A dynamic role of HAUSP in the p53-Mdm2 pathway

TGF-β SIGNAL TRANSDUCTION

Massagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571 · see citing works

Surfing the p53 network

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

Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951 · see citing works

Tumor Suppression at the Mouse INK4a Locus Mediated by the Alternative Reading Frame Product p19

Kamijo, T., Zindy, F., Roussel, M. F., Quelle, D. E., Downing, J. R., Ashmun, R. A., Grosveld, G., & Sherr, C. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80452-3 · Cited by 1,566 · 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 · 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 · see citing works

The alternative product from the human CDKN2A locus, p14ARF, participates in a regulatory feedback loop with p53 and MDM2

Stott, F. J., Bates, S., James, M. C., McConnell, B. B., Starborg, M., Brookes, S., Palmero, I., Ryan, K. M., Hara, E., Vousden, K. H., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5001 · Cited by 1,165 · see citing works

Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins

Hicke, L., & Dunn, R. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.110701.154617 · Cited by 1,106 · see citing works

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

The INK4a/ARF network in tumour suppression

Sherr, C. J. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096061 · Cited by 984 · 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 · see citing works

Human papillomavirus immortalization and transformation functions

Münger, K., & Howley, P. M. (2002) · Virus Research · doi:10.1016/s0168-1702(02)00190-9 · Cited by 768 · see citing works

The p53–Mdm2 module and the ubiquitin system

Michael, D., & Oren, M. (2002) · Seminars in Cancer Biology · doi:10.1016/s1044-579x(02)00099-8 · Cited by 759 · see citing works

Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation

Brooks, C. L., & Gu, W. J. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00003-6 · Cited by 742 · see citing works

Tumor suppression by Ink4a-Arf: progress and puzzles.

Lowe, S. W., & Sherr, C. J. (2003) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00013-8 · Cited by 699 · 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

Functions of the MDM2 oncoprotein

Freedman, D. A., Wu, L., & Levine, A. J. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050273 · Cited by 573 · 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

Regulation of p53 stability

Ashcroft, M. A., & Vousden, K. H. (1999) · Oncogene · doi:10.1038/sj.onc.1203012 · Cited by 407 · see citing works

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53

Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361 · see citing works

An epi-allelic series of p53 hypomorphs created by stable RNAi produces distinct tumor phenotypes in vivo

Hemann, M. T., Fridman, J. S., Zilfou, J. T., Hernando, E., Paddison, P. J., Cordon‐Cardo, C., Hannon, G. J., & Lowe, S. W. (2003) · Nature Genetics · doi:10.1038/ng1091 · Cited by 354 · see citing works

Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development

Migliorini, D., Denchi, E. L., Danovi, D., Jochemsen, A., Capillo, M., Gobbi, A., Helin, K., Pelicci, P. G., & Marine, J.-C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5527-5538.2002 · Cited by 313 · see citing works

Deubiquitinating Enzymes: A New Class of Biological Regulators

D’Andrea, A. D., & Pellman, D. S. (1998) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409239891204251 · Cited by 272 · see citing works

Mutual Dependence of MDM2 and MDMX in Their Functional Inactivation of p53

Gu, J., Kawai, H., Nie, L., Kitao, H., Wiederschain, D., Jochemsen, A. G., Parant, J. M., Lozano, G., & Yuan, Z.-M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200150200 · Cited by 265 · see citing works

Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms

Stad, R., Little, N. A., Xirodimas, D. P., Frenk, R., van der Eb, A. J., Lane, D. P., Saville, M. K., & Jochemsen, A. G. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve227 · Cited by 234 · 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

Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells

Hengstermann, A., Linares, L. K., Ciechanover, A. J., Whitaker, N. J., & Scheffner, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1218 · Cited by 212 · see citing works

mdmx is a negative regulator of p53 activity in vivo.

Finch, R. A., Donoviel, D. B., Potter, D., Shi, M., Fan, A., Freed, D. D., Wang, C.-Y., Zambrowicz, B., Ramírez‐Solis, R., Sands, A., et al. (2002) · PubMed · Cited by 192 · 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

Control of p53 ubiquitination and nuclear export by MDM2 and ARF.

