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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The catalytic domains of all USPs possess a characteristic papain-like fold with a "thumb, palm, fingers" sub-domain architecture.
“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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1 retracted
Moro, L., Arbini, A., Marra, E., & Greco, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604636200 · Cited by 50 · see citing works
RetractedHershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,216 · see citing works
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,731 · see citing works
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075 · see citing works
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872 · see citing works
A genomic and functional inventory of deubiquitinating enzymes.
Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854 · see citing works
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,852 · see citing works
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,718 · see citing works
Ubiquitin: structures, functions, mechanisms
Pickart, C. M., & Eddins, M. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.019 · Cited by 1,406 · see citing works
Regulation and Function of IKK and IKK-Related Kinases
Häcker, H., & Karin, M. (2006) · Science s STKE · doi:10.1126/stke.3572006re13 · Cited by 1,269 · see citing works
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,213 · see citing works
Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins
Hicke, L., & Dunn, R. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.110701.154617 · Cited by 1,106 · see citing works
Polyubiquitin chains: polymeric protein signals
Pickart, C. M., & Fushman, D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.09.009 · Cited by 1,052 · see citing works
The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination
Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israël, A., Wallach, D., & Courtois, G. (2003) · Nature · doi:10.1038/nature01802 · Cited by 1,018 · see citing works
Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome
Verma, R., Aravind, L., Oania, R. S., McDonald, W. H., Yates, J. R., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075898 · Cited by 994 · see citing works
Mechanism and function of deubiquitinating enzymes
Amerik, A. Y., & Hochstrasser, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.10.003 · Cited by 978 · see citing works
CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., & Mosialos, G. (2003) · Nature · doi:10.1038/nature01803 · Cited by 964 · see citing works
Role of Bmi-1 and Ring1A in H2A Ubiquitylation and Hox Gene Silencing
Cao, R., Tsukada, Y.-I., & Zhang, Y. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.12.002 · Cited by 847 · see citing works
Histone ubiquitination: triggering gene activity.
Weake, V. M., & Workman, J. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.02.014 · Cited by 742 · see citing works
Proteasomes and their kin: proteases in the machine age
Pickart, C. M., & Cohen, R. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1336 · Cited by 735 · see citing works
A new protease required for cell-cycle progression in yeast
Li, S., & Hochstrasser, M. (1999) · Nature · doi:10.1038/18457 · Cited by 729 · see citing works
A cryptic protease couples deubiquitination and degradation by the proteasome
Yao, T., & Cohen, R. E. (2002) · Nature · doi:10.1038/nature01071 · Cited by 727 · see citing works
Jensen, D. E., Proctor, M. L., Marquis, S. T., Gardner, H. P., Ha, S. I., Chodosh, L. A., Ishov, A. M., Tommerup, N., Vissing, H., Sekido, Y., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1201861 · Cited by 725 · see citing works
Self-citationHenry, K. W., Wyce, A., Lo, W.-S., Duggan, L. J., Emre, N. C. T., Kao, C.-F., Pillus, L., Shilatifard, A., Osley, M. A., & Berger, S. L. (2003) · Genes & Development · doi:10.1101/gad.1144003 · Cited by 714 · see citing works
Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1
Cope, G. A., Suh, G. S. B., Aravind, L., Schwarz, S. E., Zipursky, S. L., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075901 · Cited by 682 · see citing works
Proteasome subunit Rpn13 is a novel ubiquitin receptor
Husnjak, K., Elsasser, S., Zhang, N., Chen, X., Randles, L., Shi, Y., Hofmann, K., Walters, K. J., Finley, D. J., & Đikić, I. (2008) · Nature · doi:10.1038/nature06926 · Cited by 662 · see citing works
Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.-W., Gu, W. J., Cohen, R. E., & Shi, Y. (2002) · Cell · doi:10.1016/s0092-8674(02)01199-6 · Cited by 648 · see citing works
Multiple Associated Proteins Regulate Proteasome Structure and Function
Leggett, D., Hanna, J. W., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R. T., Walz, T., Ploegh, H. L., & Finley, D. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00638-x · Cited by 631 · see citing works
Barretto, N., Jukneliene, D., Ratia, K. M., Chen, Z., Mesecar, A. D., & Baker, S. C. (2005) · Journal of Virology · doi:10.1128/jvi.79.24.15189-15198.2005 · Cited by 589 · see citing works
Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family
Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588 · see citing works
Self-citationThe Deubiquitinating Enzyme USP1 Regulates the Fanconi Anemia Pathway
Nijman, S. M. B., Huang, T. T., Dirac, A. M. G., Brummelkamp, T. R., Kerkhoven, R. M., D’Andrea, A. D., & Bernards, R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.008 · Cited by 586 · see citing works
Regulation of monoubiquitinated PCNA by DUB autocleavage
Huang, T. T., Nijman, S. M. B., Mirchandani, K. D., Galardy, P. J., Cohn, M. A., Haas, W., Gygi, S. P., Ploegh, H. L., Bernards, R., & D’Andrea, A. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1378 · Cited by 585 · see citing works
Modification in reverse: the SUMO proteases
Mukhopadhyay, D., & Dasso, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.05.002 · Cited by 578 · see citing works
Regulation of ubiquitin‐dependent processes by deubiquitinating enzymes
Wilkinson, K. D. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.14.9409543 · Cited by 575 · see citing works
Self-citationA noncovalent class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication
Ratia, K. M., Pegan, S. D., Takayama, J., Sleeman, K., Coughlin, M. M., Baliji, S., Chaudhuri, R., Fu, W., Prabhakar, B. S., Johnson, M. E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805240105 · Cited by 517 · see citing works
Borodovsky, A., Kessler, B. M., Casagrande, R. J., Overkleeft, H. S., Wilkinson, K. D., & Ploegh, H. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5187 · Cited by 504 · see citing works
Self-citationThe yeast ubiquitin genes: a family of natural gene fusions.
