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

A marker for Stevens–Johnson syndrome

Chung, W., Chung, W., Hong, H., Hsih, M., Yang, L., Ho, H., Wu, J., & Chen, Y.-T. (2004) · Nature · doi:10.1038/428486a · Cited by 1,748 · 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

Purification of a RAS -Responsive Adenylyl Cyclase Complex from Saccharomyces cerevisiae by Use of an Epitope Addition Method

Field, J. M., Nikawa, J., Broek, D., MACDONALD, B. S., Rodgers, L., Wilson, I. A., Lerner, R. A., & Wigler, M. H. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.5.2159 · Cited by 949 · see citing works

Mechanisms of action of arsenic trioxide.

Miller, W. H., Schipper, H. M., Lee, J. S., Singer, J. W., & Waxman, S. (2002) · PubMed · Cited by 939 · 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

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

Tatham, M. H., Geoffroy, M., Shen, L., Plechanovová, A., Hattersley, N., Jaffray, E., Palvimo, J. J., & Hay, R. T. (2008) · Nature Cell Biology · doi:10.1038/ncb1716 · Cited by 837 · see citing works

Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1

Ishov, A. M., Sotnikov, A. G., Negorev, D. G., Vladimirova, O. V., Neff, N. F., Kamitani, T., Yeh, E. T. H., Strauss, J. F., & Maul, G. G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.221 · Cited by 825 · see citing works

Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2

Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804 · cited 1× · see citing works

TRIM family proteins: retroviral restriction and antiviral defence

Nisole, S., Stoye, J. P., & Saïb, A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1248 · Cited by 761 · see citing works

Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway

Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Pérès, L., Zhou, J., Zhu, J., Raught, B., & de Thé, H. (2008) · Nature Cell Biology · doi:10.1038/ncb1717 · Cited by 726 · 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

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

PML protein isoforms and the RBCC/TRIM motif

Jensen, K., Shiels, C., & Freemont, P. S. (2001) · Oncogene · doi:10.1038/sj.onc.1204765 · Cited by 465 · see citing works

UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity

Malakhova, O. A., Kim, K. I. I., Luo, J.-K., Zou, W., Kumar, K. G., Fuchs, S. Y., Shuai, K., & Zhang, D. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601149 · Cited by 430 · see citing works

The Disruption of ND10 during Herpes Simplex Virus Infection Correlates with the Vmw110- and Proteasome-Dependent Loss of Several PML Isoforms

Everett, R. D., Freemont, P. S., Saitoh, H., Dasso, M., Orr, A., Kathoria, M., & Parkinson, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.8.6581-6591.1998 · Cited by 399 · 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

Structure of the p53 Binding Domain of HAUSP/USP7 Bound to Epstein-Barr Nuclear Antigen 1

Saridakis, V., Sheng, Y., Sarkari, F., Holowaty, M. N., Shire, K., Nguyen, T., Zhang, R. G., Liao, J. C. C., Lee, W., Edwards, A. M., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.029 · Cited by 362 · see citing works

HSV‐1 IE protein Vmw110 causes redistribution of PML.

Everett, R. D., & Maul, G. G. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06835.x · Cited by 352 · see citing works

Loss of the Tumor Suppressor PML in Human Cancers of Multiple Histologic Origins

Gurrieri, C., Capodieci, P., Bernardi, R., Scaglioni, P. P., Nafa, K., Rush, L. J., Verbel, D., Cordon‐Cardo, C., & Pandolfi, P. P. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh043 · Cited by 331 · see citing works

PML Contributes to a Cellular Mechanism of Repression of Herpes Simplex Virus Type 1 Infection That Is Inactivated by ICP0

Everett, R. D., Rechter, S., Papior, P., Tavalai, N., Stamminger, T., & Orr, A. (2006) · Journal of Virology · doi:10.1128/jvi.00734-06 · Cited by 323 · see citing works

Molecular recognition of p53 and MDM2 by USP7/HAUSP.

