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Volumn 17, Issue 9, 2013, Pages 1091-1108

Targeting the ubiquitin-proteasome system for cancer therapy

Author keywords

Cancer therapy; Deubiquitinases; E3 ligases; Proteasome; Small molecule inhibitors; Ubiquitin

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANAPHASE PROMOTING COMPLEX; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CARFILZOMIB; CHYMOTRYPSIN; DELANZOMIB; F BOX PROTEIN; FANCONI ANEMIA PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IXAZOMIB CITRATE; NEDD8 PROTEIN; NUTLIN 3; OPROZOMIB; PEVONEDISTAT; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN MDM2; PROTEIN P27; PROTEIN P53; SALINOSPORAMIDE A; SERDEMETAN; TOSYLARGININE METHYL ESTER; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME 13;

EID: 84882575961     PISSN: 14728222     EISSN: 17447631     Source Type: Journal    
DOI: 10.1517/14728222.2013.815728     Document Type: Review
Times cited : (167)

References (96)
  • 1
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee DH, Goldberg AL. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 1998;8:397-403
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 2
    • 34347329214 scopus 로고    scopus 로고
    • Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging
    • Jin J, Li X, Gygi SP, Harper JW. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature 2007;447:1135-8
    • (2007) Nature , vol.447 , pp. 1135-1138
    • Jin, J.1    Li, X.2    Gygi, S.P.3    Harper, J.W.4
  • 3
    • 77951651753 scopus 로고    scopus 로고
    • The family of ubiquitin-conjugating enzymes (E2s): Deciding between life and death of proteins
    • van Wijk SJ, Timmers HT. The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J 2010;24:981-93
    • (2010) FASEB J , vol.24 , pp. 981-993
    • Van Wijk, S.J.1    Timmers, H.T.2
  • 4
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger MB, Hristova VA, Weissman AM. HECT and RING finger families of E3 ubiquitin ligases at a glance. J Cell Sci 2012;125:531-7
    • (2012) J Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 5
    • 77955516435 scopus 로고    scopus 로고
    • K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody
    • Matsumoto ML, Wickliffe KE, Dong KC, et al. K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody. Mol Cell 2010;39:477-84
    • (2010) Mol Cell , vol.39 , pp. 477-484
    • Matsumoto, M.L.1    Wickliffe, K.E.2    Dong, K.C.3
  • 6
    • 84861877407 scopus 로고    scopus 로고
    • The ubiquitin code
    • Komander D, Rape M. The ubiquitin code. Annu Rev Biochem 2012;81:203-29 A comprehensive review describing all aspects of the ubiquitin chains and linkage specificity.
    • (2012) Annu Rev Biochem , vol.81 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 7
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002;82:373-4288.
    • (2002) Physiol Rev , vol.82 , pp. 373-4288
    • Glickman, M.H.1    Ciechanover, A.2
  • 8
    • 0030905981 scopus 로고    scopus 로고
    • New insights into the mechanisms and importance of the proteasome in intracellular protein degradation
    • Goldberg AL, Akopian TN, Kisselev AF, et al. New insights into the mechanisms and importance of the proteasome in intracellular protein degradation. Biol Chem 1997;378:131-40
    • (1997) Biol Chem , vol.378 , pp. 131-140
    • Goldberg, A.L.1    Akopian, T.N.2    Kisselev, A.F.3
  • 9
    • 78049264771 scopus 로고    scopus 로고
    • The 26S proteasome: Assembly and function of a destructive machine
    • Gallastegui N, Groll M. The 26S proteasome: assembly and function of a destructive machine. Trends Biochem Sci 2010;35:634-42
    • (2010) Trends Biochem Sci , vol.35 , pp. 634-642
    • Gallastegui, N.1    Groll, M.2
  • 10
    • 26244445001 scopus 로고    scopus 로고
    • Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class i antigen processing
    • Strehl B, Seifert U, Kruger E, et al. Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing. Immunol Rev 2005;207:19-30
    • (2005) Immunol Rev , vol.207 , pp. 19-30
    • Strehl, B.1    Seifert, U.2    Kruger, E.3
  • 11
    • 84859164670 scopus 로고    scopus 로고
    • Immune and non-immune functions of the immunoproteasome
    • Angeles A, Fung G, Luo H. Immune and non-immune functions of the immunoproteasome. Front Biosci 2012;17:1904-16
    • (2012) Front Biosci , vol.17 , pp. 1904-1916
    • Angeles, A.1    Fung, G.2    Luo, H.3
  • 12
    • 84861380457 scopus 로고    scopus 로고
    • Deubiquitinases in cancer: New functions and therapeutic options
    • Fraile JM, Quesada V, Rodriguez D, et al. Deubiquitinases in cancer: new functions and therapeutic options. Oncogene 2012;31:2373-88
    • (2012) Oncogene , vol.31 , pp. 2373-2388
    • Fraile, J.M.1    Quesada, V.2    Rodriguez, D.3
  • 13
    • 70450270900 scopus 로고    scopus 로고
    • Awakening guardian angels: Drugging the p53 pathway
    • Brown CJ, Lain S, Verma CS, et al. Awakening guardian angels: drugging the p53 pathway. Nat Rev Cancer 2009;9:862-73
    • (2009) Nat Rev Cancer , vol.9 , pp. 862-873
    • Brown, C.J.1    Lain, S.2    Verma, C.S.3
  • 15
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie PH, Gorina S, Marechal V, et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996;274:948-5316.