Özkaynak, E., Finley, D. J., Solomon, M. J., & Varshavsky, A. J. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02384.x · Cited by 483 · see citing works
The Fanconi Anemia/BRCA pathway: new faces in the crowdPreprint
Kennedy, R. D., & D’Andrea, A. D. (2005) · Genes & Development · doi:10.1101/gad.1370505 · Cited by 464 · see citing works
Ubiquitin-mediated activation of TAK1 and IKK
Adhikari, A., Xu, M., & Chen, Z. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210413 · Cited by 455 · see citing works
Verma, R., Oania, R. S., Graumann, J., & Deshaies, R. J. (2004) · Cell · doi:10.1016/j.cell.2004.06.014 · Cited by 449 · see citing works
Distinct monoubiquitin signals in receptor endocytosis
Haglund, K. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.005 · Cited by 444 · see citing works
Structure and mechanisms of the proteasome‐associated deubiquitinating enzyme USP14
Hu, M., Li, P., Song, L., Jeffrey, P. D., Chenova, T. A., Wilkinson, K. D., Cohen, R. E., & Shi, Y. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600832 · Cited by 430 · see citing works
Self-citationZhang, X.-Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L., & McMahon, S. B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.015 · Cited by 427 · cited 1× · see citing works
“cerevisiae Ubp8 and its human ortholog, Usp22, are part of the SAGA complex (151, 155, 156, 159, 164).”
BackgroundTranscriptional regulation by histone ubiquitination and deubiquitinationPreprint
Zhang, Y. (2003) · Genes & Development · doi:10.1101/gad.1156403 · Cited by 425 · see citing works
The Cdc14B-Cdh1-Plk1 Axis Controls the G2 DNA-Damage-Response Checkpoint
Bassermann, F., Frescas, D., Guardavaccaro, D., Busino, L., Peschiaroli, A., & Pagano, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.043 · Cited by 397 · see citing works
Substrate Specificity of Deubiquitinating Enzymes: Ubiquitin C-Terminal Hydrolases
Larsen, C. N., Krantz, B. A., & Wilkinson, K. D. (1998) · Biochemistry · doi:10.1021/bi972274d · Cited by 391 · see citing works
Self-citationZhao, Y., Lang, G., Ito, S., Bonnet, J., Metzger, E., Sawatsubashi, S., Suzuki, E., Le Guezennec, X., Stunnenberg, H. G., Krasnov, A., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.011 · Cited by 382 · see citing works
AMSH is an endosome-associated ubiquitin isopeptidase
McCullough, J., Clague, M. J., & Urbé, S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401141 · Cited by 369 · see citing works
Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities
Stegmeier, F. P., Rapé, M., Draviam, V. M., Nalepa, G., Sowa, M. E., Cambronne, X. A., McDonald, E. R., Li, M. Z., Hannon, G. J., Sorger, P. K., et al. (2007) · Nature · doi:10.1038/nature05694 · Cited by 368 · see citing works
Structure of the p53 Binding Domain of HAUSP/USP7 Bound to Epstein-Barr Nuclear Antigen 1
Saridakis, V., Sheng, Y., Sarkari, F., Holowaty, M. N., Shire, K., Nguyen, T., Zhang, R. G., Liao, J. C. C., Lee, W., Edwards, A. M., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.029 · Cited by 362 · see citing works
Wiborg, O., Pedersen, M., Wind, A., et al. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03693.x · Cited by 360 · see citing works
The Yeast ULP2 (SMT4) Gene Encodes a Novel Protease Specific for the Ubiquitin-Like Smt3 Protein
Li, S., & Hochstrasser, M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2367-2377.2000 · Cited by 356 · see citing works
A UAF1-Containing Multisubunit Protein Complex Regulates the Fanconi Anemia Pathway
Cohn, M. A., Kowal, P., Yang, K., Haas, W., Huang, T. T., Gygi, S. P., & D’Andrea, A. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.031 · Cited by 355 · see citing works
Deubiquitinating Enzyme Ubp6 Functions Noncatalytically to Delay Proteasomal Degradation
Hanna, J. W., Hathaway, N. A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D. S., Leggett, D., Gygi, S. P., King, R. W., & Finley, D. J. (2006) · Cell · doi:10.1016/j.cell.2006.07.038 · Cited by 354 · see citing works
Rad23 and Rpn10 Serve as Alternative Ubiquitin Receptors for the Proteasome
Elsasser, S., Chandler-Militello, D., Mueller, B., Hanna, J. W., & Finley, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404020200 · Cited by 349 · see citing works
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D. J., Đikić, I., Walters, K. J., & Groll, M. (2008) · Nature · doi:10.1038/nature06924 · Cited by 344 · see citing works
Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
Sato, Y., Yoshikawa, A., Yamagata, A., Mimura, H., Yamashita, M., Ookata, K., Nureki, O., Iwaï, K., Komada, M., & Fukai, S. (2008) · Nature · doi:10.1038/nature07254 · Cited by 341 · see citing works
Ventii, K., Devi, N. S., Friedrich, K. L., Chernova, T. A., Tighiouart, M., Meir, E. G. V., & Wilkinson, K. D. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0365 · Cited by 337 · see citing works
Self-citationProteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
Yao, T., Song, L., Xu, W., Demartino, G., Florens, L. A., Swanson, S. K., Washburn, M. P., Conaway, R. C., Conaway, J. W., & Cohen, R. E. (2006) · Nature Cell Biology · doi:10.1038/ncb1460 · Cited by 337 · see citing works
