Emerging insights into HAUSP (USP7) in physiology, cancer and other diseases.

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

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.082307.091526 · Cited by 1,396 · see citing works

Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,027 · 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

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 · see citing works

Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde

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

Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages

Kulathu, Y., & Komander, D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3394 · Cited by 642 · see citing works

A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance.

Chauhan, D., Tian, Z., Nicholson, B., Kumar, K. G. S., Zhou, B., Carrasco, R., McDermott, J. L., Leach, C. A., Fulcinniti, M., Kodrasov, M. P., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.007 · Cited by 589 · see citing works

The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network

Song, M. S., Salmena, L., Carracedo, A., Egia, A., Lo-Coco, F., Teruya-Feldstein, J., & Pandolfi, P. P. (2008) · Nature · doi:10.1038/nature07290 · Cited by 548 · see citing works

A novel ubiquitin‐specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein

Everett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., & Parkinson, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1519 · Cited by 491 · see citing works

FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP

van der Horst, A., de Vries-Smits, A. M. M., Brenkman, A. B., van Triest, M. H., van den Broek, N. J. F., Colland, F., Maurice, M. M., & Burgering, B. M. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1469 · Cited by 479 · see citing works

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 · see citing works

Deubiquitinases in cancer: new functions and therapeutic options

Fraile, J. M., Quesada, V., Rodrı́guez, D., Freije, J. M. P., & López-Otı́n, C. (2011) · Oncogene · doi:10.1038/onc.2011.443 · Cited by 453 · see citing works

Disruption 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 · see citing works

DNMT1 Stability Is Regulated by Proteins Coordinating Deubiquitination and Acetylation-Driven Ubiquitination

Du, Z., Song, J. K., Wang, Y., Zhao, Y., Guda, K., Yang, S., Kao, H., Xu, Y., Willis, J. E., Markowitz, S. D., et al. (2010) · Science Signaling · doi:10.1126/scisignal.2001462 · Cited by 337 · see citing works

USP7 small-molecule inhibitors interfere with ubiquitin binding.

Kategaya, L., Di Lello, P., Rougé, L., Pastor, R., Clark, K. R., Drummond, J., Kleinheinz, T., Lin, E., Upton, J.-P., Prakash, S., et al. (2017) · Nature · doi:10.1038/nature24006 · Cited by 333 · see citing works

Stabilization of the Transcription Factor Foxp3 by the Deubiquitinase USP7 Increases Treg-Cell-Suppressive Capacity

van Loosdregt, J., Fleskens, V., Fu, J., Brenkman, A., Bekker, C., Pals, C., Meerding, J., Berkers, C., Barbi, J., Gröne, A., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.018 · Cited by 325 · see citing works

Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells

Colland, F., Formstecher, É., Jacq, X., Reverdy, C., Planquette, C., Conrath, S., Trouplin, V., Bianchi, J., Aushev, V. N., Camonis, J., et al. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0097 · Cited by 322 · see citing works

Monoubiquitylation promotes mitochondrial p53 translocation

Marchenko, N. D., Wolff, S., Erster, S., Becker, K., & Moll, U. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601560 · Cited by 286 · see citing works

UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair

Schwertman, P., Lagarou, A., Dekkers, D. H. W., Raams, A., van der Hoek, A. C., Laffeber, C., Hoeijmakers, J. H. J., Demmers, J. A. A., Fousteri, M., Vermeulen, W., et al. (2012) · Nature Genetics · doi:10.1038/ng.2230 · Cited by 279 · see citing works

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 · see citing works

Mechanism of USP7/HAUSP Activation by Its C-Terminal Ubiquitin-like Domain and Allosteric Regulation by GMP-Synthetase

Faesen, A. C., Dirac, A. M. G., Shanmugham, A., Ovaa, H., Anastassis Perrakis, A., & Sixma, T. K. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.034 · Cited by 251 · see citing works

A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.

Zapata, J. M., Pawlowski, K., Haas, E., Ware, C. F., Godzik, A., & Reed, J. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100354200 · Cited by 228 · see citing works

USP7 acts as a molecular rheostat to promote WASH-dependent endosomal protein recycling and is mutated in a human neurodevelopmental disorder.

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

The FoxO Family in Cardiac Function and Dysfunction

Ronnebaum, S. M., & Patterson, C. (2010) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021909-135931 · Cited by 206 · see citing works

Stabilization of histone demethylase PHF8 by USP7 promotes breast carcinogenesis.

Wang, Q., Ma, S., Song, N., Li, X., Liu, L., Yang, S., Ding, X., Shan, L., Zhou, X., Su, D., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85747 · Cited by 206 · see citing works

The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1

Felle, M., Joppien, S., Németh, A., Diermeier, S. D., Thalhammer, V., Dobner, T., Kremmer, E., Kappler, R., & Längst, G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr528 · Cited by 198 · see citing works

Protein Interaction Domains of the Ubiquitin-specific Protease, USP7/HAUSP

Holowaty, M. N., Sheng, Y., Nguyen, T., Arrowsmith, C. H., & Frappier, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307200200 · Cited by 182 · see citing works

Inactivation of HAUSP in vivo modulates p53 function.

Kon, N., Kobayashi, Y., Li, M., Brooks, C. L., Ludwig, T., & Gu, W. (2010) · Oncogene · doi:10.1038/onc.2009.427 · Cited by 176 · see citing works

USP7 Is a Tumor-Specific WNT Activator for APC-Mutated Colorectal Cancer by Mediating β-Catenin Deubiquitination

Novellasdemunt, L., Foglizzo, V., Gómez-Cuadrado, L., Antas, P., Kucharska, A., Encheva, V., Snijders, A. P., & Li, V. S. W. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.072 · Cited by 163 · see citing works

Deubiquitylase HAUSP stabilizes REST and promotes maintenance of neural progenitor cells

Huang, Z., Wu, Q., Guryanova, O. A., Cheng, L., Shou, W., Rich, J. N., & Bao, S. (2011) · Nature Cell Biology · doi:10.1038/ncb2153 · Cited by 160 · see citing works

Ubiquitin‐specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor

Maertens, G. N., Messaoudi, S. E., Elderkin, S., Hiom, K. J., & Peters, G. G. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.129 · Cited by 155 · see citing works

Epstein-Barr Nuclear Antigen 1 Contributes to Nasopharyngeal Carcinoma through Disruption of PML Nuclear Bodies

Sivachandran, N., Sarkari, F., & Frappier, L. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000170 · Cited by 153 · see citing works

Epstein‐Barr virus and the pathogenesis of Burkitt's lymphoma: More questions than answers

Bornkamm, G. W. (2008) · International Journal of Cancer · doi:10.1002/ijc.24223 · Cited by 150 · see citing works

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription

Colleran, A., Collins, P. E., O’Carroll, C., Ahmed, A., Mao, X., McManus, B., Kiely, P. A., Burstein, E., & Carmody, R. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208446110 · Cited by 150 · see citing works

ATM-Dependent Downregulation of USP7/HAUSP by PPM1G Activates p53 Response to DNA Damage

Khoronenkova, S. V., Dianova, I. I., Ternette, N., Kessler, B. M., Parsons, J. L., & Dianov, G. L. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.021 · Cited by 146 · see citing works

