The DOI matches its Crossref record; 221 of the 221 references it cites were found in a registry or an index.
Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.
Open accessAbstract
Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene products, reverse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-like) chains on target proteins. The human genome encodes nearly 100 DUBs with specificity for ubiquitin in five gene families. Most DUB activity is cryptic, and conformational rearrangements often occur during the binding of ubiquitin and/or scaffold proteins. DUBs with specificity for ubiquitin contain insertions and extensions modulating DUB substrate specificity, protein-protein interactions, and cellular localization. Binding partners and multiprotein complexes with which DUBs associate modulate DUB activity and substrate specificity. Quantitative studies of activity and protein-protein interactions, together with genetic studies and the advent of RNAi, have led to new insights into the function of yeast and human DUBs. This review discusses ubiquitin-specific DUBs, some of the generalizations emerging from recent studies of the regulation of DUB activity, and their roles in various cellular processes.
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“However, certain DUBs have been shown to exhibit specificity in hydrolyzing non-K48-linked Ub chains (Komander et al, 2009a;Reyes-Turcu et al, 2009;Mevissen et al, 2013).”
From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Reyes-Turcu et al, 2009
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“Despite differences in size, the catalytic domains of all USPs possess a characteristic papain-like fold with a “thumb, palm, fingers” sub-domain architecture (Reyes-Turcu et al., 2009)”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Reyes-Turcu et al., 2009
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Cited by
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USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin
Durcan, T. M., Tang, M. Y., Pérusse, J. R., Dashti, E. A., Aguileta, M. A., McLelland, G., Gros, P., Shaler, T. A., Faubert, D., Coulombe, B., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201489729 · Cited by 375
Exonic Mosaic Mutations Contribute Risk for Autism Spectrum Disorder
Krupp, D. R., Barnard, R. A., Duffourd, Y., Evans, S. A., Mulqueen, R. M., Bernier, R., Rivière, J.-B., Fombonne, E., & O’Roak, B. J. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.07.016 · Cited by 204
Zhong, B., Liu, X., Wang, X., Chang, S. H., Liu, X., Wang, A., Reynolds, J. M., & Dong, C. (2012) · Nature Immunology · doi:10.1038/ni.2427 · Cited by 206
Hao, Y.-H., Fountain, M. D., Fon Tacer, K., Xia, F., Bi, W., Kang, S.-H. L., Patel, A., Rosenfeld, J. A., Le Caignec, C., Isidor, B., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.033 · Cited by 206
Selective dual inhibitors of the cancer-related deubiquitylating proteases USP7 and USP47.
Weinstock, J., Wu, J., Cao, P., Kingsbury, W. D., McDermott, J. L., Kodrasov, M. P., McKelvey, D. M., Suresh Kumar, K. G., Goldenberg, S. J., Mattern, M. R., et al. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200276j · Cited by 187
Metadata
- Authors
- Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D.
- Affiliations
- Laboratory of Biochemistry and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892
- Emory University (US)
- Corresponding author
- Wilkinson, Keith D.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2009-06-01
- Volume
- 78
- Issue
- 1
- Pages
- 363-397
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- PMC
- PMC2734102
- OpenAlex
- W2139364069
- Cited by
- 1,396
- References
- 221
- Citations by year
- 2026: 31 · 2025: 70 · 2024: 79 · 2023: 57 · 2022: 77 · 2021: 90 · 2020: 114 · 2019: 70 · 2018: 66 · 2017: 94 · 2016: 85 · 2015: 76 · 2014: 109 · 2013: 102 · 2012: 113
- FWCI
- 6.96
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM030308)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- deubiquitinase, ubiquitin, ubiquitin-like proteins, polyubiquitin chains, protein-protein interaction
- MeSH terms
- Animals, Humans, Endopeptidases, Protein Structure, Tertiary, Ubiquitin, Ubiquitination
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