Zhang, Y., & Xiong, Y. (2001) · PubMed · Cited by 176 · see citing works

Aspirin, ubiquitin and cancer

Wilkinson, K. D. (2003) · Nature · doi:10.1038/424738a · Cited by 52 · see citing works

Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of p53 ubiquitination

Lim, S.-K., Shin, J. A., Kim, Y., & Baek, K. (2004) · International Journal of Oncology · doi:10.3892/ijo.24.2.357 · Cited by 30 · see citing works

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679 · see citing works

A genomic and functional inventory of deubiquitinating enzymes.

Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854 · see citing works

Modes of p53 regulation.

Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610 · see citing works

Post-translational modification of p53 in tumorigenesis

Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · 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

The complexity of p53 stabilization and activation

Lavin, M. F., & Gueven, N. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401925 · Cited by 701 · see citing works

USP10 Regulates p53 Localization and Stability by Deubiquitinating p53

Yuan, J., Luo, K., Zhang, L., Cheville, J. C., & Lou, Z. (2010) · Cell · doi:10.1016/j.cell.2009.12.032 · Cited by 637 · 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

Coping with stress: multiple ways to activate p53

Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522 · 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

The p53 orchestra: Mdm2 and Mdmx set the tone

Wade, M., Wang, Y. V., & Wahl, G. M. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.009 · Cited by 450 · 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

p53 modifications: exquisite decorations of the powerful guardian

Liu, Y., Tavana, O., & Gu, W. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz060 · Cited by 392 · 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

Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation

Feng, J., Tamaskovic, R., Yang, Z., Brazil, D. P., Merlo, A., Hess, D., & Hemmings, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404936200 · Cited by 294 · 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

The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2

Stevenson, L. F., Sparks, A., Allende‐Vega, N., Xirodimas, D. P., Lane, D. P., & Saville, M. K. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601567 · Cited by 280 · 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

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

MDMX: from bench to bedside

Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03362 · Cited by 228 · 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

USP7 inhibitor P22077 inhibits neuroblastoma growth via inducing p53-mediated apoptosis.

Fan, Y.-H., Cheng, J., Vasudevan, S. A., Dou, J., Zhang, H., Patel, R. H., Ma, I. T., Rojas, Y., Zhao, Y., Yu, Y., et al. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.400 · Cited by 199 · see citing works

Structure-guided development of a potent and selective non-covalent active-site inhibitor of USP7.

Lamberto, I., Liu, X., Seo, H.-S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.003 · Cited by 192 · 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

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

Targeting Mdm2 and Mdmx in cancer therapy: better living through medicinal chemistry?

Wade, M., & Wahl, G. M. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0423 · Cited by 170 · 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

MDM2 turnover and expression of ATRX determine the choice between quiescence and senescence in response to CDK4 inhibition

Kovatcheva, M., Liu, D. D., Dickson, M. A., Klein, M. E., O’Connor, R., Wilder, F. O., Socci, N. D., Tap, W. D., Schwartz, G. K., Singer, S., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3364 · Cited by 142 · see citing works

USP7 is a SUMO deubiquitinase essential for DNA replication.

Lecona, E., Rodriguez-Acebes, S., Specks, J., Lopez-Contreras, A. J., Ruppen, I., Murga, M., Muñoz, J., Mendez, J., & Fernandez-Capetillo, O. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3185 · Cited by 148 · see citing works

JTV1 co‐activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress

Liu, J., Chung, H., Vogt, M., Jin, Y., Malide, D., He, L., Dundr, M., & Levens, D. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.11 · Cited by 141 · see citing works

Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3

LeBron, C., Chen, L., Gilkes, D. M., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601032 · Cited by 122 · see citing works

Selective USP7 inhibition elicits cancer cell killing through a p53-dependent mechanism.

Schauer, N. J., Liu, X., Magin, R. S., Doherty, L. M., Chan, W. C., Ficarro, S. B., Hu, W., Roberts, R. M., Iacob, R. E., Stolte, B., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-62076-x · Cited by 125 · 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

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

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

USP7-specific inhibitors target and modify the enzyme’s active site via distinct chemical mechanisms.