Sheng, Y., Saridakis, V., Sarkari, F., Duan, S., Wu, T., Arrowsmith, C. H., & Frappier, L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1067 · Cited by 315 · see citing works

PML Is a Direct p53 Target that Modulates p53 Effector Functions

de Stanchina, E., Querido, E., Narita, M., Davuluri, R. V., Pandolfi, P. P., Ferbeyre, G., & Lowe, S. W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00062-0 · Cited by 312 · see citing works

A CK2-Dependent Mechanism for Degradation of the PML Tumor Suppressor

Scaglioni, P. P., Yung, T. M., Cai, L. F., Erdjument‐Bromage, H., Kaufman, A., Singh, B., Teruya‐Feldstein, J., Tempst, P., & Pandolfi, P. P. (2006) · Cell · doi:10.1016/j.cell.2006.05.041 · Cited by 293 · see citing works

The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0

Maul, G. G., & Everett, R. D. (1994) · Journal of General Virology · doi:10.1099/0022-1317-75-6-1223 · Cited by 279 · 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

Characterization of a Family of Nucleolar SUMO-specific Proteases with Preference for SUMO-2 or SUMO-3

Gong, L., & Yeh, E. T. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511658200 · Cited by 245 · see citing works

The PML growth-suppressor has an altered expression in human oncogenesis.

Koken, M. H. M., Linares‐Cruz, G., Quignon, F., Viron, A., Chelbi‐Alix, M. K., Sobczak‐Thépot, J., Juhlin, L., Degos, L., Calvo, F. M., & de Thé, H. (1995) · PubMed · Cited by 231 · see citing works

Protein Profiling with Epstein-Barr Nuclear Antigen-1 Reveals an Interaction with the Herpesvirus-associated Ubiquitin-specific Protease HAUSP/USP7

Holowaty, M. N., Zeghouf, M., Wu, H., Tellam, J., Athanasopoulos, V., Greenblatt, J., & Frappier, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303977200 · Cited by 228 · 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

Isolation of Mammalian 26S Proteasomes and p97/VCP Complexes Using the Ubiquitin-like Domain from HHR23B Reveals Novel Proteasome-Associated Proteins

Besche, H. C., Haas, W., Gygi, S. P., & Goldberg, A. L. (2009) · Biochemistry · doi:10.1021/bi802198q · Cited by 183 · 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

Alphaherpesvirus Proteins Related to Herpes Simplex Virus Type 1 ICP0 Affect Cellular Structures and Proteins

Parkinson, J., & Everett, R. D. (2000) · Journal of Virology · doi:10.1128/jvi.74.21.10006-10017.2000 · Cited by 170 · see citing works

Characterization of Endogenous Human Promyelocytic Leukemia Isoforms

Condemine, W., Takahashi, Y., Zhu, J., Puvion-Dutilleul, F., Guégan, S., Janin, A., & de Thé, H. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3792 · 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

An infrequent point mutation of the p53 gene in human nasopharyngeal carcinoma.

Sun, Y., Hegamyer, G. A., Cheng, Y. J., Hildesheim, A., Chen, J. Y., Chen, I.-H., Cao, Y., Yao, K., & Colburn, N. H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.14.6516 · Cited by 143 · see citing works

A RING Finger Ubiquitin Ligase Is Protected from Autocatalyzed Ubiquitination and Degradation by Binding to Ubiquitin-specific Protease USP7

Canning, M., Boutell, C., Parkinson, J., & Everett, R. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402885200 · Cited by 142 · 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

EBNA1-Mediated Recruitment of a Histone H2B Deubiquitylating Complex to the Epstein-Barr Virus Latent Origin of DNA Replication

Sarkari, F., Sanchez-Alcaraz, T., Wang, S., Holowaty, M. N., Sheng, Y., & Frappier, L. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000624 · Cited by 115 · see citing works

PML Residue Lysine 160 Is Required for the Degradation of PML Induced by Herpes Simplex Virus Type 1 Regulatory Protein ICP0

Boutell, C., Orr, A., & Everett, R. D. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8686-8694.2003 · Cited by 107 · see citing works

Arsenic trioxide stimulates SUMO‐2/3 modification leading to RNF4‐dependent proteolytic targeting of PML

Weisshaar, S. R., Keusekotten, K., Krause, A., Horst, C., Springer, H. M., Göttsche, K., Dohmen, R. J., & Praefcke, G. J. K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.08.008 · Cited by 105 · see citing works

PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication

Cuchet, D., Sykes, A., Nicolas, A., Orr, A., Murray, J., Sirma, H., Heeren, J., Bartelt, A., & Everett, R. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075390 · Cited by 105 · see citing works

New insights into the role of PML in tumour suppression

Salomoni, P., Ferguson, B. J., Wyllie, A., & Rich, T. (2008) · Cell Research · doi:10.1038/cr.2008.58 · Cited by 104 · see citing works