Reyes‐Turcu, F. E., Horton, J. R., Mullally, J. E., Heroux, A., Cheng, X., & Wilkinson, K. D. (2006) · Cell · doi:10.1016/j.cell.2006.02.038 · Cited by 337 · see citing works
Self-citationDiverse polyubiquitin interaction properties of ubiquitin-associated domains
Raasi, S., Varadan, R., Fushman, D., & Pickart, C. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb962 · Cited by 335 · see citing works
A Role for the Deubiquitinating Enzyme USP28 in Control of the DNA-Damage Response
Zhang, D., Zaugg, K., Mak, T. W., & Elledge, S. J. (2006) · Cell · doi:10.1016/j.cell.2006.06.039 · Cited by 325 · see citing works
Zhu, P., Zhou, W., Wang, J., Puc, J. A., Ohgi, K. A., Erdjument‐Bromage, H., Tempst, P., Glass, C. K., & Rosenfeld, M. G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.024 · Cited by 317 · see citing works
Molecular recognition of p53 and MDM2 by USP7/HAUSP.
Sheng, Y., Saridakis, V., Sarkari, F., Duan, S., Wu, T., Arrowsmith, C. H., & Frappier, L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1067 · Cited by 315 · see citing works
Fang, S., & Weissman, A. M. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4129-5 · Cited by 313 · see citing works
Crosas, B., Hanna, J. W., Kirkpatrick, D. S., Zhang, D. P., Tone, Y., Hathaway, N. A., Buecker, C., Leggett, D., Schmidt, M., King, R. W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.051 · Cited by 305 · see citing works
Regulation of cell cycle progression and gene expression by H2A deubiquitination
Joo, H.-Y., Zhai, L., Yang, C., Nie, S., Erdjument‐Bromage, H., Tempst, P., Chang, C., & Wang, H. (2007) · Nature · doi:10.1038/nature06256 · Cited by 305 · see citing works
Deubiquitination of Histone H2B by a Yeast Acetyltransferase Complex Regulates Transcription
Daniel, J. A., Torok, M. S., Sun, Z., Schieltz, D. M., Allis, C. D., Yates, J. R., & Grant, P. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300494200 · Cited by 299 · see citing works
Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T
Wilkinson, K. D., Tashayev, V. L., O'Connor, L. B., Larsen, C. N., Kasperek, E. M., & Pickart, C. M. (1995) · Biochemistry · doi:10.1021/bi00044a032 · Cited by 297 · see citing works
Self-citationHuman USP3 Is a Chromatin Modifier Required for S Phase Progression and Genome Stability
Nicassio, F., Corrado, N., Vissers, J. H. A., Areces, L. B., Bergink, S., Marteijn, J. A. F., Geverts, B., Houtsmuller, A. B., Vermeulen, W., Fiore, P. P. D., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.10.034 · Cited by 289 · see citing works
Structural basis for the specificity of ubiquitin C‐terminal hydrolases
Johnston, S. C., Riddle, S. M., Cohen, R. E., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3877 · Cited by 288 · see citing works
Mizuno, E., Iura, T., Mukai, A., Yoshimori, T., Kitamura, N., & Komada, M. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0560 · Cited by 284 · see citing works
The Doa4 Deubiquitinating Enzyme Is Required for Ubiquitin Homeostasis in Yeast
Swaminathan, S., Amerik, A. Y., & Hochstrasser, M. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2583 · Cited by 284 · see citing works
Makarova, K. S., Aravind, L., & Koonin, E. V. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01530-3 · Cited by 283 · see citing works
Otubains: a new family of cysteine proteases in the ubiquitin pathway
Balakirev, M. Y., Tcherniuk, S. O., Jaquinod, M., & Chroboczek, J. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor824 · Cited by 277 · see citing works
Komander, D., Lord, C. J., Scheel, H., Swift, S., Hofmann, K., Ashworth, A., & Barford, D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.018 · Cited by 276 · see citing works
Wilson, S. M., Bhattacharyya, B. J., Rachel, R. A., Coppola, V., Tessarollo, L., Householder, D. B., Fletcher, C., Miller, R. J., Copeland, N. G., & Jenkins, N. A. (2002) · Nature Genetics · doi:10.1038/ng1006 · Cited by 265 · see citing works
Winborn, B. J., Travis, S. M., Todi, S. V., Scaglione, K. M., Xu, P., Williams, A. J., Cohen, R. E., Peng, J., & Paulson, H. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803692200 · Cited by 261 · see citing works
Clague, M. J., & Urbé, S. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.09.002 · Cited by 258 · see citing works
Liu, Y., Lashuel, H. A., Choi, S., Xing, X., Case, A. W., Ni, J., Yeh, L.-A., Cuny, G. D., Stein, R. L., & Lansbury, P. T. (2003) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.08.010 · Cited by 255 · see citing works
A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
Hamazaki, J., Iemura, S., Natsume, T., Yashiroda, H., Tanaka, K., & Murata, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601338 · Cited by 254 · see citing works
A20 inhibits NF-κB activation by dual ubiquitin-editing functions
Heyninck, K., & Beyaert, R. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.11.001 · Cited by 252 · see citing works
