메뉴 건너뛰기




Volumn 74, Issue 18, 2014, Pages 4955-4966

Emerging potential of therapeutic targeting of ubiquitin-specific proteases in the treatment of cancer

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; PROTEASOME; PROTEINASE INHIBITOR;

EID: 84907486869     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-14-1211     Document Type: Review
Times cited : (167)

References (128)
  • 1
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J, Yang PL, Gray NS. Targeting cancer with small molecule kinase inhibitors. Nat Rev Cancer 2009;9:28-39.
    • (2009) Nat Rev Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 2
    • 79951702955 scopus 로고    scopus 로고
    • Bortezomib as the first proteasome inhibitor anticancer drug: Current status and future perspectives
    • Chen D, Frezza M, Schmitt S, Kanwar J, Dou QP. Bortezomib as the first proteasome inhibitor anticancer drug: current status and future perspectives. Curr Cancer Drug Targets 2011;11:239-53.
    • (2011) Curr Cancer Drug Targets , vol.11 , pp. 239-253
    • Chen, D.1    Frezza, M.2    Schmitt, S.3    Kanwar, J.4    Dou, Q.P.5
  • 3
    • 84866988499 scopus 로고    scopus 로고
    • Ubiquitin-based anticancer therapy: Carpet bombing with proteasome inhibitors vs surgical strikes with E1, E2, E3, or DUB inhibitors
    • Mattern MR, Wu J, Nicholson B. Ubiquitin-based anticancer therapy: carpet bombing with proteasome inhibitors vs surgical strikes with E1, E2, E3, or DUB inhibitors. Biochim Biophys Acta 2012;1823:2014-21.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 2014-2021
    • Mattern, M.R.1    Wu, J.2    Nicholson, B.3
  • 4
    • 66749083491 scopus 로고    scopus 로고
    • DUBs and cancer: The role of deubiquitinating enzymes as oncogenes, non-oncogenes and tumor suppressors
    • Hussain S, Zhang Y, Galardy PJ. DUBs and cancer: the role of deubiquitinating enzymes as oncogenes, non-oncogenes and tumor suppressors. Cell Cycle 2009;8:1688-97.
    • (2009) Cell Cycle , vol.8 , pp. 1688-1697
    • Hussain, S.1    Zhang, Y.2    Galardy, P.J.3
  • 7
    • 57249084078 scopus 로고    scopus 로고
    • Genome profiling of chronic myelomonocytic leukemia: Frequent alterations of RAS and RUNX1 genes
    • Gelsi-Boyer V, Trouplin V, Adelaide J, Aceto N, Remy V, Pinson S, et al. Genome profiling of chronic myelomonocytic leukemia: frequent alterations of RAS and RUNX1 genes. BMC Cancer 2008;8:299.
    • (2008) BMC Cancer , vol.8 , pp. 299
    • Gelsi-Boyer, V.1    Trouplin, V.2    Adelaide, J.3    Aceto, N.4    Remy, V.5    Pinson, S.6
  • 8
    • 84904069664 scopus 로고    scopus 로고
    • Whole transcriptome sequencing of a paediatric case of denovo acute myeloid leukaemia with del(5q) reveals RUNX1-USP42 and PRDM16-SKI fusion transcripts
    • Mar. 27 Epub ahead of print
    • Masetti R, Togni M, Astolfi A, Pigazzi M, Indio V, Rivalta B, et al. Whole transcriptome sequencing of a paediatric case of denovo acute myeloid leukaemia with del(5q) reveals RUNX1-USP42 and PRDM16-SKI fusion transcripts. Br J Haematol. 2014 Mar. 27 [Epub ahead of print].
    • (2014) Br J Haematol.
    • Masetti, R.1    Togni, M.2    Astolfi, A.3    Pigazzi, M.4    Indio, V.5    Rivalta, B.6
  • 9
    • 0032934989 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease, UBP43, cloned from leukemia fusion protein AML1-ETO-expressing mice, functions in hematopoietic cell differentiation
    • Liu LQ, Ilaria R Jr, Kingsley PD, Iwama A, Van Etten RA, Palis J, et al. A novel ubiquitin-specific protease, UBP43, cloned from leukemia fusion protein AML1-ETO-expressing mice, functions in hematopoietic cell differentiation. Mol Cell Biol 1999;19:3029-38.
    • (1999) Mol Cell Biol , vol.19 , pp. 3029-3038
    • Liu, L.Q.1    Ilaria, R.2    Kingsley, P.D.3    Iwama, A.4    Van Etten, R.A.5    Palis, J.6
  • 10
    • 22544438745 scopus 로고    scopus 로고
    • A leukemia-enriched cDNA microarray platform identifies new transcripts with relevance to the biology of pediatric acute lymphoblastic leukemia
    • De Pitta C, Tombolan L, Campo Dell'Orto M, Accordi B, Te Kronnie G, Romualdi C, et al. A leukemia-enriched cDNA microarray platform identifies new transcripts with relevance to the biology of pediatric acute lymphoblastic leukemia. Haematologica 2005;90:890-8.
    • (2005) Haematologica , vol.90 , pp. 890-898
    • De Pitta, C.1    Tombolan, L.2    Campo Dell'Orto, M.3    Accordi, B.4    Te Kronnie, G.5    Romualdi, C.6
  • 12
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, French DM, et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010;463:103-7.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3    Liu, J.4    Ferrando, R.5    French, D.M.6
  • 13
    • 84890200628 scopus 로고    scopus 로고
    • The role of ubiquitin modification in the regulation of p53
    • Hock AK, Vousden KH. The role of ubiquitin modification in the regulation of p53. Biochim Biophys Acta 2014;1843:137-49.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 137-149
    • Hock, A.K.1    Vousden, K.H.2
  • 14
    • 25444478027 scopus 로고    scopus 로고
    • ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation
    • Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG. ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. Cell Cycle 2005;4:1166-70.
    • (2005) Cell Cycle , vol.4 , pp. 1166-1170
    • Meulmeester, E.1    Pereg, Y.2    Shiloh, Y.3    Jochemsen, A.G.4
  • 16
    • 75749132016 scopus 로고    scopus 로고
    • USP10 regulates p53 localization and stability by deubiquitinating p53
    • Yuan J, Luo K, Zhang L, Cheville JC, Lou Z. USP10 regulates p53 localization and stability by deubiquitinating p53. Cell 2010;140:384-96.
    • (2010) Cell , vol.140 , pp. 384-396
    • Yuan, J.1    Luo, K.2    Zhang, L.3    Cheville, J.C.4    Lou, Z.5
  • 17
    • 79957900145 scopus 로고    scopus 로고
    • USP4 inhibits p53 through deubiquitinating and stabilizing ARF-BP1
    • Zhang X, Berger FG, Yang J, Lu X. USP4 inhibits p53 through deubiquitinating and stabilizing ARF-BP1. EMBO J 2011;30:2177-89.
