Roles of HAUSP-mediated p53 regulation in central nervous system development

Surfing the p53 network

Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works

Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours

Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649 · see citing works

Blinded by the Light: The Growing Complexity of p53

Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163 · see citing works

p53 in health and disease

Vousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,275 · see citing works

Tumor spectrum analysis in p53-mutant mice

Jacks, T., Remington, L., Williams, B. O., Schmitt, E. M., Halachmi, S., Bronson, R. T., & Weinberg, R. A. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00002-6 · Cited by 2,051 · see citing works

Disruption of the glucocorticoid receptor gene in the nervous system results in reduced anxiety

Tronche, F., Kellendonk, C., Kretz, O., Gass, P., Anlag, K., Orban, P. C., Bock, R., Klein, R., & Schütz, G. (1999) · Nature Genetics · doi:10.1038/12703 · Cited by 1,841 · see citing works

Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53

de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · cited 1× · see citing works

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 1× · 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

A Highly Efficient Recombineering-Based Method for Generating Conditional Knockout MutationsPreprint

Liu, P., Jenkins, N. A., & Copeland, N. G. (2003) · Genome Research · doi:10.1101/gr.749203 · Cited by 1,013 · see citing works

p53 ubiquitination: Mdm2 and beyond

Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924 · see citing works

Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation

Leng, R. P., Lin, Y., Ma, W., Wu, H., Lemmers, B., Chung, S., Parant, J. M., Lozano, G., Hakem, R., & Benchimol, S. (2003) · Cell · doi:10.1016/s0092-8674(03)00193-4 · Cited by 717 · see citing works

Neural stem and progenitor cells in nestin‐GFP transgenic mice

Mignone, J., Kukekov, V. G., Chiang, A., Steindler, D. A., & Enikolopov, G. (2004) · The Journal of Comparative Neurology · doi:10.1002/cne.10964 · Cited by 705 · see citing works

The ubiquitin ligase COP1 is a critical negative regulator of p53

Dornan, D., Wertz, I. E., Shimizu, H., Arnott, D. P., Frantz, G. D., Dowd, P., Rourke, K. O., Koeppen, H., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02514 · Cited by 700 · 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

A subset of p53-deficient embryos exhibit exencephaly

Sah, V. P., Attardi, L. D., Mulligan, G., Williams, B. O., Bronson, R. T., & Jacks, T. (1995) · Nature Genetics · doi:10.1038/ng0695-175 · Cited by 579 · 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

ARF-BP1/Mule Is a Critical Mediator of the ARF Tumor Suppressor

Chen, D., Kon, N., Li, M., Zhang, W., Qin, J., & Gu, W. J. (2005) · Cell · doi:10.1016/j.cell.2005.03.037 · Cited by 539 · see citing works

Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53

Parant, J., Chavez-Reyes, A., Little, N. A., Yan, W., Reinke, V., Jochemsen, A. G., & Lozano, G. (2001) · Nature Genetics · doi:10.1038/ng714 · Cited by 517 · 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

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

Stress Signals Utilize Multiple Pathways To Stabilize p53

Ashcroft, M. A., Taya, Y., & Vousden, K. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.3224-3233.2000 · Cited by 356 · see citing works

Keeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4

Marine, J.-C., Francoz, S., Maetens, M., Wahl, G., Toledo, F., & Lozano, G. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401912 · Cited by 352 · see citing works

Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells <i>in vivo</i>

Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260 · see citing works

Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.

Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260 · see citing works

GMP Synthetase Stimulates Histone H2B Deubiquitylation by the Epigenetic Silencer USP7

van der Knaap, J. A., Kumar, B. R. P., Moshkin, Y. M., Langenberg, K. P. S., Krijgsveld, J., Heck, A. J. R., Karch, F., & Verrijzer, C. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.013 · Cited by 258 · see citing works

Structural Basis of Competitive Recognition of p53 and MDM2 by HAUSP/USP7: Implications for the Regulation of the p53–MDM2 Pathway

Hu, M., Gu, L., Li, M., Jeffrey, P. D., Gu, W., & Shi, Y. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040027 · Cited by 251 · see citing works

Critical role for Daxx in regulating Mdm2

Tang, J., Qu, L., Zhang, J., Wang, W., Michaelson, J. S., Degenhardt, Y., El‐Deiry, W. S., & Yang, X. (2006) · Nature Cell Biology · doi:10.1038/ncb1442 · Cited by 239 · see citing works

Phosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage

Pereg, Y., Shkedy, D., de Graaf, P., Meulmeester, E., Edelson-Averbukh, M., Salek, M., Biton, S., Teunisse, A. F. A. S., Lehmann, W. D., Jochemsen, A. G., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408595102 · Cited by 181 · 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

ATM-Mediated Phosphorylations Inhibit Mdmx/Mdm2 Stabilization by HAUSP in Favor of p53 Activation

Meulmeester, E., Pereg, Y., Shiloh, Y., & Jochemsen, A. G. (2005) · Cell Cycle · doi:10.4161/cc.4.9.1981 · Cited by 166 · see citing works

Synergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development

Xiong, S., Van Pelt, C. S., Elizondo-Fraire, A. C., Liu, G., & Lozano, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508500103 · 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

Deletion of DDB1 in Mouse Brain and Lens Leads to p53-Dependent Elimination of Proliferating Cells

Cang, Y., Zhang, J., Nicholas, S. A., Bastien, J., Li, B., Zhou, P., & Goff, S. P. (2006) · Cell · doi:10.1016/j.cell.2006.09.045 · Cited by 151 · see citing works

The loss of mdm2 induces p53 mediated apoptosis

de Rozìeres, S., Maya, R. B.-Y., Oren, M., & Lozano, G. (2000) · Oncogene · doi:10.1038/sj.onc.1203468 · Cited by 144 · see citing works

A New Twist in the Feedback Loop: Stress-Activated MDM2 Destabilization is Required for p53 Activation

Stommel, J. M., & Wahl, G. M. (2005) · Cell Cycle · doi:10.4161/cc.4.3.1522 · Cited by 87 · see citing works

Increased Radioresistance and Accelerated B Cell Lymphomas in Mice with Mdmx Mutations that Prevent Modifications by DNA-Damage-Activated Kinases

Wang, Y. V., Leblanc, M., Wade, M., Jochemsen, A. G., & Wahl, G. M. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.05.008 · Cited by 79 · see citing works

The Role of Ubiquitination in the Direct Mitochondrial Death Program of p53

Marchenko, N. D., & Moll, U. M. (2007) · Cell Cycle · doi:10.4161/cc.6.14.4503 · Cited by 73 · see citing works

USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product.

Hong, S.-H., Kim, S.-J., Ka, S., Choi, I., & Kang, S. (2002) · Molecular and cellular neurosciences · doi:10.1006/mcne.2002.1103 · Cited by 71 · see citing works

Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo

Wahl, G. M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401911 · Cited by 37 · 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

Dissecting Roles of Ubiquitination in the p53 Pathway

Shan, J., Brooks, C. L., Kon, N., Li, M., & Gu, W. J. (2008) · Ernst Schering Research Foundation workshop/Ernst Schering Foundation Symposium proceedings · doi:10.1007/2789_2008_105 · Cited by 15 · see citing works

Senescence and aging: the critical roles of p53

Rufini, A., Tucci, P., Celardo, I., & Melino, G. (2013) · Oncogene · doi:10.1038/onc.2012.640 · Cited by 798 · 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

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449 · see citing works

Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death

Vucic, D., Dixit, V. M., & Wertz, I. E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3143 · Cited by 451 · see citing works

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 422 · 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