Kattenhorn, L. M., Korbel, G. A., Kessler, B. M., Spooner, E., & Ploegh, H. L. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.07.003 · Cited by 248 · see citing works
A20 Blocks Endothelial Cell Activation through a NF-κB-dependent Mechanism
Cooper, J. T., Stroka, D. M., Brostjan, C., Palmetshofer, A., Bach, F. H., & Ferran, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.18068 · Cited by 247 · see citing works
Amerik, A. Y., Swaminathan, S., Krantz, B. A., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.16.4826 · Cited by 246 · see citing works
Nakagawa, T., Kajitani, T., Togo, S., Masuko, N., Ohdan, H., Hishikawa, Y., Koji, T., Matsuyama, T., Ikura, T., Muramatsu, M., et al. (2008) · Genes & Development · doi:10.1101/gad.1609708 · Cited by 245 · see citing works
Crystal structure of a deubiquitinating enzyme (human UCH‐L3) at 1.8 å resolution
Johnston, S. C., Larsen, C. N., Cook, W. J., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3787 · Cited by 238 · see citing works
Mechanism and Consequences for Paralog-Specific Sumoylation of Ubiquitin-Specific Protease 25
Meulmeester, E., Kunze, M., Hsiao, H., Urlaub, H., & Melchior, F. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.021 · Cited by 238 · see citing works
Functional Division of Substrate Processing Cofactors of the Ubiquitin-Selective Cdc48 Chaperone
Rumpf, S., & Jentsch, S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.014 · Cited by 236 · see citing works
SseL, a Salmonella deubiquitinase required for macrophage killing and virulence
Rytkönen, A., John, P., Garmendia, J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610095104 · Cited by 235 · see citing works
hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
Qiu, X., Ouyang, S., Li, C., Miao, S., Wang, L., & Goldberg, A. L. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601450 · Cited by 234 · see citing works
Dang, L. C., Melandri, F. D., & Stein, R. L. (1998) · Biochemistry · doi:10.1021/bi9723360 · Cited by 232 · see citing works
Inhibition of the 26 S Proteasome by Polyubiquitin Chains Synthesized to Have Defined Lengths
Piotrowski, J. S., Beal, R. E., Hoffman, L. M., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23712 · Cited by 230 · see citing works
Kato, M., Miyazawa, K., & Kitamura, N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007251200 · Cited by 229 · see citing works
Koulich, E., Li, X., & Demartino, G. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1040 · Cited by 223 · see citing works
Salmonella Effector AvrA Regulation of Colonic Epithelial Cell Inflammation by Deubiquitination
Ye, Z., Petrof, E. O., Boone, D. L., Claud, E. C., & Sun, J. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070220 · Cited by 212 · see citing works
Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2
Renatus, M., Gil-Parrado, S., D'Arcy, A., Eidhoff, U., Gerhartz, B., Hassiepen, U., Pierrat, B., Riedl, R., Vinzenz, D., Worpenberg, S., et al. (2006) · Structure · doi:10.1016/j.str.2006.06.012 · Cited by 212 · see citing works
Mechanisms, biology and inhibitors of deubiquitinating enzymes
Love, K. R., Catic, A., Schlieker, C. D., & Ploegh, H. L. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.43 · Cited by 211 · see citing works
The SAGA continues: expanding the cellular role of a transcriptional co-activator complex
Baker, S. P., & Grant, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210603 · Cited by 208 · see citing works
Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export
Köhler, A., Schneider, M., Cabal, G. G., Nehrbass, U., & Hurt, E. (2008) · Nature Cell Biology · doi:10.1038/ncb1733 · Cited by 204 · see citing works
Identification and Characterization of DEN1, a Deneddylase of the ULP Family
Gan‐Erdene, T., Kolli, N., Yin, L., Wu, K. K.-Y., Pan, Z., & Wilkinson, K. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302890200 · Cited by 204 · see citing works
Self-citationAtaxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates
Zhong, X., & Pittman, R. N. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl164 · Cited by 201 · see citing works
Yoshida, H., Jono, H., Kai, H., & Li, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509526200 · Cited by 199 · see citing works
Structure of the Ubiquitin Hydrolase UCH-L3 Complexed with a Suicide Substrate
Misaghi, S., Galardy, P. J., Meester, W. J. N., Ovaa, H., Ploegh, H. L., & Gaudet, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410770200 · Cited by 193 · see citing works
Wu, K. K.-Y., Yamoah, K., Dolios, G., Gan‐Erdene, T., Tan, P., Chen, A., Lee, C.-G., Wei, N., Wilkinson, K. D., Wang, R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302888200 · Cited by 192 · see citing works
Self-citationFat facets and Liquid facets promote Delta endocytosis and Delta signaling in the signaling cells
Overstreet, E., Fitch, E., & Fischer, J. A. (2004) · Development · doi:10.1242/dev.01434 · Cited by 191 · see citing works
Erhardt, P., & Cooper, G. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17601 · Cited by 190 · see citing works
Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides.