    • (2011) EMBO J , vol.30 , pp. 2177-2189
    • Zhang, X.1    Berger, F.G.2    Yang, J.3    Lu, X.4
  • 18
    • 64149087218 scopus 로고    scopus 로고
    • Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53
    • Dayal S, Sparks A, Jacob J, Allende-Vega N, Lane DP, Saville MK. Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53. J Biol Chem 2009;284:5030-41.
    • (2009) J Biol Chem , vol.284 , pp. 5030-5041
    • Dayal, S.1    Sparks, A.2    Jacob, J.3    Allende-Vega, N.4    Lane, D.P.5    Saville, M.K.6
  • 19
    • 84901246134 scopus 로고    scopus 로고
    • USP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responses
    • Zou Q, Jin J, Hu H, Li HS, Romano S, Xiao Y, et al. USP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responses. Nat Immunol 2014;15:562-70.
    • (2014) Nat Immunol , vol.15 , pp. 562-570
    • Zou, Q.1    Jin, J.2    Hu, H.3    Li, H.S.4    Romano, S.5    Xiao, Y.6
  • 21
    • 59649114341 scopus 로고    scopus 로고
    • Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype
    • Kim JM, Parmar K, Huang M, Weinstock DM, Ruit CA, Kutok JL, et al. Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype. Dev Cell 2009;16:314-20.
    • (2009) Dev Cell , vol.16 , pp. 314-320
    • Kim, J.M.1    Parmar, K.2    Huang, M.3    Weinstock, D.M.4    Ruit, C.A.5    Kutok, J.L.6
  • 22
    • 84870862277 scopus 로고    scopus 로고
    • The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability
    • Zhang L, Lubin A, Chen H, Sun Z, Gong F. The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability. Cell Cycle 2012;11:4378-84.
    • (2012) Cell Cycle , vol.11 , pp. 4378-4384
    • Zhang, L.1    Lubin, A.2    Chen, H.3    Sun, Z.4    Gong, F.5
  • 23
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubiquitinases
    • Harhaj EW, Dixit VM. Regulation of NF-kappaB by deubiquitinases. Immunol Rev 2012;246:107-24.
    • (2012) Immunol Rev , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 24
    • 26244434134 scopus 로고    scopus 로고
    • Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB
    • Tzimas C, Michailidou G, Arsenakis M, Kieff E, Mosialos G, Hatzivassiliou EG. Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB. Cell Signal 2006;18:83-92.
    • (2006) Cell Signal , vol.18 , pp. 83-92
    • Tzimas, C.1    Michailidou, G.2    Arsenakis, M.3    Kieff, E.4    Mosialos, G.5    Hatzivassiliou, E.G.6
  • 25
    • 84873709476 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 promotes TNF-alpha-induced apoptosis by deubiquitination of RIP1 in head and neck squamous cell carcinoma
    • Hou X, Wang L, Zhang L, Pan X, Zhao W. Ubiquitin-specific protease 4 promotes TNF-alpha-induced apoptosis by deubiquitination of RIP1 in head and neck squamous cell carcinoma. FEBS Lett 2013;587:311-6.
    • (2013) FEBS Lett , vol.587 , pp. 311-316
    • Hou, X.1    Wang, L.2    Zhang, L.3    Pan, X.4    Zhao, W.5
  • 26
    • 71349086190 scopus 로고    scopus 로고
    • USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha
    • Sun W, Tan X, Shi Y, Xu G, Mao R, Gu X, et al. USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha. Cell Signal 2010;22:386-94.
    • (2010) Cell Signal , vol.22 , pp. 386-394
    • Sun, W.1    Tan, X.2    Shi, Y.3    Xu, G.4    Mao, R.5    Gu, X.6
  • 27
    • 84878393110 scopus 로고    scopus 로고
    • Overexpression of USP14 protease reduces I-kappaB protein levels and increases cytokine release in lung epithelial cells
    • Mialki RK, Zhao J, Wei J, Mallampalli DF, Zhao Y. Overexpression of USP14 protease reduces I-kappaB protein levels and increases cytokine release in lung epithelial cells. J Biol Chem 2013;288:15437-41.
    • (2013) J Biol Chem , vol.288 , pp. 15437-15441
    • Mialki, R.K.1    Zhao, J.2    Wei, J.3    Mallampalli, D.F.4    Zhao, Y.5
  • 28
    • 33947606938 scopus 로고    scopus 로고
    • CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha
    • Schweitzer K, Bozko PM, Dubiel W, Naumann M. CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha. EMBO J 2007;26:1532-41.
    • (2007) EMBO J , vol.26 , pp. 1532-1541
    • Schweitzer, K.1    Bozko, P.M.2    Dubiel, W.3    Naumann, M.4
  • 29
    • 84863191812 scopus 로고    scopus 로고
    • Ubiquitin removal in the TGF-beta pathway
    • Aggarwal K, Massague J. Ubiquitin removal in the TGF-beta pathway. Nat Cell Biol 2012;14:656-7.
    • (2012) Nat Cell Biol , vol.14 , pp. 656-657
    • Aggarwal, K.1    Massague, J.2
  • 30
    • 84873323376 scopus 로고    scopus 로고
    • Deubiquitinase FAM/USP9X interacts with the E3 ubiquitin ligase SMURF1 protein and protects it from ligase activity-dependent self-degradation
    • Xie Y, Avello M, Schirle M, McWhinnie E, Feng Y, Bric-Furlong E, et al. Deubiquitinase FAM/USP9X interacts with the E3 ubiquitin ligase SMURF1 protein and protects it from ligase activity-dependent self-degradation. J Biol Chem 2013;288:2976-85.
    • (2013) J Biol Chem , vol.288 , pp. 2976-2985
    • Xie, Y.1    Avello, M.2    Schirle, M.3    McWhinnie, E.4    Feng, Y.5    Bric-Furlong, E.6
  • 31
    • 84905496932 scopus 로고    scopus 로고
    • ID proteins regulate diverse aspects of cancer progression and provide novel therapeutic opportunities
    • May 14. Epub ahead of print
    • Nair R, Teo WS, Mittal V, Swarbrick A. ID proteins regulate diverse aspects of cancer progression and provide novel therapeutic opportunities. Mol Ther. 2014 May 14. [Epub ahead of print].
    • (2014) Mol Ther.
    • Nair, R.1    Teo, W.S.2    Mittal, V.3    Swarbrick, A.4
  • 32
    • 80052919716 scopus 로고    scopus 로고
    • USP1 deubiquitinates ID proteins to preserve a mesenchymal stem cell program in osteosarcoma
    • Williams SA, Maecker HL, French DM, Liu J, Gregg A, Silverstein LB, et al. USP1 deubiquitinates ID proteins to preserve a mesenchymal stem cell program in osteosarcoma. Cell 2011;146:918-30.
