메뉴 건너뛰기




Volumn 147, Issue , 2015, Pages 32-54

Deubiquitinase inhibition as a cancer therapeutic strategy

Author keywords

Apoptosis; Cancer therapeutics; Deubiquitinase; Proteasome; Small molecule inhibitors; unsaturated ketones

Indexed keywords

ALPHA,BETA DIENONE DERIVATIVE; ALPHA,BETA UNSATURATED KETONE DERIVATIVE; ANTINEOPLASTIC AGENT; CHALCONE DERIVATIVE; CYCLOPENTENONE DERIVATIVE; DEUBIQUITINASE; DEUBIQUITINASE INHIBITOR; KETONE DERIVATIVE; NATURAL PRODUCT; PROSTAGLANDIN DERIVATIVE; PROTEASOME; PROTEASOME INHIBITOR; PROTEINASE INHIBITOR; SMALL MOLECULE TRANSPORT AGENT; UNCLASSIFIED DRUG;

EID: 84922605325     PISSN: 01637258     EISSN: 1879016X     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2014.11.002     Document Type: Review
Times cited : (250)

References (329)
  • 3
    • 33947192876 scopus 로고    scopus 로고
    • Identification of actin as a 15-deoxy-Delta12,14-prostaglandin J2 target in neuroblastoma cells: Mass spectrometric, computational, and functional approaches to investigate the effect on cytoskeletal derangement
    • G. Aldini, M. Carini, G. Vistoli, T. Shibata, Y. Kusano, and L. Gamberoni Identification of actin as a 15-deoxy-Delta12,14-prostaglandin J2 target in neuroblastoma cells: mass spectrometric, computational, and functional approaches to investigate the effect on cytoskeletal derangement Biochemistry 46 2007 2707 2718
    • (2007) Biochemistry , vol.46 , pp. 2707-2718
    • Aldini, G.1    Carini, M.2    Vistoli, G.3    Shibata, T.4    Kusano, Y.5    Gamberoni, L.6
  • 4
    • 33750318889 scopus 로고    scopus 로고
    • Lipoxidation-derived reactive carbonyl species as potential drug targets in preventing protein carbonylation and related cellular dysfunction
    • G. Aldini, I. Dalle-Donne, R. Colombo, R. Maffei Facino, A. Milzani, and M. Carini Lipoxidation-derived reactive carbonyl species as potential drug targets in preventing protein carbonylation and related cellular dysfunction ChemMedChem 1 2006 1045 1058
    • (2006) ChemMedChem , vol.1 , pp. 1045-1058
    • Aldini, G.1    Dalle-Donne, I.2    Colombo, R.3    Maffei Facino, R.4    Milzani, A.5    Carini, M.6
  • 5
    • 33749482993 scopus 로고    scopus 로고
    • Identification of new compounds that trigger apoptosome-independent caspase activation and apoptosis
    • E. Aleo, C.J. Henderson, A. Fontanini, B. Solazzo, and C. Brancolini Identification of new compounds that trigger apoptosome-independent caspase activation and apoptosis Cancer Res 66 2006 9235 9244
    • (2006) Cancer Res , vol.66 , pp. 9235-9244
    • Aleo, E.1    Henderson, C.J.2    Fontanini, A.3    Solazzo, B.4    Brancolini, C.5
  • 6
    • 79960738330 scopus 로고    scopus 로고
    • Eeyarestatin 1 interferes with both retrograde and anterograde intracellular trafficking pathways
    • M.O. Aletrari, C. McKibbin, H. Williams, V. Pawar, P. Pietroni, and J.M. Lord Eeyarestatin 1 interferes with both retrograde and anterograde intracellular trafficking pathways PLoS One 6 2011 e22713
    • (2011) PLoS One , vol.6 , pp. e22713
    • Aletrari, M.O.1    McKibbin, C.2    Williams, H.3    Pawar, V.4    Pietroni, P.5    Lord, J.M.6
  • 7
    • 77952548140 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy
    • N. Allende-Vega, and M.K. Saville Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy Semin Cancer Biol 20 2010 29 39
    • (2010) Semin Cancer Biol , vol.20 , pp. 29-39
    • Allende-Vega, N.1    Saville, M.K.2
  • 8
    • 75149174149 scopus 로고    scopus 로고
    • MdmX is a substrate for the deubiquitinating enzyme USP2a
    • N. Allende-Vega, A. Sparks, D.P. Lane, and M.K. Saville MdmX is a substrate for the deubiquitinating enzyme USP2a Oncogene 29 2010 432 441
    • (2010) Oncogene , vol.29 , pp. 432-441
    • Allende-Vega, N.1    Sparks, A.2    Lane, D.P.3    Saville, M.K.4
  • 9
  • 10
    • 82255181181 scopus 로고    scopus 로고
    • Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes
    • M. Altun, H.B. Kramer, L.I. Willems, J.L. McDermott, C.A. Leach, and S.J. Goldenberg Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes Chem Biol 18 2011 1401 1412
    • (2011) Chem Biol , vol.18 , pp. 1401-1412
    • Altun, M.1    Kramer, H.B.2    Willems, L.I.3    McDermott, J.L.4    Leach, C.A.5    Goldenberg, S.J.6
  • 11
    • 84862973169 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia
    • M. Altun, B. Zhao, K. Velasco, H. Liu, G. Hassink, and J. Paschke Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia J Biol Chem 287 2012 1962 1969
    • (2012) J Biol Chem , vol.287 , pp. 1962-1969
    • Altun, M.1    Zhao, B.2    Velasco, K.3    Liu, H.4    Hassink, G.5    Paschke, J.6
  • 12
    • 33847254975 scopus 로고    scopus 로고
    • UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation
    • H.A. Alwan, and J.E. van Leeuwen UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation J Biol Chem 282 2007 1658 1669
    • (2007) J Biol Chem , vol.282 , pp. 1658-1669
    • Alwan, H.A.1    Van Leeuwen, J.E.2
  • 13
    • 0041816011 scopus 로고    scopus 로고
    • Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination
    • H.A. Alwan, E.J. van Zoelen, and J.E. van Leeuwen Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination J Biol Chem 278 2003 35781 35790
    • (2003) J Biol Chem , vol.278 , pp. 35781-35790
    • Alwan, H.A.1    Van Zoelen, E.J.2    Van Leeuwen, J.E.3
  • 14
    • 19344364762 scopus 로고    scopus 로고
    • JAMM: A metalloprotease-like zinc site in the proteasome and signalosome
    • X.I. Ambroggio, D.C. Rees, and R.J. Deshaies JAMM: a metalloprotease-like zinc site in the proteasome and signalosome PLoS Biol 2 2004 E2
    • (2004) PLoS Biol , vol.2 , pp. E2
    • Ambroggio, X.I.1    Rees, D.C.2    Deshaies, R.J.3
  • 15
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • A. Amerik, S. Swaminathan, B.A. Krantz, K.D. Wilkinson, and M. Hochstrasser In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome EMBO J 16 1997 4826 4838
    • (1997) EMBO J , vol.16 , pp. 4826-4838
    • Amerik, A.1    Swaminathan, S.2    Krantz, B.A.3    Wilkinson, K.D.4    Hochstrasser, M.5
  • 16
    • 77249145461 scopus 로고    scopus 로고
    • The tunable functionality of alpha, beta-unsaturated carbonyl compounds enables their differential application in biological systems
    • S. Amslinger The tunable functionality of alpha, beta-unsaturated carbonyl compounds enables their differential application in biological systems ChemMedChem 5 2010 351 356
    • (2010) ChemMedChem , vol.5 , pp. 351-356
    • Amslinger, S.1
  • 18
    • 80052332555 scopus 로고    scopus 로고
    • Stressing the ubiquitin-proteasome system without 20S proteolytic inhibition selectively kills cervical cancer cells
    • R.K. Anchoori, S.R. Khan, T. Sueblinvong, A. Felthauser, Y. Iizuka, and R. Gavioli Stressing the ubiquitin-proteasome system without 20S proteolytic inhibition selectively kills cervical cancer cells PLoS One 6 2011 e23888
    • (2011) PLoS One , vol.6 , pp. e23888
    • Anchoori, R.K.1    Khan, S.R.2    Sueblinvong, T.3    Felthauser, A.4    Iizuka, Y.5    Gavioli, R.6
  • 19
    • 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
    • B. Aressy, D. Jullien, M. Cazales, M. Marcellin, B. Bugler, and O. Burlet-Schiltz A screen for deubiquitinating enzymes involved in the G(2)/M checkpoint identifies USP50 as a regulator of HSP90-dependent Wee1 stability Cell Cycle 9 2010 3815 3822
    • (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
  • 20
    • 0038449224 scopus 로고    scopus 로고
    • Otubains: A new family of cysteine proteases in the ubiquitin pathway
    • M.Y. Balakirev, S.O. Tcherniuk, M. Jaquinod, and J. Chroboczek Otubains: a new family of cysteine proteases in the ubiquitin pathway EMBO Rep 4 2003 517 522
    • (2003) EMBO Rep , vol.4 , pp. 517-522
    • Balakirev, M.Y.1    Tcherniuk, S.O.2    Jaquinod, M.3    Chroboczek, J.4
  • 21
    • 60549090636 scopus 로고    scopus 로고
    • Induction of the lysosomal apoptosis pathway by inhibitors of the ubiquitin-proteasome system
    • M. Berndtsson, M. Beaujouin, L. Rickardson, A.M. Havelka, R. Larsson, and J. Westman Induction of the lysosomal apoptosis pathway by inhibitors of the ubiquitin-proteasome system Int J Cancer 124 2009 1463 1469
    • (2009) Int J Cancer , vol.124 , pp. 1463-1469
    • Berndtsson, M.1    Beaujouin, M.2    Rickardson, L.3    Havelka, A.M.4    Larsson, R.5    Westman, J.6
  • 23
    • 84860750274 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation
    • J.R. Blount, A.A. Burr, A. Denuc, G. Marfany, and S.V. Todi Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation PLoS One 7 2012 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
  • 25
    • 33645735557 scopus 로고    scopus 로고
    • An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis
    • A. Boeddrich, S. Gaumer, A. Haacke, N. Tzvetkov, M. Albrecht, and B.O. Evert An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis EMBO J 25 2006 1547 1558
    • (2006) EMBO J , vol.25 , pp. 1547-1558
    • Boeddrich, A.1    Gaumer, S.2    Haacke, A.3    Tzvetkov, N.4    Albrecht, M.5    Evert, B.O.6
  • 27
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • A. Borodovsky, B.M. Kessler, R. Casagrande, H.S. Overkleeft, K.D. Wilkinson, and H.L. Ploegh A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14 EMBO J 20 2001 5187 5196
    • (2001) EMBO J , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 28
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • A. Borodovsky, H. Ovaa, N. Kolli, T. Gan-Erdene, K.D. Wilkinson, and H.L. Ploegh Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family Chem Biol 9 2002 1149 1159
    • (2002) Chem Biol , vol.9 , pp. 1149-1159
    • Borodovsky, A.1    Ovaa, H.2    Kolli, N.3    Gan-Erdene, T.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 29
    • 79959694149 scopus 로고    scopus 로고
    • The nuclear deubiquitinase BAP1 is commonly inactivated by somatic mutations and 3p21.1 losses in malignant pleural mesothelioma
    • M. Bott, M. Brevet, B.S. Taylor, S. Shimizu, T. Ito, and L. Wang The nuclear deubiquitinase BAP1 is commonly inactivated by somatic mutations and 3p21.1 losses in malignant pleural mesothelioma Nat Genet 43 2011 668 672
    • (2011) Nat Genet , vol.43 , pp. 668-672
    • Bott, M.1    Brevet, M.2    Taylor, B.S.3    Shimizu, S.4    Ito, T.5    Wang, L.6
  • 30
    • 84912529600 scopus 로고    scopus 로고
    • Induction of tumor cell apoptosis by a proteasome deubiquitinase inhibitor is associated with oxidative stress
    • (EPub Oct 17)
    • S. Brnjic, M. Mazurkiewicz, M. Fryknas, C. Sun, X. Zhang, and R. Larsson Induction of tumor cell apoptosis by a proteasome deubiquitinase inhibitor is associated with oxidative stress Antioxid Redox Signal 17 2013 (EPub Oct 17)
    • (2013) Antioxid Redox Signal , vol.17
    • Brnjic, S.1    Mazurkiewicz, M.2    Fryknas, M.3    Sun, C.4    Zhang, X.5    Larsson, R.6
  • 31
    • 0028241636 scopus 로고
    • Homozygous deletion, rearrangement and hypermethylation implicate chromosome region 3p14.3-3p21.3 in sporadic breast-cancer development
    • D.L. Buchhagen, L. Qiu, and P. Etkind Homozygous deletion, rearrangement and hypermethylation implicate chromosome region 3p14.3-3p21.3 in sporadic breast-cancer development Int J Cancer 57 1994 473 479
    • (1994) Int J Cancer , vol.57 , pp. 473-479
    • Buchhagen, D.L.1    Qiu, L.2    Etkind, P.3
  • 32
    • 84894414494 scopus 로고    scopus 로고
    • Small-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome system
    • D.L. Buckley, and C.M. Crews Small-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome system Angew Chem Int Ed Engl 53 2014 2312 2330
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 2312-2330
    • Buckley, D.L.1    Crews, C.M.2
  • 33
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • B.G. Burnett, and R.N. Pittman The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation Proc Natl Acad Sci U S A 102 2005 4330 4335
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 35
    • 69949173205 scopus 로고    scopus 로고
    • Deubiquitinase activities required for hepatocyte growth factor-induced scattering of epithelial cells
    • R. Buus, M. Faronato, D.E. Hammond, S. Urbe, and M.J. Clague Deubiquitinase activities required for hepatocyte growth factor-induced scattering of epithelial cells Curr Biol 19 2009 1463 1466
    • (2009) Curr Biol , vol.19 , pp. 1463-1466
    • Buus, R.1    Faronato, M.2    Hammond, D.E.3    Urbe, S.4    Clague, M.J.5
  • 36
    • 84881137952 scopus 로고    scopus 로고
    • USP8 is a novel target for overcoming gefitinib resistance in lung cancer
    • S. Byun, S.Y. Lee, J. Lee, C.H. Jeong, L. Farrand, and S. Lim USP8 is a novel target for overcoming gefitinib resistance in lung cancer Clin Cancer Res 19 2013 3894 3904
    • (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
  • 37
    • 0033020726 scopus 로고    scopus 로고
    • A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division
    • S.Y. Cai, R.W. Babbitt, and V.T. Marchesi A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division Proc Natl Acad Sci U S A 96 1999 2828 2833
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2828-2833
    • Cai, S.Y.1    Babbitt, R.W.2    Marchesi, V.T.3
  • 38
    • 33947245587 scopus 로고    scopus 로고
    • Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1
    • Z. Cao, X. Wu, L. Yen, C. Sweeney, and K.L. Carraway III Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1 Mol Cell Biol 27 2007 2180 2188
    • (2007) Mol Cell Biol , vol.27 , pp. 2180-2188
    • Cao, Z.1    Wu, X.2    Yen, L.3    Sweeney, C.4    Carraway, K.L.5
  • 39
    • 84905262407 scopus 로고    scopus 로고
    • A putative OTU domain-containing protein 1 deubiquitinating enzyme is differentially expressed in thyroid cancer and identifies less-aggressive tumours
    • A.P. Carneiro, C.F. Reis, E.C. Morari, Y.C. Maia, R. Nascimento, and J.M. Bonatto A putative OTU domain-containing protein 1 deubiquitinating enzyme is differentially expressed in thyroid cancer and identifies less-aggressive tumours Br J Cancer 111 2014 551 558
    • (2014) Br J Cancer , vol.111 , pp. 551-558
    • Carneiro, A.P.1    Reis, C.F.2    Morari, E.C.3    Maia, Y.C.4    Nascimento, R.5    Bonatto, J.M.6
  • 40
    • 33845289459 scopus 로고    scopus 로고
    • Up-regulation of expression of the ubiquitin carboxyl-terminal hydrolase L1 gene in human airway epithelium of cigarette smokers