HSV ICP0 recruits USP7 to modulate TLR-mediated innate response

Daubeuf, S., Singh, D., Tan, Y., Liu, H., Federoff, H. J., Bowers, W. J., & Tolba, K. A. (2008) · Blood · doi:10.1182/blood-2008-07-168203 · Cited by 146 · see citing works

Deubiquitinases and the new therapeutic opportunities offered to cancer

Pfoh, R., Lacdao, I. K., & Saridakis, V. (2015) · Endocrine Related Cancer · doi:10.1530/erc-14-0516 · Cited by 140 · see citing works

Reciprocal Activities between Herpes Simplex Virus Type 1 Regulatory Protein ICP0, a Ubiquitin E3 Ligase, and Ubiquitin-Specific Protease USP7

Boutell, C., Canning, M., Orr, A., & Everett, R. D. (2005) · Journal of Virology · doi:10.1128/jvi.79.19.12342-12354.2005 · Cited by 134 · see citing works

K63-polyubiquitinated HAUSP deubiquitinates HIF-1α and dictates H3K56 acetylation promoting hypoxia-induced tumour progression

Wu, H.-T., Kuo, Y.-C., Hung, J.-J., Huang, C.-H., Chen, W.-Y., Chou, T.-Y., Chen, Y., Chen, Y.-J., Chen, Y.-J., Cheng, W.-C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13644 · Cited by 129 · see citing works

Ubiquitin‐specific protease 7 accelerates p14ARF degradation by deubiquitinating thyroid hormone receptor‐interacting protein 12 and promotes hepatocellular carcinoma progression

Cai, J., Shi, G., Dong, Z., Ke, A., Ma, H., Gao, Q., Shen, Z., Huang, X., Chen, H., Yu, D., et al. (2014) · Hepatology · doi:10.1002/hep.27682 · Cited by 123 · see citing works

The Ability of Herpes Simplex Virus Type 1 Immediate-Early Protein Vmw110 To Bind to a Ubiquitin-Specific Protease Contributes to Its Roles in the Activation of Gene Expression and Stimulation of Virus Replication

Everett, R. D., Meredith, M., & Orr, A. (1999) · Journal of Virology · doi:10.1128/jvi.73.1.417-426.1999 · Cited by 122 · see citing works

TSPYL5 suppresses p53 levels and function by physical interaction with USP7.

Epping, M. T., Meijer, L. A. T., Krijgsman, O., Bos, J. L., Pandolfi, P. P., & Bernards, R. (2011) · Nature Cell Biology · doi:10.1038/ncb2142 · Cited by 117 · see citing works

DNA damage shifts circadian clock time via Hausp-dependent Cry1 stabilization

Papp, S. J., Huber, A., Jordan, S. D., Kriebs, A., Nguyen, M., Moresco, J. J., Yates, J. R., & Lamia, K. A. (2015) · eLife · doi:10.7554/elife.04883 · Cited by 113 · see citing works

USP7 counteracts SCFβTrCP- but not APCCdh1-mediated proteolysis of Claspin

Faustrup, H., Bekker-Jensen, S., Bartek, J., Lukas, J., & Mailand, N. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807137 · Cited by 113 · see citing works

The <i>HAUSP</i> gene plays an important role in non‐small cell lung carcinogenesis through p53‐dependent pathways

Masuya, D., Huang, C., Liu, D., Nakashima, T., Yokomise, H., Ueno, M., Nakashima, N., & Sumitomo, S. (2006) · The Journal of Pathology · doi:10.1002/path.1931 · Cited by 103 · see citing works

Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization.

Fernández‐Montalván, A., Bouwmeester, T., Joberty, G., Mader, R., Mahnke, M., Pierrat, B., Schlaeppi, J., Worpenberg, S., & Gerhartz, B. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05952.x · Cited by 96 · see citing works

Regulation of USP7: A High Incidence of E3 Complexes

Kim, R. Q., & Sixma, T. K. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.028 · Cited by 96 · see citing works

The role of deubiquitinating enzymes in apoptosis

Ramakrishna, S., Suresh, B., & Baek, K. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0504-6 · Cited by 94 · see citing works

The Ubiquitin Ligase RNF220 Enhances Canonical Wnt Signaling through USP7-Mediated Deubiquitination of β-Catenin

Ma, P., Yang, X., Kong, Q., Li, C., Yang, S., Li, Y., & Mao, B. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00731-14 · Cited by 93 · see citing works

USP7 controls Chk1 protein stability by direct deubiquitination.

Alonso-de Vega, I., Martín, Y., & Smits, V. A. (2014) · Cell Cycle · doi:10.4161/15384101.2014.973324 · Cited by 92 · see citing works

Deubiquitination of Ci/Gli by Usp7/HAUSP Regulates Hedgehog Signaling

Zhou, Z., Yao, X., Li, S., Xiong, Y., Dong, X., Zhao, Y., Jiang, J., & Zhang, Q. H. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.05.016 · Cited by 88 · see citing works

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 · see citing works

The RNA‐binding E3 ubiquitin ligase MEX‐3C links ubiquitination with MHC‐I mRNA degradation

Cano, F., Bye, H., Duncan, L. M., Buchet-Poyau, K., Billaud, M., Wills, M. R., & Lehner, P. J. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.218 · Cited by 83 · see citing works

Bilateral inhibition of HAUSP deubiquitinase by a viral interferon regulatory factor protein

Lee, H.-R., Choi, W., Lee, S., Hwang, J., Hwang, E., Guchhait, K., Haas, J., Tóth, Z., Jeon, Y. H., Oh, T.-K., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2142 · Cited by 81 · see citing works

Spongiacidin C, a pyrrole alkaloid from the marine sponge Stylissa massa, functions as a USP7 inhibitor

Yamaguchi, M., Miyazaki, M., Kodrasov, M. P., Rotinsulu, H., Losung, F., Mangindaan, R. E. P., de Voogd, N. J., Yokosawa, H., Nicholson, B., & Tsukamoto, S. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.04.066 · Cited by 78 · see citing works

Therapeutic inhibition of USP7-PTEN network in chronic lymphocytic leukemia: a strategy to overcome TP53 mutated/deleted clones

Carrà, G., Panuzzo, C., Torti, D., Parvis, G. E., Crivellaro, S., Familiari, U., Volante, M., Morena, D., Lingua, M. F., Brancaccio, M., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16348 · Cited by 78 · see citing works

USP7 is essential for maintaining Rad18 stability and DNA damage tolerance.

Zlatanou, A., Sabbioneda, S., Miller, E. S., Greenwalt, A., Aggathanggelou, A., Maurice, M. M., Lehmann, A. R., Stankovic, T., Reverdy, C., Colland, F., et al. (2016) · Oncogene · doi:10.1038/onc.2015.149 · Cited by 77 · see citing works

p53 apoptotic pathway molecules are frequently and simultaneously altered in nonsmall cell lung carcinoma

Mori, S., Ito, G., Usami, N., Yoshioka, H., Ueda, Y., Kodama, Y., Takahashi, M., Fong, K. M., Shimokata, K., & Sekido, Y. (2004) · Cancer · doi:10.1002/cncr.20164 · Cited by 76 · see citing works

USP7 inhibition alters homologous recombination repair and targets CLL cells independently of ATM/p53 functional status.