Pickart, C. M., & Rose, I. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39538-8 · Cited by 187 · see citing works
Nicastro, G., Menon, R. P., Masino, L., Knowles, P. P., McDonald, N. Q., & Pastore, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501732102 · Cited by 187 · see citing works
Das, C., Hoang, Q. Q., Kreinbring, C. A., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510403103 · Cited by 187 · see citing works
Protein partners of deubiquitinating enzymes
Ventii, K., & Wilkinson, K. D. (2008) · Biochemical Journal · doi:10.1042/bj20080798 · Cited by 185 · see citing works
Self-citationStructural basis for distinct roles of Lys63‐ and Lys48‐linked polyubiquitin chains
Tenno, T., Fujiwara, K., Tochio, H., Iwaï, K., Morita, E., Hayashi, H., Murata, S., Hiroaki, H., Sato, M., Tanaka, K., et al. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00780.x · Cited by 182 · see citing works
Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
Wang, Q., Li, L., & Ye, Y. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605100 · Cited by 180 · see citing works
Emre, N. C. T., Ingvarsdottir, K., Wyce, A., Wood, A., Krogan, N. J., Henry, K. W., Li, K., Marmorstein, R., Greenblatt, J., Shilatifard, A., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.007 · Cited by 178 · see citing works
Positive and negative signaling components involved in TNFα-induced NF-κB activation
Li, H., & Lin, X. (2008) · Cytokine · doi:10.1016/j.cyto.2007.09.016 · Cited by 176 · see citing works
Mu, J., Wáng, Y., Luo, H., Leng, M., Zhang, J., Yang, T., Besusso, D., Jung, S. Y., & Qin, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700079200 · Cited by 172 · see citing works
Proteasome-associated proteins: regulation of a proteolytic machine
Schmidt, M., Hanna, J. W., Elsasser, S., & Finley, D. J. (2005) · Biological Chemistry · doi:10.1515/bc.2005.085 · Cited by 171 · see citing works
Chai, Y., Berke, S. J. S., Cohen, R. E., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310939200 · Cited by 171 · see citing works
Crystal Structure and Solution NMR Studies of Lys48-linked Tetraubiquitin at Neutral pH
Eddins, M. J., Varadan, R., Fushman, D., Pickart, C. M., & Wolberger, C. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.065 · Cited by 171 · see citing works
Structure of the A20 OTU domain and mechanistic insights into deubiquitination
Komander, D., & Barford, D. (2007) · Biochemical Journal · doi:10.1042/bj20071399 · Cited by 170 · see citing works
Hutti, J. E., Turk, B. E., Asara, J. M., Ma, A. I., Cantley, L. C., & Abbott, D. W. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01101-07 · Cited by 169 · see citing works
Row, P. E., Liu, H., Hayes, S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704009200 · Cited by 167 · see citing works
Gardner, R. G., Nelson, Z. W., & Gottschling, D. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.6123-6139.2005 · Cited by 165 · see citing works
Molecular Basis for the Unique Deubiquitinating Activity of the NF-κB Inhibitor A20
Lin, S., Chung, J. Y., Lamothe, B., Rajashankar, K. R., Lu, M., Lo, Y.-C., Lam, A. Y., Darnay, B. G., & Wu, H. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.092 · Cited by 162 · see citing works
Deubiquitinating function of ataxin-3: Insights from the solution structure of the Josephin domain
Mao, Y., Senic-Matuglia, F., Fiore, P. P. D., Polo, S., Hodsdon, M. E., & Camilli, P. V. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506344102 · Cited by 162 · see citing works
Complementary Roles for Rpn11 and Ubp6 in Deubiquitination and Proteolysis by the Proteasome
Guterman, A., & Glickman, M. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307050200 · Cited by 161 · see citing works
A Novel Type of Deubiquitinating Enzyme
Evans, P. C., Smith, T., Lai, M.-J., Williams, M., Burke, D. F., Heyninck, K., Kreike, M., Beyaert, R., Blundell, T. L., & Kilshaw, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301863200 · Cited by 161 · see citing works
Chlamydia trachomatis‐derived deubiquitinating enzymes in mammalian cells during infection
Misaghi, S., Balsara, Z. R., Catic, A., et al. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05199.x · Cited by 159 · see citing works
Schoenfeld, A. R., Apgar, S., Dolios, G., Wang, R., & Aaronson, S. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7444-7455.2004 · Cited by 157 · see citing works
Yao, T., Song, L., Jin, J.-J., Cai, Y., Takahashi, H., Swanson, S., Washburn, M., Florens, L., Conaway, R., Cohen, R., et al. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.08.027 · Cited by 156 · see citing works
Structure of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed
Cook, W. J., Jeffrey, L. C., Kasperek, E. M., & Pickart, C. M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1169 · Cited by 156 · see citing works
The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily
Baker, R. T., & Philip G. Board (1987) · Nucleic Acids Research · doi:10.1093/nar/15.2.443 · Cited by 154 · see citing works