    • B.J. Carolan, A. Heguy, B.G. Harvey, P.L. Leopold, B. Ferris, and R.G. Crystal Up-regulation of expression of the ubiquitin carboxyl-terminal hydrolase L1 gene in human airway epithelium of cigarette smokers Cancer Res 66 2006 10729 10740
    • (2006) Cancer Res , vol.66 , pp. 10729-10740
    • Carolan, B.J.1    Heguy, A.2    Harvey, B.G.3    Leopold, P.L.4    Ferris, B.5    Crystal, R.G.6
  • 41
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • V. Chau, J.W. Tobias, A. Bachmair, D. Marriott, D.J. Ecker, and D.K. Gonda A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein Science 243 1989 1576 1583
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6
  • 42
    • 84866021069 scopus 로고    scopus 로고
    • A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance
    • D. Chauhan, Z. Tian, B. Nicholson, K.G. Kumar, B. Zhou, and R. Carrasco A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance Cancer Cell 22 2012 345 358
    • (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
  • 43
    • 33744944054 scopus 로고    scopus 로고
    • BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation
    • X. Chen, C.A. Arciero, C. Wang, D. Broccoli, and A.K. Godwin BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation Cancer Res 66 2006 5039 5046
    • (2006) Cancer Res , vol.66 , pp. 5039-5046
    • Chen, X.1    Arciero, C.A.2    Wang, C.3    Broccoli, D.4    Godwin, A.K.5
  • 44
    • 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
    • J. Chen, T.S. Dexheimer, Y. Ai, Q. Liang, M.A. Villamil, and J. Inglese Selective and cell-active inhibitors of the USP1/ UAF1 deubiquitinase complex reverse cisplatin resistance in non-small cell lung cancer cells Chem Biol 18 2011 1390 1400
    • (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
  • 45
    • 0036745763 scopus 로고    scopus 로고
    • CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells
    • Z. Chen, V.B. Indjeian, M. McManus, L. Wang, and B.D. Dynlacht CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells Dev Cell 3 2002 339 350
    • (2002) Dev Cell , vol.3 , pp. 339-350
    • Chen, Z.1    Indjeian, V.B.2    McManus, M.3    Wang, L.4    Dynlacht, B.D.5
  • 46
    • 0035992398 scopus 로고    scopus 로고
    • Proteomic analysis of lung adenocarcinoma: Identification of a highly expressed set of proteins in tumors
    • G. Chen, T.G. Gharib, C.C. Huang, D.G. Thomas, K.A. Shedden, and J.M. Taylor Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors Clin Cancer Res 8 2002 2298 2305
    • (2002) Clin Cancer Res , vol.8 , pp. 2298-2305
    • Chen, G.1    Gharib, T.G.2    Huang, C.C.3    Thomas, D.G.4    Shedden, K.A.5    Taylor, J.M.6
  • 47
    • 46449099079 scopus 로고    scopus 로고
    • Microtubule depolymerization and phosphorylation of c-Jun N-terminal kinase-1 and p38 were involved in gambogic acid induced cell cycle arrest and apoptosis in human breast carcinoma MCF-7 cells
    • J. Chen, H.Y. Gu, N. Lu, Y. Yang, W. Liu, and Q. Qi Microtubule depolymerization and phosphorylation of c-Jun N-terminal kinase-1 and p38 were involved in gambogic acid induced cell cycle arrest and apoptosis in human breast carcinoma MCF-7 cells Life Sci 83 2008 103 109
    • (2008) Life Sci , vol.83 , pp. 103-109
    • Chen, J.1    Gu, H.Y.2    Lu, N.3    Yang, Y.4    Liu, W.5    Qi, Q.6
  • 48
    • 69749110327 scopus 로고    scopus 로고
    • The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions
    • P.C. Chen, L.N. Qin, X.M. Li, B.J. Walters, J.A. Wilson, and L. Mei The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions J Neurosci 29 2009 10909 10919
    • (2009) J Neurosci , vol.29 , pp. 10909-10919
    • Chen, P.C.1    Qin, L.N.2    Li, X.M.3    Walters, B.J.4    Wilson, J.A.5    Mei, L.6
  • 49
    • 77955710477 scopus 로고    scopus 로고
    • The ubiquitin-specific protease 17 is involved in virus-triggered type i IFN signaling
    • R. Chen, L. Zhang, B. Zhong, B. Tan, Y. Liu, and H.B. Shu The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling Cell Res 20 2010 802 811
    • (2010) Cell Res , vol.20 , pp. 802-811
    • Chen, R.1    Zhang, L.2    Zhong, B.3    Tan, B.4    Liu, Y.5    Shu, H.B.6
  • 50
    • 77449131731 scopus 로고    scopus 로고
    • Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase
    • M. Cholay, C. Reverdy, R. Benarous, F. Colland, and L. Daviet Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase Exp Cell Res 316 2010 667 675
    • (2010) Exp Cell Res , vol.316 , pp. 667-675
    • Cholay, M.1    Reverdy, C.2    Benarous, R.3    Colland, F.4    Daviet, L.5
  • 51
    • 0033643742 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mode of action and clinical implications
    • A. Ciechanover, A. Orian, and A.L. Schwartz The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications J Cell Biochem Suppl 34 2000 40 51
    • (2000) J Cell Biochem Suppl , vol.34 , pp. 40-51
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 53
    • 84922591036 scopus 로고    scopus 로고
    • Ubiquitination and cancer: Histone H2B monoubiquitination - Roles to play in human malignancy
    • (EPub June 2)
    • A.J. Cole, R.J. Clifton-Bligh, and D.J. Marsh Ubiquitination and cancer: histone H2B monoubiquitination - roles to play in human malignancy Endocr Relat Cancer 2014 (EPub June 2)
    • (2014) Endocr Relat Cancer
    • Cole, A.J.1    Clifton-Bligh, R.J.2    Marsh, D.J.3
  • 54
    • 68849126660 scopus 로고    scopus 로고
    • Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells
    • F. Colland, E. Formstecher, X. Jacq, C. Reverdy, C. Planquette, and S. Conrath Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells Mol Cancer Ther 8 2009 2286 2295
    • (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
  • 55
    • 77950678464 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 9-oxo-9H-indeno[1,2-b]pyrazine-2,3-dicarbonitrile analogues as potential inhibitors of deubiquitinating enzymes
    • M. Colombo, S. Vallese, I. Peretto, X. Jacq, J.C. Rain, and F. Colland Synthesis and biological evaluation of 9-oxo-9H-indeno[1,2-b]pyrazine-2,3-dicarbonitrile analogues as potential inhibitors of deubiquitinating enzymes ChemMedChem 5 2010 552 558
    • (2010) ChemMedChem , vol.5 , pp. 552-558
    • Colombo, M.1    Vallese, S.2    Peretto, I.3    Jacq, X.4    Rain, J.C.5    Colland, F.6
  • 56
    • 17144423926 scopus 로고    scopus 로고
    • Studies on the reactivity of CDDO, a promising new chemopreventive and chemotherapeutic agent: Implications for a molecular mechanism of action
    • R.D. Couch, R.G. Browning, T. Honda, G.W. Gribble, D.L. Wright, and M.B. Sporn Studies on the reactivity of CDDO, a promising new chemopreventive and chemotherapeutic agent: implications for a molecular mechanism of action Bioorg Med Chem Lett 15 2005 2215 2219
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 2215-2219
    • Couch, R.D.1    Browning, R.G.2    Honda, T.3    Gribble, G.W.4    Wright, D.L.5    Sporn, M.B.6
  • 57
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • O. Coux, K. Tanaka, and A.L. Goldberg Structure and functions of the 20S and 26S proteasomes Annu Rev Biochem 65 1996 801 847
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 58
    • 70849133790 scopus 로고    scopus 로고
    • Eeyarestatin i inhibits Sec61-mediated protein translocation at the endoplasmic reticulum
    • B.C. Cross, C. McKibbin, A.C. Callan, P. Roboti, M. Piacenti, and C. Rabu Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum J Cell Sci 122 2009 4393 4400
    • (2009) J Cell Sci , vol.122 , pp. 4393-4400
    • Cross, B.C.1    McKibbin, C.2    Callan, A.C.3    Roboti, P.4    Piacenti, M.5    Rabu, C.6
  • 59
    • 84898040489 scopus 로고    scopus 로고
    • USP3 inhibits type i interferon signaling by deubiquitinating RIG-I-like receptors
    • J. Cui, Y. Song, Y. Li, Q. Zhu, P. Tan, and Y. Qin USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors Cell Res 24 2014 400 416
    • (2014) Cell Res , vol.24 , pp. 400-416
    • Cui, J.1    Song, Y.2    Li, Y.3    Zhu, Q.4    Tan, P.5    Qin, Y.6
  • 61
    • 85047690484 scopus 로고    scopus 로고
    • Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation
    • C. Curcio-Morelli, A.M. Zavacki, M. Christofollete, B. Gereben, B.C. de Freitas, and J.W. Harney Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation J Clin Invest 112 2003 189 196
    • (2003) J Clin Invest , vol.112 , pp. 189-196
    • Curcio-Morelli, C.1    Zavacki, A.M.2    Christofollete, M.3    Gereben, B.4    De Freitas, B.C.5    Harney, J.W.6
  • 62
    • 84858035855 scopus 로고    scopus 로고
    • Shotgun proteomics and network analysis of neuroblastoma cell lines treated with curcumin
    • S. D'Aguanno, I. D'Agnano, M. De Canio, C. Rossi, S. Bernardini, and G. Federici Shotgun proteomics and network analysis of neuroblastoma cell lines treated with curcumin Mol Biosyst 8 2012 1068 1077
    • (2012) Mol Biosyst , vol.8 , pp. 1068-1077
    • D'Aguanno, S.1    D'Agnano, I.2    De Canio, M.3    Rossi, C.4    Bernardini, S.5    Federici, G.6
  • 65
    • 64149087218 scopus 로고    scopus 로고
    • Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53
    • S. Dayal, A. Sparks, J. Jacob, N. Allende-Vega, D.P. Lane, and M.K. Saville Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53 J Biol Chem 284 2009 5030 5041
    • (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
  • 66
    • 79953235713 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility
    • M. de la Vega, A.A. Kelvin, D.J. Dunican, C. McFarlane, J.F. Burrows, and J. Jaworski The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility Nat Commun 2 2011 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
  • 67
    • 0028848212 scopus 로고
    • Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats
    • Q. Deveraux, C. Jensen, and M. Rechsteiner Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats J Biol Chem 270 1995 23726 23729
    • (1995) J Biol Chem , vol.270 , pp. 23726-23729
    • Deveraux, Q.1    Jensen, C.2    Rechsteiner, M.3
  • 69
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signalling connection
    • P.P. Di Fiore, S. Polo, and K. Hofmann When ubiquitin meets ubiquitin receptors: a signalling connection Nat Rev Mol Cell Biol 4 2003 491 497
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 72
    • 79952730520 scopus 로고    scopus 로고
    • A20, ABIN-1/2, and CARD11 mutations and their prognostic value in gastrointestinal diffuse large B-cell lymphoma
    • G. Dong, E. Chanudet, N. Zeng, A. Appert, Y.W. Chen, and W.Y. Au A20, ABIN-1/2, and CARD11 mutations and their prognostic value in gastrointestinal diffuse large B-cell lymphoma Clin Cancer Res 17 2011 1440 1451
    • (2011) Clin Cancer Res , vol.17 , pp. 1440-1451
    • Dong, G.1    Chanudet, E.2    Zeng, N.3    Appert, A.4    Chen, Y.W.5    Au, W.Y.6
  • 73
    • 0345276495 scopus 로고    scopus 로고
    • Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair
    • Y. Dong, M.A. Hakimi, X. Chen, E. Kumaraswamy, N.S. Cooch, and A.K. Godwin Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair Mol Cell 12 2003 1087 1099
    • (2003) Mol Cell , vol.12 , pp. 1087-1099
    • Dong, Y.1    Hakimi, M.A.2    Chen, X.3    Kumaraswamy, E.4    Cooch, N.S.5    Godwin, A.K.6
  • 74
    • 79955985329 scopus 로고    scopus 로고
    • USP10 deubiquitylates the histone variant H2A.Z and both are required for androgen receptor-mediated gene activation
    • R. Draker, E. Sarcinella, and P. Cheung USP10 deubiquitylates the histone variant H2A.Z and both are required for androgen receptor-mediated gene activation Nucleic Acids Res 39 2011 3529 3542
    • (2011) Nucleic Acids Res , vol.39 , pp. 3529-3542
    • Draker, R.1    Sarcinella, E.2    Cheung, P.3
  • 75
    • 58149093172 scopus 로고    scopus 로고
    • FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination
    • S. Dupont, A. Mamidi, M. Cordenonsi, M. Montagner, L. Zacchigna, and M. Adorno FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination Cell 136 2009 123 135
    • (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
  • 76
    • 0041998173 scopus 로고    scopus 로고
    • Differential expression and function of A20 and TRAF1 in Hodgkin lymphoma and anaplastic large cell lymphoma and their induction by CD30 stimulation
    • H. Durkop, B. Hirsch, C. Hahn, H.D. Foss, and H. Stein Differential expression and function of A20 and TRAF1 in Hodgkin lymphoma and anaplastic large cell lymphoma and their induction by CD30 stimulation J Pathol 200 2003 229 239
    • (2003) J Pathol , vol.200 , pp. 229-239
    • Durkop, H.1    Hirsch, B.2    Hahn, C.3    Foss, H.D.4    Stein, H.5
  • 77
    • 84857085837 scopus 로고    scopus 로고
    • Pharmacological targets in the ubiquitin system offer new ways of treating cancer, neurodegenerative disorders and infectious diseases
    • M.J. Edelmann, B. Nicholson, and B.M. Kessler Pharmacological targets in the ubiquitin system offer new ways of treating cancer, neurodegenerative disorders and infectious diseases Expert Rev Mol Med 13 2011 e35
    • (2011) Expert Rev Mol Med , vol.13 , pp. e35
    • Edelmann, M.J.1    Nicholson, B.2    Kessler, B.M.3
  • 78
    • 84858004513 scopus 로고    scopus 로고
    • USP15 stabilizes TGF-beta receptor i and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma
    • P.J. Eichhorn, L. Rodon, A. Gonzalez-Junca, A. Dirac, M. Gili, and E. Martinez-Saez USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma Nat Med 18 2012 429 435
    • (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
  • 79
    • 84890190983 scopus 로고    scopus 로고
    • Regulation of proteolysis by human deubiquitinating enzymes
    • Z.M. Eletr, and K.D. Wilkinson Regulation of proteolysis by human deubiquitinating enzymes Biochim Biophys Acta 1843 2014 114 128
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 114-128
    • Eletr, Z.M.1    Wilkinson, K.D.2
  • 80
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • S. Elsasser, D. Chandler-Militello, B. Muller, J. Hanna, and D. Finley Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome J Biol Chem 279 2004 26817 26822
    • (2004) J Biol Chem , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 81
    • 43749122598 scopus 로고    scopus 로고
    • NF-kappaB suppression by the deubiquitinating enzyme Cezanne: A novel negative feedback loop in pro-inflammatory signaling
    • K. Enesa, M. Zakkar, H. Chaudhury, A. Luong le, L. Rawlinson, and J.C. Mason NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling J Biol Chem 283 2008 7036 7045
    • (2008) J Biol Chem , vol.283 , pp. 7036-7045
    • Enesa, K.1    Zakkar, M.2    Chaudhury, H.3    Luong Le, A.4    Rawlinson, L.5    Mason, J.C.6