Agathanggelou, A., Smith, E., Davies, N. J., Kwok, M., Zlatanou, A., Oldreive, C. E., Mao, J., Da Costa, D., Yadollahi, S., Perry, T., et al. (2017) · Blood · doi:10.1182/blood-2016-12-758219 · Cited by 75 · see citing works

BCR-ABL disrupts PTEN nuclear-cytoplasmic shuttling through phosphorylation-dependent activation of HAUSP

Morotti, A., Panuzzo, C., Crivellaro, S., Pergolizzi, B., Familiari, U., Berger, A. H., Saglio, G. N., & Pandolfi, P. P. (2013) · Leukemia · doi:10.1038/leu.2013.370 · Cited by 74 · see citing works

Proteomic Profiling of the Human Cytomegalovirus UL35 Gene Products Reveals a Role for UL35 in the DNA Repair Response

Salsman, J., Jagannathan, M., Paladino, P., Chan, P.-K., Dellaire, G., Raught, B., & Frappier, L. (2011) · Journal of Virology · doi:10.1128/jvi.05442-11 · Cited by 73 · see citing works

DUBbing Cancer: Deubiquitylating Enzymes Involved in Epigenetics, DNA Damage and the Cell Cycle As Therapeutic Targets

Pinto-Fernández, A., & Kessler, B. M. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00133 · Cited by 73 · see citing works

Crystal Structure of USP7 Ubiquitin-like Domains with an ICP0 Peptide Reveals a Novel Mechanism Used by Viral and Cellular Proteins to Target USP7

Pfoh, R., Lacdao, I. K., Georges, A. A., Capar, A., Zheng, H. X., Frappier, L., & Saridakis, V. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004950 · Cited by 72 · see citing works

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 · see citing works

The Deubiquitinating Enzyme USP7 Regulates Androgen Receptor Activity by Modulating Its Binding to Chromatin

Chen, S.-T., Okada, M., Nakato, R., Izumi, K., Bando, M., & Shirahige, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.628255 · Cited by 69 · see citing works

Expression of USP7 and MARCH7 Is Correlated with Poor Prognosis in Epithelial Ovarian Cancer

Zhang, L., Wang, H., Tian, L., & Li, H. (2016) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.239.165 · Cited by 67 · see citing works

USP7 promotes cell proliferation through the stabilization of Ki-67 protein in non-small cell lung cancer cells.

Zhang, C., Lu, J., Zhang, Q.-W., Zhao, W., Guo, J.-H., Liu, S.-L., Wu, Y.-L., Jiang, B., & Gao, F.-H. (2016) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2016.08.025 · Cited by 67 · see citing works

USP7 and Daxx regulate mitosis progression and taxane sensitivity by affecting stability of Aurora-A kinase.

Giovinazzi, S., Morozov, V. M., Summers, M. K., Reinhold, W. C., & Ishov, A. M. (2013) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2012.169 · Cited by 65 · see citing works

The Ubiquitin-Specific Protease USP7 Modulates the Replication of Kaposi's Sarcoma-Associated Herpesvirus Latent Episomal DNA

Jäger, W., Santag, S., Weidner-Glunde, M., Gellermann, E., Kati, S., Pietrek, M., Viejo‐Borbolla, A., & Schulz, T. F. (2012) · Journal of Virology · doi:10.1128/jvi.06840-11 · Cited by 65 · see citing works

A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model.

Becker, K., Marchenko, N., Palacios, G., & Moll, U. M. (2008) · Cell Cycle · doi:10.4161/cc.7.9.5756 · Cited by 63 · see citing works

USP7 modulates UV-induced PCNA monoubiquitination by regulating DNA polymerase eta stability.

Qian, J., Pentz, K., Zhu, Q., Wang, Q., He, J., Srivastava, A. K., & Wani, A. A. (2015) · Oncogene · doi:10.1038/onc.2014.394 · Cited by 61 · see citing works

Expression of HAUSP in gliomas correlates with disease progression and survival of patients

Cheng, C., Niu, C., Yang, Y., Wang, Y., & Lu, M. (2013) · Oncology Reports · doi:10.3892/or.2013.2342 · Cited by 61 · see citing works

DUB3 and USP7 de-ubiquitinating enzymes control replication inhibitor Geminin: molecular characterization and associations with breast cancer.

Hernández-Pérez, S., Cabrera, E., Salido, E., Lim, M., Reid, L., Lakhani, S. R., Khanna, K. K., Saunus, J. M., & Freire, R. (2017) · Oncogene · doi:10.1038/onc.2017.21 · Cited by 61 · see citing works

The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies.

Sarkari, F., Wang, X., Nguyen, T., & Frappier, L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016598 · Cited by 59 · see citing works

HAUSP , a novel deubiquitinase for Rb – MDM 2 the critical regulator

Bhattacharya, S., & Ghosh, M. K. (2014) · FEBS Journal · doi:10.1111/febs.12843 · Cited by 57 · see citing works

Deubiquitinating Enzymes as Therapeutic Targets in Cancer

Lim, K., & Baek, K. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319220013 · Cited by 55 · see citing works

USP7 enforces heterochromatinization of p53 target promoters by protecting SUV39H1 from MDM2-mediated degradation.

Mungamuri, S. K., Qiao, R. F., Yao, S., Manfredi, J. J., Gu, W., & Aaronson, S. A. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.049 · Cited by 54 · see citing works

Protein deubiquitinase USP7 is required for osteogenic differentiation of human adipose-derived stem cells

Tang, Y., Lv, L., Li, W., Zhang, X., Jiang, Y., Ge, W., & Zhou, Y. (2017) · Stem Cell Research & Therapy · doi:10.1186/s13287-017-0637-8 · Cited by 54 · see citing works

FBXW7 and USP7 regulate CCDC6 turnover during the cell cycle and affect cancer drugs susceptibility in NSCLC

Morra, F., Luise, C., Merolla, F., Poser, I., Visconti, R., Ilardi, G., Paladino, S., Inuzuka, H., Guggino, G., Monaco, R., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3708 · Cited by 53 · see citing works

Deubiquitination of Chfr, a checkpoint protein, by USP7/HAUSP regulates its stability and activity

Oh, Y. M., Yoo, S. J., & Seol, J. H. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.193 · Cited by 52 · see citing works

Nucleophosmin/B26 regulates PTEN through interaction with HAUSP in acute myeloid leukemia

Noguera, N. I., Song, M. S., Divona, M., Catalano, G., Calvo, K. L., García, F., Ottone, T., Florenzano, F., Faraoni, I., Battistini, L., et al. (2012) · Leukemia · doi:10.1038/leu.2012.314 · Cited by 50 · see citing works

Identification of Kaposi Sarcoma Herpesvirus (KSHV) vIRF1 Protein as a Novel Interaction Partner of Human Deubiquitinase USP7

Chavoshi, S., Egorova, O., Lacdao, I. K., Farhadi, S., Sheng, Y., & Saridakis, V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.710632 · Cited by 49 · see citing works

STAT3 repressed USP7 expression is crucial for colon cancer development

Zhi, Y., ShouJun, H., Shan, Y., Haijun, L., Yume, X., Kai, Y., Li, X.-W., & Xue-li, Z. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.025 · Cited by 48 · see citing works

Proteome Changes Induced by Knock-Down of the Deubiquitylating Enzyme HAUSP/USP7

Kessler, B. M., Fortunati, E., Melis, M. H. M., Pals, C. E. G. M., Clevers, H. C., & Maurice, M. M. (2007) · Journal of Proteome Research · doi:10.1021/pr0702161 · Cited by 47 · see citing works

A Ubiquitin-specific Protease Possesses a Decisive Role for Adenovirus Replication and Oncogene-mediated Transformation