Avvakumov, G. V., Walker, J. R., Xue, S., Finerty, P. J., MacKenzie, F., Newman, E. M., & Dhe‐Paganon, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606704200 · Cited by 154 · see citing works
Small Ubiquitin-related Modifier (SUMO)-specific Proteases
Mikolajczyk, J., Drąg, M., Békés, M., Cao, J. T., Ronai, Z. A., & Salvesen, G. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702444200 · Cited by 152 · see citing works
A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae
Schlieker, C. D., Korbel, G. A., Kattenhorn, L. M., & Ploegh, H. L. (2005) · Journal of Virology · doi:10.1128/jvi.79.24.15582-15585.2005 · Cited by 150 · see citing works
Zhang, X., Pfeiffer, H. K., Thorne, A. W., & McMahon, S. B. (2008) · Cell Cycle · doi:10.4161/cc.7.11.5962 · Cited by 149 · see citing works
Polyubiquitin Binding and Disassembly By Deubiquitinating Enzymes
Reyes‐Turcu, F. E., & Wilkinson, K. D. (2009) · Chemical Reviews · doi:10.1021/cr800470j · Cited by 148 · see citing works
Self-citationNegrate, G. L., Faustin, B., Welsh, K., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.7.5045 · Cited by 147 · see citing works
Structural and functional analysis of ataxin‐2 and ataxin‐3
Albrecht, M., Golatta, M., Wüllner, U., & Lengauer, T. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04245.x · Cited by 140 · see citing works
Ingvarsdottir, K., Krogan, N. J., Emre, N. C. T., Wyce, A., Thompson, N. J., Emili, A., Hughes, T. R., Greenblatt, J., & Berger, S. L. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1162-1172.2005 · Cited by 137 · see citing works
Doelling, J. H., Yan, N., Kurepa, J., Walker, J. M., & Vierstra, R. D. (2001) · The Plant Journal · doi:10.1046/j.1365-313x.2001.01106.x · Cited by 136 · see citing works
Recognition of Polyubiquitin Isoforms by the Multiple Ubiquitin Binding Modules of Isopeptidase T
Reyes‐Turcu, F. E., Shanks, J. R., Komander, D., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800947200 · Cited by 134 · see citing works
Self-citationCharacterization of ubiquitin and ubiquitin‐like‐protein isopeptidase activities
Nicholson, B., Leach, C. A., Goldenberg, S. J., Francis, D. M., Kodrasov, M. P., Tian, X., Shanks, J. R., Sterner, D. E., Bernal, A., Mattern, M. R., et al. (2008) · Protein Science · doi:10.1110/ps.083450408 · Cited by 133 · see citing works
Self-citationKöhler, A., Pascual‐García, P., Llopis, A., Zapater, M., Posas, F., Hurt, E., & Rodríguez‐Navarro, S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-02-0098 · Cited by 133 · see citing works
Regulation of IκB Kinase-related Kinases and Antiviral Responses by Tumor Suppressor CYLD
Zhang, M., Wu, X., Lee, A. J., Jin, W., Chang, M., Wright, A., Imaizumi, T., & Sun, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801451200 · Cited by 131 · see citing works
Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice
Anderson, C., Crimmins, S. L., Wilson, J. A., Korbel, G., Ploegh, H. L., & Wilson, S. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03409.x · Cited by 128 · see citing works
Fbw7 and Usp28 Regulate Myc Protein Stability in Response to DNA Damage
Popov, N., Herold, S., Prada, M. L., Schülein‐Völk, C., & Eilers, M. (2007) · Cell Cycle · doi:10.4161/cc.6.19.4804 · Cited by 125 · see citing works
Goodrich, J. S., Clouse, K. N., & Schüpbach, T. (2004) · Development · doi:10.1242/dev.01078 · Cited by 124 · see citing works
Bacterial Interference of Ubiquitination and Deubiquitination
Rytkönen, A., & Holden, D. W. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.02.003 · Cited by 121 · see citing works
Mullally, J. E., Moos, P. J., Edes, K., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102198200 · Cited by 119 · see citing works
Methylation of H3 Lysine 4 at Euchromatin Promotes Sir3p Association with Heterochromatin
Santos-Rosa, H., Bannister, A. J., Dehé, P.-M., Géli, V., & Kouzarides, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407949200 · Cited by 117 · see citing works
14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK
Al-Hakim, A., Göransson, O., Deák, M., Toth, R. L., Campbell, D. G., MORRICE, N. A., Prescott, A. R., & Alessi, D. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02670 · Cited by 117 · see citing works
Deubiquitinating Enzymes are IN(Trinsic to Proteasome Function)
Guterman, A., & Glickman, M. H. (2004) · Current Protein and Peptide Science · doi:10.2174/1389203043379756 · Cited by 114 · see citing works
Negrate, G. L., Krieg, A. H., Faustin, B., Loeffler, M. W., Godzik, A., Krajewski, S., & Reed, J. C. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01178.x · Cited by 114 · see citing works
Chernova, T. A., Allen, K., Wesoloski, L. M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310283200 · Cited by 113 · see citing works
DUB-2 Is a Member of a Novel Family of Cytokine-inducible Deubiquitinating Enzymes
Zhu, Y., Lambert, K., Corless, C. N., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., & D’Andrea, A. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.51 · Cited by 112 · see citing works
Multi-tasking on chromatin with the SAGA coactivator complexes.