  • 82
    • 84861553163 scopus 로고    scopus 로고
    • Functional asymmetries of proteasome translocase pore
    • J. Erales, M.A. Hoyt, F. Troll, and P. Coffino Functional asymmetries of proteasome translocase pore J Biol Chem 287 2012 18535 18543
    • (2012) J Biol Chem , vol.287 , pp. 18535-18543
    • Erales, J.1    Hoyt, M.A.2    Troll, F.3    Coffino, P.4
  • 83
    • 11844294713 scopus 로고    scopus 로고
    • Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis
    • H. Erdal, M. Berndtsson, J. Castro, U. Brunk, M.C. Shoshan, and S. Linder Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis Proc Natl Acad Sci U S A 102 2005 192 197
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 192-197
    • Erdal, H.1    Berndtsson, M.2    Castro, J.3    Brunk, U.4    Shoshan, M.C.5    Linder, S.6
  • 85
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • R.D. Everett, M. Meredith, A. Orr, A. Cross, M. Kathoria, and J. Parkinson A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein EMBO J 16 1997 1519 1530
    • (1997) EMBO J , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 86
    • 21644477778 scopus 로고    scopus 로고
    • Thioredoxin reductase is irreversibly modified by curcumin: A novel molecular mechanism for its anticancer activity
    • J. Fang, J. Lu, and A. Holmgren Thioredoxin reductase is irreversibly modified by curcumin: a novel molecular mechanism for its anticancer activity J Biol Chem 280 2005 25284 25290
    • (2005) J Biol Chem , vol.280 , pp. 25284-25290
    • Fang, J.1    Lu, J.2    Holmgren, A.3
  • 87
    • 84925960491 scopus 로고    scopus 로고
    • Haploinsufficiency of XPO1 and USP34 by a de novo 230 kb deletion in 2p15, in a patient with mild intellectual disability and cranio-facial dysmorphisms
    • M. Fannemel, T. Baroy, A. Holmgren, O.K. Rodningen, T.M. Haugsand, and B. Hansen Haploinsufficiency of XPO1 and USP34 by a de novo 230 kb deletion in 2p15, in a patient with mild intellectual disability and cranio-facial dysmorphisms Eur J Med Genet 57 2014 513 519
    • (2014) Eur J Med Genet , vol.57 , pp. 513-519
    • Fannemel, M.1    Baroy, T.2    Holmgren, A.3    Rodningen, O.K.4    Haugsand, T.M.5    Hansen, B.6
  • 88
    • 77956987105 scopus 로고    scopus 로고
    • Silencing of the UCHL1 gene in giant cell tumors of bone
    • J. Fellenberg, B. Lehner, and D. Witte Silencing of the UCHL1 gene in giant cell tumors of bone Int J Cancer 127 2010 1804 1812
    • (2010) Int J Cancer , vol.127 , pp. 1804-1812
    • Fellenberg, J.1    Lehner, B.2    Witte, D.3
  • 89
    • 84879116556 scopus 로고    scopus 로고
    • Gambogic acid is cytotoxic to cancer cells through inhibition of the ubiquitin-proteasome system
    • J. Felth, K. Lesiak-Mieczkowska, P. D'Arcy, C. Haglund, J. Gullbo, and R. Larsson Gambogic acid is cytotoxic to cancer cells through inhibition of the ubiquitin-proteasome system Invest New Drugs 31 2013 587 598
    • (2013) Invest New Drugs , vol.31 , pp. 587-598
    • Felth, J.1    Lesiak-Mieczkowska, K.2    D'Arcy, P.3    Haglund, C.4    Gullbo, J.5    Larsson, R.6
  • 90
    • 1642505493 scopus 로고    scopus 로고
    • Dissection of the dislocation pathway for type i membrane proteins with a new small molecule inhibitor, eeyarestatin
    • E. Fiebiger, C. Hirsch, J.M. Vyas, E. Gordon, H.L. Ploegh, and D. Tortorella Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin Mol Biol Cell 15 2004 1635 1646
    • (2004) Mol Biol Cell , vol.15 , pp. 1635-1646
    • Fiebiger, E.1    Hirsch, C.2    Vyas, J.M.3    Gordon, E.4    Ploegh, H.L.5    Tortorella, D.6
  • 91
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • D. Finley Recognition and processing of ubiquitin-protein conjugates by the proteasome Annu Rev Biochem 78 2009 477 513
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 92
    • 0027087073 scopus 로고
    • The fat facets gene is required for Drosophila eye and embryo development
    • J.A. Fischer-Vize, G.M. Rubin, and R. Lehmann The fat facets gene is required for Drosophila eye and embryo development Development 116 1992 985 1000
    • (1992) Development , vol.116 , pp. 985-1000
    • Fischer-Vize, J.A.1    Rubin, G.M.2    Lehmann, R.3
  • 93
    • 0020501863 scopus 로고
    • Albumin-catalyzed metabolism of prostaglandin D2. Identification of products formed in vitro
    • F.A. Fitzpatrick, and M.A. Wynalda Albumin-catalyzed metabolism of prostaglandin D2. Identification of products formed in vitro J Biol Chem 258 1983 11713 11718
    • (1983) J Biol Chem , vol.258 , pp. 11713-11718
    • Fitzpatrick, F.A.1    Wynalda, M.A.2
  • 94
    • 84856604061 scopus 로고    scopus 로고
    • GSK-3beta regulates cell growth, migration, and angiogenesis via Fbw7 and USP28-dependent degradation of HIF-1alpha
    • D. Flugel, A. Gorlach, and T. Kietzmann GSK-3beta regulates cell growth, migration, and angiogenesis via Fbw7 and USP28-dependent degradation of HIF-1alpha Blood 119 2012 1292 1301
    • (2012) Blood , vol.119 , pp. 1292-1301
    • Flugel, D.1    Gorlach, A.2    Kietzmann, T.3
  • 95
    • 66349117098 scopus 로고    scopus 로고
    • The isopeptidase inhibitor G5 triggers a caspase-independent necrotic death in cells resistant to apoptosis: A comparative study with the proteasome inhibitor bortezomib
    • A. Fontanini, C. Foti, H. Potu, E. Crivellato, R. Maestro, and P. Bernardi The isopeptidase inhibitor G5 triggers a caspase-independent necrotic death in cells resistant to apoptosis: a comparative study with the proteasome inhibitor bortezomib J Biol Chem 284 2009 8369 8381
    • (2009) J Biol Chem , vol.284 , pp. 8369-8381
    • Fontanini, A.1    Foti, C.2    Potu, H.3    Crivellato, E.4    Maestro, R.5    Bernardi, P.6
  • 96
    • 84901418451 scopus 로고    scopus 로고
    • Network analyses reveal pervasive functional regulation between proteases in the human protease web
    • N. Fortelny, J.H. Cox, R. Kappelhoff, A.E. Starr, P.F. Lange, and P. Pavlidis Network analyses reveal pervasive functional regulation between proteases in the human protease web PLoS Biol 12 2014 e1001869
    • (2014) PLoS Biol , vol.12 , pp. e1001869
    • Fortelny, N.1    Cox, J.H.2    Kappelhoff, R.3    Starr, A.E.4    Lange, P.F.5    Pavlidis, P.6
  • 98
    • 84861968321 scopus 로고    scopus 로고
    • RNF20 and USP44 regulate stem cell differentiation by modulating H2B monoubiquitylation
    • G. Fuchs, E. Shema, R. Vesterman, E. Kotler, Z. Wolchinsky, and S. Wilder RNF20 and USP44 regulate stem cell differentiation by modulating H2B monoubiquitylation Mol Cell 46 2012 662 673
    • (2012) Mol Cell , vol.46 , pp. 662-673
    • Fuchs, G.1    Shema, E.2    Vesterman, R.3    Kotler, E.4    Wolchinsky, Z.5    Wilder, S.6
  • 99
    • 36249026236 scopus 로고    scopus 로고
    • Identification of methylation-silenced genes in colorectal cancer cell lines: Genomic screening using oligonucleotide arrays
    • S. Fukutomi, N. Seki, K. Koda, and M. Miyazaki Identification of methylation-silenced genes in colorectal cancer cell lines: genomic screening using oligonucleotide arrays Scand J Gastroenterol 42 2007 1486 1494
    • (2007) Scand J Gastroenterol , vol.42 , pp. 1486-1494
    • Fukutomi, S.1    Seki, N.2    Koda, K.3    Miyazaki, M.4
  • 100
    • 0032545386 scopus 로고    scopus 로고
    • Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid
    • S. Fulda, C. Scaffidi, S.A. Susin, P.H. Krammer, G. Kroemer, and M.E. Peter Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid J Biol Chem 273 1998 33942 33948
    • (1998) J Biol Chem , vol.273 , pp. 33942-33948
    • Fulda, S.1    Scaffidi, C.2    Susin, S.A.3    Krammer, P.H.4    Kroemer, G.5    Peter, M.E.6
  • 102
    • 34047273206 scopus 로고    scopus 로고
    • Novel n-3 fatty acid oxidation products activate Nrf2 by destabilizing the association between Keap1 and Cullin3
    • L. Gao, J. Wang, K.R. Sekhar, H. Yin, N.F. Yared, and S.N. Schneider Novel n-3 fatty acid oxidation products activate Nrf2 by destabilizing the association between Keap1 and Cullin3 J Biol Chem 282 2007 2529 2537
    • (2007) J Biol Chem , vol.282 , pp. 2529-2537
    • Gao, L.1    Wang, J.2    Sekhar, K.R.3    Yin, H.4    Yared, N.F.5    Schneider, S.N.6
  • 103
    • 21844478747 scopus 로고    scopus 로고
    • Integrative genomic analyses identify MITF as a lineage survival oncogene amplified in malignant melanoma
    • L.A. Garraway, H.R. Widlund, M.A. Rubin, G. Getz, A.J. Berger, and S. Ramaswamy Integrative genomic analyses identify MITF as a lineage survival oncogene amplified in malignant melanoma Nature 436 2005 117 122
    • (2005) Nature , vol.436 , pp. 117-122
    • Garraway, L.A.1    Widlund, H.R.2    Rubin, M.A.3    Getz, G.4    Berger, A.J.5    Ramaswamy, S.6
  • 104
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • M.H. Glickman, D.M. Rubin, O. Coux, I. Wefes, G. Pfeifer, and Z. Cjeka A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3 Cell 94 1998 615 623
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6
  • 105
    • 33744906046 scopus 로고    scopus 로고
    • Genomic models of metastatic cancer: Functional analysis of death-from-cancer signature genes reveals aneuploid, anoikis-resistant, metastasis-enabling phenotype with altered cell cycle control and activated Polycomb Group (PcG) protein chromatin silencing pathway
    • G.V. Glinsky Genomic models of metastatic cancer: functional analysis of death-from-cancer signature genes reveals aneuploid, anoikis-resistant, metastasis-enabling phenotype with altered cell cycle control and activated Polycomb Group (PcG) protein chromatin silencing pathway Cell Cycle 5 2006 1208 1216
    • (2006) Cell Cycle , vol.5 , pp. 1208-1216
    • Glinsky, G.V.1
  • 106
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • A.L. Goldberg Protein degradation and protection against misfolded or damaged proteins Nature 426 2003 895 899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 107
    • 12144286902 scopus 로고    scopus 로고
    • The isopeptidase USP2a regulates the stability of fatty acid synthase in prostate cancer
    • E. Graner, D. Tang, S. Rossi, A. Baron, T. Migita, and L.J. Weinstein The isopeptidase USP2a regulates the stability of fatty acid synthase in prostate cancer Cancer Cell 5 2004 253 261
    • (2004) Cancer Cell , vol.5 , pp. 253-261
    • Graner, E.1    Tang, D.2    Rossi, S.3    Baron, A.4    Migita, T.5    Weinstein, L.J.6
  • 109
    • 84902977773 scopus 로고    scopus 로고
    • USP28 is a potential prognostic marker for bladder cancer
    • G. Guo, Y. Xu, M. Gong, Y. Cao, and R. An USP28 is a potential prognostic marker for bladder cancer Tumour Biol 35 2014 4017 4022
    • (2014) Tumour Biol , vol.35 , pp. 4017-4022
    • Guo, G.1    Xu, Y.2    Gong, M.3    Cao, Y.4    An, R.5
  • 110
    • 84898747281 scopus 로고    scopus 로고
    • MiR-218 regulates focal adhesion kinase-dependent TGFbeta signaling in fibroblasts
    • F. Guo, D.E. Carter, and A. Leask miR-218 regulates focal adhesion kinase-dependent TGFbeta signaling in fibroblasts Mol Biol Cell 25 2014 1151 1158
    • (2014) Mol Biol Cell , vol.25 , pp. 1151-1158
    • Guo, F.1    Carter, D.E.2    Leask, A.3
  • 111
    • 78649959433 scopus 로고    scopus 로고
    • Blockade of the ubiquitin protease UBP43 destabilizes transcription factor PML/RARalpha and inhibits the growth of acute promyelocytic leukemia
    • Y. Guo, A.V. Dolinko, F. Chinyengetere, B. Stanton, J.M. Bomberger, and E. Demidenko Blockade of the ubiquitin protease UBP43 destabilizes transcription factor PML/RARalpha and inhibits the growth of acute promyelocytic leukemia Cancer Res 70 2010 9875 9885
    • (2010) Cancer Res , vol.70 , pp. 9875-9885
    • Guo, Y.1    Dolinko, A.V.2    Chinyengetere, F.3    Stanton, B.4    Bomberger, J.M.5    Demidenko, E.6
  • 112
    • 0347087494 scopus 로고    scopus 로고
    • Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome
    • A. Guterman, and M.H. Glickman Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome J Biol Chem 279 2004 1729 1738
    • (2004) J Biol Chem , vol.279 , pp. 1729-1738
    • Guterman, A.1    Glickman, M.H.2
  • 113
    • 0023160888 scopus 로고
    • Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin
    • A.L. Haas, P. Ahrens, P.M. Bright, and H. Ankel Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin J Biol Chem 262 1987 11315 11323
    • (1987) J Biol Chem , vol.262 , pp. 11315-11323
    • Haas, A.L.1    Ahrens, P.2    Bright, P.M.3    Ankel, H.4
  • 114
    • 0026530899 scopus 로고
    • A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation
    • T. Hadari, J.V. Warms, I.A. Rose, and A. Hershko A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation J Biol Chem 267 1992 719 727
    • (1992) J Biol Chem , vol.267 , pp. 719-727
    • Hadari, T.1    Warms, J.V.2    Rose, I.A.3    Hershko, A.4
  • 115
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • K. Haglund, and I. Dikic Ubiquitylation and cell signaling EMBO J 24 2005 3353 3359
    • (2005) EMBO J , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 116
  • 117
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • J. Hamazaki, S. Iemura, T. Natsume, H. Yashiroda, K. Tanaka, and S. Murata A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes EMBO J 25 2006 4524 4536
    • (2006) EMBO J , vol.25 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 118
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation
    • J. Hanna, N.A. Hathaway, Y. Tone, B. Crosas, S. Elsasser, and D.S. Kirkpatrick Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation Cell 127 2006 99 111
    • (2006) Cell , vol.127 , pp. 99-111
    • Hanna, J.1    Hathaway, N.A.2    Tone, Y.3    Crosas, B.4    Elsasser, S.5    Kirkpatrick, D.S.6
  • 119
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubiquitinases
    • E.W. Harhaj, and V.M. Dixit Regulation of NF-kappaB by deubiquitinases Immunol Rev 246 2012 107 124
    • (2012) Immunol Rev , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 120
    • 1342300578 scopus 로고    scopus 로고
    • Integral UBL domain proteins: A family of proteasome interacting proteins
    • R. Hartmann-Petersen, and C. Gordon Integral UBL domain proteins: a family of proteasome interacting proteins Semin Cell Dev Biol 15 2004 247 259
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 247-259
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 121
    • 67650087753 scopus 로고    scopus 로고
    • The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates
    • G.C. Hassink, B. Zhao, R. Sompallae, M. Altun, S. Gastaldello, and N.V. Zinin The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates EMBO Rep 10 2009 755 761