Ching, W., Koyuncu, E., Singh, S. K., Arbelo-Roman, C., Härtl, B., Kremmer, E., Speiseder, T., Meier, C., & Dobner, T. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003273 · Cited by 47 · see citing works

The stress-responsive gene ATF3 regulates the histone acetyltransferase Tip60

Cui, H., Guo, M., Xu, D. M., Ding, Z., Zhou, G., Ding, H., Zhang, J., Tang, Y., & Yan, C. (2015) · Nature Communications · doi:10.1038/ncomms7752 · Cited by 46 · see citing works

USP7 Attenuates Hepatic Gluconeogenesis Through Modulation of FoxO1 Gene Promoter Occupancy

Hall, J. A., Tabata, M., Rodgers, J. T., & Puigserver, P. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1420 · Cited by 46 · see citing works

HAUSP-nucleolin interaction is regulated by p53-Mdm2 complex in response to DNA damage response

Lim, K., Park, J.-J., Gu, B., Kim, J.-O., Park, S. G., & Baek, K. (2015) · Scientific Reports · doi:10.1038/srep12793 · Cited by 42 · see citing works

USP7/HAUSP stimulates repair of oxidative DNA lesions

Khoronenkova, S. V., Dianova, I. I., Parsons, J. L., & Dianov, G. L. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1210 · Cited by 40 · see citing works

Cell Death and Deubiquitinases: Perspectives in Cancer

Bhattacharya, S., & Ghosh, M. K. (2014) · BioMed Research International · doi:10.1155/2014/435197 · Cited by 38 · see citing works

HAUSP as a therapeutic target for hematopoietic tumors (review)

Cheon, K., & Baek, K. (2006) · International Journal of Oncology · doi:10.3892/ijo.28.5.1209 · Cited by 37 · see citing works

Stabilization of Ultraviolet (UV)-stimulated Scaffold Protein A by Interaction with Ubiquitin-specific Peptidase 7 Is Essential for Transcription-coupled Nucleotide Excision Repair

Higa, M., Zhang, X., Tanaka, K., & Saijo, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.724658 · Cited by 37 · see citing works

The ubiquitin–proteasome pathway in thymocyte apoptosis: caspase-dependent processing of the deubiquitinating enzyme USP7 (HAUSP)

Vugmeyster, Y., Borodovsky, A., Maurice, M. M., Maehr, R., Furman, M. H., & Ploegh, H. L. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(02)00123-2 · Cited by 36 · see citing works

Daxx is reciprocally regulated by Mdm2 and Hausp

Tang, J., Qu, L., Pang, M., & Yang, X. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.051 · Cited by 34 · see citing works

Herpesvirus-associated Ubiquitin-specific Protease (HAUSP) Modulates Peroxisome Proliferator-activated Receptor γ (PPARγ) Stability through Its Deubiquitinating Activity

Lee, K. W., Cho, J. G., Kim, C. M., Kang, A. Y., Kim, M., Ahn, B. Y., Chung, S. S., Lim, K., Baek, K., Sung, J.-H., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.496331 · Cited by 33 · see citing works

HSCARG downregulates NF-κB signaling by interacting with USP7 and inhibiting NEMO ubiquitination

Li, T., Guan, J., Li, S.-Z., Zhang, X., & Zheng, X. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.197 · Cited by 32 · see citing works

Metformin Inhibits Esophagus Cancer Proliferation through Upregulation of USP7

Xu, Y., & Lu, S. Y. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000354517 · Cited by 32 · see citing works

HAUSP regulates c-MYC expression via de-ubiquitination of TRRAP

Bhattacharya, S., & Ghosh, M. K. (2015) · Cellular Oncology · doi:10.1007/s13402-015-0228-6 · Cited by 31 · see citing works

HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized

Lee, H., Kim, M., Kim, Y., Oh, Y., & Baek, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.07.048 · Cited by 30 · see citing works

MicroRNA-205 regulates ubiquitin specific peptidase 7 protein expression in hepatocellular carcinoma cells

Zhu, L. W., Liu, R., Zhang, W., Qian, S., & Wang, J. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3998 · Cited by 30 · see citing works

WDR79 promotes the proliferation of non-small cell lung cancer cells via USP7-mediated regulation of the Mdm2-p53 pathway

Sun, Y., Cao, L., Sheng, X., Chen, J., Zhou, Y., Yang, C., Deng, T., Ma, H., Feng, P., Liu, J., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.162 · Cited by 30 · see citing works

FoxO6 inhibits cell proliferation in lung carcinoma through up-regulation of USP7

HU, H.-J., Zhang, L., Wang, Z., & GUO, X.-X. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3362 · Cited by 28 · see citing works

Genome-wide association study of antibody level response to NDV and IBV in Jinghai yellow chicken based on SLAF-seq technology

Wang, W., Zhang, T., Zhang, G., Wang, J., Han, K., Wang, Y., & Zhang, Y. (2015) · Journal of Applied Genetics · doi:10.1007/s13353-014-0269-y · Cited by 27 · see citing works

The stability of epigenetic factor ASXL1 is regulated through ubiquitination and USP7-mediated deubiquitination

Inoue, D., Nishimura, K., Kozuka‐Hata, H., Oyama, M., & Kitamura, T. (2015) · Leukemia · doi:10.1038/leu.2015.90 · Cited by 26 · see citing works

Balancing Mdm2 — a Daxx–HAUSP matter

Ronai, Z. A. (2006) · Nature Cell Biology · doi:10.1038/ncb0806-790 · Cited by 25 · see citing works

Biological functions of hyaluronan and cytokine-inducible deubiquitinating enzymes

Ramakrishna, S., Suresh, B., & Baek, K. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.11.006 · Cited by 24 · see citing works

MBD4 Interacts With and Recruits USP7 to Heterochromatic Foci

Meng, H., Harrison, D. J., & Meehan, R. R. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25001 · Cited by 23 · see citing works

Ubiquitination/deubiquitination and acetylation/deacetylation: Making DNMT1 stability more coordinated

Qi, H., & Shao, Z. (2011) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.3 · Cited by 16 · see citing works

Does Wnt/β-catenin pathway contribute to the stability of DNMT1 expression in urological cancer cell lines?

Varol, N., Konaç, E., & Bilen, C. Y. (2014) · Experimental Biology and Medicine · doi:10.1177/1535370214556951 · Cited by 14 · see citing works

STIP is a critical nuclear scaffolding protein linking USP7 to p53-Mdm2 pathway regulation

Ye, M., Tang, Y.-N., Tang, S.-J., Liu, J., Wu, K., Yao, S., Sun, Y., Zhou, L. J., Deng, T., Chen, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5303 · Cited by 12 · see citing works

Assignment 1 of herpesvirus-associated ubiquitin-specific protease gene HAUSP to human chromosome band 16p13.3 by in situ hybridization

Robinson, P. A., Lomonte, P., Leek, J. P., Markham, A. F., & Everett, R. D. (1998) · Cytogenetic and Genome Research · doi:10.1159/000015142 · Cited by 7 · see citing works

The targetable role of herpes virus-associated ubiquitin-specific protease (HAUSP) in p190 BCR-ABL leukemia

Carrà, G., Panuzzo, C., Crivellaro, S., Morena, D., Taulli, R., Guerrasio, A., Saglio, G. N., & Morotti, A. (2016) · Oncology Letters · doi:10.3892/ol.2016.5073 · Cited by 5 · see citing works