    • (1996) Science , vol.274 , pp. 948-5316
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 16
    • 33244490784 scopus 로고    scopus 로고
    • Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: Implications for the regulation of the p53-MDM2 pathway
    • Hu M, Gu L, Li M, et al. Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway. PLoS Biol 2006;4:e27
    • (2006) PLoS Biol , vol.4
    • Hu, M.1    Gu, L.2    Li, M.3
  • 17
    • 0037325853 scopus 로고    scopus 로고
    • Deregulated degradation of the cdk inhibitor p27 and malignant transformation
    • Bloom J, Pagano M. Deregulated degradation of the cdk inhibitor p27 and malignant transformation. Semin Cancer Biol 2003;13:41-7
    • (2003) Semin Cancer Biol , vol.13 , pp. 41-47
    • Bloom, J.1    Pagano, M.2
  • 18
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng N, Schulman BA, Song L, et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 2002;416:703-9
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1    Schulman, B.A.2    Song, L.3
  • 19
    • 0035476237 scopus 로고    scopus 로고
    • High expression of S-phase kinase-interacting protein 2, human F-box protein, correlates with poor prognosis in oral squamous cell carcinomas
    • Kudo Y, Kitajima S, Sato S, et al. High expression of S-phase kinase-interacting protein 2, human F-box protein, correlates with poor prognosis in oral squamous cell carcinomas. Cancer Res 2001;61:7044-7
    • (2001) Cancer Res , vol.61 , pp. 7044-7047
    • Kudo, Y.1    Kitajima, S.2    Sato, S.3
  • 20
    • 0035942224 scopus 로고    scopus 로고
    • Skp2 is oncogenic and overexpressed in human cancers
    • Gstaiger M, Jordan R, Lim M, et al. Skp2 is oncogenic and overexpressed in human cancers. Proc Natl Acad Sci USA 2001;98:5043-8
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5043-5048
    • Gstaiger, M.1    Jordan, R.2    Lim, M.3
  • 21
    • 0035340719 scopus 로고    scopus 로고
    • Inverse relation between levels of p27(Kip1) and of its ubiquitin ligase subunit Skp2 in colorectal carcinomas
    • Hershko D, Bornstein G, Ben-Izhak O, et al. Inverse relation between levels of p27(Kip1) and of its ubiquitin ligase subunit Skp2 in colorectal carcinomas. Cancer 2001;91:1745-51
    • (2001) Cancer , vol.91 , pp. 1745-1751
    • Hershko, D.1    Bornstein, G.2    Ben-Izhak, O.3
  • 22
    • 0036645405 scopus 로고    scopus 로고
    • Clinical and biological significance of S-phase kinase-associated protein 2 (Skp2) gene expression in gastric carcinoma: Modulation of malignant phenotype by Skp2 overexpression, possibly via p27 proteolysis
    • Masuda TA, Inoue H, Sonoda H, et al. Clinical and biological significance of S-phase kinase-associated protein 2 (Skp2) gene expression in gastric carcinoma: modulation of malignant phenotype by Skp2 overexpression, possibly via p27 proteolysis. Cancer Res 2002;62:3819-25
    • (2002) Cancer Res , vol.62 , pp. 3819-3825
    • Masuda, T.A.1    Inoue, H.2    Sonoda, H.3
  • 23
    • 0036102867 scopus 로고    scopus 로고
    • S-phase kinase-associated protein 2 expression in non-Hodgkin's lymphoma inversely correlates with p27 expression and defines cells in S phase
    • Chiarle R, Fan Y, Piva R, et al. S-phase kinase-associated protein 2 expression in non-Hodgkin's lymphoma inversely correlates with p27 expression and defines cells in S phase. Am J Pathol 2002;160:1457-66
    • (2002) Am J Pathol , vol.160 , pp. 1457-1466
    • Chiarle, R.1    Fan, Y.2    Piva, R.3
  • 24
    • 70349339322 scopus 로고    scopus 로고
    • Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
    • Merlet J, Burger J, Gomes JE, Pintard L. Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization. Cell Mol Life Sci 2009;66:1924-38
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1924-1938
    • Merlet, J.1    Burger, J.2    Gomes, J.E.3    Pintard, L.4
  • 25
    • 2442649167 scopus 로고    scopus 로고
    • Blockade of ubiquitin-conjugating enzyme CDC34 enhances anti-myeloma activity of Bortezomib/Proteasome inhibitor PS-341
    • Chauhan D, Li G, Hideshima T, et al. Blockade of ubiquitin-conjugating enzyme CDC34 enhances anti-myeloma activity of Bortezomib/Proteasome inhibitor PS-341. Oncogene 2004;23:3597-602