HAUSP deubiquitinates and stabilizes N-Myc in neuroblastoma

Tavana, O., Li, D., Dai, C., López, G., Banerjee, D., Kon, N., Chen, C., Califano, A., Yamashiro, D. J., Sun, H., et al. (2016) · Nature Medicine · doi:10.1038/nm.4180 · Cited by 202 · see citing works

p53 regulation by ubiquitin

Brooks, C. L., & Gu, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.022 · Cited by 186 · see citing works

USP7: Structure, substrate specificity, and inhibition

Pozhidaeva, A., & Bezsonova, I. (2019) · DNA Repair · doi:10.1016/j.dnarep.2019.02.005 · Cited by 178 · see citing works

Limiting the power of p53 through the ubiquitin proteasome pathwayPreprint

Pant, V., & Lozano, G. (2014) · Genes & Development · doi:10.1101/gad.247452.114 · Cited by 165 · see citing works

Mechanisms of p53 degradation

Chao, C. C. ‐. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.08.015 · Cited by 152 · see citing works

Balancing act: deubiquitinating enzymes in the nervous system

Todi, S. V., & Paulson, H. L. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.05.004 · Cited by 141 · see citing works

USP7 inhibitor P5091 inhibits Wnt signaling and colorectal tumor growth

An, T., Gong, Y., Li, X., Kong, L., Ma, P., Gong, L., Zhu, H., Yu, C., Liu, J., Zhou, H., et al. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.02.011 · Cited by 137 · see citing works

Nucleotide Biosynthetic Enzyme GMP Synthase Is a TRIM21-Controlled Relay of p53 Stabilization

Reddy, B. A., van der Knaap, J. A., Bot, A. G. M., Mohd-Sarip, A., Dekkers, D. H. W., Timmermans, M. A. M., Martens, J. W. M., Demmers, J., & Verrijzer, C. P. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.017 · Cited by 131 · see citing works

Ubiquitin-specific Protease-7 Inhibition Impairs Tip60-dependent Foxp3 + T-regulatory Cell Function and Promotes Antitumor Immunity

Wang, L., Kumar, S., Dahiya, S., Wang, F., Wu, J., Newick, K., Han, R., Samanta, A., Beier, U. H., Akimova, T., et al. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.10.018 · Cited by 121 · 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

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

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

A RUNX2 stabilization pathway mediates physiologic and pathologic bone formation

Kim, J., Yang, Y.-S., Park, K. H., Ge, X., Xu, R., Li, N., Song, M., Chun, H., Bok, S., Charles, J. F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16038-6 · Cited by 96 · see citing works

USP7 Cooperates with NOTCH1 to Drive the Oncogenic Transcriptional Program in T-Cell Leukemia

Jin, Q., Martinez, C. A., Arcipowski, K. M., Zhu, Y., Gutierrez-Diaz, B. T., Wang, K. K., Johnson, M. R., Volk, A. G., Wang, F., Wu, J., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-1740 · Cited by 95 · see citing works

The emerging nature of Ubiquitin-specific protease 7 (USP7): a new target in cancer therapy

Nininahazwe, L., Liu, B., He, C., Zhang, H., & Chen, Z. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.10.028 · Cited by 92 · see citing works

An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes

Ristic, G., Tsou, W., & Todi, S. V. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00072 · Cited by 86 · see citing works

A complex of the ubiquitin ligase TRIM32 and the deubiquitinase USP7 balances the level of c-Myc ubiquitination and thereby determines neural stem cell fate specification

Nicklas, S., Hillje, A., Okawa, S., Rudolph, I., Collmann, F. M., van Wuellen, T., del Sol, A., & Schwamborn, J. C. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0144-1 · Cited by 84 · see citing works

Pathogenic variants in USP7 cause a neurodevelopmental disorder with speech delays, altered behavior, and neurologic anomalies.