Nek2 Stabilization By Usp7 Leads to Activation of NF-Kb in Multiple Myeloma

Franqui-Machin, R., Zhan, X., Xu, H., Frech, I., Tricot, G. J. K., & Zhan, F. (2016) · Blood · doi:10.1182/blood.v128.22.4418.4418 · Cited by 1 · see citing works

Targeting p53 pathways: mechanisms, structures, and advances in therapy

Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016 · see citing works

Ubiquitin–proteasome system (UPS) as a target for anticancer treatment

Park, J., Cho, J., & Song, E. J. (2020) · Archives of Pharmacal Research · doi:10.1007/s12272-020-01281-8 · Cited by 412 · see citing works

Mitochondrial quality control in cardiac microvascular ischemia-reperfusion injury: New insights into the mechanisms and therapeutic potentials

Wang, J., Toan, S., & Zhou, H. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104771 · Cited by 185 · see citing works

Advances in Discovering Deubiquitinating Enzyme (DUB) Inhibitors

Schauer, N. J., Magin, R. S., Liu, X., Doherty, L. M., & Buhrlage, S. J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01138 · Cited by 183 · see citing works

Targeting USP7-Mediated Deubiquitination of MDM2/MDMX-p53 Pathway for Cancer Therapy: Are We There Yet?

Qi, S., Cheng, G., Cheng, X., Xu, Z., Xu, B., Zhang, W., & Qin, J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00233 · Cited by 162 · see citing works

USP7 inhibits Wnt/β-catenin signaling through promoting stabilization of Axin

Ji, L., Lu, B., Zamponi, R., Charlat, O., Aversa, R. J., Yang, Z., Sigoillot, F. D., Zhu, X., Hu, T., Reece-Hoyes, J. S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12143-3 · Cited by 129 · see citing works

Targeting ubiquitin specific proteases (USPs) in cancer immunotherapy: from basic research to preclinical application

Gao, H., Yin, J., Ji, C., Yu, X., Xue, J., Guan, X., Zhang, S., Liu, X., & Xing, F. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02805-y · Cited by 129 · see citing works

Neuroinflammation inhibition by small-molecule targeting USP7 noncatalytic domain for neurodegenerative disease therapy

Zhang, X.-W., Feng, N., Liu, Y.-C., Guo, Q., Wang, J., Bai, Y.-Z., Ye, X., Yang, Z., Yang, H., Liu, Y., et al. (2022) · Science Advances · doi:10.1126/sciadv.abo0789 · Cited by 120 · see citing works

Merkel Cell Polyomavirus and Merkel Cell Carcinoma

Pietropaolo, V., Prezioso, C., & Moens, U. L. (2020) · Cancers · doi:10.3390/cancers12071774 · Cited by 116 · see citing works

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 · see citing works

m6A eraser FTO impairs gemcitabine resistance in pancreatic cancer through influencing NEDD4 mRNA stability by regulating the PTEN/PI3K/AKT pathway

Lin, K., Zhou, E., Shi, T., Zhang, S., Zhang, J., Zheng, Z., Pan, Y., Gao, W., & Yu, Y. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02792-0 · Cited by 91 · see citing works

Targeting the Ubiquitin–Proteasome System and Recent Advances in Cancer Therapy

Spano, D., & Catara, G. (2023) · Cells · doi:10.3390/cells13010029 · Cited by 85 · see citing works

Molecular Mechanisms of DUBs Regulation in Signaling and Disease

Li, Y., & Reverter, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22030986 · Cited by 82 · see citing works

Discovery of Potent, Selective, and Orally Bioavailable Inhibitors of USP7 with In Vivo Antitumor Activity

Leger, P. R., Hu, D. X., Biannic, B., Bui, M., Han, X., Karbarz, E., Maung, J., Okano, A., Osipov, M., Shibuya, G. M., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00245 · Cited by 77 · see citing works

USP7 deubiquitinates and stabilizes EZH2 in prostate cancer cells

Lee, J. E., Park, C. M., & Kim, J. H. (2020) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2019-0338 · Cited by 70 · see citing works

Inhibition of USP7 induces p53-independent tumor growth suppression in triple-negative breast cancers by destabilizing FOXM1

Yi, J., Li, H., Chu, B., Kon, N., Hu, X., Hu, J., Xiong, Y., Kanıskan, H. Ü., Jin, J. J., & Gu, W. J. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01180-7 · Cited by 69 · see citing works

USP7 deubiquitinates and stabilizes NOTCH1 in T-cell acute lymphoblastic leukemia

Shan, H., Li, X., Xiao, X., Dai, Y., Huang, J., Song, J., Liu, M., Yang, L., Lei, H., Tong, Y., et al. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-018-0028-3 · Cited by 66 · see citing works

Highlights in USP7 inhibitors for cancer treatment

Oliveira, R. I., Guedes, R. A., & Salvador, J. A. R. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.1005727 · Cited by 63 · see citing works

PTEN inhibition attenuates endothelial cell apoptosis in coronary heart disease via modulating the AMPK–CREB–Mfn2‐mitophagy signaling pathway

Li, P., Wang, J., Zhao, X., Ru, J., Tian, T., An, Y., Tang, L., & Bai, Y. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29366 · Cited by 58 · see citing works

Flap endonuclease 1 Facilitated Hepatocellular Carcinoma Progression by Enhancing USP7/MDM2-mediated P53 Inactivation

Bian, S., Ni, W., Zhu, M., Zhang, X., Qiang, Y., Zhang, J., Ni, Z., Shen, Y., Qiu, S., Song, Q., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.68179 · Cited by 57 · see citing works

Nuclear deubiquitination in the spotlight: the multifaceted nature of USP7 biology in disease

Rawat, R., Starczynowski, D. T., & Ntziachristos, P. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.02.008 · Cited by 53 · see citing works

EZH2 Regulates Protein Stability via Recruiting USP7 to Mediate Neuronal Gene Expression in Cancer Cells

Lei, A., Chen, L., Zhang, M., Yang, X., Xu, L., Cao, N., Zhang, Z., & Cao, Y. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00422 · Cited by 53 · see citing works

Recent advances on the intervention sites targeting USP7-MDM2-p53 in cancer therapy

Harakandi, C., Nininahazwe, L., Xu, H., Liu, B., He, C., Zheng, Y., & Zhang, H. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105273 · Cited by 52 · see citing works

The deubiquitinase USP7 uses a distinct ubiquitin-like domain to deubiquitinate NF-ĸB subunits

Mitxitorena, I., Somma, D., Mitchell, J. P., Lepistö, M., Tyrchan, C., Smith, E., Kiely, P. A., Walden, H., Keeshan, K., & Carmody, R. J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014113 · Cited by 51 · see citing works

USP7 as an emerging therapeutic target: A key regulator of protein homeostasis

Guo, N.-J., Wang, B., Zhang, Y., Kang, H., Nie, H., Feng, M.-K., Zhang, X.-Y., Zhao, L., Wang, N., Liu, H., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130309 · Cited by 50 · see citing works

CRISPR/Cas9 application in cancer therapy: a pioneering genome editing tool

Baghini, S. S., Gardanova, Z. R., Abadi, S. A. H., Zaman, B. A., İlhan, A., Shomali, N., Adili, A., Moghaddar, R., & Yaseri, A. F. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00336-6 · Cited by 46 · see citing works