    • (2011) Cell , vol.146 , pp. 918-930
    • Williams, S.A.1    Maecker, H.L.2    French, D.M.3    Liu, J.4    Gregg, A.5    Silverstein, L.B.6
  • 33
    • 68849126660 scopus 로고    scopus 로고
    • Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells
    • Colland F, Formstecher E, Jacq X, Reverdy C, Planquette C, Conrath S, et al. Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells. Mol Cancer Ther 2009;8:2286-95.
    • (2009) Mol Cancer Ther , vol.8 , pp. 2286-2295
    • Colland, F.1    Formstecher, E.2    Jacq, X.3    Reverdy, C.4    Planquette, C.5    Conrath, S.6
  • 34
    • 84866021069 scopus 로고    scopus 로고
    • 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 KG, Zhou B, Carrasco R, et al. A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance. Cancer Cell 2012;22:345-58.
    • (2012) Cancer Cell , vol.22 , pp. 345-358
    • Chauhan, D.1    Tian, Z.2    Nicholson, B.3    Kumar, K.G.4    Zhou, B.5    Carrasco, R.6
  • 35
    • 84897022669 scopus 로고    scopus 로고
    • A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance
    • Tian Z, D'Arcy P, Wang X, Ray A, Tai YT, Hu Y, et al. A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance. Blood 2014;123:706-16.
    • (2014) Blood , vol.123 , pp. 706-716
    • Tian, Z.1    D'Arcy, P.2    Wang, X.3    Ray, A.4    Tai, Y.T.5    Hu, Y.6
  • 36
    • 82255194029 scopus 로고    scopus 로고
    • Selective and cell-active inhibitors of the USP1/UAF1 deubiquitinase complex reverse cisplatin resistance in non-small cell lung cancer cells
    • Chen J, Dexheimer TS, Ai Y, Liang Q, Villamil MA, Inglese J, et al. Selective and cell-active inhibitors of the USP1/UAF1 deubiquitinase complex reverse cisplatin resistance in non-small cell lung cancer cells. Chem Biol 2011;18:1390-400.
    • (2011) Chem Biol , vol.18 , pp. 1390-1400
    • Chen, J.1    Dexheimer, T.S.2    Ai, Y.3    Liang, Q.4    Villamil, M.A.5    Inglese, J.6
  • 37
  • 39
    • 78549247880 scopus 로고    scopus 로고
    • Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis
    • Kapuria V, Peterson LF, Fang D, Bornmann WG, Talpaz M, Donato NJ. Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis. Cancer Res 2010;70:9265-76.
    • (2010) Cancer Res , vol.70 , pp. 9265-9276
    • Kapuria, V.1    Peterson, L.F.2    Fang, D.3    Bornmann, W.G.4    Talpaz, M.5    Donato, N.J.6
  • 41
    • 39549106692 scopus 로고    scopus 로고
    • The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module
    • Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, et al. The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol Cell 2008;29:451-64.
    • (2008) Mol Cell , vol.29 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3    Swift, S.4    Hofmann, K.5    Ashworth, A.6
  • 42
    • 84872184573 scopus 로고    scopus 로고
    • CYLD inhibits melanoma growth and progression through suppression of the JNK/AP-1 and beta1-integrin signaling pathways
    • Ke H, Augustine CK, Gandham VD, Jin JY, Tyler DS, Akiyama SK, et al. CYLD inhibits melanoma growth and progression through suppression of the JNK/AP-1 and beta1-integrin signaling pathways. J Invest Dermatol 2013;133:221-9.
    • (2013) J Invest Dermatol , vol.133 , pp. 221-229
    • Ke, H.1    Augustine, C.K.2    Gandham, V.D.3    Jin, J.Y.4    Tyler, D.S.5    Akiyama, S.K.6
  • 43
    • 84893089028 scopus 로고    scopus 로고
    • CYLD controls c-MYC expression through the JNK-dependent signaling pathway in hepatocellular carcinoma
    • Pannem RR, Dorn C, Ahlqvist K, Bosserhoff AK, Hellerbrand C, Massoumi R. CYLD controls c-MYC expression through the JNK-dependent signaling pathway in hepatocellular carcinoma. Carcinogenesis 2014;35:461-8.
    • (2014) Carcinogenesis , vol.35 , pp. 461-468
    • Pannem, R.R.1    Dorn, C.2    Ahlqvist, K.3    Bosserhoff, A.K.4    Hellerbrand, C.5    Massoumi, R.6
  • 44
    • 34250368115 scopus 로고    scopus 로고
    • Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses
    • Reiley WW, Jin W, Lee AJ, Wright A, Wu X, Tewalt EF, et al. Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses. J Exp Med 2007;204:1475-85.
    • (2007) J Exp Med , vol.204 , pp. 1475-1485
    • Reiley, W.W.1    Jin, W.2    Lee, A.J.3    Wright, A.4    Wu, X.5    Tewalt, E.F.6
  • 46
  • 47
    • 84873085753 scopus 로고    scopus 로고
    • A strategy for modulation of enzymes in the ubiquitin system
    • Ernst A, Avvakumov G, Tong J, Fan Y, Zhao Y, Alberts P, et al. A strategy for modulation of enzymes in the ubiquitin system. Science 2013;339:590-5.
    • (2013) Science , vol.339 , pp. 590-595
    • Ernst, A.1    Avvakumov, G.2    Tong, J.3    Fan, Y.4    Zhao, Y.5    Alberts, P.6
  • 49
    • 84874332545 scopus 로고    scopus 로고
    • USP2a negatively regulates IL-1beta- and virus-induced NF-kappaB activation by deubiquitinating TRAF6
    • He X, Li Y, Li C, Liu LJ, Zhang XD, Liu Y, et al. USP2a negatively regulates IL-1beta- and virus-induced NF-kappaB activation by deubiquitinating TRAF6. J Mol Cell Biol 2013;5:39-47.
    • (2013) J Mol Cell Biol , vol.5 , pp. 39-47
    • He, X.1    Li, Y.2    Li, C.3    Liu, L.J.4    Zhang, X.D.5    Liu, Y.6
  • 50
    • 84876669324 scopus 로고    scopus 로고
    • Up-regulation of USP2a and FASN in gliomas correlates strongly with glioma grade
    • Tao BB, He H, Shi XH, Wang CL, Li WQ, Li B, et al. Up-regulation of USP2a and FASN in gliomas correlates strongly with glioma grade. J Clin Neurosci 2013;20:717-20.