Epstein-Barr Virus Nuclear Antigen 1 Hijacks the Host Kinase CK2 To Disrupt PML Nuclear Bodies

Sivachandran, N., Cao, J. Y., & Frappier, L. (2010) · Journal of Virology · doi:10.1128/jvi.01183-10 · Cited by 100 · see citing works

The Ubiquitin E3 Ligase MARCH7 is Differentially Regulated by the Deubiquitylating Enzymes USP7 and USP9X

Nathan, J. A., Sengupta, S., Wood, S. A., Admon, A., Markson, G., Sanderson, C. M., & Lehner, P. J. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00747.x · Cited by 97 · see citing works

Herpes Simplex Virus Type 1 Immediate-Early Protein Vmw110 Binds Strongly and Specifically to a 135-kDa Cellular Protein

Meredith, M., Orr, A., & Everett, R. D. (1994) · Virology · doi:10.1006/viro.1994.1209 · Cited by 85 · see citing works

Separation of Sequence Requirements for HSV-1 Vmw110 Multimerisation and Interaction with a 135-kDa Cellular Protein

Meredith, M., Orr, A., Elliott, M., & Everett, R. D. (1995) · Virology · doi:10.1006/viro.1995.1241 · Cited by 84 · see citing works

Heterogeneous nuclear expression of the promyelocytic leukemia (PML) protein in normal and neoplastic human tissues.

Gambacorta, M., Flenghi, L., Fagioli, M., Pileri, S. A., Leoncini, L., Bigerna, B., Pacini, R., Tanci, L. N., Pasqualucci, L., Ascani, S., et al. (1996) · Europe PMC (PubMed Central) · Cited by 80 · see citing works

SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies

Häkli, M., Karvonen, U., Jänne, O., & Palvimo, J. J. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.10.029 · Cited by 74 · see citing works

Affinity Purification Strategy to Capture Human Endogenous Proteasome Complexes Diversity and to Identify Proteasome-interacting Proteins

Bousquet, M., Baudelet, É., Guèrin, F., Matondo, M., Uttenweiler‐Joseph, S., Burlet‐Schiltz, O., & Monsarrat, B. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800193-mcp200 · Cited by 68 · see citing works

The Deubiquitinating Enzyme USP11 Controls an IκB Kinase α (IKKα)-p53 Signaling Pathway in Response to Tumor Necrosis Factor α (TNFα)

Yamaguchi, T., Kimura, J., Miki, Y., & Yoshida, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706282200 · Cited by 64 · see citing works

Nucleosome Assembly Proteins Bind to Epstein-Barr Virus Nuclear Antigen 1 and Affect Its Functions in DNA Replication and Transcriptional Activation

Wang, S., & Frappier, L. (2009) · Journal of Virology · doi:10.1128/jvi.00931-09 · Cited by 53 · see citing works

Targeting Promyelocytic Leukemia Protein: A Means to Regulating PML Nuclear Bodies

Reineke, E. L., & Kao, H. (2009) · International Journal of Biological Sciences · doi:10.7150/ijbs.5.366 · Cited by 47 · see citing works

STAT-1- and IRF-3-Dependent Pathways Are Not Essential for Repression of ICP0-Null Mutant Herpes Simplex Virus Type 1 in Human Fibroblasts

Everett, R. D., Young, D. F., Randall, R. E., & Orr, A. (2008) · Journal of Virology · doi:10.1128/jvi.00613-08 · Cited by 42 · see citing works

The IL-6 family of cytokines modulates STAT3 activation by desumoylation of PML through SENP1 induction

Ohbayashi, N., Kawakami, S., Muromoto, R., Togi, S., Ikeda, O., Kamitani, S., Sekine, Y., Honjoh, T., & Matsuda, T. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.04.179 · Cited by 24 · see citing works

Identification of a novel higher molecular weight isoform of USP7/HAUSP that interacts with the Herpes simplex virus type-1 immediate early protein ICP0

Antrobus, R., & Boutell, C. (2008) · Virus Research · doi:10.1016/j.virusres.2008.05.017 · Cited by 15 · 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

CK2 and PML: Regulating the Regulator

Lallemand-Breitenbach, V., & de Thé, H. (2006) · Cell · doi:10.1016/j.cell.2006.07.004 · Cited by 11 · see citing works

Epstein–Barr virus latent genes

Kang, M.-S., & Kieff, E. D. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.84 · Cited by 359 · see citing works