Pharmacological inhibition of USP7 promotes antitumor immunity and contributes to colon cancer therapy

Fu, C., Zhu, X., Xu, P., & Li, Y. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s182806 · Cited by 45 · see citing works

Ubiquitin-specific protease 7 is a drug-able target that promotes hepatocellular carcinoma and chemoresistance

Zhang, W., Zhang, J., Xu, C., Zhang, S., Bian, S., Jiang, F., Ni, W., Qu, L., Lu, C., Ni, R., et al. (2020) · Cancer Cell International · doi:10.1186/s12935-020-1109-2 · Cited by 43 · see citing works

Targeting the USP7/RRM2 axis drives senescence and sensitizes melanoma cells to HDAC/LSD1 inhibitors

Granieri, L., Marocchi, F., Melixetian, M. B., Mohammadi, N., Nicoli, P., Cuomo, A., Bonaldi, T., Confalonieri, S., Pisati, F., Giardina, G., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111396 · Cited by 42 · see citing works

USP7 Inhibitors in Cancer Immunotherapy: Current Status and Perspective

Korenev, G., Yakukhnov, S., Druk, A., Golovina, A., Chasov, V. V., Mirgayazova, R., Ivanov, R. A., & Bulatov, E. (2022) · Cancers · doi:10.3390/cancers14225539 · Cited by 41 · see citing works

Inhibition of ubiquitin-specific protease 7 sensitizes acute myeloid leukemia to chemotherapy

Cartel, M., Mouchel, P., Gotanègre, M., David, L., Bertoli, S., Mas, V. M., Besson, A., Sarry, J., Manenti, S., & Didier, C. (2020) · Leukemia · doi:10.1038/s41375-020-0878-x · Cited by 41 · see citing works

Novel, Selective Inhibitors of USP7 Uncover Multiple Mechanisms of Antitumor Activity In Vitro and In Vivo

Ohol, Y. M., Sun, M. T., Cutler, G., Leger, P. R., Hu, D. X., Biannic, B., Rana, P., Cho, C., Jacobson, S., Wong, S., et al. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0184 · Cited by 41 · see citing works

USP7 targets XIAP for cancer progression: Establishment of a p53-independent therapeutic avenue for glioma

Saha, G., Sarkar, S., Mohanta, P. S., Kumar, K., Chakrabarti, S., Basu, M., & Ghosh, M. K. (2022) · Oncogene · doi:10.1038/s41388-022-02486-5 · Cited by 41 · see citing works

USP7 Induces Chemoresistance in Triple-Negative Breast Cancer via Deubiquitination and Stabilization of ABCB1

Lin, Y., Lin, J., Liu, Y.-E., Chen, Y.-C., Liu, S.-T., Hsu, K., Chen, D., & Wu, H.-T. (2022) · Cells · doi:10.3390/cells11203294 · Cited by 39 · see citing works

Reversal of viral and epigenetic HLA class I repression in Merkel cell carcinoma

Lee, P. C., Klaeger, S., Le, P. M., Korthauer, K. D., Cheng, J., Ananthapadmanabhan, V., Frost, T. C., Stevens, J. D., Wong, A. Y. L., Iorgulescu, J. B., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci151666 · Cited by 38 · see citing works

USP7-SOX9-miR-96-5p-NLRP3 Network Regulates Myocardial Injury and Cardiomyocyte Pyroptosis in Sepsis

Gong, X., Li, Y., He, Y., & Zhou, F. (2022) · Human Gene Therapy · doi:10.1089/hum.2022.078 · Cited by 38 · see citing works

Renal tubular cell death and inflammation response are regulated by the MAPK-ERK-CREB signaling pathway under hypoxia-reoxygenation injury

Dong, Q. R., Jie, Y., Ma, J., Li, C., Xin, T., & Yang, D. (2019) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2019.1698050 · Cited by 36 · see citing works

Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases

Gadhave, K., Kumar, P., Kapuganti, S. K., Uversky, V. N., & Giri, R. (2020) · Biomolecules · doi:10.3390/biom10050796 · Cited by 36 · see citing works

IU1 suppresses proliferation of cervical cancer cells through MDM2 degradation

Liu, X., Wang, J., Yuan, X., Yang, S., Xu, X., Li, K., He, Y., Wei, L., Zhang, J., & Tian, Y. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.47999 · Cited by 36 · see citing works

The USP7-TRIM27 axis mediates non-canonical PRC1.1 function and is a druggable target in leukemia

Maat, H., Atsma, T. J., Hogeling, S. M., López, A. R., Jaques, J., Olthuis, M., de Vries, M. P., Gravesteijn, C., Brouwers-Vos, A. Z., van der Meer, N. K., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102435 · Cited by 36 · see citing works

The tumour-promoting role of protein homeostasis: Implications for cancer immunotherapy

Liang, R., Tan, H., Jin, H., Wang, J., Tang, Z., & Lu, X. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216354 · Cited by 34 · see citing works

Role of deubiquitinases in DNA damage response

Le, J. P., Perez, E., Nemzow, L., & Gong, F. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.02.011 · Cited by 34 · see citing works

Deubiquitinase USP7 contributes to the pathogenicity of spinal and bulbar muscular atrophy

Pluciennik, A., Liu, Y., Molotsky, E., Marsh, G. B., Ranxhi, B., Arnold, F. J., St.-Cyr, S., Davidson, B. L., Pourshafie, N., Lieberman, A. P., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci134565 · Cited by 30 · see citing works

USP7 inhibits TIMP2 by up-regulating the expression of EZH2 to activate the NF-κB/PD-L1 axis to promote the development of cervical cancer

Li, N., Geng, F., Liang, S., & Qin, X. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110351 · Cited by 29 · see citing works

USP7 Inhibits Osteoclastogenesis via Dual Effects of Attenuating TRAF6/TAK1 Axis and Stimulating STING Signaling

Xie, Z., Wu, Y., Shen, Y., Guo, J., Yuan, P., Ma, Q., Wang, S., Jie, Z., Zhou, H., Fan, S., et al. (2023) · Aging and Disease · doi:10.14336/ad.2023.0325-1 · Cited by 28 · see citing works

Strategies that regulate LSD1 for novel therapeutics

Li, M., Dai, M., Cheng, B., Li, S., Guo, E., Fu, J., Ma, T., & Yu, B. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.01.005 · Cited by 27 · see citing works

Deubiquitinases: Pro-oncogenic Activity and Therapeutic Targeting in Blood Malignancies

Gutierrez-Diaz, B. T., Gu, W. J., & Ntziachristos, P. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.02.004 · Cited by 26 · see citing works

p53: from understanding its structure to advances in therapeutic targeting

Wang, W., Liu, X., Liu, H., Abolhassani, H., Yan, H., Zhang, H., & Wang, X. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02549-5 · Cited by 25 · see citing works

DUBs Activating the Hedgehog Signaling Pathway: A Promising Therapeutic Target in Cancer

Bufalieri, F., Severini, L. L., Caimano, M., Infante, P., & Marcotullio, L. D. (2020) · Cancers · doi:10.3390/cancers12061518 · Cited by 25 · see citing works

Assay Systems for Profiling Deubiquitinating Activity

Cho, J., Park, J., Kim, E. E., & Song, E. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165638 · Cited by 24 · see citing works

Mitochondria, mitophagy, and the role of deubiquitinases as novel therapeutic targets in liver pathology