Daniel, J. A., & Grant, P. A. (2007) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2006.09.008 · Cited by 111 · see citing works
Hassiepen, U., Eidhoff, U., Meder, G., et al. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.07.034 · Cited by 110 · see citing works
Screen for ISG15-crossreactive Deubiquitinases
Catic, A., Fiebiger, E., Korbel, G. A., Blom, D., Galardy, P. J., & Ploegh, H. L. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000679 · Cited by 108 · see citing works
Mizuno, E., Kitamura, N., & Komada, M. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.028 · Cited by 105 · see citing works
Novel Predicted Peptidases with a Potential Role in the Ubiquitin Signaling Pathway
Iyer, L. M., Koonin, E. V., & Aravind, L. (2004) · Cell Cycle · doi:10.4161/cc.3.11.1206 · Cited by 104 · see citing works
The CAP-Gly Domain of CYLD Associates with the Proline-Rich Sequence in NEMO/IKKγ
Saito, K., Kigawa, T., Koshiba, S., Sato, K. Z., Matsuo, Y., Sakamoto, A., Takagi, T., Shirouzu, M., Yabuki, T., Nunokawa, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.07.012 · Cited by 103 · see citing works
Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein
Messick, T. E., Russell, N. S., Iwata, A. J., Sarachan, K. L., Shiekhattar, R., Shanks, J. R., Reyes‐Turcu, F. E., Wilkinson, K. D., & Marmorstein, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m704398200 · Cited by 102 · see citing works
Self-citationSulea, T. I., Lindner, H. A., Purisima, E. O., et al. (2005) · Journal of Virology · doi:10.1128/jvi.79.7.4550-4551.2005 · Cited by 101 · see citing works
Reverse the curse—the role of deubiquitination in cell cycle control
Song, L., & Rapé, M. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.012 · Cited by 100 · see citing works
Human disorders of ubiquitination and proteasomal degradation
Jiang, Y., & Beaudet, A. L. (2004) · Current Opinion in Pediatrics · doi:10.1097/01.mop.0000133634.79661.cd · Cited by 96 · see citing works
Role of Bmi1 in H2A Ubiquitylation and Hox Gene Silencing
Wei, J., Zhai, L., Xu, J. Q., & Wang, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600826200 · Cited by 91 · see citing works
Cai, S., Babbitt, R. W., & Marchesi, V. T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2828 · Cited by 89 · see citing works
Crystal structure of human otubain 2
Nanao, M., Tcherniuk, S. O., Chroboczek, J., et al. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400201 · Cited by 89 · see citing works
Identification and Characterization of a Drosophila Proteasome Regulatory Network
Lundgren, J., Masson, P., Mirzaei, Z., & Young, P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.11.4662-4675.2005 · Cited by 89 · see citing works
Uch2/Uch37 is the Major Deubiquitinating Enzyme Associated with the 26 S Proteasome in Fission Yeast
Stone, M., Hartmann‐Petersen, R., Seeger, M., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.057 · Cited by 85 · see citing works
Dual mechanisms specify Doa4‐mediated deubiquitination at multivesicular bodies
Richter, C. M., West, M., & Odorizzi, G. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601692 · Cited by 85 · see citing works
Mermerian, A. H., Case, A. W., Stein, R. L., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.04.027 · Cited by 84 · see citing works
Rad23 and Rpn10: perennial wallflowers join the m�l�e
Madura, K. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.10.008 · Cited by 82 · see citing works
Tumor suppressor CYLD: negative regulation of NF-κB signaling and more
Courtois, G. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7465-4 · Cited by 81 · see citing works
Transgenic Rescue ofataxiaMice with Neuronal-Specific Expression of Ubiquitin-Specific Protease 14
Crimmins, S. L., Jin, Y. N., Wheeler, C. G., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3600-06.2006 · Cited by 80 · see citing works
The many faces of ubiquitinated histone H2A: insights from the DUBs
Vissers, J. H. A., Nicassio, F., van Lohuizen, M., Fiore, P. P. D., & Citterio, E. (2008) · Cell Division · doi:10.1186/1747-1028-3-8 · Cited by 80 · see citing works
Wilkinson, K. D., Gan‐Erdene, T., & Kolli, N. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99003-4 · Cited by 79 · see citing works
Self-citationElaD, a Deubiquitinating Protease Expressed by E. coli
Catic, A., Misaghi, S., Korbel, G. A., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000381 · Cited by 79 · see citing works
Structure of a new crystal form of tetraubiquitin
Phillips, C. L., Thrower, J. S., Pickart, C. M., & Hill, C. P. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490001800x · Cited by 76 · see citing works
Steinhauer, W. R., Walsh, R., & Kalfayan, L. J. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.12.5726 · Cited by 70 · see citing works
Deubiquitination in virus infection
Lindner, H. A. (2007) · Virology · doi:10.1016/j.virol.2006.12.035 · Cited by 69 · see citing works
Kinetic studies of isopeptidase T: modulation of peptidase activity by ubiquitin
Stein, R. L., Chen, Z., & Melandri, F. D. (1995) · Biochemistry · doi:10.1021/bi00039a017 · Cited by 66 · see citing works
Yamaguchi, T., Kimura, J., Miki, Y., & Yoshida, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706282200 · Cited by 64 · see citing works