    • (2013) J Clin Neurosci , vol.20 , pp. 717-720
    • Tao, B.B.1    He, H.2    Shi, X.H.3    Wang, C.L.4    Li, W.Q.5    Li, B.6
  • 51
    • 36049036216 scopus 로고    scopus 로고
    • Human USP3 is a chromatin modifier required for S phase progression and genome stability
    • Nicassio F, Corrado N, Vissers JH, Areces LB, Bergink S, Marteijn JA, et al. Human USP3 is a chromatin modifier required for S phase progression and genome stability. Curr Biol 2007;17:1972-7.
    • (2007) Curr Biol , vol.17 , pp. 1972-1977
    • Nicassio, F.1    Corrado, N.2    Vissers, J.H.3    Areces, L.B.4    Bergink, S.5    Marteijn, J.A.6
  • 52
    • 84892609034 scopus 로고    scopus 로고
    • USP3 controls BRCA1 "foci"
    • Raychaudhuri P. USP3 controls BRCA1 "foci". Cell Cycle 2014;13:183.
    • (2014) Cell Cycle , vol.13 , pp. 183
    • Raychaudhuri, P.1
  • 53
    • 84892562030 scopus 로고    scopus 로고
    • USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15
    • Sharma N, Zhu Q, Wani G, He J, Wang QE, Wani AA. USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15. Cell Cycle 2014;13:106-14.
    • (2014) Cell Cycle , vol.13 , pp. 106-114
    • Sharma, N.1    Zhu, Q.2    Wani, G.3    He, J.4    Wang, Q.E.5    Wani, A.A.6
  • 55
    • 80052691620 scopus 로고    scopus 로고
    • USP4 targets TAK1 to downregulate TNFalpha-induced NF-kappaB activation
    • Fan YH, Yu Y, Mao RF, Tan XJ, Xu GF, Zhang H, et al. USP4 targets TAK1 to downregulate TNFalpha-induced NF-kappaB activation. Cell Death Differ 2011;18:1547-60.
    • (2011) Cell Death Differ , vol.18 , pp. 1547-1560
    • Fan, Y.H.1    Yu, Y.2    Mao, R.F.3    Tan, X.J.4    Xu, G.F.5    Zhang, H.6
  • 56
    • 83555162507 scopus 로고    scopus 로고
    • Regulation of p53 stability and function by the deubiquitinating enzyme USP42
    • Hock AK, Vigneron AM, Carter S, Ludwig RL, Vousden KH. Regulation of p53 stability and function by the deubiquitinating enzyme USP42. EMBO J 2011;30:4921-30.
    • (2011) EMBO J , vol.30 , pp. 4921-4930
    • Hock, A.K.1    Vigneron, A.M.2    Carter, S.3    Ludwig, R.L.4    Vousden, K.H.5
  • 57
    • 84863218422 scopus 로고    scopus 로고
    • USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-beta type I receptor
    • Zhang L, Zhou F, Drabsch Y, Gao R, Snaar-Jagalska BE, Mickanin C, et al. USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-beta type I receptor. Nat Cell Biol 2012;14:717-26.
    • (2012) Nat Cell Biol , vol.14 , pp. 717-726
    • Zhang, L.1    Zhou, F.2    Drabsch, Y.3    Gao, R.4    Snaar-Jagalska, B.E.5    Mickanin, C.6
  • 58
    • 72949089936 scopus 로고    scopus 로고
    • The ubiquitin specific protease 4 (USP4) is a new player in the Wnt signalling pathway
    • Zhao B, Schlesiger C, Masucci MG, Lindsten K. The ubiquitin specific protease 4 (USP4) is a new player in the Wnt signalling pathway. J Cell Mol Med 2009;13:1886-95.
    • (2009) J Cell Mol Med , vol.13 , pp. 1886-1895
    • Zhao, B.1    Schlesiger, C.2    Masucci, M.G.3    Lindsten, K.4
  • 59
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, Wilkinson KD. The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 2006;124:1197-208.
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5    Wilkinson, K.D.6
  • 61
    • 84867900618 scopus 로고    scopus 로고
    • PTBP1-dependent regulation of USP5 alternative RNA splicing plays a role in glioblastoma tumorigenesis
    • Izaguirre DI, Zhu W, Hai T, Cheung HC, Krahe R, Cote GJ. PTBP1-dependent regulation of USP5 alternative RNA splicing plays a role in glioblastoma tumorigenesis. Mol Carcinog 2012;51:895-906.
    • (2012) Mol Carcinog , vol.51 , pp. 895-906
    • Izaguirre, D.I.1    Zhu, W.2    Hai, T.3    Cheung, H.C.4    Krahe, R.5    Cote, G.J.6
  • 62
    • 84898015292 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 5 is required for the efficient repair of DNA double-strand breaks
    • Nakajima S, Lan L, Wei L, Hsieh CL, Rapic-Otrin V, Yasui A, et al. Ubiquitin-specific protease 5 is required for the efficient repair of DNA double-strand breaks. PLoS ONE 2014;9:e84899.
    • (2014) PLoS ONE , vol.9 , pp. e84899
    • Nakajima, S.1    Lan, L.2    Wei, L.3    Hsieh, C.L.4    Rapic-Otrin, V.5    Yasui, A.6
  • 64
    • 84864374400 scopus 로고    scopus 로고
    • Atypical mechanism of NF-kappaB activation by TRE17/ubiquitin-specific protease 6 (USP6) oncogene and its requirement in tumorigenesis
    • Pringle LM, Young R, Quick L, Riquelme DN, Oliveira AM, May MJ, et al. Atypical mechanism of NF-kappaB activation by TRE17/ubiquitin-specific protease 6 (USP6) oncogene and its requirement in tumorigenesis. Oncogene 2012;31:3525-35.
    • (2012) Oncogene , vol.31 , pp. 3525-3535
    • Pringle, L.M.1    Young, R.2    Quick, L.3    Riquelme, D.N.4    Oliveira, A.M.5    May, M.J.6
  • 65
    • 77954061516 scopus 로고    scopus 로고
    • TRE17/USP6 oncogene translocated in aneurysmal bone cyst induces matrix metalloproteinase production via activation of NF-kappaB
    • Ye Y, Pringle LM, Lau AW, Riquelme DN, Wang H, Jiang T, et al. TRE17/USP6 oncogene translocated in aneurysmal bone cyst induces matrix metalloproteinase production via activation of NF-kappaB. Oncogene 2010;29:3619-29.
    • (2010) Oncogene , vol.29 , pp. 3619-3629
    • Ye, Y.1    Pringle, L.M.2    Lau, A.W.3    Riquelme, D.N.4    Wang, H.5    Jiang, T.6
  • 66
    • 0037184947 scopus 로고    scopus 로고
    • 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 JW, et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002;111:1041-54.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6
  • 67
    • 33244490784 scopus 로고    scopus 로고
    • 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 PD, Gu W, Shi Y. Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway. PLoS Biol 2006;4:e27.
