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Mechanism of USP7/HAUSP Activation by Its C-Terminal Ubiquitin-like Domain and Allosteric Regulation by GMP-Synthetase
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“The deubiquitinating enzyme (DUB) ubiquitin-specific protease 7 (USP7), also known as herpes virus-associated ubiquitin-specific protease (HAUSP), regulates the function of the tumor suppressor p53 that is mutated or inactivated in 50% of human cancers (Vogelstein et al., 2000).”
BackgroundA 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
Self-citationUbiquitination regulates PTEN nuclear import and tumor suppression
Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748
A dynamic role of HAUSP in the p53-Mdm2 pathway
Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679
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
Self-citationDisruption of HAUSP gene stabilizes p53.
Cummins, J. M., Rago, C., Kohli, M., Kinzler, K. W., Lengauer, C., & Vogelstein, B. (2004) · Nature · doi:10.1038/nature02501 · Cited by 379
HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53
Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361
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
Cited by
Deubiquitylating enzymes and drug discovery: emerging opportunities
Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940
Breaking the chains: deubiquitylating enzyme specificity begets function
Clague, M. J., Urbé, S., & Komander, D. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0099-1 · Cited by 832
Molecular basis of USP7 inhibition by selective small-molecule inhibitors.
Turnbull, A. P., Ioannidis, S., Krajewski, W. W., Pinto-Fernandez, A., Heride, C., Martin, A. C. L., Tonkin, L. M., Townsend, E. C., Buker, S. M., Lancia, D. R., et al. (2017) · Nature · doi:10.1038/nature24451 · Cited by 463
Deubiquitylases From Genes to Organism
Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 425
Discovery of specific inhibitors of human USP7/HAUSP deubiquitinating enzyme.
Reverdy, C., Conrath, S., Lopez, R., Planquette, C., Atmanene, C., Collura, V., Harpon, J., Battaglia, V., Vivat, V., Sippl, W., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.02.007 · Cited by 270
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
Structure-guided development of a potent and selective non-covalent active-site inhibitor of USP7.
Lamberto, I., Liu, X., Seo, H.-S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.003 · Cited by 192
USP7: Structure, substrate specificity, and inhibition
Pozhidaeva, A., & Bezsonova, I. (2019) · DNA Repair · doi:10.1016/j.dnarep.2019.02.005 · Cited by 178
“DUBs deubiquitinate both poly- and monoubiquitinated proteins and thus change their fate.”
BackgroundInfluentialEmerging insights into HAUSP (USP7) in physiology, cancer and other diseases.
Bhattacharya, S., Chakraborty, D., Basu, M., & Ghosh, M. K. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-018-0012-y · Cited by 162
Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation.
Cheng, J., Yang, H., Fang, J., Ma, L., Gong, R., Wang, P., Li, Z., & Xu, Y. (2015) · Nature Communications · doi:10.1038/ncomms8023 · Cited by 158
USP7 Is a Master Regulator of Genome Stability
Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114
Pozhidaeva, A., Valles, G., Wang, F., Wu, J., Sterner, D. E., Nguyen, P., Weinstock, J., Kumar, K. G. S., Kanyo, J., Wright, D., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.004 · Cited by 107
Molecular understanding of USP7 substrate recognition and c-terminal activation.
Rougé, L., Bainbridge, T. W., Kwok, M., Tong, R., Di Lello, P., Wertz, I. E., Maurer, T., Ernst, J. A., & Murray, J. (2016) · Structure · doi:10.1016/j.str.2016.05.020 · Cited by 108
USP7 deubiquitinase promotes ubiquitin-dependent DNA damage signaling by stabilizing RNF168.
Zhu, Q., Sharma, N., He, J., Wani, G., & Wani, A. A. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1007785 · Cited by 87
A role for USP7 in DNA replication.
Jagannathan, M., Nguyen, T., Gallo, D., Luthra, N., Brown, G. W., Saridakis, V., & Frappier, L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00639-13 · Cited by 71
USP7 is a suppressor of PCNA ubiquitination and oxidative-stress-induced mutagenesis in human cells.
Kashiwaba, S.-I., Kanao, R., Masuda, Y., Kusumoto-Matsuo, R., Hanaoka, F., & Masutani, C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.014 · Cited by 71
Giovinazzi, S., Morozov, V. M., Summers, M. K., Reinhold, W. C., & Ishov, A. M. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.169 · Cited by 65
The USP7 protein interaction network and its roles in tumorigenesis
Al-Eidan, A., Wang, Y., Skipp, P., & Ewing, R. M. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2020.10.004 · Cited by 57
Qin, X., Wang, R., Xu, H., Tu, L., Chen, H., Li, H., Liu, N., Wang, J., Li, S., Yin, F., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.2022360 · Cited by 55
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity.
Kim, R. Q., Geurink, P. P., Mulder, M. P. C., Fish, A., Ekkebus, R., El Oualid, F., van Dijk, W. J., van Dalen, D., Ovaa, H., van Ingen, H., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08231-5 · Cited by 41
Self-citationTRIMming p53’s anticancer activity
Elabd, S., Meroni, G., & Blattner, C. (2016) · Oncogene · doi:10.1038/onc.2016.33 · Cited by 43
Bashore, C., Jaishankar, P., Skelton, N. J., Fuhrmann, J., Hearn, B. R., Liu, P. S., Renslo, A. R., & Dueber, E. C. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00031 · Cited by 34
Rennie, M. L., Gundogdu, M., Arkinson, C., Liness, S., Frame, S., & Walden, H. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01184 · Cited by 27
The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics
Llerena Schiffmacher, D. A., Lee, S.-H., Kliza, K. W., Theil, A. F., Akita, M., Helfricht, A., Bezstarosti, K., Gonzalo-Hansen, C., van Attikum, H., Verlaan-de Vries, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50584-7 · Cited by 19
Self-citationMasuda, Y., Kanao, R., Kawai, H., Kukimoto, I., & Masutani, C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005167 · Cited by 18
USP7 protects TFEB from proteasome-mediated degradation
Keshri, S., Vicinanza, M., Takla, M., & Rubinsztein, D. C. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114872 · Cited by 13
Structural insights into ubiquitin chain cleavage by Legionella ovarian tumor deubiquitinases
Kang, S., Kim, G., Choi, M., Jeong, M., van der Heden van Noort, G. J., Roh, S.-H., & Shin, D. (2023) · Life Science Alliance · doi:10.26508/lsa.202201876 · Cited by 9
Metadata
- Authors
- Faesen, A. C., Dirac, A. M. G., Shanmugham, A., Ovaa, H., Perrakis, A., & Sixma, T. K.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 44
- Issue
- 1
- Pages
- 147-159
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2037239543
- Cited by
- 248
- References
- 17
- FWCI
- 5.17
- Type
- journal article
- Language
- en
- Open access
- bronze
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