Aryapour, E., & Kietzmann, T. (2022) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30312 · Cited by 24 · see citing works

USP7 substrates identified by proteomics analysis reveal the specificity of USP7Preprint

Nie, L., Wang, C., Liu, X., Teng, H., Li, S., Huang, M., Feng, X., Pei, G., Hang, Q., Zhao, Z., et al. (2022) · Genes & Development · doi:10.1101/gad.349848.122 · Cited by 24 · see citing works

USP7 represses lineage differentiation genes in mouse embryonic stem cells by both catalytic and noncatalytic activities

Liu, C., Sun, L., Tan, Y., Wang, Q. T., Luo, T., Li, C., Yao, N., Xie, Y., Yi, X., Zhu, Y., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade3888 · Cited by 23 · see citing works

USP7 imparts partial EMT state in colorectal cancer by stabilizing the RNA helicase DDX3X and augmenting Wnt/β-catenin signaling

Basu, B., Karmakar, S., Basu, M., & Ghosh, M. K. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119446 · Cited by 24 · see citing works

Ubiquitin-Specific Protease 7 (USP7) as a Promising Therapeutic Target for Drug Discovery: From Mechanisms to Therapies

Song, Y., Ren, X., Xiong, J., Wang, W., Zhao, Q., Chang, J., & Yu, B. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00102 · Cited by 22 · see citing works

Signaling Activation and Modulation in Extrafollicular B Cell Responses

Staniek, J., & Rizzi, M. (2025) · Immunological Reviews · doi:10.1111/imr.70004 · Cited by 21 · see citing works

The ubiquitin-proteasome system in the regulation of tumor dormancy and recurrence

Alhasan, B. A., Morozov, A. V., Guzhova, I. V., & Margulis, B. A. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189119 · Cited by 20 · see citing works

E3 ligases and DUBs target ferroptosis: A potential therapeutic strategy for neurodegenerative diseases

Lu, L., Jifu, C., Xia, J., & Wang, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116753 · Cited by 20 · see citing works

USP7 stabilizes EZH2 and enhances cancer malignant progression.

Zheng, N., Chu, M., Lin, M., He, Y., & Wang, Z. P. (2020) · PubMed Central · Cited by 20 · see citing works

USP7 deubiquitinates and stabilizes SIRT1.

Song, N., Cao, C., Tian, S., Long, M., & Liu, L. (2020) · The Anatomical Record · doi:10.1002/ar.24252 · Cited by 19 · see citing works

Ubiquitination and deubiquitination in the regulation of epithelial-mesenchymal transition in cancer: Shifting gears at the molecular level

Basu, B., & Ghosh, M. K. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119261 · Cited by 19 · see citing works

Role of the DUB enzyme USP7 in dendritic arborization, neuronal migration, and autistic-like behaviors in mice

Qiao, H., Tian, Y., Huo, Y., & Man, H. (2022) · iScience · doi:10.1016/j.isci.2022.104595 · Cited by 18 · see citing works

Programmed Death Ligand 1 Regulatory Crosstalk with Ubiquitination and Deubiquitination: Implications in Cancer Immunotherapy

Kim, S.-B., Hwang, S., Cha, J.-Y., & Lee, H.-J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052939 · Cited by 18 · see citing works

Cerebral ischemia‐reperfusion is modulated by macrophage‐stimulating 1 through the MAPK‐ERK signaling pathway

Zhou, D., Zhang, M., Min, L., Jiang, K., & Jiang, Y. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29603 · Cited by 18 · see citing works

A feedforward circuit shaped by ECT2 and USP7 contributes to breast carcinogenesis

Zhang, Q., Cao, C., Gong, W., Bao, K., Wang, Q., Wang, Y., Bi, L., Ma, S., Zhao, J., Liu, L., et al. (2020) · Theranostics · doi:10.7150/thno.46878 · Cited by 18 · see citing works

The key vulnerabilities and therapeutic opportunities in the USP7-p53/MDM2 axis in cancer

Saha, G., & Ghosh, M. K. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119908 · Cited by 17 · see citing works

Ubiquitin Ligases in Control: Regulating NLRP3 Inflammasome Activation

Beesetti, S. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl25970 · Cited by 17 · see citing works

LATS2 promotes cardiomyocyte H9C2 cells apoptosis via the Prx3-Mfn2-mitophagy pathways

Tian, Y., Lv, W., Lu, C., Zhao, X., Zhang, C., & Song, H. (2019) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2019.1701031 · Cited by 17 · see citing works

Deubiquitinases: Modulators of Different Types of Regulated Cell Death

Lee, C.-S., Kim, S., Hwang, G., & Song, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094352 · Cited by 17 · see citing works

Genetically encoded fluorescent unnatural amino acids and FRET probes for detecting deubiquitinase activities

Li, M., Wang, F., Yan, L., Lu, M., Zhang, Y., & Peng, T. (2022) · Chemical Communications · doi:10.1039/d2cc03623a · Cited by 17 · see citing works

Redox‐Induced Stabilization of AMBRA1 by USP7 Promotes Intestinal Oxidative Stress and Colitis Through Antagonizing DUB3‐Mediated NRF2 Deubiquitination

Xu, W., Hua, Z., Wang, Y., Tang, W., Ge, W., Chen, Y., Wang, Z., Gu, Y., Liu, C., & Du, P. (2025) · Advanced Science · doi:10.1002/advs.202411320 · Cited by 16 · see citing works

Novel modulators of p53-signaling encoded by unknown genes of emerging viruses

Alzhanova, D. V., Corcoran, K., Bailey, A., Long, K. M., Taft-Benz, S., Graham, R. L., Broussard, G. S., Heise, M. T., Neumann, G., Halfmann, P., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009033 · Cited by 16 · see citing works

Deubiquitylation and stabilization of ARMC5 by ubiquitin‐specific processing protease 7 (USP7) are critical for RCC proliferation

Yan, G., Liu, N., Tian, J., Fu, Y., Wei, W., Zou, J., Li, S., Wang, Q., Li, K., & Wang, J. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16306 · Cited by 16 · see citing works

USP7 promotes PINK1/Parkin-dependent mitophagy to ameliorate cerebral ischemia–reperfusion injury by deubiquitinating and stabilizing SIRT1

Hou, D., Hu, Y., Tian, Y., Yu, D., & Yang, G. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149638 · Cited by 15 · see citing works

AML with complex karyotype: extreme genomic complexity revealed by combined long-read sequencing and Hi-C technology

Klever, M.-K., Sträng, E., Hetzel, S., Jungnitsch, J., Dolnik, A., Schöpflin, R., Schrezenmeier, J., Schick, F., Blau, O., Westermann, J., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2023010887 · Cited by 15 · see citing works

Role of melatonin in mitigation of insulin resistance and ensuing diabetic cardiomyopathy

Nath, A., Ghosh, S., & Bandyopadhyay, D. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122993 · Cited by 15 · see citing works

MKP1 reduces neuroinflammation via inhibiting endoplasmic reticulum stress and mitochondrial dysfunction

Huang, D., & Jiang, Y. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29308 · Cited by 15 · see citing works

PE_PGRS38 Interaction With HAUSP Downregulates Antimycobacterial Host Defense via TRAF6

Kim, J., Kim, H. K., Cho, E., Mun, S., Jang, S., Jang, J., & Yang, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.862628 · Cited by 14 · see citing works