    • (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
  • 123
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • A. Hershko, H. Heller, S. Elias, and A. Ciechanover Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown J Biol Chem 258 1983 8206 8214
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 124
    • 21844464322 scopus 로고    scopus 로고
    • The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1
    • B.K. Hetfeld, A. Helfrich, B. Kapelari, H. Scheel, K. Hofmann, and A. Guterman The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1 Curr Biol 15 2005 1217 1221
    • (2005) Curr Biol , vol.15 , pp. 1217-1221
    • Hetfeld, B.K.1    Helfrich, A.2    Kapelari, B.3    Scheel, H.4    Hofmann, K.5    Guterman, A.6
  • 125
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • L. Hicke Protein regulation by monoubiquitin Nat Rev Mol Cell Biol 2 2001 195 201
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 126
    • 83555162507 scopus 로고    scopus 로고
    • Regulation of p53 stability and function by the deubiquitinating enzyme USP42
    • A.K. Hock, A.M. Vigneron, S. Carter, R.L. Ludwig, and K.H. Vousden Regulation of p53 stability and function by the deubiquitinating enzyme USP42 EMBO J 30 2011 4921 4930
    • (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
  • 127
    • 70350504882 scopus 로고    scopus 로고
    • TNFAIP3/A20 functions as a novel tumor suppressor gene in several subtypes of non-Hodgkin lymphomas
    • K. Honma, S. Tsuzuki, M. Nakagawa, H. Tagawa, S. Nakamura, and Y. Morishima TNFAIP3/A20 functions as a novel tumor suppressor gene in several subtypes of non-Hodgkin lymphomas Blood 114 2009 2467 2475
    • (2009) Blood , vol.114 , pp. 2467-2475
    • Honma, K.1    Tsuzuki, S.2    Nakagawa, M.3    Tagawa, H.4    Nakamura, S.5    Morishima, Y.6
  • 128
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • M. Hu, P. Li, L. Song, P.D. Jeffrey, T.A. Chenova, and K.D. Wilkinson Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14 EMBO J 24 2005 3747 3756
    • (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
  • 129
    • 33646196532 scopus 로고    scopus 로고
    • Regulation of DNA repair by ubiquitylation
    • T.T. Huang, and A.D. D'Andrea Regulation of DNA repair by ubiquitylation Nat Rev Mol Cell Biol 7 2006 323 334
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 323-334
    • Huang, T.T.1    D'Andrea, A.D.2
  • 134
    • 66749083491 scopus 로고    scopus 로고
    • DUBs and cancer: The role of deubiquitinating enzymes as oncogenes, non-oncogenes and tumor suppressors
    • S. Hussain, Y. Zhang, and P.J. Galardy DUBs and cancer: the role of deubiquitinating enzymes as oncogenes, non-oncogenes and tumor suppressors Cell Cycle 8 2009 1688 1697
    • (2009) Cell Cycle , vol.8 , pp. 1688-1697
    • Hussain, S.1    Zhang, Y.2    Galardy, P.J.3
  • 136
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26 S proteasome
    • T. Ishii, T. Sakurai, H. Usami, and K. Uchida Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome Biochemistry 44 2005 13893 13901
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 137
    • 6344238985 scopus 로고    scopus 로고
    • Induction of reversible cysteine-targeted protein oxidation by an endogenous electrophile 15-deoxy-delta12,14-prostaglandin J2
    • T. Ishii, and K. Uchida Induction of reversible cysteine-targeted protein oxidation by an endogenous electrophile 15-deoxy-delta12,14-prostaglandin J2 Chem Res Toxicol 17 2004 1313 1322
    • (2004) Chem Res Toxicol , vol.17 , pp. 1313-1322
    • Ishii, T.1    Uchida, K.2
  • 138
    • 84860755914 scopus 로고    scopus 로고
    • Chalcone-based small-molecule inhibitors attenuate malignant phenotype via targeting deubiquitinating enzymes
    • O.A. Issaenko, and A.Y. Amerik Chalcone-based small-molecule inhibitors attenuate malignant phenotype via targeting deubiquitinating enzymes Cell Cycle 11 2012 1804 1817
    • (2012) Cell Cycle , vol.11 , pp. 1804-1817
    • Issaenko, O.A.1    Amerik, A.Y.2
  • 139
    • 72149130935 scopus 로고    scopus 로고
    • The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 S proteasome
    • A.D. Jacobson, N.Y. Zhang, P. Xu, K.J. Han, S. Noone, and J. Peng The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 S proteasome J Biol Chem 284 2009 35485 35494
    • (2009) J Biol Chem , vol.284 , pp. 35485-35494
    • Jacobson, A.D.1    Zhang, N.Y.2    Xu, P.3    Han, K.J.4    Noone, S.5    Peng, J.6
  • 140
    • 15144342687 scopus 로고    scopus 로고
    • BAP1: A novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression
    • D.E. Jensen, M. Proctor, S.T. Marquis, H.P. Gardner, S.I. Ha, and L.A. Chodosh BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression Oncogene 16 1998 1097 1112
    • (1998) Oncogene , vol.16 , pp. 1097-1112
    • Jensen, D.E.1    Proctor, M.2    Marquis, S.T.3    Gardner, H.P.4    Ha, S.I.5    Chodosh, L.A.6
  • 141
    • 0010267472 scopus 로고    scopus 로고
    • Defining biochemical functions for the BRCA1 tumor suppressor protein: Analysis of the BRCA1 binding protein BAP1
    • D.E. Jensen, and F.J. Rauscher III Defining biochemical functions for the BRCA1 tumor suppressor protein: analysis of the BRCA1 binding protein BAP1 Cancer Lett 143 Suppl. 1 1999 S13 S17
    • (1999) Cancer Lett , vol.143 , pp. S13-S17
    • Jensen, D.E.1    Rauscher, F.J.2
  • 142
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • S. Jentsch, and S. Schlenker Selective protein degradation: a journey's end within the proteasome Cell 82 1995 881 884
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 143
    • 79953185042 scopus 로고    scopus 로고
    • Regulation of histone H2A and H2B deubiquitination and Xenopus development by USP12 and USP46
    • H.Y. Joo, A. Jones, C. Yang, L. Zhai, A.D. t Smith, and Z. Zhang Regulation of histone H2A and H2B deubiquitination and Xenopus development by USP12 and USP46 J Biol Chem 286 2011 7190 7201
    • (2011) J Biol Chem , vol.286 , pp. 7190-7201
    • Joo, H.Y.1    Jones, A.2    Yang, C.3    Zhai, L.4    Smith, A.D.T.5    Zhang, Z.6
  • 144
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • H.Y. Joo, L. Zhai, C. Yang, S. Nie, H. Erdjument-Bromage, and P. Tempst Regulation of cell cycle progression and gene expression by H2A deubiquitination Nature 449 2007 1068 1072
    • (2007) Nature , vol.449 , pp. 1068-1072
    • Joo, H.Y.1    Zhai, L.2    Yang, C.3    Nie, S.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 146
    • 78549247880 scopus 로고    scopus 로고
    • Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis
    • V. Kapuria, L.F. Peterson, D. Fang, W.G. Bornmann, M. Talpaz, and N.J. Donato Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis Cancer Res 70 2010 9265 9276
    • (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
  • 147
    • 0028143527 scopus 로고
    • CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1
    • Y. Kawaguchi, T. Okamoto, M. Taniwaki, M. Aizawa, M. Inoue, and S. Katayama CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1 Nat Genet 8 1994 221 228
    • (1994) Nat Genet , vol.8 , pp. 221-228
    • Kawaguchi, Y.1    Okamoto, T.2    Taniwaki, M.3    Aizawa, M.4    Inoue, M.5    Katayama, S.6
  • 148
    • 36448943427 scopus 로고    scopus 로고
    • DUBA: A deubiquitinase that regulates type i interferon production
    • N. Kayagaki, Q. Phung, S. Chan, R. Chaudhari, C. Quan, and K.M. O'Rourke DUBA: a deubiquitinase that regulates type I interferon production Science 318 2007 1628 1632
    • (2007) Science , vol.318 , pp. 1628-1632
    • Kayagaki, N.1    Phung, Q.2    Chan, S.3    Chaudhari, R.4    Quan, C.5    O'Rourke, K.M.6
  • 149
    • 84863356095 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP2a enhances tumor progression by targeting cyclin A1 in bladder cancer
    • J. Kim, W.J. Kim, Z. Liu, M. Loda, and M.R. Freeman The ubiquitin-specific protease USP2a enhances tumor progression by targeting cyclin A1 in bladder cancer Cell Cycle 11 2012 1123 1130
    • (2012) Cell Cycle , vol.11 , pp. 1123-1130
    • Kim, J.1    Kim, W.J.2    Liu, Z.3    Loda, M.4    Freeman, M.R.5
  • 150
    • 77951880356 scopus 로고    scopus 로고
    • 15-Deoxy-Delta(12,14)-prostaglandin J(2) stabilizes, but functionally inactivates p53 by binding to the cysteine 277 residue
    • D.H. Kim, E.H. Kim, H.K. Na, Y. Sun, and Y.J. Surh 15-Deoxy-Delta(12,14)-prostaglandin J(2) stabilizes, but functionally inactivates p53 by binding to the cysteine 277 residue Oncogene 29 2010 2560 2576
    • (2010) Oncogene , vol.29 , pp. 2560-2576
    • Kim, D.H.1    Kim, E.H.2    Na, H.K.3    Sun, Y.4    Surh, Y.J.5
  • 151
    • 0033824287 scopus 로고    scopus 로고
    • Discovery of a novel, paternally expressed ubiquitin-specific processing protease gene through comparative analysis of an imprinted region of mouse chromosome 7 and human chromosome 19q13.4
    • J. Kim, V.N. Noskov, X. Lu, A. Bergmann, X. Ren, and T. Warth Discovery of a novel, paternally expressed ubiquitin-specific processing protease gene through comparative analysis of an imprinted region of mouse chromosome 7 and human chromosome 19q13.4 Genome Res 10 2000 1138 1147
    • (2000) Genome Res , vol.10 , pp. 1138-1147
    • Kim, J.1    Noskov, V.N.2    Lu, X.3    Bergmann, A.4    Ren, X.5    Warth, T.6
  • 152
    • 77951069130 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandin-induced unfolding and aggregation of the Parkinson disease-associated UCH-L1
    • L.M. Koharudin, H. Liu, R. Di Maio, R.B. Kodali, S.H. Graham, and A.M. Gronenborn Cyclopentenone prostaglandin-induced unfolding and aggregation of the Parkinson disease-associated UCH-L1 Proc Natl Acad Sci U S A 107 2010 6835 6840
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 6835-6840
    • Koharudin, L.M.1    Liu, H.2    Di Maio, R.3    Kodali, R.B.4    Graham, S.H.5    Gronenborn, A.M.6
  • 153
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • D. Komander, M.J. Clague, and S. Urbe Breaking the chains: structure and function of the deubiquitinases Nat Rev Mol Cell Biol 10 2009 550 563
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 154
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • E. Koulich, X. Li, and G.N. DeMartino Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome Mol Biol Cell 19 2008 1072 1082
    • (2008) Mol Biol Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    Demartino, G.N.3
  • 156
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Y.A. Lam, W. Xu, G.N. DeMartino, and R.E. Cohen Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome Nature 385 1997 737 740
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    Demartino, G.N.3    Cohen, R.E.4
  • 157
    • 33749335282 scopus 로고    scopus 로고
    • The Connectivity Map: Using gene-expression signatures to connect small molecules, genes, and disease
    • J. Lamb, E.D. Crawford, D. Peck, J.W. Modell, I.C. Blat, and M.J. Wrobel The Connectivity Map: using gene-expression signatures to connect small molecules, genes, and disease Science 313 2006 1929 1935
    • (2006) Science , vol.313 , pp. 1929-1935
    • Lamb, J.1    Crawford, E.D.2    Peck, D.3    Modell, J.W.4    Blat, I.C.5    Wrobel, M.J.6
  • 159
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • (R110.003871)
    • M.J. Lee, B.H. Lee, J. Hanna, R.W. King, and D. Finley Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes Mol Cell Proteomics 10 2011 (R110.003871)
    • (2011) Mol Cell Proteomics , vol.10
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 160
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • B.H. Lee, M.J. Lee, S. Park, D.C. Oh, S. Elsasser, and P.C. Chen Enhancement of proteasome activity by a small-molecule inhibitor of USP14 Nature 467 2010 179 184
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1    Lee, M.J.2    Park, S.3    Oh, D.C.4    Elsasser, S.5    Chen, P.C.6
  • 161
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • M. Li, C.L. Brooks, N. Kon, and W. Gu A dynamic role of HAUSP in the p53-Mdm2 pathway Mol Cell 13 2004 879 886
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 162
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • M. Li, D. Chen, A. Shiloh, J. Luo, A.Y. Nikolaev, and J. Qin Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization Nature 416 2002 648 653
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6
  • 163
    • 84874990849 scopus 로고    scopus 로고
    • USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110
    • J. Li, V. D'Angiolella, E.S. Seeley, S. Kim, T. Kobayashi, and W. Fu USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110 Nature 495 2013 255 259
    • (2013) Nature , vol.495 , pp. 255-259
    • Li, J.1    D'Angiolella, V.2    Seeley, E.S.3    Kim, S.4    Kobayashi, T.5    Fu, W.6
  • 164
    • 2942575072 scopus 로고    scopus 로고
    • Delta12-prostaglandin J2 inhibits the ubiquitin hydrolase UCH-L1 and elicits ubiquitin-protein aggregation without proteasome inhibition
    • Z. Li, F. Melandri, I. Berdo, M. Jansen, L. Hunter, and S. Wright Delta12-prostaglandin J2 inhibits the ubiquitin hydrolase UCH-L1 and elicits ubiquitin-protein aggregation without proteasome inhibition Biochem Biophys Res Commun 319 2004 1171 1180
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1171-1180
    • Li, Z.1    Melandri, F.2    Berdo, I.3    Jansen, M.4    Hunter, L.5    Wright, S.6
  • 165
    • 0037085456 scopus 로고    scopus 로고
    • Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein
    • Z. Li, X. Na, D. Wang, S.R. Schoen, E.M. Messing, and G. Wu Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein J Biol Chem 277 2002 4656 4662
    • (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
  • 166
    • 0034720458 scopus 로고    scopus 로고
    • Identification of a 26S proteasome-associated UCH in fission yeast
    • T. Li, N.I. Naqvi, H. Yang, and T.S. Teo Identification of a 26S proteasome-associated UCH in fission yeast Biochem Biophys Res Commun 272 2000 270 275
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 270-275
    • Li, T.1    Naqvi, N.I.2    Yang, H.3    Teo, T.S.4
  • 167
    • 84910145108 scopus 로고    scopus 로고
    • MiRNA-200c inhibits invasion and metastasis of human non-small cell lung cancer by directly targeting ubiquitin specific peptidase 25
    • Y. Li, Q. Tan, M. Yan, L. Liu, H. Lin, and F. Zhao miRNA-200c inhibits invasion and metastasis of human non-small cell lung cancer by directly targeting ubiquitin specific peptidase 25 Mol Cancer 13 2014 166