Mimnaugh, E. G., Kayastha, G., McGovern, N., et al. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400924 · Cited by 61 · see citing works
DOT4 Links Silencing and Cell Growth in Saccharomyces cerevisiae
Kahana, A., & Gottschling, D. E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.6608 · Cited by 59 · see citing works
Deubiquitinating Enzymes: Their Functions and Substrate Specificity
Soboleva, T., & Baker, R. T. (2004) · Current Protein and Peptide Science · doi:10.2174/1389203043379765 · Cited by 58 · see citing works
Controlling Receptor Downregulation by Ubiquitination and Deubiquitination
Komada, M. (2008) · Current Drug Discovery Technologies · doi:10.2174/157016308783769469 · Cited by 55 · see citing works
The Murine DUB-1 Gene Is Specifically Induced by the βc Subunit of the Interleukin-3 Receptor
Zhu, Y., Pless, M., Inhorn, R. C., et al. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4808 · Cited by 55 · see citing works
UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself
Wada, K., & Kamitani, T. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.144 · Cited by 53 · see citing works
Calcium/Calmodulin Regulates Ubiquitination of the Ubiquitin-specific Protease TRE17/USP6
Shen, C., Ye, Y., Robertson, S. E., Lau, A. W., Mak, D. D., & Chou, M. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505220200 · Cited by 52 · see citing works
Fujiwara, T., Saito, A., Suzuki, M., et al. (1998) · Genomics · doi:10.1006/geno.1998.5554 · Cited by 45 · see citing works
Baek, K., Kim, M., Kim, Y., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m304774200 · Cited by 45 · see citing works
Cytokine-Regulated Protein Degradation by the Ubiquitination System
Baek, K. (2006) · Current Protein and Peptide Science · doi:10.2174/138920306776359740 · Cited by 44 · see citing works
DUB-2A, a new member of the DUB subfamily of hematopoietic deubiquitinating enzymes
Baek, K., Mondoux, M. A., Jaster, R., et al. (2001) · Blood · doi:10.1182/blood.v98.3.636 · Cited by 44 · see citing works
Lindsey, D. F., Amerik, A. Y., Deery, W. J., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.29178 · Cited by 42 · see citing works
Wilkinson, K. D., Laleli-Sahin, E., Urbauer, J. L., Larsen, C. N., Shih, G. H., Haas, A. L., Walsh, S. T. R., & Wand, A. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3038 · Cited by 41 · see citing works
Self-citationEpstein-Barr Virus Encodes Three Bona Fide Ubiquitin-Specific Proteases
Sompallae, R. R., Gastaldello, S., Hildebrand, S., Zinin, N., Hassink, G. C., Lindsten, K., Haas, J., Persson, B., & Masucci, M. G. (2008) · Journal of Virology · doi:10.1128/jvi.01113-08 · Cited by 40 · see citing works
Dubbing SAGA Unveils New Epigenetic Crosstalk
Pijnappel, W. W. M. P., & Timmers, H. T. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.01.007 · Cited by 37 · see citing works
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- [6]Fang S Weissman AM A field guide to ubiquitylation. Cell Mol Life Sci 2004 61 1546 61 15224180 PMC11138666
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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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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“fingers” sub-domain architecture (Reyes-Turcu et al., 2009) (Figure 1).”
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Hou, P., Ma, X., Zhang, Q., Wu, C.-J., Liao, W., Li, J., Wang, H., Zhao, J., Zhou, X., Guan, C., et al. (2019) · Genes & Development · doi:10.1101/gad.326314.119 · Cited by 96 · see citing works
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Dar, A., Shibata, E., & Dutta, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00358-13 · Cited by 83 · see citing works
Cellular and disease functions of the Prader–Willi Syndrome gene<i>MAGEL2</i>
Tacer, K. F., & Potts, P. R. (2017) · Biochemical Journal · doi:10.1042/bcj20160616 · Cited by 81 · see citing works
Tian, X., Isamiddinova, N. S., Peroutka, R. J., Goldenberg, S. J., Mattern, M. R., Nicholson, B., & Leach, C. (2011) · ASSAY and Drug Development Technologies · doi:10.1089/adt.2010.0317 · Cited by 76 · see citing works
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Wang, L., Hu, T., Shen, Z., Zheng, Y., Geng, Q., Li, L., Sha, B., Li, M., Sun, Y., Guo, Y., et al. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05341-3 · Cited by 45 · see citing works
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Masuda, Y., Kanao, R., Kawai, H., Kukimoto, I., & Masutani, C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005167 · Cited by 18 · see citing works
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Bjij, I., Ramharack, P., Khan, S., Cherqaoui, D., & Soliman, M. E. S. (2019) · Molecules · doi:10.3390/molecules24173125 · Cited by 6 · see citing works
Jung, J. W., Choi, J. C., Kim, J. Y., Park, I. W., Choi, B. W., Shin, J. W., & Christman, J. W. (2011) · Tuberculosis and Respiratory Diseases · doi:10.4046/trd.2011.70.2.113 · Cited by 2 · see citing works
- 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
- Physical Sciences › Materials Science › Materials Chemistry › 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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