    • (2004) Oncogene , vol.23 , pp. 3597-3602
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 26
    • 77649237309 scopus 로고    scopus 로고
    • NF-kappaB and cancer: How intimate is this relationship
    • Prasad S, Ravindran J, Aggarwal BB. NF-kappaB and cancer: how intimate is this relationship. Mol Cell Biochem 2010;336:25-37
    • (2010) Mol Cell Biochem , vol.336 , pp. 25-37
    • Prasad, S.1    Ravindran, J.2    Aggarwal, B.B.3
  • 27
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-kappaB activation
    • Iwai K. Diverse ubiquitin signaling in NF-kappaB activation. Trends Cell Biol 2012;22:355-6428.
    • (2012) Trends Cell Biol , vol.22 , pp. 355-6428
    • Iwai, K.1
  • 28
    • 35148886143 scopus 로고    scopus 로고
    • Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics
    • Yang Y, Kitagaki J, Dai RM, et al. Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics. Cancer Res 2007;67:9472-81
    • (2007) Cancer Res , vol.67 , pp. 9472-9481
    • Yang, Y.1    Kitagaki, J.2    Dai, R.M.3
  • 29
    • 77950421253 scopus 로고    scopus 로고
    • The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma
    • Xu GW, Ali M, Wood TE, et al. The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma. Blood 2010;115:2251-930.
    • (2010) Blood , vol.115 , pp. 2251-2930
    • Xu, G.W.1    Ali, M.2    Wood, T.E.3
  • 30
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, et al. An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 2009;458:732-631.
    • (2009) Nature , vol.458 , pp. 732-631
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3
  • 31
    • 77956578834 scopus 로고    scopus 로고
    • MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: Rationale for treatment of NF-{kappa}B-dependent lymphoma
    • Milhollen MA, Traore T, Adams-Duffy J, et al. MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: rationale for treatment of NF-{kappa}B-dependent lymphoma. Blood 2010;116:1515-2332.
    • (2010) Blood , vol.116 , pp. 1515-2332
    • Milhollen, M.A.1    Traore, T.2    Adams-Duffy, J.3
  • 32
    • 73649110303 scopus 로고    scopus 로고
    • Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: The NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ
    • Brownell JE, Sintchak MD, Gavin JM, et al. Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ. Mol Cell 2010;37:102-11
    • (2010) Mol Cell , vol.37 , pp. 102-111
    • Brownell, J.E.1    Sintchak, M.D.2    Gavin, J.M.3
  • 33
    • 79959656754 scopus 로고    scopus 로고
    • An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme
    • Ceccarelli DF, Tang X, Pelletier B, et al. An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme. Cell 2011;145:1075-8734.
    • (2011) Cell , vol.145 , pp. 1075-8734
    • Ceccarelli, D.F.1    Tang, X.2    Pelletier, B.3
  • 34
    • 84865415118 scopus 로고    scopus 로고
    • Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A
    • Pulvino M, Liang Y, Oleksyn D, et al. Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A. Blood 2012;120:1668-77
    • (2012) Blood , vol.120 , pp. 1668-1677
    • Pulvino, M.1    Liang, Y.2    Oleksyn, D.3
  • 35
    • 77955341070 scopus 로고    scopus 로고
    • Protein-protein interaction antagonists as novel inhibitors of non-canonical polyubiquitylation
    • Scheper J, Guerra-Rebollo M, Sanclimens G, et al. Protein-protein interaction antagonists as novel inhibitors of non-canonical polyubiquitylation. PLoS One 2010;5:e11403
    • (2010) PLoS One , vol.5
    • Scheper, J.1    Guerra-Rebollo, M.2    Sanclimens, G.3
  • 36
    • 84876494247 scopus 로고    scopus 로고
    • Novel inhibitors of rad6 ubiquitin conjugating enzyme: Design, synthesis, identification, and functional characterization
    • Sanders MA, Brahemi G, Nangia-Makker P, et al. Novel inhibitors of rad6 ubiquitin conjugating enzyme: design, synthesis, identification, and functional characterization. Mol Cancer Ther 2013;12:373-83
    • (2013) Mol Cancer Ther , vol.12 , pp. 373-383
    • Sanders, M.A.1    Brahemi, G.2    Nangia-Makker, P.3
  • 37
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004;303:844-838.