    • (2014) Mol Cancer , vol.13 , pp. 166
    • Li, Y.1    Tan, Q.2    Yan, M.3    Liu, L.4    Lin, H.5    Zhao, F.6
  • 168
    • 84894462315 scopus 로고    scopus 로고
    • Monoubiquitination is critical for ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (Otub1) to suppress UbcH5 enzyme and stabilize p53 protein
    • Y. Li, X.X. Sun, J. Elferich, U. Shinde, L.L. David, and M.S. Dai Monoubiquitination is critical for ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (Otub1) to suppress UbcH5 enzyme and stabilize p53 protein J Biol Chem 289 2014 5097 5108
    • (2014) J Biol Chem , vol.289 , pp. 5097-5108
    • Li, Y.1    Sun, X.X.2    Elferich, J.3    Shinde, U.4    David, L.L.5    Dai, M.S.6
  • 169
    • 17644421091 scopus 로고    scopus 로고
    • VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha
    • Z. Li, D. Wang, E.M. Messing, and G. Wu VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha EMBO Rep 6 2005 373 378
    • (2005) EMBO Rep , vol.6 , pp. 373-378
    • Li, Z.1    Wang, D.2    Messing, E.M.3    Wu, G.4
  • 170
    • 77951168849 scopus 로고    scopus 로고
    • Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6
    • S. Li, H. Zheng, A.P. Mao, B. Zhong, Y. Li, and Y. Liu Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6 J Biol Chem 285 2010 4291 4297
    • (2010) J Biol Chem , vol.285 , pp. 4291-4297
    • Li, S.1    Zheng, H.2    Mao, A.P.3    Zhong, B.4    Li, Y.5    Liu, Y.6
  • 171
    • 84861461517 scopus 로고    scopus 로고
    • USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development
    • Z. Lin, H. Yang, Q. Kong, J. Li, S.M. Lee, and B. Gao USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development Mol Cell 46 2012 484 494
    • (2012) Mol Cell , vol.46 , pp. 484-494
    • Lin, Z.1    Yang, H.2    Kong, Q.3    Li, J.4    Lee, S.M.5    Gao, B.6
  • 172
    • 84890979013 scopus 로고    scopus 로고
    • USP10 antagonizes c-Myc transcriptional activation through SIRT6 stabilization to suppress tumor formation
    • Z. Lin, H. Yang, C. Tan, J. Li, Z. Liu, and Q. Quan USP10 antagonizes c-Myc transcriptional activation through SIRT6 stabilization to suppress tumor formation Cell Rep 5 2013 1639 1649
    • (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
  • 173
    • 0141706672 scopus 로고    scopus 로고
    • Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells
    • Y.H. Ling, L. Liebes, Y. Zou, and R. Perez-Soler Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells J Biol Chem 278 2003 33714 33723
    • (2003) J Biol Chem , vol.278 , pp. 33714-33723
    • Ling, Y.H.1    Liebes, L.2    Zou, Y.3    Perez-Soler, R.4
  • 174
    • 80053501671 scopus 로고    scopus 로고
    • Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13
    • J. Liu, H. Xia, M. Kim, L. Xu, Y. Li, and L. Zhang Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13 Cell 147 2011 223 234
    • (2011) Cell , vol.147 , pp. 223-234
    • Liu, J.1    Xia, H.2    Kim, M.3    Xu, L.4    Li, Y.5    Zhang, L.6
  • 175
    • 79952282523 scopus 로고    scopus 로고
    • JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress
    • J. Liu, H.J. Chung, M. Vogt, Y. Jin, D. Malide, and L. He JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress EMBO J 30 2011 846 858
    • (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
  • 176
    • 78650598280 scopus 로고    scopus 로고
    • Modification of ubiquitin-C-terminal hydrolase-L1 by cyclopentenone prostaglandins exacerbates hypoxic injury
    • H. Liu, W. Li, M. Ahmad, T.M. Miller, M.E. Rose, and S.M. Poloyac Modification of ubiquitin-C-terminal hydrolase-L1 by cyclopentenone prostaglandins exacerbates hypoxic injury Neurobiol Dis 41 2011 318 328
    • (2011) Neurobiol Dis , vol.41 , pp. 318-328
    • Liu, H.1    Li, W.2    Ahmad, M.3    Miller, T.M.4    Rose, M.E.5    Poloyac, S.M.6
  • 177
    • 12444269118 scopus 로고    scopus 로고
    • Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line
    • Y. Liu, H.A. Lashuel, S. Choi, X. Xing, A. Case, and J. Ni Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line Chem Biol 10 2003 837 846
    • (2003) Chem Biol , vol.10 , pp. 837-846
    • Liu, Y.1    Lashuel, H.A.2    Choi, S.3    Xing, X.4    Case, A.5    Ni, J.6
  • 178
    • 84874301754 scopus 로고    scopus 로고
    • Developing irreversible inhibitors of the protein kinase cysteinome
    • Q. Liu, Y. Sabnis, Z. Zhao, T. Zhang, S.J. Buhrlage, and L.H. Jones Developing irreversible inhibitors of the protein kinase cysteinome Chem Biol 20 2013 146 159
    • (2013) Chem Biol , vol.20 , pp. 146-159
    • Liu, Q.1    Sabnis, Y.2    Zhao, Z.3    Zhang, T.4    Buhrlage, S.J.5    Jones, L.H.6
  • 179
    • 0026722530 scopus 로고
    • The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins
    • K.R. Loeb, and A.L. Haas The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins J Biol Chem 267 1992 7806 7813
    • (1992) J Biol Chem , vol.267 , pp. 7806-7813
    • Loeb, K.R.1    Haas, A.L.2
  • 180
    • 84857868182 scopus 로고    scopus 로고
    • Application of the Hard and Soft, Acids and Bases (HSAB) theory to toxicant-target interactions
    • R.M. Lopachin, T. Gavin, A. Decaprio, and D.S. Barber Application of the Hard and Soft, Acids and Bases (HSAB) theory to toxicant-target interactions Chem Res Toxicol 25 2012 239 251
    • (2012) Chem Res Toxicol , vol.25 , pp. 239-251
    • Lopachin, R.M.1    Gavin, T.2    Decaprio, A.3    Barber, D.S.4
  • 181
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. Acidophilum at 3.4 A resolution
    • J. Lowe, D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution Science 268 1995 533 539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 182
    • 58249113974 scopus 로고    scopus 로고
    • USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1
    • Y. Lu, O.A. Adegoke, A. Nepveu, K.I. Nakayama, N. Bedard, and D. Cheng USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1 Mol Cell Biol 29 2009 547 558
    • (2009) Mol Cell Biol , vol.29 , pp. 547-558
    • Lu, Y.1    Adegoke, O.A.2    Nepveu, A.3    Nakayama, K.I.4    Bedard, N.5    Cheng, D.6
  • 183
    • 79251541181 scopus 로고    scopus 로고
    • Identification of distinctive patterns of USP19-mediated growth regulation in normal and malignant cells
    • Y. Lu, N. Bedard, S. Chevalier, and S.S. Wing Identification of distinctive patterns of USP19-mediated growth regulation in normal and malignant cells PLoS One 6 2011 e15936
    • (2011) PLoS One , vol.6 , pp. e15936
    • Lu, Y.1    Bedard, N.2    Chevalier, S.3    Wing, S.S.4
  • 185
    • 79956128376 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP34 regulates axin stability and Wnt/beta-catenin signaling
    • T.T. Lui, C. Lacroix, S.M. Ahmed, S.J. Goldenberg, C.A. Leach, and A.M. Daulat The ubiquitin-specific protease USP34 regulates axin stability and Wnt/beta-catenin signaling Mol Cell Biol 31 2011 2053 2065
    • (2011) Mol Cell Biol , vol.31 , pp. 2053-2065
    • Lui, T.T.1    Lacroix, C.2    Ahmed, S.M.3    Goldenberg, S.J.4    Leach, C.A.5    Daulat, A.M.6
  • 186
    • 0042091963 scopus 로고    scopus 로고
    • Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13
    • J. Lundgren, P. Masson, C.A. Realini, and P. Young Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13 Mol Cell Biol 23 2003 5320 5330
    • (2003) Mol Cell Biol , vol.23 , pp. 5320-5330
    • Lundgren, J.1    Masson, P.2    Realini, C.A.3    Young, P.4
  • 187
    • 84885452884 scopus 로고    scopus 로고
    • OTUD5 regulates p53 stability by deubiquitinating p53
    • J. Luo, Z. Lu, X. Lu, L. Chen, J. Cao, and S. Zhang OTUD5 regulates p53 stability by deubiquitinating p53 PLoS One 8 2013 e77682
    • (2013) PLoS One , vol.8 , pp. e77682
    • Luo, J.1    Lu, Z.2    Lu, X.3    Chen, L.4    Cao, J.5    Zhang, S.6
  • 188
    • 84867898782 scopus 로고    scopus 로고
    • A20: Linking a complex regulator of ubiquitylation to immunity and human disease
    • A. Ma, and B.A. Malynn A20: linking a complex regulator of ubiquitylation to immunity and human disease Nat Rev Immunol 12 2012 774 785
    • (2012) Nat Rev Immunol , vol.12 , pp. 774-785
    • Ma, A.1    Malynn, B.A.2
  • 189
    • 77955419051 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor
    • G.N. Maertens, S. El Messaoudi-Aubert, S. Elderkin, K. Hiom, and G. Peters Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor EMBO J 29 2010 2553 2565
    • (2010) EMBO J , vol.29 , pp. 2553-2565
    • Maertens, G.N.1    El Messaoudi-Aubert, S.2    Elderkin, S.3    Hiom, K.4    Peters, G.5
  • 191
    • 79955534260 scopus 로고    scopus 로고
    • ClpX(P) generates mechanical force to unfold and translocate its protein substrates
    • R.A. Maillard, G. Chistol, M. Sen, M. Righini, J. Tan, and C.M. Kaiser ClpX(P) generates mechanical force to unfold and translocate its protein substrates Cell 145 2011 459 469
    • (2011) Cell , vol.145 , pp. 459-469
    • Maillard, R.A.1    Chistol, G.2    Sen, M.3    Righini, M.4    Tan, J.5    Kaiser, C.M.6
  • 193
    • 33745761009 scopus 로고    scopus 로고
    • UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity
    • O.A. Malakhova, K.I. Kim, J.K. Luo, W. Zou, K.G. Kumar, and S.Y. Fuchs UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity EMBO J 25 2006 2358 2367
    • (2006) EMBO J , vol.25 , pp. 2358-2367
    • Malakhova, O.A.1    Kim, K.I.2    Luo, J.K.3    Zou, W.4    Kumar, K.G.5    Fuchs, S.Y.6
  • 194
    • 55549088522 scopus 로고    scopus 로고
    • + ClpX machine grip substrates to drive translocation and unfolding
    • + ClpX machine grip substrates to drive translocation and unfolding Nat Struct Mol Biol 15 2008 1147 1151
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1147-1151
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 196
    • 33646531810 scopus 로고    scopus 로고
    • Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-kappaB signaling
    • R. Massoumi, K. Chmielarska, K. Hennecke, A. Pfeifer, and R. Fassler Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-kappaB signaling Cell 125 2006 665 677
    • (2006) Cell , vol.125 , pp. 665-677
    • Massoumi, R.1    Chmielarska, K.2    Hennecke, K.3    Pfeifer, A.4    Fassler, R.5
  • 197
    • 34248350363 scopus 로고    scopus 로고
    • MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
    • V. Maytal-Kivity, N. Reis, K. Hofmann, and M.H. Glickman MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function BMC Biochem 3 2002 28
    • (2002) BMC Biochem , vol.3 , pp. 28
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3    Glickman, M.H.4
  • 198
    • 77956373713 scopus 로고    scopus 로고
    • Regulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13)
    • T. Mazumdar, F.M. Gorgun, Y. Sha, A. Tyryshkin, S. Zeng, and R. Hartmann-Petersen Regulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13) Proc Natl Acad Sci U S A 107 2010 13854 13859
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13854-13859
    • Mazumdar, T.1    Gorgun, F.M.2    Sha, Y.3    Tyryshkin, A.4    Zeng, S.5    Hartmann-Petersen, R.6
  • 199
    • 18444418797 scopus 로고    scopus 로고
    • Bcl2 regulation by the melanocyte master regulator Mitf modulates lineage survival and melanoma cell viability
    • G.G. McGill, M. Horstmann, H.R. Widlund, J. Du, G. Motyckova, and E.K. Nishimura Bcl2 regulation by the melanocyte master regulator Mitf modulates lineage survival and melanoma cell viability Cell 109 2002 707 718
    • (2002) Cell , vol.109 , pp. 707-718
    • McGill, G.G.1    Horstmann, M.2    Widlund, H.R.3    Du, J.4    Motyckova, G.5    Nishimura, E.K.6
  • 200
    • 80053911021 scopus 로고    scopus 로고
    • The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2
    • Y. Mei, A.A. Hahn, S. Hu, and X. Yang The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2 J Biol Chem 286 2011 35380 35387
    • (2011) J Biol Chem , vol.286 , pp. 35380-35387
    • Mei, Y.1    Hahn, A.A.2    Hu, S.3    Yang, X.4
  • 201
    • 0842281498 scopus 로고    scopus 로고
    • Aurora kinases link chromosome segregation and cell division to cancer susceptibility
    • P. Meraldi, R. Honda, and E.A. Nigg Aurora kinases link chromosome segregation and cell division to cancer susceptibility Curr Opin Genet Dev 14 2004 29 36
    • (2004) Curr Opin Genet Dev , vol.14 , pp. 29-36
    • Meraldi, P.1    Honda, R.2    Nigg, E.A.3
  • 202
    • 34250160956 scopus 로고    scopus 로고
    • Structure-activity relationship, kinetic mechanism, and selectivity for a new class of ubiquitin C-terminal hydrolase-L1 (UCH-L1) inhibitors
    • A.H. Mermerian, A. Case, R.L. Stein, and G.D. Cuny Structure-activity relationship, kinetic mechanism, and selectivity for a new class of ubiquitin C-terminal hydrolase-L1 (UCH-L1) inhibitors Bioorg Med Chem Lett 17 2007 3729 3732
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 3729-3732
    • Mermerian, A.H.1    Case, A.2    Stein, R.L.3    Cuny, G.D.4
  • 203
    • 64649106796 scopus 로고    scopus 로고
    • Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1
    • S. Misaghi, S. Ottosen, A. Izrael-Tomasevic, D. Arnott, M. Lamkanfi, and J. Lee Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1 Mol Cell Biol 29 2009 2181 2192
    • (2009) Mol Cell Biol , vol.29 , pp. 2181-2192
    • Misaghi, S.1    Ottosen, S.2    Izrael-Tomasevic, A.3    Arnott, D.4    Lamkanfi, M.5    Lee, J.6
  • 204
    • 0037428454 scopus 로고    scopus 로고
    • Electrophilic prostaglandins and lipid aldehydes repress redox-sensitive transcription factors p53 and hypoxia-inducible factor by impairing the selenoprotein thioredoxin reductase
    • P.J. Moos, K. Edes, P. Cassidy, E. Massuda, and F.A. Fitzpatrick Electrophilic prostaglandins and lipid aldehydes repress redox-sensitive transcription factors p53 and hypoxia-inducible factor by impairing the selenoprotein thioredoxin reductase J Biol Chem 278 2003 745 750
    • (2003) J Biol Chem , vol.278 , pp. 745-750
    • Moos, P.J.1    Edes, K.2    Cassidy, P.3    Massuda, E.4    Fitzpatrick, F.A.5
  • 205
    • 84865455417 scopus 로고    scopus 로고
    • The ubiquitin-specific protease 12 (USP12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation
    • J. Moretti, P. Chastagner, C.C. Liang, M.A. Cohn, A. Israel, and C. Brou The ubiquitin-specific protease 12 (USP12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation J Biol Chem 287 2012 29429 29441
    • (2012) J Biol Chem , vol.287 , pp. 29429-29441
    • Moretti, J.1    Chastagner, P.2    Liang, C.C.3    Cohn, M.A.4    Israel, A.5    Brou, C.6
  • 206
    • 0036070772 scopus 로고    scopus 로고
    • Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death
    • J.E. Mullally, and F.A. Fitzpatrick Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death Mol Pharmacol 62 2002 351 358
    • (2002) Mol Pharmacol , vol.62 , pp. 351-358
    • Mullally, J.E.1    Fitzpatrick, F.A.2
  • 207
    • 0035839603 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway
    • J.E. Mullally, P.J. Moos, K. Edes, and F.A. Fitzpatrick Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway J Biol Chem 276 2001 30366 30373
    • (2001) J Biol Chem , vol.276 , pp. 30366-30373
    • Mullally, J.E.1    Moos, P.J.2    Edes, K.3    Fitzpatrick, F.A.4
  • 208
    • 79958030960 scopus 로고    scopus 로고
    • The USP1/UAF1 complex promotes double-strand break repair through homologous recombination
    • J. Murai, K. Yang, D. Dejsuphong, K. Hirota, S. Takeda, and A.D. D'Andrea The USP1/UAF1 complex promotes double-strand break repair through homologous recombination Mol Cell Biol 31 2011 2462 2469
    • (2011) Mol Cell Biol , vol.31 , pp. 2462-2469
    • Murai, J.1    Yang, K.2    Dejsuphong, D.3    Hirota, K.4    Takeda, S.5    D'Andrea, A.D.6
  • 209
    • 71449117666 scopus 로고    scopus 로고
    • Ubiquitin-like sequence in ASK1 plays critical roles in the recognition and stabilization by USP9X and oxidative stress-induced cell death
    • H. Nagai, T. Noguchi, K. Homma, K. Katagiri, K. Takeda, and A. Matsuzawa Ubiquitin-like sequence in ASK1 plays critical roles in the recognition and stabilization by USP9X and oxidative stress-induced cell death Mol Cell 36 2009 805 818
    • (2009) Mol Cell , vol.36 , pp. 805-818
    • Nagai, H.1    Noguchi, T.2    Homma, K.3    Katagiri, K.4    Takeda, K.5    Matsuzawa, A.6
  • 210
    • 38149081168 scopus 로고    scopus 로고
    • Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation
    • T. Nakagawa, T. Kajitani, S. Togo, N. Masuko, H. Ohdan, and Y. Hishikawa Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation Genes Dev 22 2008 37 49
    • (2008) Genes Dev , vol.22 , pp. 37-49
    • Nakagawa, T.1    Kajitani, T.2    Togo, S.3    Masuko, N.4    Ohdan, H.5    Hishikawa, Y.6
  • 211
    • 0023006057 scopus 로고
    • Site and mechanism of growth inhibition by prostaglandins. I. Active transport and intracellular accumulation of cyclopentenone prostaglandins, a reaction leading to growth inhibition
    • S. Narumiya, and M. Fukushima Site and mechanism of growth inhibition by prostaglandins. I. Active transport and intracellular accumulation of cyclopentenone prostaglandins, a reaction leading to growth inhibition J Pharmacol Exp Ther 239 1986 500 505
    • (1986) J Pharmacol Exp Ther , vol.239 , pp. 500-505
    • Narumiya, S.1    Fukushima, M.2
  • 216
    • 66549086135 scopus 로고    scopus 로고
    • The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas
    • U. Novak, A. Rinaldi, I. Kwee, S.V. Nandula, P.M. Rancoita, and M. Compagno The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas Blood 113 2009 4918 4921
    • (2009) Blood , vol.113 , pp. 4918-4921
    • Novak, U.1    Rinaldi, A.2    Kwee, I.3    Nandula, S.V.4    Rancoita, P.M.5    Compagno, M.6
  • 217
    • 84856846038 scopus 로고    scopus 로고
    • Targeting deubiquitinases enabled by chemical synthesis of proteins
    • S. Ohayon, L. Spasser, A. Aharoni, and A. Brik Targeting deubiquitinases enabled by chemical synthesis of proteins J Am Chem Soc 134 2012 3281 3289
    • (2012) J Am Chem Soc , vol.134 , pp. 3281-3289
    • Ohayon, S.1    Spasser, L.2    Aharoni, A.3    Brik, A.4
  • 218
    • 84896731040 scopus 로고    scopus 로고
    • The USP21 short variant (USP21SV) lacking NES, located mostly in the nucleus in vivo, activates transcription by deubiquitylating ubH2A in vitro
    • H. Okuda, H. Ohdan, M. Nakayama, H. Koseki, T. Nakagawa, and T. Ito The USP21 short variant (USP21SV) lacking NES, located mostly in the nucleus in vivo, activates transcription by deubiquitylating ubH2A in vitro PLoS One 8 2013 e79813
    • (2013) PLoS One , vol.8 , pp. e79813
    • Okuda, H.1    Ohdan, H.2    Nakayama, M.3    Koseki, H.4    Nakagawa, T.5    Ito, T.6
  • 220
    • 2942667930 scopus 로고    scopus 로고
    • Point mutations in the RUNX1/AML1 gene: Another actor in RUNX leukemia
    • M. Osato Point mutations in the RUNX1/AML1 gene: another actor in RUNX leukemia Oncogene 23 2004 4284 4296
    • (2004) Oncogene , vol.23 , pp. 4284-4296
    • Osato, M.1
  • 221
    • 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
    • A. Panner, C.A. Crane, C. Weng, A. Feletti, S. Fang, and A.T. Parsa Ubiquitin-specific protease 8 links the PTEN-Akt-AIP4 pathway to the control of FLIPS stability and TRAIL sensitivity in glioblastoma multiforme Cancer Res 70 2010 5046 5053
    • (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
  • 222
    • 79951997444 scopus 로고    scopus 로고
    • USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase beta
    • J.L. Parsons, I.I. Dianova, S.V. Khoronenkova, M.J. Edelmann, B.M. Kessler, and G.L. Dianov USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase beta Mol Cell 41 2011 609 615
    • (2011) Mol Cell , vol.41 , pp. 609-615
    • Parsons, J.L.1    Dianova, I.I.2    Khoronenkova, S.V.3    Edelmann, M.J.4    Kessler, B.M.5    Dianov, G.L.6
  • 223
    • 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
    • K. Paulsson, A.N. Bekassy, T. Olofsson, F. Mitelman, B. Johansson, and I. Panagopoulos 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 20 2006 224 229
    • (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
  • 226
    • 77949265991 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival
    • A. Peschiaroli, J.R. Skaar, M. Pagano, and G. Melino The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival Oncogene 29 2010 1384 1393
    • (2010) Oncogene , vol.29 , pp. 1384-1393
    • Peschiaroli, A.1    Skaar, J.R.2    Pagano, M.3    Melino, G.4
  • 227
    • 71149107057 scopus 로고    scopus 로고
    • Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening
    • A. Peth, H.C. Besche, and A.L. Goldberg Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening Mol Cell 36 2009 794 804
    • (2009) Mol Cell , vol.36 , pp. 794-804
    • Peth, A.1    Besche, H.C.2    Goldberg, A.L.3
  • 228
    • 77954605430 scopus 로고    scopus 로고
    • Degrasyn potentiates the antitumor effects of bortezomib in mantle cell lymphoma cells in vitro and in vivo: Therapeutic implications
    • L.V. Pham, A.T. Tamayo, C. Li, W. Bornmann, W. Priebe, and R.J. Ford Degrasyn potentiates the antitumor effects of bortezomib in mantle cell lymphoma cells in vitro and in vivo: therapeutic implications Mol Cancer Ther 9 2010 2026 2036
    • (2010) Mol Cancer Ther , vol.9 , pp. 2026-2036
    • Pham, L.V.1    Tamayo, A.T.2    Li, C.3    Bornmann, W.4    Priebe, W.5    Ford, R.J.6
  • 229
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • C.M. Pickart, and M.J. Eddins Ubiquitin: structures, functions, mechanisms Biochim Biophys Acta 1695 2004 55 72
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 230
    • 0028847024 scopus 로고
    • Discovery of betulinic acid as a selective inhibitor of human melanoma that functions by induction of apoptosis
    • E. Pisha, H. Chai, I.S. Lee, T.E. Chagwedera, N.R. Farnsworth, and G.A. Cordell Discovery of betulinic acid as a selective inhibitor of human melanoma that functions by induction of apoptosis Nat Med 1 1995 1046 1051
    • (1995) Nat Med , vol.1 , pp. 1046-1051
    • Pisha, E.1    Chai, H.2    Lee, I.S.3    Chagwedera, T.E.4    Farnsworth, N.R.5    Cordell, G.A.6
  • 231
    • 0036038158 scopus 로고    scopus 로고
    • Phenotype diversity in familial cylindromatosis: A frameshift mutation in the tumor suppressor gene CYLD underlies different tumors of skin appendages
    • P. Poblete Gutierrez, T. Eggermann, D. Holler, F.K. Jugert, T. Beermann, and E.I. Grussendorf-Conen Phenotype diversity in familial cylindromatosis: a frameshift mutation in the tumor suppressor gene CYLD underlies different tumors of skin appendages J Invest Dermatol 119 2002 527 531
    • (2002) J Invest Dermatol , vol.119 , pp. 527-531
    • Poblete Gutierrez, P.1    Eggermann, T.2    Holler, D.3    Jugert, F.K.4    Beermann, T.5    Grussendorf-Conen, E.I.6
  • 233
    • 0026600786 scopus 로고
    • Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum
    • G. Puhler, S. Weinkauf, L. Bachmann, S. Muller, A. Engel, and R. Hegerl Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum EMBO J 11 1992 1607 1616
    • (1992) EMBO J , vol.11 , pp. 1607-1616
    • Puhler, G.1    Weinkauf, S.2    Bachmann, L.3    Muller, S.4    Engel, A.5    Hegerl, R.6
  • 234
    • 56949096780 scopus 로고    scopus 로고
    • Involvement of matrix metalloproteinase 2 and 9 in gambogic acid induced suppression of MDA-MB-435 human breast carcinoma cell lung metastasis
    • Q. Qi, H. Gu, Y. Yang, N. Lu, J. Zhao, and W. Liu Involvement of matrix metalloproteinase 2 and 9 in gambogic acid induced suppression of MDA-MB-435 human breast carcinoma cell lung metastasis J Mol Med (Berl) 86 2008 1367 1377
    • (2008) J Mol Med (Berl) , vol.86 , pp. 1367-1377
    • Qi, Q.1    Gu, H.2    Yang, Y.3    Lu, N.4    Zhao, J.5    Liu, W.6
  • 235
    • 0037069388 scopus 로고    scopus 로고
    • Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3
    • X.B. Qiu, and A.L. Goldberg Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3 Proc Natl Acad Sci U S A 99 2002 14843 14848
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14843-14848
    • Qiu, X.B.1    Goldberg, A.L.2
  • 236
    • 33845713194 scopus 로고    scopus 로고
    • HRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • X.B. Qiu, S.Y. Ouyang, C.J. Li, S. Miao, L. Wang, and A.L. Goldberg hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37 EMBO J 25 2006 5742 5753
    • (2006) EMBO J , vol.25 , pp. 5742-5753
    • Qiu, X.B.1    Ouyang, S.Y.2    Li, C.J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 237
    • 42949096020 scopus 로고    scopus 로고
    • Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases
    • J. Rabl, D.M. Smith, Y. Yu, S.C. Chang, A.L. Goldberg, and Y. Cheng Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases Mol Cell 30 2008 360 368
    • (2008) Mol Cell , vol.30 , pp. 360-368
    • Rabl, J.1    Smith, D.M.2    Yu, Y.3    Chang, S.C.4    Goldberg, A.L.5    Cheng, Y.6
  • 238
    • 79960427057 scopus 로고    scopus 로고
    • Selective killing of cancer cells by a small molecule targeting the stress response to ROS
    • L. Raj, T. Ide, A.U. Gurkar, M. Foley, M. Schenone, and X. Li Selective killing of cancer cells by a small molecule targeting the stress response to ROS Nature 475 2011 231 234
    • (2011) Nature , vol.475 , pp. 231-234
    • Raj, L.1    Ide, T.2    Gurkar, A.U.3    Foley, M.4    Schenone, M.5    Li, X.6
  • 239
    • 78650967382 scopus 로고    scopus 로고
    • The role of deubiquitinating enzymes in apoptosis
    • S. Ramakrishna, B. Suresh, and K.H. Baek The role of deubiquitinating enzymes in apoptosis Cell Mol Life Sci 68 2011 15 26
    • (2011) Cell Mol Life Sci , vol.68 , pp. 15-26
    • Ramakrishna, S.1    Suresh, B.2    Baek, K.H.3
  • 241
    • 84873738624 scopus 로고    scopus 로고
    • Betulinic acid selectively increases protein degradation and enhances prostate cancer-specific apoptosis: Possible role for inhibition of deubiquitinase activity
    • T. Reiner, R. Parrondo, A. de Las Pozas, D. Palenzuela, and C. Perez-Stable Betulinic acid selectively increases protein degradation and enhances prostate cancer-specific apoptosis: possible role for inhibition of deubiquitinase activity PLoS One 8 2013 e56234
    • (2013) PLoS One , vol.8 , pp. e56234
    • Reiner, T.1    Parrondo, R.2    De Las Pozas, A.3    Palenzuela, D.4    Perez-Stable, C.5
  • 242
    • 34249893910 scopus 로고    scopus 로고
    • Modification and activation of Ras proteins by electrophilic prostanoids with different structure are site-selective
    • M. Renedo, J. Gayarre, C.A. Garcia-Dominguez, A. Perez-Rodriguez, A. Prieto, and F.J. Canada Modification and activation of Ras proteins by electrophilic prostanoids with different structure are site-selective Biochemistry 46 2007 6607 6616
    • (2007) Biochemistry , vol.46 , pp. 6607-6616
    • Renedo, M.1    Gayarre, J.2    Garcia-Dominguez, C.A.3    Perez-Rodriguez, A.4    Prieto, A.5    Canada, F.J.6
  • 244
  • 245
    • 0031709394 scopus 로고    scopus 로고
    • A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology
    • T. Rinaldi, C. Ricci, D. Porro, M. Bolotin-Fukuhara, and L. Frontali A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology Mol Biol Cell 9 1998 2917 2931
    • (1998) Mol Biol Cell , vol.9 , pp. 2917-2931
    • Rinaldi, T.1    Ricci, C.2    Porro, D.3    Bolotin-Fukuhara, M.4    Frontali, L.5
  • 246
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class i molecules
    • K.L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, and L. Dick Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules Cell 78 1994 761 771
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6
  • 247
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • P.E. Row, I.A. Prior, J. McCullough, M.J. Clague, and S. Urbe The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation J Biol Chem 281 2006 12618 12624
    • (2006) J Biol Chem , vol.281 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbe, S.5
  • 248
    • 77949733627 scopus 로고    scopus 로고
    • Emerging roles of deubiquitinases in cancer-associated pathways
    • J.J. Sacco, J.M. Coulson, M.J. Clague, and S. Urbe Emerging roles of deubiquitinases in cancer-associated pathways IUBMB Life 62 2010 140 157
    • (2010) IUBMB Life , vol.62 , pp. 140-157
    • Sacco, J.J.1    Coulson, J.M.2    Clague, M.J.3    Urbe, S.4
  • 249
    • 84906235090 scopus 로고    scopus 로고
    • The deubiquitylase Ataxin-3 restricts PTEN transcription in lung cancer cells
    • J.J. Sacco, T.Y. Yau, S. Darling, V. Patel, H. Liu, and S. Urbe The deubiquitylase Ataxin-3 restricts PTEN transcription in lung cancer cells Oncogene 33 2014 4265 4272
    • (2014) Oncogene , vol.33 , pp. 4265-4272
    • Sacco, J.J.1    Yau, T.Y.2    Darling, S.3    Patel, V.4    Liu, H.5    Urbe, S.6
  • 250
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Y. Saeki, T. Kudo, T. Sone, Y. Kikuchi, H. Yokosawa, and A. Toh-e Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome EMBO J 28 2009 359 371
    • (2009) EMBO J , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-E, A.6
  • 251
    • 84863230500 scopus 로고    scopus 로고