Differential Roles of PML Isoforms

Nisole, S., Maroui, M. A., Mascle, X. H., Aubry, M., & Chelbi‐Alix, M. K. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00125 · Cited by 168 · see citing works

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

Bhattacharya, S., Chakraborty, D., Basu, M., & Ghosh, M. K. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-018-0012-y · Cited by 162 · see citing works

Contributions of Epstein–Barr Nuclear Antigen 1 (EBNA1) to Cell Immortalization and Survival

Frappier, L. (2012) · Viruses · doi:10.3390/v4091537 · Cited by 127 · see citing works

Functions of the Epstein-Barr Virus EBNA1 Protein in Viral Reactivation and Lytic Infection

Sivachandran, N., Wang, X., & Frappier, L. (2012) · Journal of Virology · doi:10.1128/jvi.00013-12 · Cited by 124 · 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

USP7 - a crucial regulator of cancer hallmarks

Saha, G., Roy, S., Basu, M., & Ghosh, M. K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188903 · Cited by 106 · see citing works

The Epstein-Barr Virus EBNA1 Protein

Frappier, L. (2012) · Scientifica · doi:10.6064/2012/438204 · Cited by 97 · see citing works

Contributions of the Epstein-Barr Virus EBNA1 Protein to Gastric Carcinoma

Sivachandran, N., Dawson, W. O., Young, L. S., Liu, F., Middeldorp, J. M., & Frappier, L. (2011) · Journal of Virology · doi:10.1128/jvi.05623-11 · Cited by 95 · see citing works

The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein

Guan, D., Factor, D. C., Liu, Y., Wang, Z., & Kao, H.-Y. (2012) · Oncogene · doi:10.1038/onc.2012.406 · Cited by 90 · see citing works

EBNA1

Frappier, L. (2015) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-22834-1_1 · Cited by 78 · 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

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

Identification and Characterization of USP7 Targets in Cancer Cells

Georges, A. A., Marcon, E., Greenblatt, J. F., & Frappier, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-34197-x · Cited by 63 · see citing works

Gene expression control by protein deubiquitinases

Frappier, L., & Verrijzer, C. P. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.02.005 · Cited by 58 · see citing works

Epigenetic regulation of EBV and KSHV latency

Chen, H.-S., Lu, F. Y., & Lieberman, P. M. (2013) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.03.004 · Cited by 57 · see citing works

TSPYL5 depletion induces specific death of ALT cells through USP7-dependent proteasomal degradation of POT1.

Episkopou, H., Diman, A., Claude, E., Viceconte, N., & Decottignies, A. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.05.027 · Cited by 55 · see citing works

Concerted SUMO-targeted ubiquitin ligase activities of TOPORS and RNF4 are essential for stress management and cell proliferation

Liu, J. C. Y., Ackermann, L., Hoffmann, S., Gál, Z., Hendriks, I. A., Jain, C., Morlot, L., Tatham, M. H., McLelland, G., Hay, R. T., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01294-7 · Cited by 54 · see citing works

USP7 deubiquitinase controls HIV-1 production by stabilizing Tat protein

Ali, A., Raja, R., Farooqui, S. R., Ahmad, S., & Banerjea, A. C. (2017) · Biochemical Journal · doi:10.1042/bcj20160304 · Cited by 54 · see citing works

African swine fever virus replication events and cell nucleus: New insights and perspectives

Simões, M., Freitas, F. B., Leitão, A., Martins, C. L. V., & Ferreira, F. (2019) · Virus Research · doi:10.1016/j.virusres.2019.197667 · Cited by 53 · see citing works

Contribution of the C-terminal Regions of Promyelocytic Leukemia Protein (PML) Isoforms II and V to PML Nuclear Body Formation

Geng, Y., Monajembashi, S., Shao, A., Cui, D., He, W., Chen, Z., Hemmerich, P. H., & Tang, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374769 · Cited by 49 · 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

Identification of Herpesvirus Proteins That Contribute to G 1 /S Arrest

Paladino, P., Marcon, E., Greenblatt, J. F., & Frappier, L. (2014) · Journal of Virology · doi:10.1128/jvi.00059-14 · Cited by 48 · see citing works

Ubiquitin-specific Protease 7 Is a Regulator of Ubiquitin-conjugating Enzyme UbE2E1

Sarkari, F., Wheaton, K., Delfa, A. L., Mohamed, M., Shaikh, F., Khatun, R., Arrowsmith, C. H., Frappier, L., Saridakis, V., & Sheng, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.469262 · 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