    • (2004) Science , vol.303 , pp. 844-838
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 38
    • 33745154819 scopus 로고    scopus 로고
    • Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction
    • Ding K, Lu Y, Nikolovska-Coleska Z, et al. Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction. J Med Chem 2006;49:3432-5
    • (2006) J Med Chem , vol.49 , pp. 3432-3435
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 39
    • 22944473048 scopus 로고    scopus 로고
    • Structure-based design of potent non-peptide MDM2 inhibitors
    • Ding K, Lu Y, Nikolovska-Coleska Z, et al. Structure-based design of potent non-peptide MDM2 inhibitors. J Am Chem Soc 2005;127:10130-1
    • (2005) J Am Chem Soc , vol.127 , pp. 10130-10131
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 40
    • 41649102468 scopus 로고    scopus 로고
    • Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition
    • Shangary S, Qin D, McEachern D, et al. Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition. Proc Natl Acad Sci USA 2008;105:3933-8
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3933-3938
    • Shangary, S.1    Qin, D.2    McEachern, D.3
  • 41
    • 72549094296 scopus 로고    scopus 로고
    • An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals
    • Mohammad RM, Wu J, Azmi AS, et al. An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals. Mol Cancer 2009;8:115
    • (2009) Mol Cancer , vol.8 , pp. 115
    • Mohammad, R.M.1    Wu, J.2    Azmi, A.S.3
  • 43
    • 33644873086 scopus 로고    scopus 로고
    • Benzodiazepinedione inhibitors of the Hdm2: P53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo
    • Koblish HK, Zhao S, Franks CF, et al. Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo. Mol Cancer Ther 2006;5:160-9
    • (2006) Mol Cancer Ther , vol.5 , pp. 160-169
    • Koblish, H.K.1    Zhao, S.2    Franks, C.F.3
  • 44
    • 13944274061 scopus 로고    scopus 로고
    • Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells
    • Grasberger BL, Lu T, Schubert C, et al. Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells. J Med Chem 2005;48:909-12
    • (2005) J Med Chem , vol.48 , pp. 909-912
    • Grasberger, B.L.1    Lu, T.2    Schubert, C.3
  • 45
    • 84873055344 scopus 로고    scopus 로고
    • MDM2, MDMX and p53 in oncogenesis and cancer therapy
    • Wade M, Li YC, Wahl GM. MDM2, MDMX and p53 in oncogenesis and cancer therapy. Nat Rev Cancer 2013;13:83-96
    • (2013) Nat Rev Cancer , vol.13 , pp. 83-96
    • Wade, M.1    Li, Y.C.2    Wahl, G.M.3
  • 46
    • 20444369867 scopus 로고    scopus 로고
    • Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
    • Yang Y, Ludwig RL, Jensen JP, et al. Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells. Cancer Cell 2005;7:547-59
    • (2005) Cancer Cell , vol.7 , pp. 547-559
    • Yang, Y.1    Ludwig, R.L.2    Jensen, J.P.3
  • 47
    • 53349153446 scopus 로고    scopus 로고
    • Targeting tumor cells expressing p53 with a water-soluble inhibitor of Hdm2
    • Kitagaki J, Agama KK, Pommier Y, et al. Targeting tumor cells expressing p53 with a water-soluble inhibitor of Hdm2. Mol Cancer Ther 2008;7:2445-54
    • (2008) Mol Cancer Ther , vol.7 , pp. 2445-2454
    • Kitagaki, J.1    Agama, K.K.2    Pommier, Y.3
  • 48
    • 84865149674 scopus 로고    scopus 로고
    • Discovery of Mdm2-MdmX E3 ligase inhibitors using a cell-based ubiquitination assay
    • Herman AG, Hayano M, Poyurovsky MV, et al. Discovery of Mdm2-MdmX E3 ligase inhibitors using a cell-based ubiquitination assay. Cancer Discov 2011;1:312-25
    • (2011) Cancer Discov , vol.1 , pp. 312-325
    • Herman, A.G.1    Hayano, M.2    Poyurovsky, M.V.3
  • 49
    • 77951224332 scopus 로고    scopus 로고
    • Identification and characterization of the first small molecule inhibitor of MDMX
    • Reed D, Shen Y, Shelat AA, et al. Identification and characterization of the first small molecule inhibitor of MDMX. J Biol Chem 2010;285:10786-96
    • (2010) J Biol Chem , vol.285 , pp. 10786-10796
    • Reed, D.1    Shen, Y.2    Shelat, A.A.3
  • 50
    • 84863966819 scopus 로고    scopus 로고
    • Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization
    • Graves B, Thompson T, Xia M, et al. Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization. Proc Natl Acad Sci USA 2012;109:11788-93
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 11788-11793
    • Graves, B.1    Thompson, T.2    Xia, M.3
  • 51
    • 47149092405 scopus 로고    scopus 로고
    • Targeting the p27 E3 ligase SCF(Skp2) results in p27-and Skp2-mediated cellcycle arrest and activation of autophagy
    • Chen Q, Xie W, Kuhn DJ, et al. Targeting the p27 E3 ligase SCF(Skp2) results in p27-and Skp2-mediated cellcycle arrest and activation of autophagy. Blood 2008;111:4690-9
    • (2008) Blood , vol.111 , pp. 4690-4699
    • Chen, Q.1    Xie, W.2    Kuhn, D.J.3
  • 52
    • 84871569969 scopus 로고    scopus 로고
    • Specific small molecule inhibitors of Skp2-mediated p27 degradation
    • Wu L, Grigoryan AV, Li Y, et al. Specific small molecule inhibitors of Skp2-mediated p27 degradation. Chem Biol 2012;19:1515-24
    • (2012) Chem Biol , vol.19 , pp. 1515-1524
    • Wu, L.1    Grigoryan, A.V.2    Li, Y.3
  • 53
    • 77957947338 scopus 로고    scopus 로고
    • Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage
    • Zeng X, Sigoillot F, Gaur S, et al. Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage. Cancer Cell 2010;18:382-95
    • (2010) Cancer Cell , vol.18 , pp. 382-395
    • Zeng, X.1    Sigoillot, F.2    Gaur, S.3
  • 54
    • 84899158409 scopus 로고    scopus 로고
    • From bortezomib to other inhibitors of the proteasome and beyond
    • Buac D, Shen M, Schmitt S, et al. From bortezomib to other inhibitors of the proteasome and beyond. Curr Pharm Des 2013;19(22):4025-38
    • (2013) Curr Pharm des , vol.19 , Issue.22 , pp. 4025-4038
    • Buac, D.1    Shen, M.2    Schmitt, S.3
  • 55
    • 84882614053 scopus 로고    scopus 로고
    • Proteasome inhibition as a novel strategy for cancer treatment
    • In: Johnson DE, editor. Springer, New York
    • Shen M, Dou QP. Proteasome inhibition as a novel strategy for cancer treatment. In: Johnson DE, editor. Cell death signaling in cancer biology and treatment. Springer, New York; 2013. p. 303-29
    • (2013) Cell Death Signaling in Cancer Biology and Treatment , pp. 303-329
    • Shen, M.1    Dou, Q.P.2
  • 56
    • 78149299837 scopus 로고    scopus 로고
    • Proteasome inhibitors: Dozens of molecules and still counting
    • de Bettignies G, Coux O. Proteasome inhibitors: dozens of molecules and still counting. Biochimie 2010;92:1530-4557.
    • (2010) Biochimie , vol.92 , pp. 1530-4557
    • De Bettignies, G.1    Coux, O.2
  • 57
    • 84856373151 scopus 로고    scopus 로고
    • Proteasome inhibitors: An expanding army attacking a unique target
    • Kisselev AF, van der Linden WA, Overkleeft HS. Proteasome inhibitors: an expanding army attacking a unique target. Chem Biol 2012;19:99-11558.
    • (2012) Chem Biol , vol.19 , pp. 99-11558
    • Kisselev, A.F.1    Van Der Linden, W.A.2    Overkleeft, H.S.3
  • 58
    • 33947659939 scopus 로고    scopus 로고
    • 20S proteasome and its inhibitors: Crystallographic knowledge for drug development
    • Borissenko L, Groll M. 20S proteasome and its inhibitors: crystallographic knowledge for drug development. Chem Rev 2007;107:687-71759.
    • (2007) Chem Rev , vol.107 , pp. 687-71759
    • Borissenko, L.1    Groll, M.2
  • 59
    • 0037441760 scopus 로고    scopus 로고
    • Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341
    • Hideshima T, Mitsiades C, Akiyama M, et al. Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341. Blood 2003;101:1530-460.
    • (2003) Blood , vol.101 , pp. 1530-2460
    • Hideshima, T.1    Mitsiades, C.2    Akiyama, M.3
  • 60
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T, Richardson P, Chauhan D, et al. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res 2001;61:3071-6
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 61
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M, Tam SW, Theodoras AM, et al. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995;269:682-562.