Melatonin receptor protects cardiomyocyte against oxidative stress-induced apoptosis through the MAPK-ERK signaling pathway

Li, P., Hu, F., Cao, X., Luo, L., & Tu, Q. (2020) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2020.1719151 · Cited by 14 · see citing works

WD repeat-containing protein 1 maintains β-Catenin activity to promote pancreatic cancer aggressiveness

Li, H., Liu, X., Jiang, S., Zhou, X., Yao, L., Yang, D., Jiang, Y., Gu, J., Mao, Y., Li, J., et al. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-0929-0 · Cited by 14 · see citing works

Prognostic role of USP7 expression in cancer patients: A systematic review and meta-analysis

Kisaï, K., & Koji, S. (2021) · Pathology - Research and Practice · doi:10.1016/j.prp.2021.153621 · Cited by 14 · see citing works

USP7 Inhibition Suppresses Neuroblastoma Growth via Induction of p53-Mediated Apoptosis and EZH2 and N-Myc Downregulation

Clorennec, C. L., Lee, K. S., Huo, Y., & Zage, P. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813780 · Cited by 14 · see citing works

Gene analysis of major signaling pathways regulated by gonadotropins in human ovarian granulosa tumor cells (KGN)†

Tremblay, P. G., & Sirard, M. (2020) · Biology of Reproduction · doi:10.1093/biolre/ioaa079 · Cited by 14 · see citing works

Deubiquitinating Enzyme USP7 Is Required for Self-Renewal and Multipotency of Human Bone Marrow-Derived Mesenchymal Stromal Cells

Kim, Y. J., Park, K. H., Lee, K., Chun, Y., & Lee, J. W. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158674 · Cited by 13 · see citing works

BK Channel Deficiency in Osteoblasts Reduces Bone Formation via the Wnt/β-Catenin Pathway

Jiang, L., Yang, Q., Jianjun, G., Yang, J., He, J., Xin, H., & Zhang, X. (2021) · Molecules and Cells · doi:10.14348/molcells.2021.0004 · Cited by 12 · see citing works

Design, synthesis and biological evaluation of 2-aminopyridine derivatives as USP7 inhibitors

Xu, X., Wang, M., Xu, H., Liu, N., Chen, K., Luo, C., Chen, S., & Chen, H. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106128 · Cited by 12 · see citing works

Liraglutide reduces hyperglycemia-induced cardiomyocyte death through activating glucagon-like peptide 1 receptor and targeting AMPK pathway

Ma, G., Liu, Y., Wang, Y., Wen, Z., Li, X., Zhai, H., Li, M., & Luo, J. (2020) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2020.1719517 · Cited by 12 · see citing works

The roles of ribosomal proteins in nasopharyngeal cancer: culprits, sentinels or both

Sim, E. U., Lee, C. W., & Narayanan, K. (2021) · Biomarker Research · doi:10.1186/s40364-021-00311-x · Cited by 12 · see citing works

The prognostic value of USP7 and p53 in advanced hypopharyngeal carcinoma

Sun, J., Lin, L., Zhang, J., Hu, C., & Wang, J. (2021) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2020.151695 · Cited by 11 · see citing works

EVC-EVC2 complex stability and ciliary targeting are regulated by modification with ubiquitin and SUMO

Barbeito, P., Martin-Morales, R., Palencia‐Campos, A., Cerrolaza, J., Rivas-Santos, C., Gallego-Colastra, L., Caparros-Martin, J. A., Martin-Bravo, C., Martín-Hurtado, A., Sánchez-Bellver, L., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1190258 · Cited by 10 · see citing works

USP7 reduces the level of nuclear DICER , impairing DNA damage response and promoting cancer progression

Liu, X., Lu, R., Yang, Q., He, J., Huang, C., Cao, Y., Zhou, Z., Huang, J., Li, L., Chen, R., et al. (2023) · Molecular Oncology · doi:10.1002/1878-0261.13543 · Cited by 10 · see citing works

Ubiquitin‐specific peptidase 7 (USP7) and USP10 mediate deubiquitination of human NHE3 regulating its expression and activity

Han, Y., & Yun, C. C. (2020) · The FASEB Journal · doi:10.1096/fj.202001875r · Cited by 10 · see citing works

IKZF1 selectively enhances homologous recombination repair by interacting with CtIP and USP7 in multiple myeloma

Liu, M., Zhang, Y., Wu, Y., Jin, J., Cao, Y., Fang, Z., Geng, L., Yang, L., Yu, M., Bu, Z., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.70960 · Cited by 10 · see citing works

In vivo CRISPR screens identify Mga as an immunotherapy target in triple-negative breast cancer

Xu, F., Yang, C. Q., Huang, Y., Su, D., Wang, C., Wilson, L., Yin, L., Tang, M., Li, S., Chen, Z., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2406325121 · Cited by 9 · see citing works

Involvement of USP7 in aggravating Kawasaki disease by promoting TGFβ2 signaling mediated endothelial-mesenchymal transition and coronary artery remodeling

Qian, G., Wang, Y., Yao, H., Zhang, Z.-M., Wang, W., Xu, L., Li, W., Huang, L., Li, X., Gao, Y., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113823 · Cited by 9 · see citing works

Ubiquitin-specific proteases as therapeutic targets in paediatric primary bone tumours?

Mullard, M., Lavaud, M., Regnier, L., Tesfaye, R. A., Ory, B., Rédiní, F., & Verrecchia, F. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114797 · Cited by 9 · see citing works

NURR1 inhibition reduces hypoxia-mediated cardiomyocyte necrosis via blocking Mst1-JNK-mPTP pathway

Ma, G., & Liu, Y. (2019) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2019.1690514 · Cited by 9 · see citing works

Yes-associated protein reduces neuroinflammation through upregulation of Sirt3 and inhibition of JNK signaling pathway

Yang, Y., Gong, Z., & Wang, Z. (2019) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2019.1705339 · Cited by 9 · see citing works

Comprehensive analysis of the relationship between ubiquitin-specific protease 21 (USP21) and prognosis, tumor microenvironment infiltration, and therapy response in colorectal cancer

Nie, H., Yu, Y., Wang, F., Huang, X., Wang, H., Wang, J., Tao, M., Ning, Y., Zhou, J., Zhao, Q., et al. (2024) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-024-03731-4 · Cited by 8 · see citing works

USP7 regulates growth and maintains the stemness of p53-mutant colorectal cancer cells via stabilizing of mutant p53

Li, X., Pan, J., & Zheng, P. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1427663 · Cited by 8 · see citing works

HAUSP

(2011) · Springer eBooks · doi:10.1007/978-3-642-16483-5_2574

Herpesvirus-associated ubiquitin-specific protease in tumor

Ren, Y. (2009) · Guoji zhongliuxue zazhi · doi:10.3760/cma.j.issn.1673-422x.2009.06.005

Herpesvirus-Associated Ubiquitin-Specific Protease De-ubiquitinase

Brooks, C. L., & Gu, W. J. (2011) · Springer eBooks · doi:10.1007/978-3-642-16483-5_2690

Targeting HAUSP: Killing Two Birds with One Stone

Brooks, C. L., & Gu, W. J. (2009) · Springer eBooks · doi:10.1007/978-0-387-69147-3_3

Modulation of the p53/MDM2 interplay by HAUSP inhibitors

Tavana, O., & Gu, W. J. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw049 · Cited by 108 · see citing works