    • (2006) PLoS Biol , vol.4 , pp. e27
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 69
    • 84905484055 scopus 로고    scopus 로고
    • A 2.2 A resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding
    • Molland K, Zhou Q, Mesecar AD. A 2.2 A resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding. Acta Crystallogr F Struct Biol Commun 2014;70(Pt 3):283-7.
    • (2014) Acta Crystallogr F Struct Biol Commun , vol.70 , pp. 283-287
    • Molland, K.1    Zhou, Q.2    Mesecar, A.D.3
  • 70
    • 20144386721 scopus 로고    scopus 로고
    • Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization
    • Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, et al. Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. Mol Cell 2005;18:25-36.
    • (2005) Mol Cell , vol.18 , pp. 25-36
    • Saridakis, V.1    Sheng, Y.2    Sarkari, F.3    Holowaty, M.N.4    Shire, K.5    Nguyen, T.6
  • 71
    • 33646835771 scopus 로고    scopus 로고
    • HAUSP as a therapeutic target for hematopoietic tumors (review)
    • Cheon KW, Baek KH. HAUSP as a therapeutic target for hematopoietic tumors (review). Int J Oncol 2006;28:1209-15.
    • (2006) Int J Oncol , vol.28 , pp. 1209-1215
    • Cheon, K.W.1    Baek, K.H.2
  • 73
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov GV, Walker JR, Xue S, Finerty PJ Jr, Mackenzie F, Newman EM, et al. Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J Biol Chem 2006;281:38061-70.
    • (2006) J Biol Chem , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6
  • 74
    • 84864848052 scopus 로고    scopus 로고
    • A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity
    • Samara NL, Ringel AE, Wolberger C. A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity. Structure 2012;20:1414-24.
    • (2012) Structure , vol.20 , pp. 1414-1424
    • Samara, N.L.1    Ringel, A.E.2    Wolberger, C.3
  • 75
    • 77952519938 scopus 로고    scopus 로고
    • Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module
    • Kohler A, Zimmerman E, Schneider M, Hurt E, Zheng N. Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 2010;141:606-17.
    • (2010) Cell , vol.141 , pp. 606-617
    • Kohler, A.1    Zimmerman, E.2    Schneider, M.3    Hurt, E.4    Zheng, N.5
  • 76
    • 78549264851 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP8 promotes trafficking and degradation of the chemokine receptor 4 at the sorting endosome
    • Berlin I, Higginbotham KM, Dise RS, Sierra MI, Nash PD. The deubiquitinating enzyme USP8 promotes trafficking and degradation of the chemokine receptor 4 at the sorting endosome. J Biol Chem 2010;285:37895-908.
    • (2010) J Biol Chem , vol.285 , pp. 37895-37908
    • Berlin, I.1    Higginbotham, K.M.2    Dise, R.S.3    Sierra, M.I.4    Nash, P.D.5
  • 77
    • 84881137952 scopus 로고    scopus 로고
    • USP8 is a novel target for overcoming gefitinib resistance in lung cancer
    • Byun S, Lee SY, Lee J, Jeong CH, Farrand L, Lim S, et al. USP8 is a novel target for overcoming gefitinib resistance in lung cancer. Clin Cancer Res 2013;19:3894-904.
    • (2013) Clin Cancer Res , vol.19 , pp. 3894-3904
    • Byun, S.1    Lee, S.Y.2    Lee, J.3    Jeong, C.H.4    Farrand, L.5    Lim, S.6
  • 78
    • 77953732982 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 8 links the PTEN-Akt-AIP4 pathway to the control of FLIPS stability and TRAIL sensitivity in glioblastoma multiforme
    • Panner A, Crane CA, Weng C, Feletti A, Fang S, Parsa AT, et al. Ubiquitin-specific protease 8 links the PTEN-Akt-AIP4 pathway to the control of FLIPS stability and TRAIL sensitivity in glioblastoma multiforme. Cancer Res 2010;70:5046-53.
    • (2010) Cancer Res , vol.70 , pp. 5046-5053
    • Panner, A.1    Crane, C.A.2    Weng, C.3    Feletti, A.4    Fang, S.5    Parsa, A.T.6
  • 79
    • 84863012620 scopus 로고    scopus 로고
    • USP8 promotes smoothened signaling by preventing its ubiquitination and changing its subcellular localization
    • Xia R, Jia H, Fan J, Liu Y, Jia J. USP8 promotes smoothened signaling by preventing its ubiquitination and changing its subcellular localization. PLoS Biol 2012;10:e1001238.
    • (2012) PLoS Biol , vol.10 , pp. e1001238
    • Xia, R.1    Jia, H.2    Fan, J.3    Liu, Y.4    Jia, J.5
  • 80
    • 84877113183 scopus 로고    scopus 로고
    • The SOX2-interactome in brain cancer cells identifies the requirement of MSI2 and USP9X for the growth of brain tumor cells
    • Cox JL, Wilder PJ, Gilmore JM, Wuebben EL, Washburn MP, Rizzino A. The SOX2-interactome in brain cancer cells identifies the requirement of MSI2 and USP9X for the growth of brain tumor cells. PLoS ONE 2013;8:e62857.
    • (2013) PLoS ONE , vol.8 , pp. e62857
    • Cox, J.L.1    Wilder, P.J.2    Gilmore, J.M.3    Wuebben, E.L.4    Washburn, M.P.5    Rizzino, A.6
  • 81
    • 58149093172 scopus 로고    scopus 로고
    • FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination
    • Dupont S, Mamidi A, Cordenonsi M, Montagner M, Zacchigna L, Adorno M, et al. FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination. Cell 2009;136:123-35.
    • (2009) Cell , vol.136 , pp. 123-135
    • Dupont, S.1    Mamidi, A.2    Cordenonsi, M.3    Montagner, M.4    Zacchigna, L.5    Adorno, M.6
  • 82
    • 84886037235 scopus 로고    scopus 로고
    • USP9X expression correlates with tumor progression and poor prognosis in esophageal squamous cell carcinoma
    • Peng J, Hu Q, Liu W, He X, Cui L, Chen X, et al. USP9X expression correlates with tumor progression and poor prognosis in esophageal squamous cell carcinoma. Diagn Pathol 2013;8:177.
    • (2013) Diagn Pathol , vol.8 , pp. 177
    • Peng, J.1    Hu, Q.2    Liu, W.3    He, X.4    Cui, L.5    Chen, X.6
  • 83
    • 79953072934 scopus 로고    scopus 로고
    • Bcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis
    • Sun H, Kapuria V, Peterson LF, Fang D, Bornmann WG, Bartholomeusz G, et al. Bcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis. Blood 2011;117:3151-62.