    • (1995) Science , vol.269 , pp. 682-562
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3
  • 62
    • 0028342731 scopus 로고
    • Complete reconstitution of conjugation and subsequentdegradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system
    • Shkedy D, Gonen H, Bercovich B, Ciechanover A. Complete reconstitution of conjugation and subsequentdegradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system. FEBS Lett 1994;348:126-30
    • (1994) FEBS Lett , vol.348 , pp. 126-130
    • Shkedy, D.1    Gonen, H.2    Bercovich, B.3    Ciechanover, A.4
  • 63
    • 0034574498 scopus 로고    scopus 로고
    • The ubiquitin-dependent proteolytic system and other potential targets for the modulation of nuclear factor-kB (NF-kB)
    • Magnani M, Crinelli R, Bianchi M, Antonelli A. The ubiquitin-dependent proteolytic system and other potential targets for the modulation of nuclear factor-kB (NF-kB). Curr Drug Targets 2000;1:387-99
    • (2000) Curr Drug Targets , vol.1 , pp. 387-399
    • Magnani, M.1    Crinelli, R.2    Bianchi, M.3    Antonelli, A.4
  • 64
    • 0242496212 scopus 로고    scopus 로고
    • Molecular sequelae of proteasome inhibition in human multiple myeloma cells
    • Mitsiades N, Mitsiades CS, Poulaki V, et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci USA 2002;99:14374-965.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14374-14965
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 65
    • 34548280809 scopus 로고    scopus 로고
    • Proteasome inhibition specifically sensitizes leukemic cells to anthracyclin-induced apoptosis through the accumulation of Bim and Bax pro-apoptotic proteins
    • Pigneux A, Mahon FX, Moreau-Gaudry F, et al. Proteasome inhibition specifically sensitizes leukemic cells to anthracyclin-induced apoptosis through the accumulation of Bim and Bax pro-apoptotic proteins. Cancer Biol Ther 2007;6:603-11
    • (2007) Cancer Biol Ther , vol.6 , pp. 603-611
    • Pigneux, A.1    Mahon, F.X.2    Moreau-Gaudry, F.3
  • 66
    • 7644242953 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells
    • Fribley A, Zeng Q, Wang CY. Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells. Mol Cell Biol 2004;24:9695-704
    • (2004) Mol Cell Biol , vol.24 , pp. 9695-9704
    • Fribley, A.1    Zeng, Q.2    Wang, C.Y.3
  • 68
    • 52049086674 scopus 로고    scopus 로고
    • Overexpression of the PSMB5 gene contributes to bortezomib resistance in T-lymphoblastic lymphoma/leukemia cells derived from Jurkat line
    • Lu S, Chen Z, Yang J, et al. Overexpression of the PSMB5 gene contributes to bortezomib resistance in T-lymphoblastic lymphoma/leukemia cells derived from Jurkat line. Exp Hematol 2008;36:1278-84
    • (2008) Exp Hematol , vol.36 , pp. 1278-1284
    • Lu, S.1    Chen, Z.2    Yang, J.3
  • 69
    • 53049106912 scopus 로고    scopus 로고
    • Molecular basis of bortezomib resistance: Proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein
    • Oerlemans R, Franke NE, Assaraf YG, et al. Molecular basis of bortezomib resistance: proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein. Blood 2008;112:2489-99
    • (2008) Blood , vol.112 , pp. 2489-2499
    • Oerlemans, R.1    Franke, N.E.2    Assaraf, Y.G.3
  • 70
    • 84859648046 scopus 로고    scopus 로고
    • Impaired bortezomib binding to mutant beta5 subunit of the proteasome is the underlying basis for bortezomib resistance in leukemia cells
    • Franke NE, Niewerth D, Assaraf YG, et al. Impaired bortezomib binding to mutant beta5 subunit of the proteasome is the underlying basis for bortezomib resistance in leukemia cells. Leukemia 2012;26(4):757-68
    • (2012) Leukemia , vol.26 , Issue.4 , pp. 757-768
    • Franke, N.E.1    Niewerth, D.2    Assaraf, Y.G.3
  • 71
    • 70449713654 scopus 로고    scopus 로고
    • GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib
    • Kern J, Untergasser G, Zenzmaier C, et al. GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib. Blood 2009;114:3960-7
    • (2009) Blood , vol.114 , pp. 3960-3967
    • Kern, J.1    Untergasser, G.2    Zenzmaier, C.3
  • 72
    • 70450285396 scopus 로고    scopus 로고
    • Acquisition of a multidrug-resistant phenotype with a proteasome inhibitor in multiple myeloma
    • Gutman D, Morales AA, Boise LH. Acquisition of a multidrug-resistant phenotype with a proteasome inhibitor in multiple myeloma. Leukemia 2009;23:2181-3
    • (2009) Leukemia , vol.23 , pp. 2181-2183
    • Gutman, D.1    Morales, A.A.2    Boise, L.H.3
  • 73
    • 52449135431 scopus 로고    scopus 로고
    • Bortezomib-resistant nuclear factor-kappaB activity in multiple myeloma cells
    • Markovina S, Callander NS, O'Connor SL, et al. Bortezomib-resistant nuclear factor-kappaB activity in multiple myeloma cells. Mol Cancer Res 2008;6:1356-64