Chromatin Structure of Epstein–Barr Virus Latent Episomes

Lieberman, P. M. (2015) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-22822-8_5 · Cited by 47 · see citing works

Alterations of Nuclear Architecture and Epigenetic Signatures during African Swine Fever Virus Infection

Simões, M., Rino, J., Pinheiro, I., Martins, C. L. V., & Ferreira, F. (2015) · Viruses · doi:10.3390/v7092858 · Cited by 43 · see citing works

A Survey of the Interactome of Kaposi's Sarcoma-Associated Herpesvirus ORF45 Revealed Its Binding to Viral ORF33 and Cellular USP7, Resulting in Stabilization of ORF33 That Is Required for Production of Progeny Viruses

Gillen, J., Li, W., Liang, Q., Avey, D. R., Wu, J., Wu, F., Myoung, J., & Zhu, F. (2015) · Journal of Virology · doi:10.1128/jvi.02925-14 · Cited by 39 · see citing works

USP7 Regulates Cytokinesis through FBXO38 and KIF20B

Georges, A. A., Coyaud, É., Marcon, E., Greenblatt, J. F., Raught, B., & Frappier, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-39368-y · Cited by 38 · see citing works

USP7 manipulation by viral proteins

Bojagora, A., & Saridakis, V. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198076 · Cited by 33 · see citing works

Targeting Deubiquitinating Enzymes in Glioblastoma Multiforme: Expectations and Challenges

Jin, W., Mao, X., & Qiu, G. (2016) · Medicinal Research Reviews · doi:10.1002/med.21421 · Cited by 32 · see citing works

Human Herpesvirus 8 Interferon Regulatory Factors 1 and 3 Mediate Replication and Latency Activities via Interactions with USP7 Deubiquitinase

Xiang, Q., Ju, H., Li, Q., Mei, S.-C., Chen, D., Choi, Y. B., & Nicholas, J. (2018) · Journal of Virology · doi:10.1128/jvi.02003-17 · Cited by 31 · 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

USP7/HAUSP Promotes the Sequence-Specific DNA Binding Activity of p53

Sarkari, F., Sheng, Y., & Frappier, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013040 · Cited by 30 · see citing works

Incoming human papillomavirus 16 genome is lost in PML protein-deficient HaCaT keratinocytes

Bienkowska‐Haba, M., Łuszczek, W., Keiffer, T. R., Guion, L. G. M., DiGiuseppe, S., Scott, R. S., & Sapp, M. J. (2016) · Cellular Microbiology · doi:10.1111/cmi.12708 · Cited by 27 · see citing works

Identification of RNF168 as a PML nuclear body regulator

Shire, K., Wong, A. I., Tatham, M. H., Anderson, O. F., Ripsman, D., Gulstene, S., Moffat, J., Hay, R. T., & Frappier, L. (2015) · Journal of Cell Science · doi:10.1242/jcs.176446 · Cited by 22 · see citing works

Overexpression of the Ubiquitin-Specific Protease 7 Resulting from Transfection or Mutations in the ICP0 Binding Site Accelerates Rather than Depresses Herpes Simplex Virus 1 Gene Expression

Kalamvoki, M., Gu, H., & Roizman, B. (2012) · Journal of Virology · doi:10.1128/jvi.01981-12 · Cited by 17 · see citing works

The PML hub: An emerging actor of leukemia therapies

Rérolle, D., & de Thé, H. (2023) · The Journal of Experimental Medicine · doi:10.1084/jem.20221213 · Cited by 16 · see citing works

HAUSP stabilizes Cdc25A and protects cervical cancer cells from DNA damage response

Das, S., Chandrasekaran, A. P., Jo, K.-S., Ko, N. R., Oh, S. J., Kim, K.-S., & Ramakrishna, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118835 · Cited by 16 · see citing works

Epstein-Barr Virus and the Pathogenesis of Nasopharyngeal Carcinomas

Gourzonès, C., Busson, P., & Raab‐Traub, N. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5947-7_4 · Cited by 15 · see citing works

USP8 promotes intracellular infection by enhancing ESCRT-mediated membrane repair, limiting xenophagy, and reducing oxidative stress

Chandra, P., & Philips, J. A. (2024) · Autophagy · doi:10.1080/15548627.2024.2395134 · Cited by 13 · 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

Potential clinical treatment prospects behind the molecular mechanism of alternative lengthening of telomeres (ALT)