    • Assembly and function of the proteasome
    • Y. Saeki, and K. Tanaka Assembly and function of the proteasome Methods Mol Biol 832 2012 315 337
    • (2012) Methods Mol Biol , vol.832 , pp. 315-337
    • Saeki, Y.1    Tanaka, K.2
  • 252
    • 66049124247 scopus 로고    scopus 로고
    • TNFAIP3 (A20) is a tumor suppressor gene in Hodgkin lymphoma and primary mediastinal B cell lymphoma
    • R. Schmitz, M.L. Hansmann, V. Bohle, J.I. Martin-Subero, S. Hartmann, and G. Mechtersheimer TNFAIP3 (A20) is a tumor suppressor gene in Hodgkin lymphoma and primary mediastinal B cell lymphoma J Exp Med 206 2009 981 989
    • (2009) J Exp Med , vol.206 , pp. 981-989
    • Schmitz, R.1    Hansmann, M.L.2    Bohle, V.3    Martin-Subero, J.I.4    Hartmann, S.5    Mechtersheimer, G.6
  • 253
    • 4344717012 scopus 로고    scopus 로고
    • BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage
    • A.R. Schoenfeld, S. Apgar, G. Dolios, R. Wang, and S.A. Aaronson BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage Mol Cell Biol 24 2004 7444 7455
    • (2004) Mol Cell Biol , vol.24 , pp. 7444-7455
    • Schoenfeld, A.R.1    Apgar, S.2    Dolios, G.3    Wang, R.4    Aaronson, S.A.5
  • 254
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • U. Schubert, L.C. Anton, J. Gibbs, C.C. Norbury, J.W. Yewdell, and J.R. Bennink Rapid degradation of a large fraction of newly synthesized proteins by proteasomes Nature 404 2000 770 774
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 255
    • 84891946419 scopus 로고    scopus 로고
    • Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance
    • P.A. Schwartz, P. Kuzmic, J. Solowiej, S. Bergqvist, B. Bolanos, and C. Almaden Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance Proc Natl Acad Sci U S A 111 2014 173 178
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 173-178
    • Schwartz, P.A.1    Kuzmic, P.2    Solowiej, J.3    Bergqvist, S.4    Bolanos, B.5    Almaden, C.6
  • 256
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • M. Schwickart, X. Huang, J.R. Lill, J. Liu, R. Ferrando, and D.M. French Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival Nature 463 2010 103 107
    • (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
  • 257
    • 0037673562 scopus 로고    scopus 로고
    • The comparative proteomics of ubiquitination in mouse
    • C.A. Semple, R.G. Group, and G.S.L. Members The comparative proteomics of ubiquitination in mouse Genome Res 13 2003 1389 1394
    • (2003) Genome Res , vol.13 , pp. 1389-1394
    • Semple, C.A.1    Group, R.G.2    Members, G.S.L.3
  • 259
    • 70449105984 scopus 로고    scopus 로고
    • Suppression of cancer cell growth by promoting cyclin D1 degradation
    • J. Shan, W. Zhao, and W. Gu Suppression of cancer cell growth by promoting cyclin D1 degradation Mol Cell 36 2009 469 476
    • (2009) Mol Cell , vol.36 , pp. 469-476
    • Shan, J.1    Zhao, W.2    Gu, W.3
  • 260
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
    • G. Shao, D.R. Lilli, J. Patterson-Fortin, K.A. Coleman, D.E. Morrissey, and R.A. Greenberg The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks Proc Natl Acad Sci U S A 106 2009 3166 3171
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3166-3171
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 261
    • 84858120447 scopus 로고    scopus 로고
    • Regulation of NF-kappaB signaling by the A20 deubiquitinase
    • N. Shembade, and E.W. Harhaj Regulation of NF-kappaB signaling by the A20 deubiquitinase Cell Mol Immunol 9 2012 123 130
    • (2012) Cell Mol Immunol , vol.9 , pp. 123-130
    • Shembade, N.1    Harhaj, E.W.2
  • 262
    • 84860797975 scopus 로고    scopus 로고
    • Identification of small molecule TRABID deubiquitinase inhibitors by computation-based virtual screen
    • T. Shi, J. Bao, N.X. Wang, J. Zheng, and D. Wu Identification of small molecule TRABID deubiquitinase inhibitors by computation-based virtual screen BMC Chem Biol 12 2012 4
    • (2012) BMC Chem Biol , vol.12 , pp. 4
    • Shi, T.1    Bao, J.2    Wang, N.X.3    Zheng, J.4    Wu, D.5
  • 263
    • 80655149454 scopus 로고    scopus 로고
    • Ubiquitin-specific cysteine protease 2a (USP2a) regulates the stability of Aurora-A
    • Y. Shi, L.R. Solomon, A. Pereda-Lopez, V.L. Giranda, Y. Luo, and E.F. Johnson Ubiquitin-specific cysteine protease 2a (USP2a) regulates the stability of Aurora-A J Biol Chem 286 2011 38960 38968
    • (2011) J Biol Chem , vol.286 , pp. 38960-38968
    • Shi, Y.1    Solomon, L.R.2    Pereda-Lopez, A.3    Giranda, V.L.4    Luo, Y.5    Johnson, E.F.6
  • 265
    • 17144381253 scopus 로고    scopus 로고
    • Alpha, beta-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor gamma
    • T. Shiraki, N. Kamiya, S. Shiki, T.S. Kodama, A. Kakizuka, and H. Jingami Alpha, beta-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor gamma J Biol Chem 280 2005 14145 14153
    • (2005) J Biol Chem , vol.280 , pp. 14145-14153
    • Shiraki, T.1    Kamiya, N.2    Shiki, S.3    Kodama, T.S.4    Kakizuka, A.5    Jingami, H.6
  • 267
    • 0031860081 scopus 로고    scopus 로고
    • Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers
    • G. Shoba, D. Joy, T. Joseph, M. Majeed, R. Rajendran, and P.S. Srinivas Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers Planta Med 64 1998 353 356
    • (1998) Planta Med , vol.64 , pp. 353-356
    • Shoba, G.1    Joy, D.2    Joseph, T.3    Majeed, M.4    Rajendran, R.5    Srinivas, P.S.6
  • 268
    • 84885183894 scopus 로고    scopus 로고
    • The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response
    • M. Simicek, S. Lievens, M. Laga, D. Guzenko, V.N. Aushev, and P. Kalev The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response Nat Cell Biol 15 2013 1220 1230
    • (2013) Nat Cell Biol , vol.15 , pp. 1220-1230
    • Simicek, M.1    Lievens, S.2    Laga, M.3    Guzenko, D.4    Aushev, V.N.5    Kalev, P.6
  • 270
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • D.M. Smith, S.C. Chang, S. Park, D. Finley, Y. Cheng, and A.L. Goldberg Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry Mol Cell 27 2007 731 744
    • (2007) Mol Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 271
    • 34249949779 scopus 로고    scopus 로고
    • RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites
    • B. Sobhian, G. Shao, D.R. Lilli, A.C. Culhane, L.A. Moreau, and B. Xia RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites Science 316 2007 1198 1202
    • (2007) Science , vol.316 , pp. 1198-1202
    • Sobhian, B.1    Shao, G.2    Lilli, D.R.3    Culhane, A.C.4    Moreau, L.A.5    Xia, B.6
  • 272
    • 67650215581 scopus 로고    scopus 로고
    • OTU domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity
    • V. Stanisic, A. Malovannaya, J. Qin, D.M. Lonard, and B.W. O'Malley OTU domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity J Biol Chem 284 2009 16135 16145
    • (2009) J Biol Chem , vol.284 , pp. 16135-16145
    • Stanisic, V.1    Malovannaya, A.2    Qin, J.3    Lonard, D.M.4    O'Malley, B.W.5
  • 273
    • 34247376926 scopus 로고    scopus 로고
    • Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities
    • F. Stegmeier, M. Rape, V.M. Draviam, G. Nalepa, M.E. Sowa, and X.L. Ang Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities Nature 446 2007 876 881
    • (2007) Nature , vol.446 , pp. 876-881
    • Stegmeier, F.1    Rape, M.2    Draviam, V.M.3    Nalepa, G.4    Sowa, M.E.5    Ang, X.L.6
  • 276
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • G.S. Stewart, S. Panier, K. Townsend, A.K. Al-Hakim, N.K. Kolas, and E.S. Miller The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage Cell 136 2009 420 434
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1    Panier, S.2    Townsend, K.3    Al-Hakim, A.K.4    Kolas, N.K.5    Miller, E.S.6
  • 277
    • 84856415004 scopus 로고    scopus 로고
    • Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1
    • X.X. Sun, K.B. Challagundla, and M.S. Dai Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1 EMBO J 31 2012 576 592
    • (2012) EMBO J , vol.31 , pp. 576-592
    • Sun, X.X.1    Challagundla, K.B.2    Dai, M.S.3
  • 278
    • 71349086190 scopus 로고    scopus 로고
    • USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha
    • W. Sun, X. Tan, Y. Shi, G. Xu, R. Mao, and X. Gu USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha Cell Signal 22 2010 386 394
    • (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
  • 279
    • 0030897596 scopus 로고    scopus 로고
    • Chemical implications for antitumor and antiviral prostaglandins: Reaction of Δ7-prostaglandin A1 and prostaglandin A1 methyl esters with thiols
    • M. Suzuki, M. Mori, T. Niwa, R. Hirata, K. Furuta, and T. Ishikawa Chemical implications for antitumor and antiviral prostaglandins: reaction of Δ7-prostaglandin A1 and prostaglandin A1 methyl esters with thiols J Am Chem Soc 119 1997 2376 2385
    • (1997) J Am Chem Soc , vol.119 , pp. 2376-2385
    • Suzuki, M.1    Mori, M.2    Niwa, T.3    Hirata, R.4    Furuta, K.5    Ishikawa, T.6
  • 280
    • 84885940995 scopus 로고    scopus 로고
    • The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks
    • S O.W
    • S.M. Sy, J. Jiang, O, W. S., Y. Deng, and M.S. Huen The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks Nucleic Acids Res 41 2013 8572 8580
    • (2013) Nucleic Acids Res , vol.41 , pp. 8572-8580
    • Sy, S.M.1    Jiang, J.2    Deng, Y.3    Huen, M.S.4
  • 281
    • 54949145341 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress contributes to the cell death induced by UCH-L1 inhibitor
    • Y.Y. Tan, H.Y. Zhou, Z.Q. Wang, and S.D. Chen Endoplasmic reticulum stress contributes to the cell death induced by UCH-L1 inhibitor Mol Cell Biochem 318 2008 109 115
    • (2008) Mol Cell Biochem , vol.318 , pp. 109-115
    • Tan, Y.Y.1    Zhou, H.Y.2    Wang, Z.Q.3    Chen, S.D.4
  • 282
    • 0020546084 scopus 로고
    • ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin
    • K. Tanaka, L. Waxman, and A.L. Goldberg ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin J Cell Biol 96 1983 1580 1585
    • (1983) J Cell Biol , vol.96 , pp. 1580-1585
    • Tanaka, K.1    Waxman, L.2    Goldberg, A.L.3
  • 283
    • 77649259009 scopus 로고    scopus 로고
    • Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling through K63-linked ubiquitination of Dvl
    • D.V. Tauriello, A. Haegebarth, I. Kuper, M.J. Edelmann, M. Henraat, and M.R. Canninga-van Dijk Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling through K63-linked ubiquitination of Dvl Mol Cell 37 2010 607 619
    • (2010) Mol Cell , vol.37 , pp. 607-619
    • Tauriello, D.V.1    Haegebarth, A.2    Kuper, I.3    Edelmann, M.J.4    Henraat, M.5    Canninga-Van Dijk, M.R.6
  • 284
    • 44149121239 scopus 로고    scopus 로고
    • The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss
    • T. Terzian, Y.A. Suh, T. Iwakuma, S.M. Post, M. Neumann, and G.A. Lang The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss Genes Dev 22 2008 1337 1344
    • (2008) Genes Dev , vol.22 , pp. 1337-1344
    • Terzian, T.1    Suh, Y.A.2    Iwakuma, T.3    Post, S.M.4    Neumann, M.5    Lang, G.A.6
  • 285
    • 80053598334 scopus 로고    scopus 로고
    • Isoform-specific localization of the deubiquitinase USP33 to the Golgi apparatus
    • C. Thorne, R.L. Eccles, J.M. Coulson, S. Urbe, and M.J. Clague Isoform-specific localization of the deubiquitinase USP33 to the Golgi apparatus Traffic 12 2011 1563 1574
    • (2011) Traffic , vol.12 , pp. 1563-1574
    • Thorne, C.1    Eccles, R.L.2    Coulson, J.M.3    Urbe, S.4    Clague, M.J.5
  • 286
    • 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
    • Z. Tian, P. D'Arcy, X. Wang, A. Ray, Y.T. Tai, and Y. Hu A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance Blood 125 2013 706 716
    • (2013) Blood , vol.125 , pp. 706-716
    • Tian, Z.1    D'Arcy, P.2    Wang, X.3    Ray, A.4    Tai, Y.T.5    Hu, Y.6
  • 287
    • 79953778442 scopus 로고    scopus 로고
    • Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescence-based multiplex assay format
    • X. Tian, N.S. Isamiddinova, R.J. Peroutka, S.J. Goldenberg, M.R. Mattern, and B. Nicholson Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescence-based multiplex assay format Assay Drug Dev Technol 9 2011 165 173
    • (2011) Assay Drug Dev Technol , vol.9 , pp. 165-173
    • Tian, X.1    Isamiddinova, N.S.2    Peroutka, R.J.3    Goldenberg, S.J.4    Mattern, M.R.5    Nicholson, B.6
  • 288
    • 77951945222 scopus 로고    scopus 로고
    • Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: Implications for proteasome structure and assembly
    • R.J. Tomko Jr., M. Funakoshi, K. Schneider, J. Wang, and M. Hochstrasser Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly Mol Cell 38 2010 393 403
    • (2010) Mol Cell , vol.38 , pp. 393-403
    • Tomko, Jr.R.J.1    Funakoshi, M.2    Schneider, K.3    Wang, J.4    Hochstrasser, M.5
  • 289
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • E. Trompouki, E. Hatzivassiliou, T. Tsichritzis, H. Farmer, A. Ashworth, and G. Mosialos CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members Nature 424 2003 793 796
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 291
    • 84863363343 scopus 로고    scopus 로고
    • Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions
    • S. Urbe, H. Liu, S.D. Hayes, C. Heride, D.J. Rigden, and M.J. Clague Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions Mol Biol Cell 23 2012 1095 1103
    • (2012) Mol Biol Cell , vol.23 , pp. 1095-1103
    • Urbe, S.1    Liu, H.2    Hayes, S.D.3    Heride, C.4    Rigden, D.J.5    Clague, M.J.6
  • 292
    • 84856844697 scopus 로고    scopus 로고
    • Arterivirus and nairovirus ovarian tumor domain-containing deubiquitinases target activated RIG-I to control innate immune signaling
    • P.B. van Kasteren, C. Beugeling, D.K. Ninaber, N. Frias-Staheli, S. van Boheemen, and A. Garcia-Sastre Arterivirus and nairovirus ovarian tumor domain-containing deubiquitinases target activated RIG-I to control innate immune signaling J Virol 86 2012 773 785
    • (2012) J Virol , vol.86 , pp. 773-785
    • Van Kasteren, P.B.1    Beugeling, C.2    Ninaber, D.K.3    Frias-Staheli, N.4    Van Boheemen, S.5    Garcia-Sastre, A.6
  • 294
    • 34447507710 scopus 로고    scopus 로고
    • A20/TNFAIP3, a new estrogen-regulated gene that confers tamoxifen resistance in breast cancer cells