    • (2008) Mol Cancer Res , vol.6 , pp. 1356-1364
    • Markovina, S.1    Callander, N.S.2    O'connor, S.L.3
  • 74
    • 84855430944 scopus 로고    scopus 로고
    • Molecular pathways: Targeting proteasomal protein degradation in cancer
    • Molineaux SM. Molecular pathways: targeting proteasomal protein degradation in cancer. Clin Cancer Res 2012;18:15-20
    • (2012) Clin Cancer Res , vol.18 , pp. 15-20
    • Molineaux, S.M.1
  • 76
    • 36148944490 scopus 로고    scopus 로고
    • Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma
    • Kuhn DJ, Chen Q, Voorhees PM, et al. Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma. Blood 2007;110:3281-90
    • (2007) Blood , vol.110 , pp. 3281-3290
    • Kuhn, D.J.1    Chen, Q.2    Voorhees, P.M.3
  • 77
    • 78649755360 scopus 로고    scopus 로고
    • A novel orally active proteasome inhibitor ONX 0912 triggers in vitro and in vivo cytotoxicity in multiple myeloma
    • Chauhan D, Singh AV, Aujay M, et al. A novel orally active proteasome inhibitor ONX 0912 triggers in vitro and in vivo cytotoxicity in multiple myeloma. Blood 2010;116:4906-15
    • (2010) Blood , vol.116 , pp. 4906-4915
    • Chauhan, D.1    Singh, A.V.2    Aujay, M.3
  • 78
    • 67650388103 scopus 로고    scopus 로고
    • A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis
    • Muchamuel T, Basler M, Aujay MA, et al. A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis. Nat Med 2009;15:781-7
    • (2009) Nat Med , vol.15 , pp. 781-787
    • Muchamuel, T.1    Basler, M.2    Aujay, M.A.3
  • 79
    • 77955069156 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system by natural products for cancer therapy
    • Tsukamoto S, Yokosawa H. Inhibition of the ubiquitin-proteasome system by natural products for cancer therapy. Planta Med 2010;76:1064-74
    • (2010) Planta Med , vol.76 , pp. 1064-1074
    • Tsukamoto, S.1    Yokosawa, H.2
  • 80
    • 66549099025 scopus 로고    scopus 로고
    • Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors
    • Kuhn DJ, Hunsucker SA, Chen Q, et al. Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors. Blood 2009;113:4667-76
    • (2009) Blood , vol.113 , pp. 4667-4676
    • Kuhn, D.J.1    Hunsucker, S.A.2    Chen, Q.3
  • 81
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • Nam S, Smith DM, Dou QP. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J Biol Chem 2001;276:13322-30
    • (2001) J Biol Chem , vol.276 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 82
    • 33646406554 scopus 로고    scopus 로고
    • Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine, " is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice
    • Yang H, Chen D, Cui QC, et al. Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine, " is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res 2006;66:4758-65
    • (2006) Cancer Res , vol.66 , pp. 4758-4765
    • Yang, H.1    Chen, D.2    Cui, Q.C.3
  • 83
    • 54749132655 scopus 로고    scopus 로고
    • Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo
    • Milacic V, Banerjee S, Landis-Piwowar KR, et al. Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo. Cancer Res 2008;68:7283-92
    • (2008) Cancer Res , vol.68 , pp. 7283-7292
    • Milacic, V.1    Banerjee, S.2    Landis-Piwowar, K.R.3
  • 84
    • 65249101693 scopus 로고    scopus 로고
    • Homology modeling and docking analysis of the interaction between polyphenols and mammalian 20S proteasomes
    • Mozzicafreddo M, Cuccioloni M, Cecarini V, et al. Homology modeling and docking analysis of the interaction between polyphenols and mammalian 20S proteasomes. J Chem Inf Model 2009;49:401-9
    • (2009) J Chem Inf Model , vol.49 , pp. 401-409
    • Mozzicafreddo, M.1    Cuccioloni, M.2    Cecarini, V.3
  • 86
    • 45849099115 scopus 로고    scopus 로고
    • Argyrin a reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition
    • Nickeleit I, Zender S, Sasse F, et al. Argyrin a reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition. Cancer Cell 2008;14:23-35
    • (2008) Cancer Cell , vol.14 , pp. 23-35
    • Nickeleit, I.1    Zender, S.2    Sasse, F.3
  • 87
    • 6044271376 scopus 로고    scopus 로고
    • Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain
    • Verma R, Peters NR, D'Onofrio M, et al. Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain. Science 2004;306:117-20
    • (2004) Science , vol.306 , pp. 117-120
    • Verma, R.1    Peters, N.R.2    D'onofrio, M.3
  • 88
    • 84856085129 scopus 로고    scopus 로고
    • Inhibition of proteasome deubiquitinating activity as a new cancer therapy
    • D'Arcy P, Brnjic S, Olofsson MH, et al. Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat Med 2011;17:1636-4089.