Fountain, M. D., Oleson, D. S., Rech, M. E., Segebrecht, L., Hunter, J. V., McCarthy, J. M., Lupo, P. J., Holtgrewe, M., Moran, R., Rosenfeld, J. A., et al. (2019) · Genetics in Medicine · doi:10.1038/s41436-019-0433-1 · Cited by 80 · see citing works

The Mdm network and its regulation of p53 activities: a rheostat of cancer risk

Eischen, C. M., & Lozano, G. (2014) · Human Mutation · doi:10.1002/humu.22524 · Cited by 79 · see citing works

Functional analysis of deubiquitylating enzymes in tumorigenesis and development

Cheng, J., Guo, J., North, B. J., Wang, B., Cui, C., Li, H., Tao, K., Zhang, L., & Wei, W. (2019) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2019.188312 · Cited by 74 · 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

The role of UBL domains in ubiquitin-specific proteases

Faesen, A. C., Luna‐Vargas, M. P. A., & Sixma, T. K. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120004 · Cited by 66 · 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 role of ubiquitination in health and disease

Liao, Y., Zhang, W., Liu, Y., Zhu, C., & Zou, Z. (2024) · MedComm · doi:10.1002/mco2.736 · Cited by 67 · see citing works

USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

Lecona, E., Narendra, V. K., & Reinberg, D. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01197-14 · Cited by 59 · see citing works

USP7 is a novel deubiquitinase sustaining PLK1 protein stability and regulating chromosome alignment in mitosis.

Peng, Y., Liu, Y., Gao, Y., Yuan, B., Qi, X., Fu, Y., Zhu, Q., Cao, T., Zhang, S., Yin, L., et al. (2019) · Journal of Experimental &amp; Clinical Cancer Research · doi:10.1186/s13046-019-1457-8 · Cited by 54 · 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

Structurally-defined deubiquitinase inhibitors provide opportunities to investigate disease mechanisms

Wertz, I. E., & Murray, J. M. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.02.003 · Cited by 48 · see citing works

Targeting ubiquitination in disease and therapy

Yang, X., Lan, T., Zhang, B., Tao, X., Qi, W., Xie, K., Cai, Y., Liu, C., Han, J., & Wu, H. M. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02392-8 · Cited by 53 · see citing works

Chemical Approaches to Intervening in Ubiquitin Specific Protease 7 (USP7) Function for Oncology and Immune Oncology Therapies

Wu, J., Kumar, S., Wang, F., Wang, H., Chen, L., Arsenault, P., Mattern, M. R., & Weinstock, J. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00498 · Cited by 45 · see citing works

Deubiquitinases in Neurodegeneration

Bello, A. I., Goswami, R., Brown, S. L., Costanzo, K. M., Shores, T., Allan, S. K., Odah, R., & Mohan, R. D. (2022) · Cells · doi:10.3390/cells11030556 · Cited by 40 · see citing works

USP7 limits CDK1 activity throughout the cell cycle

Galarreta, A., Valledor, P., Ubieto‐Capella, P., Lafarga, V., Zarzuela, E., Muñoz, J., Malumbres, M., Lecona, E., & Fernández-Capetillo, Ó. (2021) · The EMBO Journal · doi:10.15252/embj.201899692 · Cited by 37 · see citing works

Deubiquitylase USP7 regulates human terminal erythroid differentiation by stabilizing GATA1

Liang, L., Peng, Y., Zhang, J., Zhang, Y., Roy, M., Han, X., Xiao, X., Sun, S., Liu, H., Nie, L., et al. (2019) · Haematologica · doi:10.3324/haematol.2018.206227 · Cited by 37 · see citing works

The DUB Club: Deubiquitinating Enzymes and Neurodevelopmental Disorders

Jolly, L. A., Kumar, R., Penzes, P., Piper, M., & Gécz, J. (2022) · Biological Psychiatry · doi:10.1016/j.biopsych.2022.03.022 · Cited by 35 · see citing works

Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders.