    • (2011) Blood , vol.117 , pp. 3151-3162
    • Sun, H.1    Kapuria, V.2    Peterson, L.F.3    Fang, D.4    Bornmann, W.G.5    Bartholomeusz, G.6
  • 84
    • 34250798032 scopus 로고    scopus 로고
    • Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics
    • Deng S, Zhou H, Xiong R, Lu Y, Yan D, Xing T, et al. Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics. Breast Cancer Res Treat 2007;104:21-30.
    • (2007) Breast Cancer Res Treat , vol.104 , pp. 21-30
    • Deng, S.1    Zhou, H.2    Xiong, R.3    Lu, Y.4    Yan, D.5    Xing, T.6
  • 85
    • 84890979013 scopus 로고    scopus 로고
    • USP10 antagonizes c-Myc transcriptional activation through SIRT6 stabilization to suppress tumor formation
    • Lin Z, Yang H, Tan C, Li J, Liu Z, Quan Q, et al. USP10 antagonizes c-Myc transcriptional activation through SIRT6 stabilization to suppress tumor formation. Cell Rep 2013;5:1639-49.
    • (2013) Cell Rep , vol.5 , pp. 1639-1649
    • Lin, Z.1    Yang, H.2    Tan, C.3    Li, J.4    Liu, Z.5    Quan, Q.6
  • 86
    • 84898927674 scopus 로고    scopus 로고
    • Prognostic significance of USP10 as a tumor-associated marker in gastric carcinoma
    • Zeng Z, Wu HX, Zhan N, Huang YB, Wang ZS, Yang GF, et al. Prognostic significance of USP10 as a tumor-associated marker in gastric carcinoma. Tumour Biol 2014;35:3845-53.
    • (2014) Tumour Biol , vol.35 , pp. 3845-3853
    • Zeng, Z.1    Wu, H.X.2    Zhan, N.3    Huang, Y.B.4    Wang, Z.S.5    Yang, G.F.6
  • 87
    • 84900525660 scopus 로고    scopus 로고
    • Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains
    • Harper S, Gratton HE, Cornaciu I, Oberer M, Scott DJ, Emsley J, et al. Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains. Biochem 2014;53:2966-78.
    • (2014) Biochem , vol.53 , pp. 2966-2978
    • Harper, S.1    Gratton, H.E.2    Cornaciu, I.3    Oberer, M.4    Scott, D.J.5    Emsley, J.6
  • 89
    • 84873807725 scopus 로고    scopus 로고
    • USP-11 as a predictive and prognostic factor following neoadjuvant therapy in women with breast cancer
    • Bayraktar S, Gutierrez Barrera AM, Liu D, Pusztai L, Litton J, Valero V, et al. USP-11 as a predictive and prognostic factor following neoadjuvant therapy in women with breast cancer. Cancer J 2013;19:10-7.
    • (2013) Cancer J , vol.19 , pp. 10-17
    • Bayraktar, S.1    Gutierrez Barrera, A.M.2    Liu, D.3    Pusztai, L.4    Litton, J.5    Valero, V.6
  • 90
    • 84882800748 scopus 로고    scopus 로고
    • Mitoxantrone targets human ubiquitin-specific peptidase 11 (USP11) and is a potent inhibitor of pancreatic cancer cell survival
    • Burkhart RA, Peng Y, Norris ZA, Tholey RM, Talbott VA, Liang Q, et al. Mitoxantrone targets human ubiquitin-specific peptidase 11 (USP11) and is a potent inhibitor of pancreatic cancer cell survival. Mol Cancer Res 2013;11:901-11.
    • (2013) Mol Cancer Res , vol.11 , pp. 901-911
    • Burkhart, R.A.1    Peng, Y.2    Norris, Z.A.3    Tholey, R.M.4    Talbott, V.A.5    Liang, Q.6
  • 91
    • 79953235713 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility
    • De La Vega M, Kelvin AA, Dunican DJ, McFarlane C, Burrows JF, Jaworski J, et al. The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility. Nat Commun 2011;2:259.
    • (2011) Nat Commun , vol.2 , pp. 259
    • De La Vega, M.1    Kelvin, A.A.2    Dunican, D.J.3    McFarlane, C.4    Burrows, J.F.5    Jaworski, J.6
  • 92
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu M, Li P, Song L, Jeffrey PD, Chenova TA, Wilkinson KD, et al. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J 2005;24:3747-56.
    • (2005) EMBO J , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5    Wilkinson, K.D.6
  • 93
    • 33645748749 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 14 expression in colorectal cancer is associated with liver and lymph node metastases
    • Shinji S, Naito Z, Ishiwata S, Ishiwata T, Tanaka N, Furukawa K, et al. Ubiquitin-specific protease 14 expression in colorectal cancer is associated with liver and lymph node metastases. Oncol Rep 2006;15:539-43.
    • (2006) Oncol Rep , vol.15 , pp. 539-543
    • Shinji, S.1    Naito, Z.2    Ishiwata, S.3    Ishiwata, T.4    Tanaka, N.5    Furukawa, K.6
  • 94
    • 84878208622 scopus 로고    scopus 로고
    • Over-expression of deubiquitinating enzyme USP14 in lung adenocarcinoma promotes proliferation through the accumulation of beta-catenin
    • Wu N, Liu C, Bai C, Han YP, Cho WC, Li Q. Over-expression of deubiquitinating enzyme USP14 in lung adenocarcinoma promotes proliferation through the accumulation of beta-catenin. Int J Mol Sci 2013;14:10749-60.
    • (2013) Int J Mol Sci , vol.14 , pp. 10749-10760
    • Wu, N.1    Liu, C.2    Bai, C.3    Han, Y.P.4    Cho, W.C.5    Li, Q.6
  • 96
    • 80052693126 scopus 로고    scopus 로고
    • Structure of the USP15 N-terminal domains: A beta-hairpin mediates close association between the DUSP and UBL domains
    • Harper S, Besong TM, Emsley J, Scott DJ, Dreveny I. Structure of the USP15 N-terminal domains: a beta-hairpin mediates close association between the DUSP and UBL domains. Biochem 2011;50:7995-8004.
    • (2011) Biochem , vol.50 , pp. 7995-8004
    • Harper, S.1    Besong, T.M.2    Emsley, J.3    Scott, D.J.4    Dreveny, I.5
  • 97
  • 98
    • 84858004513 scopus 로고    scopus 로고
    • USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma
    • Eichhorn PJ, Rodon L, Gonzalez-Junca A, Dirac A, Gili M, Martinez-Saez E, et al. USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma. Nat Med 2012;18:429-35.
