mediated signaling events. Functional roles of individual DUBs from each of five subfamilies in specific cellular processes are highlighted with an emphasis on those linked to pathological conditions where the association is supported by whole organism models. We then specifically consider the role of DUBs associated with protein degradative machineries and the influence of specific DUBs upon expression of receptors and channels at the plasma membrane.
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Citations
Cites
1 retracted
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“Proposed orthologs of human DUBs assigned in silico as bidirectional best hits (9, 280) against the species shown by reciprocal BLAST analysis (10) H. sapiens D. rerio D. melanogaster C. elegans S. pombe S. cerevisiae USP1 O94782 F1QNF4 Q8I077 USP2 O75604 E7FEC1 Q9VR54 USP3 Q9Y6I4 E7FC36 USP4 Q13107 USP5 P45974 Q1MT86…”
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Metadata
- Authors
- Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2013-07
- Volume
- 93
- Issue
- 3
- Pages
- 1289-1315
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W1970826261
- Cited by
- 425
- References
- 296
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- closed
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