Das, S., Ramakrishna, S., & Kim, K.-S. (2020) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2020.2289 · Cited by 33 · see citing works

Tissue-specific expression of p73 C-terminal isoforms in mice

Grespi, F., Amelio, I., Tucci, P., Annicchiarico‐Petruzzelli, M., & Melino, G. (2012) · Cell Cycle · doi:10.4161/cc.22787 · Cited by 29 · see citing works

FOXL2 interaction with different binding partners regulates the dynamics of ovarian development

Migale, R., Neumann, M., Mitter, R., Rafiee, M., Wood, S., Olsen, J., & Lovell-Badge, R. H. (2024) · Science Advances · doi:10.1126/sciadv.adl0788 · Cited by 26 · 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

Deubiquitinases in cell death and inflammation

Newton, K., & Gitlin, A. D. (2022) · Biochemical Journal · doi:10.1042/bcj20210735 · Cited by 25 · see citing works

Brain patterning perturbations following PTEN loss

Veleva-Rotse, B. O., & Barnes, A. P. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00035 · Cited by 22 · see citing works

Independent functions of DNMT1 and USP7 at replication foci

Yarychkivska, O., Tavana, O., Gu, W. J., & Bestor, T. H. (2018) · Epigenetics & Chromatin · doi:10.1186/s13072-018-0179-z · Cited by 22 · see citing works

USP7 inactivation suppresses APC-mutant intestinal hyperproliferation and tumor development

Novellasdemunt, L., Kucharska, A., Baulies, A., Hutton, C., Vlachogiannis, G., Repana, D., Rowan, A., Suárez‐Bonnet, A., Ciccarelli, F. D., Valeri, N., et al. (2023) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.12.013 · Cited by 19 · see citing works

USP7 controls NGN3 stability and pancreatic endocrine lineage development

Manea, T., Nelson, J. K., Garrone, C. M., Hansson, K., Evans, I. M., Behrens, A., & Sancho, R. (2023) · Nature Communications · doi:10.1038/s41467-023-38146-9 · Cited by 19 · see citing works

From Flies to Mice: The Emerging Role of Non-Canonical PRC1 Members in Mammalian Development

Bajusz, I., Kovács, G. E., & Pirity, M. K. (2018) · Epigenomes · doi:10.3390/epigenomes2010004 · Cited by 19 · see citing works

Targeting HAUSP in both p53 wildtype and p53-mutant tumors

Tavana, O., Sun, H., & Gu, W. J. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1456293 · 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

Therapeutic targeting of ubiquitin-specific protease 7 (USP7): Mechanistic insights, dysregulation, and advances in drug discovery

El-Hamaky, A. A., El‐Hamamsy, M. H., El-Moselhy, T. F., Sharafeldin, N., & Tawfik, H. O. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117872 · Cited by 17 · see citing works

Oncogenic deubiquitination controls tyrosine kinase signaling and therapy response in acute lymphoblastic leukemia

Jin, Q., Gutierrez-Diaz, B. T., Pieters, T., Zhou, Y., Narang, S., Fijałkowski, I., Borin, C., Laere, J. V., Payton, M. A., Cho, B.-K., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq8437 · Cited by 16 · see citing works

HAUSP promoted the growth of glioma cells in vitro and in vivo via stabilizing NANOG

Cheng, C., Dong, Y., Niu, W., & Niu, C. (2020) · Pathology - Research and Practice · doi:10.1016/j.prp.2020.152883 · Cited by 13 · see citing works

Deubiquitinase USP7 regulates Drosophila aging through ubiquitination and autophagy

Cui, L., Song, W., Zeng, Y. Y., Wu, Q., Fan, Z., Huang, T., Zeng, B., Zhang, M., Ni, Q., Li, Y., et al. (2020) · Aging · doi:10.18632/aging.104067 · Cited by 12 · see citing works