    • (2012) Nat Med , vol.18 , pp. 429-435
    • Eichhorn, P.J.1    Rodon, L.2    Gonzalez-Junca, A.3    Dirac, A.4    Gili, M.5    Martinez-Saez, E.6
  • 100
    • 34249707437 scopus 로고    scopus 로고
    • Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin
    • Pai MT, Tzeng SR, Kovacs JJ, Keaton MA, Li SS, Yao TP, et al. Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin. J Mol Biol 2007;370:290-302.
    • (2007) J Mol Biol , vol.370 , pp. 290-302
    • Pai, M.T.1    Tzeng, S.R.2    Kovacs, J.J.3    Keaton, M.A.4    Li, S.S.5    Yao, T.P.6
  • 102
    • 77951048024 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP17 is highly expressed in tumor biopsies, is cell cycle regulated, and is required for G1-S progression
    • McFarlane C, Kelvin AA, De La Vega M, Govender U, Scott CJ, Burrows JF, et al. The deubiquitinating enzyme USP17 is highly expressed in tumor biopsies, is cell cycle regulated, and is required for G1-S progression. Cancer Res 2010;70:3329-39.
    • (2010) Cancer Res , vol.70 , pp. 3329-3339
    • McFarlane, C.1    Kelvin, A.A.2    De La Vega, M.3    Govender, U.4    Scott, C.J.5    Burrows, J.F.6
  • 103
    • 84886741837 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP17 is associated with non-small cell lung cancer (NSCLC) recurrence and metastasis
    • McFarlane C, McFarlane S, Paul I, Arthur K, Scheaff M, Kerr K, et al. The deubiquitinating enzyme USP17 is associated with non-small cell lung cancer (NSCLC) recurrence and metastasis. Oncotarget 2013;4:1836-43.
    • (2013) Oncotarget , vol.4 , pp. 1836-1843
    • McFarlane, C.1    McFarlane, S.2    Paul, I.3    Arthur, K.4    Scheaff, M.5    Kerr, K.6
  • 104
    • 34347394323 scopus 로고    scopus 로고
    • Ubp43 regulates BCR-ABL leukemogenesis via the type 1 interferon receptor signaling
    • Yan M, Luo JK, Ritchie KJ, Sakai I, Takeuchi K, Ren R, et al. Ubp43 regulates BCR-ABL leukemogenesis via the type 1 interferon receptor signaling. Blood 2007;110:305-12.
    • (2007) Blood , vol.110 , pp. 305-312
    • Yan, M.1    Luo, J.K.2    Ritchie, K.J.3    Sakai, I.4    Takeuchi, K.5    Ren, R.6
  • 105
    • 67650087753 scopus 로고    scopus 로고
    • The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates
    • Hassink GC, Zhao B, Sompallae R, Altun M, Gastaldello S, Zinin NV, et al. The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates. EMBO Rep 2009;10:755-61.
    • (2009) EMBO Rep , vol.10 , pp. 755-761
    • Hassink, G.C.1    Zhao, B.2    Sompallae, R.3    Altun, M.4    Gastaldello, S.5    Zinin, N.V.6
  • 106
    • 84896702633 scopus 로고    scopus 로고
    • Characterization of the deubiquitinating activity of USP19 and its role in endoplasmic reticulum-associated degradation
    • Lee JG, Kim W, Gygi S, Ye Y. Characterization of the deubiquitinating activity of USP19 and its role in endoplasmic reticulum-associated degradation. J Biol Chem 2014;289:3510-7.
    • (2014) J Biol Chem , vol.289 , pp. 3510-3517
    • Lee, J.G.1    Kim, W.2    Gygi, S.3    Ye, Y.4
  • 107
    • 0036290499 scopus 로고    scopus 로고
    • Identificationofa deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor
    • Li Z, Wang D, Na X, Schoen SR, Messing EM, Wu G. Identificationofa deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor. Biochem Biophys Res Commun 2002;294:700-9.
    • (2002) Biochem Biophys Res Commun , vol.294 , pp. 700-709
    • Li, Z.1    Wang, D.2    Na, X.3    Schoen, S.R.4    Messing, E.M.5    Wu, G.6
  • 108
    • 80052049291 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 20 targets TRAF6 and human T cell leukemia virus type 1 tax to negatively regulate NF-kappaB signaling
    • Yasunaga J, Lin FC, Lu X, Jeang KT. Ubiquitin-specific peptidase 20 targets TRAF6 and human T cell leukemia virus type 1 tax to negatively regulate NF-kappaB signaling. J Virol 2011;85:6212-9.
    • (2011) J Virol , vol.85 , pp. 6212-6219
    • Yasunaga, J.1    Lin, F.C.2    Lu, X.3    Jeang, K.T.4
  • 110
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitinspecific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G, Tan X, Wang H, Sun W, Shi Y, Burlingame S, et al. Ubiquitinspecific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1. J Biol Chem 2010;285:969-78.
    • (2010) J Biol Chem , vol.285 , pp. 969-978
    • Xu, G.1    Tan, X.2    Wang, H.3    Sun, W.4    Shi, Y.5    Burlingame, S.6
  • 111
    • 84899824037 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 22, a histone deubiquitinating enzyme, is a novel poor prognostic factor for salivary adenoid cystic carcinoma
    • Dai W, Yao Y, Zhou Q, Sun CF. Ubiquitin-specific peptidase 22, a histone deubiquitinating enzyme, is a novel poor prognostic factor for salivary adenoid cystic carcinoma. PLoS ONE 2014;9:e87148.
    • (2014) PLoS ONE , vol.9 , pp. e87148
    • Dai, W.1    Yao, Y.2    Zhou, Q.3    Sun, C.F.4
  • 112
    • 84894263893 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 22: A novel molecular biomarker in glioma prognosis and therapeutics
    • Liang J, Zhang X, Xie S, Zhou X, Shi Q, Hu J, et al. Ubiquitin-specific protease 22: a novel molecular biomarker in glioma prognosis and therapeutics. Med Oncol 2014;31:899.
    • (2014) Med Oncol , vol.31 , pp. 899
    • Liang, J.1    Zhang, X.2    Xie, S.3    Zhou, X.4    Shi, Q.5    Hu, J.6
  • 113
    • 84880632246 scopus 로고    scopus 로고
    • Overexpression of ubiquitin-specific protease 22 predicts poor survival in patients with early-stage non-small cell lung cancer
    • Ning J, Zhang J, Liu W, Lang Y, Xue Y, Xu S. Overexpression of ubiquitin-specific protease 22 predicts poor survival in patients with early-stage non-small cell lung cancer. Eur J Histochem 2012;56:e46.