    • J.A. Vendrell, S. Ghayad, S. Ben-Larbi, C. Dumontet, N. Mechti, and P.A. Cohen A20/TNFAIP3, a new estrogen-regulated gene that confers tamoxifen resistance in breast cancer cells Oncogene 26 2007 4656 4667
    • (2007) Oncogene , vol.26 , pp. 4656-4667
    • Vendrell, J.A.1    Ghayad, S.2    Ben-Larbi, S.3    Dumontet, C.4    Mechti, N.5    Cohen, P.A.6
  • 295
    • 52049085265 scopus 로고    scopus 로고
    • BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization
    • K.H. Ventii, N.S. Devi, K.L. Friedrich, T.A. Chernova, M. Tighiouart, and E.G. Van Meir BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization Cancer Res 68 2008 6953 6962
    • (2008) Cancer Res , vol.68 , pp. 6953-6962
    • Ventii, K.H.1    Devi, N.S.2    Friedrich, K.L.3    Chernova, T.A.4    Tighiouart, M.5    Van Meir, E.G.6
  • 296
    • 1842450526 scopus 로고    scopus 로고
    • Punaglandins, chlorinated prostaglandins, function as potent Michael receptors to inhibit ubiquitin isopeptidase activity
    • S.M. Verbitski, J.E. Mullally, F.A. Fitzpatrick, and C.M. Ireland Punaglandins, chlorinated prostaglandins, function as potent Michael receptors to inhibit ubiquitin isopeptidase activity J Med Chem 47 2004 2062 2070
    • (2004) J Med Chem , vol.47 , pp. 2062-2070
    • Verbitski, S.M.1    Mullally, J.E.2    Fitzpatrick, F.A.3    Ireland, C.M.4
  • 297
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • R. Verma, L. Aravind, R. Oania, W.H. McDonald, J.R. Yates III, and E.V. Koonin Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome Science 298 2002 611 615
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6
  • 298
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • D. Voges, P. Zwickl, and W. Baumeister The 26S proteasome: a molecular machine designed for controlled proteolysis Annu Rev Biochem 68 1999 1015 1068
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 299
    • 33746366513 scopus 로고    scopus 로고
    • Prostaglandin J2 alters pro-survival and pro-death gene expression patterns and 26 S proteasome assembly in human neuroblastoma cells
    • Z. Wang, V.M. Aris, K.D. Ogburn, P. Soteropoulos, and M.E. Figueiredo-Pereira Prostaglandin J2 alters pro-survival and pro-death gene expression patterns and 26 S proteasome assembly in human neuroblastoma cells J Biol Chem 281 2006 21377 21386
    • (2006) J Biol Chem , vol.281 , pp. 21377-21386
    • Wang, Z.1    Aris, V.M.2    Ogburn, K.D.3    Soteropoulos, P.4    Figueiredo-Pereira, M.E.5
  • 300
    • 79952837091 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus negatively regulates the type i interferon pathway by acting as a viral deubiquitinase
    • D. Wang, L. Fang, P. Li, L. Sun, J. Fan, and Q. Zhang The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase J Virol 85 2011 3758 3766
    • (2011) J Virol , vol.85 , pp. 3758-3766
    • Wang, D.1    Fang, L.2    Li, P.3    Sun, L.4    Fan, J.5    Zhang, Q.6
  • 301
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by Eeyarestatin i
    • Q. Wang, L. Li, and Y. Ye Inhibition of p97-dependent protein degradation by Eeyarestatin I J Biol Chem 283 2008 7445 7454
    • (2008) J Biol Chem , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 302
    • 60549109872 scopus 로고    scopus 로고
    • ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells
    • Q. Wang, H. Mora-Jensen, M.A. Weniger, P. Perez-Galan, C. Wolford, and T. Hai ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells Proc Natl Acad Sci U S A 106 2009 2200 2205
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2200-2205
    • Wang, Q.1    Mora-Jensen, H.2    Weniger, M.A.3    Perez-Galan, P.4    Wolford, C.5    Hai, T.6
  • 303
    • 84902986661 scopus 로고    scopus 로고
    • The 19S deubiquitinase inhibitor b-AP15 is enriched in cells and elicits rapid commitment to cell death
    • X. Wang, W. Stafford, M. Mazurkiewicz, M. Fryknas, S. Brjnic, and X. Zhang The 19S deubiquitinase inhibitor b-AP15 is enriched in cells and elicits rapid commitment to cell death Mol Pharmacol 85 2014 932 945
    • (2014) Mol Pharmacol , vol.85 , pp. 932-945
    • Wang, X.1    Stafford, W.2    Mazurkiewicz, M.3    Fryknas, M.4    Brjnic, S.5    Zhang, X.6
  • 304
    • 84865207113 scopus 로고    scopus 로고
    • Ataxin-3 regulates aggresome formation of copper-zinc superoxide dismutase (SOD1) by editing K63-linked polyubiquitin chains
    • H. Wang, Z. Ying, and G. Wang Ataxin-3 regulates aggresome formation of copper-zinc superoxide dismutase (SOD1) by editing K63-linked polyubiquitin chains J Biol Chem 287 2012 28576 28585
    • (2012) J Biol Chem , vol.287 , pp. 28576-28585
    • Wang, H.1    Ying, Z.2    Wang, G.3
  • 305
    • 17344364820 scopus 로고    scopus 로고
    • CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability
    • S. Wee, R.K. Geyer, T. Toda, and D.A. Wolf CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability Nat Cell Biol 7 2005 387 391
    • (2005) Nat Cell Biol , vol.7 , pp. 387-391
    • Wee, S.1    Geyer, R.K.2    Toda, T.3    Wolf, D.A.4
  • 306
    • 78650078496 scopus 로고    scopus 로고
    • Quantitative reactivity profiling predicts functional cysteines in proteomes
    • E. Weerapana, C. Wang, G.M. Simon, F. Richter, S. Khare, and M.B. Dillon Quantitative reactivity profiling predicts functional cysteines in proteomes Nature 468 2010 790 795
    • (2010) Nature , vol.468 , pp. 790-795
    • Weerapana, E.1    Wang, C.2    Simon, G.M.3    Richter, F.4    Khare, S.5    Dillon, M.B.6
  • 308
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • I.E. Wertz, K.M. O'Rourke, H. Zhou, M. Eby, L. Aravind, and S. Seshagiri De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling Nature 430 2004 694 699
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5    Seshagiri, S.6
  • 309
    • 0036842130 scopus 로고    scopus 로고
    • Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease
    • S.M. Wilson, B. Bhattacharyya, R.A. Rachel, V. Coppola, L. Tessarollo, and D.B. Householder Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease Nat Genet 32 2002 420 425
    • (2002) Nat Genet , vol.32 , pp. 420-425
    • Wilson, S.M.1    Bhattacharyya, B.2    Rachel, R.A.3    Coppola, V.4    Tessarollo, L.5    Householder, D.B.6
  • 310
    • 0037189946 scopus 로고    scopus 로고
    • Proteasome inhibitors stimulate activator protein-1 pathway via reactive oxygen species production
    • H.M. Wu, K.H. Chi, and W.W. Lin Proteasome inhibitors stimulate activator protein-1 pathway via reactive oxygen species production FEBS Lett 526 2002 101 105
    • (2002) FEBS Lett , vol.526 , pp. 101-105
    • Wu, H.M.1    Chi, K.H.2    Lin, W.W.3
  • 311
    • 4344646977 scopus 로고    scopus 로고
    • Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8
    • X. Wu, L. Yen, L. Irwin, C. Sweeney, and K.L. Carraway III Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8 Mol Cell Biol 24 2004 7748 7757
    • (2004) Mol Cell Biol , vol.24 , pp. 7748-7757
    • Wu, X.1    Yen, L.2    Irwin, L.3    Sweeney, C.4    Carraway, K.L.5
  • 312
    • 20344405555 scopus 로고    scopus 로고
    • Gambogic acid inhibits proliferation of human lung carcinoma SPC-A1 cells in vivo and in vitro and represses telomerase activity and telomerase reverse transcriptase mRNA expression in the cells
    • Z.Q. Wu, Q.L. Guo, Q.D. You, L. Zhao, and H.Y. Gu Gambogic acid inhibits proliferation of human lung carcinoma SPC-A1 cells in vivo and in vitro and represses telomerase activity and telomerase reverse transcriptase mRNA expression in the cells Biol Pharm Bull 27 2004 1769 1774
    • (2004) Biol Pharm Bull , vol.27 , pp. 1769-1774
    • Wu, Z.Q.1    Guo, Q.L.2    You, Q.D.3    Zhao, L.4    Gu, H.Y.5
  • 313
    • 84885868036 scopus 로고    scopus 로고
    • The deubiquitinase USP28 stabilizes LSD1 and confers stem-cell-like traits to breast cancer cells
    • Y. Wu, Y. Wang, X.H. Yang, T. Kang, Y. Zhao, and C. Wang The deubiquitinase USP28 stabilizes LSD1 and confers stem-cell-like traits to breast cancer cells Cell Rep 5 2013 224 236
    • (2013) Cell Rep , vol.5 , pp. 224-236
    • Wu, Y.1    Wang, Y.2    Yang, X.H.3    Kang, T.4    Zhao, Y.5    Wang, C.6
  • 314
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • P. Xu, D.M. Duong, N.T. Seyfried, D. Cheng, Y. Xie, and J. Robert Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation Cell 137 2009 133 145
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6
  • 315
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • T. Yao, and R.E. Cohen A cryptic protease couples deubiquitination and degradation by the proteasome Nature 419 2002 403 407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 316
    • 33748188085 scopus 로고    scopus 로고
    • Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
    • T. Yao, L. Song, W. Xu, G.N. DeMartino, L. Florens, and S.K. Swanson Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1 Nat Cell Biol 8 2006 994 1002
    • (2006) Nat Cell Biol , vol.8 , pp. 994-1002
    • Yao, T.1    Song, L.2    Xu, W.3    Demartino, G.N.4    Florens, L.5    Swanson, S.K.6
  • 317
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Y. Ye, and M. Rape Building ubiquitin chains: E2 enzymes at work Nat Rev Mol Cell Biol 10 2009 755 764
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 318
    • 40949101023 scopus 로고    scopus 로고
    • Gambogic acid inhibits angiogenesis and prostate tumor growth by suppressing vascular endothelial growth factor receptor 2 signaling
    • T. Yi, Z. Yi, S.G. Cho, J. Luo, M.K. Pandey, and B.B. Aggarwal Gambogic acid inhibits angiogenesis and prostate tumor growth by suppressing vascular endothelial growth factor receptor 2 signaling Cancer Res 68 2008 1843 1850
    • (2008) Cancer Res , vol.68 , pp. 1843-1850
    • Yi, T.1    Yi, Z.2    Cho, S.G.3    Luo, J.4    Pandey, M.K.5    Aggarwal, B.B.6
  • 319
    • 75749132016 scopus 로고    scopus 로고
    • USP10 regulates p53 localization and stability by deubiquitinating p53
    • J. Yuan, K. Luo, L. Zhang, J.C. Cheville, and Z. Lou USP10 regulates p53 localization and stability by deubiquitinating p53 Cell 140 2010 384 396
    • (2010) Cell , vol.140 , pp. 384-396
    • Yuan, J.1    Luo, K.2    Zhang, L.3    Cheville, J.C.4    Lou, Z.5
  • 320
    • 70149121734 scopus 로고    scopus 로고
    • Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in inhibiting breast cancer cell migration
    • J. Yuasa-Kawada, M. Kinoshita-Kawada, Y. Rao, and J.Y. Wu Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in inhibiting breast cancer cell migration Proc Natl Acad Sci U S A 106 2009 14530 14535
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14530-14535
    • Yuasa-Kawada, J.1    Kinoshita-Kawada, M.2    Rao, Y.3    Wu, J.Y.4
  • 321
    • 84870562210 scopus 로고    scopus 로고
    • USP44 regulates centrosome positioning to prevent aneuploidy and suppress tumorigenesis
    • Y. Zhang, O. Foreman, D.A. Wigle, F. Kosari, G. Vasmatzis, and J.L. Salisbury USP44 regulates centrosome positioning to prevent aneuploidy and suppress tumorigenesis J Clin Invest 122 2012 4362 4374
    • (2012) J Clin Invest , vol.122 , pp. 4362-4374
    • Zhang, Y.1    Foreman, O.2    Wigle, D.A.3    Kosari, F.4    Vasmatzis, G.5    Salisbury, J.L.6
  • 322
    • 0347320714 scopus 로고    scopus 로고
    • Discovery, characterization and SAR of gambogic acid as a potent apoptosis inducer by a HTS assay
    • H.Z. Zhang, S. Kasibhatla, Y. Wang, J. Herich, J. Guastella, and B. Tseng Discovery, characterization and SAR of gambogic acid as a potent apoptosis inducer by a HTS assay Bioorg Med Chem 12 2004 309 317
    • (2004) Bioorg Med Chem , vol.12 , pp. 309-317
    • Zhang, H.Z.1    Kasibhatla, S.2    Wang, Y.3    Herich, J.4    Guastella, J.5    Tseng, B.6
  • 323
    • 80051654271 scopus 로고    scopus 로고
    • Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia
    • Y. Zhang, J. van Deursen, and P.J. Galardy Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia PLoS One 6 2011 e23389
    • (2011) PLoS One , vol.6 , pp. e23389
    • Zhang, Y.1    Van Deursen, J.2    Galardy, P.J.3
  • 324
    • 65649123769 scopus 로고    scopus 로고
    • Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii
    • F. Zhang, Z. Wu, P. Zhang, G. Tian, D. Finley, and Y. Shi Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii Mol Cell 34 2009 485 496
    • (2009) Mol Cell , vol.34 , pp. 485-496
    • Zhang, F.1    Wu, Z.2    Zhang, P.3    Tian, G.4    Finley, D.5    Shi, Y.6
  • 325
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • D. Zhang, K. Zaugg, T.W. Mak, and S.J. Elledge A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response Cell 126 2006 529 542
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 326
    • 38149068875 scopus 로고    scopus 로고
    • A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing
    • Y. Zhao, G. Lang, S. Ito, J. Bonnet, E. Metzger, and S. Sawatsubashi A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing Mol Cell 29 2008 92 101
    • (2008) Mol Cell , vol.29 , pp. 92-101
    • Zhao, Y.1    Lang, G.2    Ito, S.3    Bonnet, J.4    Metzger, E.5    Sawatsubashi, S.6
  • 327
    • 84894087907 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases 25 negatively regulates virus-induced type i interferon signaling
    • H. Zhong, D. Wang, L. Fang, H. Zhang, R. Luo, and M. Shang Ubiquitin-specific proteases 25 negatively regulates virus-induced type I interferon signaling PLoS One 8 2013 e80976
    • (2013) PLoS One , vol.8 , pp. e80976
    • Zhong, H.1    Wang, D.2    Fang, L.3    Zhang, H.4    Luo, R.5    Shang, M.6
  • 328
    • 84882265186 scopus 로고    scopus 로고
    • Deubiquitinase inhibition of 19S regulatory particles by 4-arylidene curcumin analog AC17 causes NF-kappaB inhibition and p53 reactivation in human lung cancer cells
    • B. Zhou, Y. Zuo, B. Li, H. Wang, H. Liu, and X. Wang Deubiquitinase inhibition of 19S regulatory particles by 4-arylidene curcumin analog AC17 causes NF-kappaB inhibition and p53 reactivation in human lung cancer cells Mol Cancer Ther 12 2013 1381 1392
    • (2013) Mol Cancer Ther , vol.12 , pp. 1381-1392
    • Zhou, B.1    Zuo, Y.2    Li, B.3    Wang, H.4    Liu, H.5    Wang, X.6
  • 329
    • 0026600718 scopus 로고
    • Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase
    • P. Zwickl, A. Grziwa, G. Puhler, B. Dahlmann, F. Lottspeich, and W. Baumeister Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase Biochemistry 31 1992 964 972
    • (1992) Biochemistry , vol.31 , pp. 964-972
    • Zwickl, P.1    Grziwa, A.2    Puhler, G.3    Dahlmann, B.4    Lottspeich, F.5    Baumeister, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.