The Hao-Fountain syndrome protein USP7 regulates neuronal connectivity in the brain via a novel p53-independent ubiquitin signaling pathway

Chen, H., Ferguson, C., Mitchell, D. C., Risch, I., Titus, A., Paulo, J. A., Hwang, A., Beck, L. P., Lin, T., Gu, W. J., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115231 · Cited by 11 · see citing works

Ubiquitin‐specific protease 7 ( USP 7) is essential for endometrial stromal cell decidualization in mice

Gao, Y., Wang, Y., Zhou, C., Kong, S., Lu, J., Wang, H., & Yang, J. (2019) · Development Growth & Differentiation · doi:10.1111/dgd.12594 · Cited by 10 · see citing works

Small-molecule allosteric activator of ubiquitin-specific protease 7 (USP7)

Maisonet, I. J., Sharafi, M., Korchak, E. J., Salazar‐Chaparro, A. F., Bratt, A. S., Parikh, T., Varca, A. C., Shah, B., Darnowski, M. G., Chung, M., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2510496122 · Cited by 6 · see citing works

Understanding the Interactions of Ubiquitin-Specific Protease 7 with Its Substrates through Molecular Dynamics Simulations: Insights into the Role of Its C-Terminal Domains in Substrate Recognition

Velázquez‐Libera, J. L., Caballero, J., Alzate‐Morales, J. H., Ruiz‐Pernía, J. J., & Tuñón, I. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01971 · Cited by 6 · see citing works

Hao-Fountain syndrome protein USP7 controls neuronal differentiation via BCOR–ncPRC1.1Preprint

van der Meer, J. W., Larue, A., van der Knaap, J. A., Chalkley, G. E., Sijm, A., Beikmohammadi, L., Kozhevnikova, E. N., van der Vaart, A., Tilly, B. C., Bezstarosti, K., et al. (2025) · Genes & Development · doi:10.1101/gad.352272.124 · Cited by 6 · see citing works

Insights into the Structural and Energetic Descriptions of Ubiquitin Specific Protease 7 (USP7) Catalytic Mechanisms by Hybrid QM/MM Simulations.

Velázquez‐Libera, J. L., Caballero, J., Alzate‐Morales, J. H., Ruiz‐Pernía, J. J., & Tuñón, I. (2023) · ChemCatChem · doi:10.1002/cctc.202300344 · Cited by 5 · see citing works

Malva sylvestris Flower Extract Exhibits Antineoplastic Potential Against Human Colon Cancer Cell Lines and Induces CDK2 Transcript Instability via Plant miR160-5p

Villani, V., & Gismondi, A. (2026) · Nutrients · doi:10.3390/nu18030495 · Cited by 3 · see citing works

Should Deubiquitinating Enzymes be Targeted for Therapy?

Todi, S. V. (2012) · Clinical Pharmacology & Biopharmaceutics · doi:10.4172/2167-065x.1000e108 · Cited by 3 · see citing works

Organ defects of the Usp7 mutant mouse strain indicate the essential role of K63-polyubiquitinated Usp7 in organ formation

Wu, H., Lin, Y., Chew, S. H., & Wu, K. (2022) · Biomedical Journal · doi:10.1016/j.bj.2022.02.002 · Cited by 3 · see citing works

Molecular signatures in Mendelian neurodevelopment: a focus on ubiquitination driven DNA methylation aberrations

van der Laan, L., ten Voorde, N., Mannens, M. M. A. M., & Henneman, P. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1446686 · Cited by 3 · see citing works

Deubiquitinating Enzymes in Model Systems and Therapy: Redundancy and Compensation Have Implications

Zachariah, S., & Gray, D. A. (2019) · BioEssays · doi:10.1002/bies.201900112 · Cited by 3 · see citing works

HAUSP Stabilizes SOX2 through Deubiquitination to Maintain Self-renewal and Tumorigenic Potential of Glioma Stem CellsPreprint