Sun, H., Chen, G., Guo, B., Lv, S., & Yuan, G. (2023) · Journal of Cancer · doi:10.7150/jca.80097 · Cited by 11 · see citing works

A Role for the Nucleosome Assembly Proteins TAF-Iβ and NAP1 in the Activation of BZLF1 Expression and Epstein-Barr Virus Reactivation

Mansouri, S., Wang, S., & Frappier, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063802 · 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

EBNA1

Frappier, L. (2025) · Current topics in microbiology and immunology · doi:10.1007/82_2025_299 · Cited by 5 · see citing works

Manipulation of PML Nuclear Bodies and DNA Damage Responses by DNA Viruses

Frappier, L. (2016) · Springer eBooks · doi:10.1007/978-3-319-38882-3_13 · Cited by 4 · see citing works

Rotavirus NSP1 localizes in the nucleus to disrupt PML nuclear bodies during infectionPreprint

Murphy, S. K., & Arnold, M. M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/619932 · Cited by 4 · see citing works

USP7 at PML Nuclear Bodies: A Protein Interaction Network Perspective

Silonov, S. A., Ведешкина, Е., Mokin, Y. I., Sukailo, D. A., Smirnov, E. Y., Reushev, V. A., Константинович, Т. К., Константинович, Т. К., & Fonin, A. V. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27094106 · Cited by 1 · see citing works

TRIM27 in HSV-1 Infection: A Story of Loss and Death

Conwell, S. E. (2015) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)

Cellular Effects of EBNA1

Frappier, L. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6886-8_5

Identifikation nukleärer und subnukleärer Lokalisationssignale in der humanen Inositol-1,3,4,5,6-pentakisphosphat 2-Kinase (IP5K)

Kobras, M. (2012)

Rhesus rhadinovirus vIRF R12 disrupts the PML-nuclear body via proteasome-dependent protein degradation pathway

Gao, L. (2015) · OHSU Digital Commons · doi:10.6083/m44q7s0g

Structural Insight into the Mechanisms of Activation and Substrate Specificity of Human Deubiquitinating Enzyme USP7

Pozhidaeva, A. (2016) · OpenCommons at University of Connecticut (University of Connecticut)

Mechanisms of Regulation of Promyelocytic Leukemia (PML) Proteins by Epstein-Barr Nuclear Antigen 1 (EBNA1) and Ubiquitin Specific Protease 7 (USP7)

Landry, C. H. (2013) · TSpace (University of Toronto)

USP22 controls tumorigenicity by regulating interferon responses and the stability of the tumor suppressor PML

Kowald, L. (2022) · doi:10.21248/gups.73710

Identification of new regulators for PML nuclear bodies

Snollaerts, T. (2016) · theses.fr (ABES) · doi:10.70675/a97a0132zae2fz4278zad92z5e4b56df97b2

A study on the role of PML in acute myeloid leukemia response to chemotherapy

Rérolle, D. (2024) · theses.fr (ABES) · doi:10.70675/b8e14224z7fb4z48a1zbe13zbd80a1788e94

USP7 at PML Nuclear Bodies: A Protein Interaction Network Perspective

Silonov, S. A., Ведешкина, Е., Mokin, Y. I., Sukailo, D. A., Smirnov, E. Y., Reushev, V. A., Константинович, Т. К., Константинович, Т. К., & Fonin, A. V. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27094106 · Cited by 1 · see citing works

Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins

Chelbi‐Alix, M. K., & de Thé, H. (1999) · Oncogene · doi:10.1038/sj.onc.1202366 · Cited by 331 · see citing works

The Disruption of ND10 during Herpes Simplex Virus Infection Correlates with the Vmw110- and Proteasome-Dependent Loss of Several PML Isoforms

Everett, R. D., Freemont, P. S., Saitoh, H., Dasso, M., Orr, A., Kathoria, M., & Parkinson, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.8.6581-6591.1998 · Cited by 399 · see citing works

Ubiquitin-dependent Degradation of p73 Is Inhibited by PML

Bernassola, F., Salomoni, P., Oberst, A., Como, C. J. D., Pagano, M., Melino, G., & Pandolfi, P. P. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20031943 · Cited by 118 · see citing works

Promyelocytic Leukemia-Nuclear Body Proteins: Herpesvirus Enemies, Accomplices, or Both?

Saffert, R. T., & Kalejta, R. F. (2008) · Future Virology · doi:10.2217/17460794.3.3.265 · Cited by 44 · see citing works