Pozhidaeva, A., Valles, G., Wang, F., Wu, J., Sterner, D. E., Nguyen, P., Weinstock, J., Kumar, K. G. S., Kanyo, J., Wright, D., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.004 · Cited by 107 · see citing works

Molecular understanding of USP7 substrate recognition and c-terminal activation.

Rougé, L., Bainbridge, T. W., Kwok, M., Tong, R., Di Lello, P., Wertz, I. E., Maurer, T., Ernst, J. A., & Murray, J. (2016) · Structure · doi:10.1016/j.str.2016.05.020 · Cited by 108 · see citing works

MdmX is a substrate for the deubiquitinating enzyme USP2a

Allende-Vega, N., Sparks, A., Lane, D. P., & Saville, M. K. (2010) · Oncogene · doi:10.1038/onc.2009.330 · Cited by 100 · 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

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

Kon, N., Zhong, J., Kobayashi, Y., Li, M., Szabolcs, M., Ludwig, T., Canoll, P. D., & Gu, W. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.12 · Cited by 79 · see citing works

Deubiquitination of Tip60 by USP7 determines the activity of the p53-dependent apoptotic pathway.

Dar, A., Shibata, E., & Dutta, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00358-13 · Cited by 83 · 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

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

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

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

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

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

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

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

Further insight into substrate recognition by USP7: structural and biochemical analysis of the HdmX and Hdm2 interactions with USP7.

Sarkari, F., La Delfa, A., Arrowsmith, C. H., Frappier, L., Sheng, Y., & Saridakis, V. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.017 · Cited by 54 · see citing works

BRE/BRCC45 regulates CDC25A stability by recruiting USP7 in response to DNA damage.

Biswas, K., Philip, S., Yadav, A., Martin, B. K., Burkett, S., Singh, V., Babbar, A., North, S. L., Chang, S., & Sharan, S. K. (2018) · Nature Communications · doi:10.1038/s41467-018-03020-6 · Cited by 41 · see citing works

USP7 regulates the stability and function of HLTF through deubiquitination.

Qing, P., Han, L., Bin, L., Yan, L., & Ping, W. X. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23317 · Cited by 35 · see citing works

The roles of MDM2 and MDMX phosphorylation in stress signaling to p53

Chen, J. (2012) · Genes & Cancer · doi:10.1177/1947601912454733 · Cited by 33 · see citing works

Cytoplasmic tethering is involved in synergistic inhibition of p53 by Mdmx and Mdm2

Ohtsubo, C., Shiokawa, D., Kodama, M., Gaiddon, C., Nakagama, H., Jochemsen, A. G., Taya, Y., & Okamoto, K. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01180.x · Cited by 32 · 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

Preferential digestion of PCNA-ubiquitin and p53-ubiquitin linkages by USP7 to remove polyubiquitin chains from substrates.

Masuda, Y., Kanao, R., Kawai, H., Kukimoto, I., & Masutani, C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005167 · Cited by 18 · see citing works

USP7 protects TFEB from proteasome-mediated degradation

Keshri, S., Vicinanza, M., Takla, M., & Rubinsztein, D. C. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114872 · Cited by 8 · see citing works

ИСПОЛЬЗОВAНИЕ ПОТЕНЦИAЛA СОЦИAЛЬНЫХ ПAРТНЕРОВ В ПОДГОТОВКЕ БУДУЩИХ ПЕДAГОГОВ

Атабекова, Б. Б. (2024) · Habaršy. Pedagogika ġylymdary seriâsy · doi:10.51889/2959-5762.2023.80.4.019

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Ozaki, T., Hanaoka, E., Naka, M., et al. (1999) · DNA and Cell Biology · doi:10.1089/104454999315222 · Cited by 22 · see citing works

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Grimm, B. (2002) · Journal of Molluscan Studies · doi:10.1093/mollus/68.1.25 · Cited by 41 · see citing works

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Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

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Catherall, P. L. (1970) · Plant Pathology · doi:10.1111/j.1365-3059.1970.tb00999.x · Cited by 6 · see citing works