Huang, Z., Zhai, K., Wu, Q., Fang, X., Huang, Q., Tao, W., Lathia, J. D., Yu, J. S., Rich, J. N., & Bao, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.09.447550 · Cited by 3 · see citing works

Usp7 Regulates Glial Lineage Cell-Specific Transcription Factors by Modulating Histone H2B Monoubiquitination

Kim, D.-H., Kim, S. L., Singh, V., & Ramakrishna, S. (2024) · International Journal of Stem Cells · doi:10.15283/ijsc23202 · Cited by 2 · see citing works

S18-phosphorylation of USP7 regulates interaction with TCEAL4 that defines specific complexes and potentially distinct functionsPreprint

Querques, F., Darling, S., Cheetham‐Wilkinson, I. J., Kim, R. Q., Hapangama, D. K., Sixma, T. K., & Coulson, J. M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.07.451439 · Cited by 2 · see citing works

USP15 mutation associated with autism spectrum disorder alters progenitor fate and neuronal maturation in human brain organoids

Park, T. S., Koh, I. G., Sung, S., Park, H., Kim, J., Lee, S., Lee, J. Y., Ko, H., Han, J. H., Bong, G., et al. (2026) · Molecules and Cells · doi:10.1016/j.mocell.2026.100387 · Cited by 1 · see citing works

Generation and analyses of mouse models for USP18 and USP15 via gene targeting

Hannß, R. (2012) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-14193

Natural Genetic Variation Underlying UVR Sensitivity in Drosophila melanogaster

Chana, K. (2015) · Leicester Research Archive (University of Leicester)

The role of PATZ1 transcription factor in the DNA damage response

Deniz, E. (2014) · Sabanci University

p53 and Aging

Dogra, N., & Mukhopadhyay, T. (2020) · Springer eBooks · doi:10.1007/978-981-32-9005-1_5

Expression of Tp53 and USP7 during development of lungs in mouse model.

Mughal, A., Hu, M., Amjad, Z., Parveen, K., & Mustansar, T. (2020) · INTERNATIONAL JOURNAL OF ENDORSING HEALTH SCIENCE RESEARCH (IJEHSR) · doi:10.29052/ijehsr.v8.i4.2020.173-179

Conditional deletion of MDM2 in neurons impairs neuronal homeostasis and cognitive ability

Jin, Y., Cui, H., Kang, J., Chen, W., Zhang, C., Zhang, C., Han, Y., & Meng, X. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.05.003

Proteome-wide Ubiquitinome Profiling Reveals Substrate-specific Dynamics Within the USP7 Network

van der Meer, J. W., van der Knaap, J. A., Sijm, A., Bezstarosti, K., Dekkers, D. H. W., Doff, W. A. S., Demmers, J., & Verrijzer, C. P. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101602

USP7 maintains hematopoietic stem cell dormancy and function by stabilizing HMGA2Preprint

Nouhaud, A., Anna, D., Bouttier, M., Rigaud, Q., Enfedaque, P., Somaï, H., Hébrard, S., Prade, N., Dufrechou, S., Musiani, D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.03.731117

BindingDB Entry 50001159: Chemical Approaches to Intervening in Ubiquitin Specific Protease 7 (USP7) Function for Oncology and Immune Oncology Therapies.

BindingDB (2020) · UC San Diego · doi:10.7270/q2cr5wvg

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

HAUSP is Required for p53 Destabilization

Cummins, J. M., & Vogelstein, B. (2004) · Cell Cycle · doi:10.4161/cc.3.6.924 · Cited by 188 · see citing works

Expression and functional analyses of mHAUSP regulating apoptosis of cervical adenocarcinoma cells

Yoo, K., Lee, H.-J., Lee, H., Lee, K.-Y., Lee, S., Chung, H., & Baek, K. (2005) · International Journal of Oncology · doi:10.3892/ijo.27.1.97 · Cited by 12 · 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

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