    • (2012) Eur J Histochem , vol.56 , pp. e46
    • Ning, J.1    Zhang, J.2    Liu, W.3    Lang, Y.4    Xue, Y.5    Xu, S.6
  • 114
    • 84880074284 scopus 로고    scopus 로고
    • Increased expression of USP22 is associated with disease progression and patient prognosis of salivary duct carcinoma
    • Piao S, Ma J, Wang W, Liu Y, Zhang M, Chen H, et al. Increased expression of USP22 is associated with disease progression and patient prognosis of salivary duct carcinoma. Oral Oncol 2013;49:796-801.
    • (2013) Oral Oncol , vol.49 , pp. 796-801
    • Piao, S.1    Ma, J.2    Wang, W.3    Liu, Y.4    Zhang, M.5    Chen, H.6
  • 116
    • 84878726206 scopus 로고    scopus 로고
    • Prognostic significance of USP22 as an oncogene in papillary thyroid carcinoma
    • Wang H, Li YP, Chen JH, Yuan SF, Wang L, Zhang JL, et al. Prognostic significance of USP22 as an oncogene in papillary thyroid carcinoma. Tumour Biol 2013;34:1635-9.
    • (2013) Tumour Biol , vol.34 , pp. 1635-1639
    • Wang, H.1    Li, Y.P.2    Chen, J.H.3    Yuan, S.F.4    Wang, L.5    Zhang, J.L.6
  • 117
    • 84860750274 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation
    • Blount JR, Burr AA, Denuc A, Marfany G, Todi SV. Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation. PLoS ONE 2012;7:e36542.
    • (2012) PLoS ONE , vol.7 , pp. e36542
    • Blount, J.R.1    Burr, A.A.2    Denuc, A.3    Marfany, G.4    Todi, S.V.5
  • 118
    • 84877973388 scopus 로고    scopus 로고
    • Ubiquitinspecific protease 25 regulates TLR4-dependent innate immune responses through deubiquitination of the adaptor protein TRAF3
    • Zhong B, Liu X, Wang X, Liu X, Li H, Darnay BG, et al. Ubiquitinspecific protease 25 regulates TLR4-dependent innate immune responses through deubiquitination of the adaptor protein TRAF3. Sci Signal 2013;6: ra35.
    • (2013) Sci Signal , vol.6 , pp. ra35
    • Zhong, B.1    Liu, X.2    Wang, X.3    Liu, X.4    Li, H.5    Darnay, B.G.6
  • 119
    • 79952282523 scopus 로고    scopus 로고
    • JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress
    • Liu J, Chung HJ, Vogt M, Jin Y, Malide D, He L, et al. JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress. EMBO J 2011;30:846-58.
    • (2011) EMBO J , vol.30 , pp. 846-858
    • Liu, J.1    Chung, H.J.2    Vogt, M.3    Jin, Y.4    Malide, D.5    He, L.6
  • 122
    • 84871393383 scopus 로고    scopus 로고
    • Structural analysis of the genome of breast cancer cell line ZR-75-30 identifies twelve expressed fusion genes
    • Schulte I, Batty EM, Pole JC, Blood KA, Mo S, Cooke SL, et al. Structural analysis of the genome of breast cancer cell line ZR-75-30 identifies twelve expressed fusion genes. BMC Genomics 2012;13:719.
    • (2012) BMC Genomics , vol.13 , pp. 719
    • Schulte, I.1    Batty, E.M.2    Pole, J.C.3    Blood, K.A.4    Mo, S.5    Cooke, S.L.6
  • 123
    • 34548438569 scopus 로고    scopus 로고
    • The solution structure of the ZnF UBP domain of USP33/VDU1
    • Allen MD, Bycroft M. The solution structure of the ZnF UBP domain of USP33/VDU1. Protein Sci 2007;16:2072-5.
    • (2007) Protein Sci , vol.16 , pp. 2072-2075
    • Allen, M.D.1    Bycroft, M.2
  • 124
    • 0037085456 scopus 로고    scopus 로고
    • Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein
    • Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G. Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. J Biol Chem 2002;277:4656-62.
    • (2002) J Biol Chem , vol.277 , pp. 4656-4662
    • Li, Z.1    Na, X.2    Wang, D.3    Schoen, S.R.4    Messing, E.M.5    Wu, G.6
  • 125
    • 31444449609 scopus 로고    scopus 로고
    • A novel and cytogenetically cryptic t (7;21) (p22; q22) in acute myeloid leukemia results in fusion of RUNX1 with the ubiquitin-specific protease gene USP42
    • Paulsson K, Bekassy AN, Olofsson T, Mitelman F, Johansson B, Panagopoulos I. A novel and cytogenetically cryptic t (7;21) (p22; q22) in acute myeloid leukemia results in fusion of RUNX1 with the ubiquitin-specific protease gene USP42. Leukemia 2006;20:224-9.
    • (2006) Leukemia , vol.20 , pp. 224-229
    • Paulsson, K.1    Bekassy, A.N.2    Olofsson, T.3    Mitelman, F.4    Johansson, B.5    Panagopoulos, I.6
  • 126
    • 77957002197 scopus 로고    scopus 로고
    • A screen for deubiquitinating enzymes involved in the G (2)/M checkpoint identifies USP50 as a regulator of HSP90-dependent Wee1 stability
    • Aressy B, Jullien D, Cazales M, Marcellin M, Bugler B, Burlet-Schiltz O, et al. A screen for deubiquitinating enzymes involved in the G (2)/M checkpoint identifies USP50 as a regulator of HSP90-dependent Wee1 stability. Cell Cycle 2010;9:3815-22.
    • (2010) Cell Cycle , vol.9 , pp. 3815-3822
    • Aressy, B.1    Jullien, D.2    Cazales, M.3    Marcellin, M.4    Bugler, B.5    Burlet-Schiltz, O.6
  • 127
    • 84903536551 scopus 로고    scopus 로고
    • Dub3 controls DNA damage signalling by direct deubiquitination of H2AX
    • Delgado-Diaz MR, Martin Y, Berg A, Freire R, Smits VA. Dub3 controls DNA damage signalling by direct deubiquitination of H2AX. Mol Oncol 2014;8:884-93.
    • (2014) Mol Oncol , vol.8 , pp. 884-893
    • Delgado-Diaz, M.R.1    Martin, Y.2    Berg, A.3    Freire, R.4    Smits, V.A.5
  • 128
    • 77950517895 scopus 로고    scopus 로고
    • Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A
    • Pereg Y, Liu BY, O'Rourke KM, Sagolla M, Dey A, Komuves L, et al. Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A. Nat Cell Biol 2010;12:400-6.
    • (2010) Nat Cell Biol , vol.12 , pp. 400-406
    • Pereg, Y.1    Liu, B.Y.2    O'Rourke, K.M.3    Sagolla, M.4    Dey, A.5    Komuves, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.