    • (2011) Nat Med , vol.17 , pp. 1636-4089
    • D'arcy, P.1    Brnjic, S.2    Olofsson, M.H.3
  • 89
    • 84866021069 scopus 로고    scopus 로고
    • A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance
    • Chauhan D, Tian Z, Nicholson B, et al. A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance. Cancer Cell 2012;22:345-5890.
    • (2012) Cancer Cell , vol.22 , pp. 345-5890
    • Chauhan, D.1    Tian, Z.2    Nicholson, B.3
  • 90
    • 82255181181 scopus 로고    scopus 로고
    • Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes
    • Altun M, Kramer HB, Willems LI, et al. Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes. Chem Biol 2011;18:1401-12
    • (2011) Chem Biol , vol.18 , pp. 1401-1412
    • Altun, M.1    Kramer, H.B.2    Willems, L.I.3
  • 91
    • 84860112066 scopus 로고    scopus 로고
    • Discovery of specific inhibitors of humanUSP7/HAUSP deubiquitinating enzyme
    • Reverdy C, Conrath S, Lopez R, et al. Discovery of specific inhibitors of humanUSP7/HAUSP deubiquitinating enzyme. Chem Biol 2012;19:467-77
    • (2012) Chem Biol , vol.19 , pp. 467-477
    • Reverdy, C.1    Conrath, S.2    Lopez, R.3
  • 92
    • 78549247880 scopus 로고    scopus 로고
    • Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis
    • Kapuria V, Peterson LF, Fang D, et al. Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis. Cancer Res 2010;70:9265-76
    • (2010) Cancer Res , vol.70 , pp. 9265-9276
    • Kapuria, V.1    Peterson, L.F.2    Fang, D.3
  • 93
    • 34147155353 scopus 로고    scopus 로고
    • Activation of a novel Bcr/Abl destruction pathway by WP1130 induces apoptosis of chronic myelogenous leukemia cells
    • Bartholomeusz GA, Talpaz M, Kapuria V, et al. Activation of a novel Bcr/Abl destruction pathway by WP1130 induces apoptosis of chronic myelogenous leukemia cells. Blood 2007;109:3470-8
    • (2007) Blood , vol.109 , pp. 3470-3478
    • Bartholomeusz, G.A.1    Talpaz, M.2    Kapuria, V.3
  • 94
    • 34248597738 scopus 로고    scopus 로고
    • Degrasyn activates proteasomal-dependent degradation of c-Myc
    • Bartholomeusz G, Talpaz M, Bornmann W, et al. Degrasyn activates proteasomal-dependent degradation of c-Myc. Cancer Res 2007;67:3912-18
    • (2007) Cancer Res , vol.67 , pp. 3912-3918
    • Bartholomeusz, G.1    Talpaz, M.2    Bornmann, W.3
  • 95
    • 77954605430 scopus 로고    scopus 로고
    • Degrasyn potentiates the antitumor effects of bortezomib in mantle cell lymphoma cells in vitro and in vivo: Therapeutic implications
    • Pham LV, Tamayo AT, Li C, et al. Degrasyn potentiates the antitumor effects of bortezomib in mantle cell lymphoma cells in vitro and in vivo: therapeutic implications. Mol Cancer Ther 2010;9:2026-36
    • (2010) Mol Cancer Ther , vol.9 , pp. 2026-2036
    • Pham, L.V.1    Tamayo, A.T.2    Li, C.3
  • 96
    • 10344260649 scopus 로고    scopus 로고
    • Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase
    • Kamura T, Hara T, Matsumoto M, et al. Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nat Cell Biol 2004;6:1229-35
    • (2004) Nat Cell Biol , vol.6 , pp. 1229-1235
    • Kamura, T.1    Hara, T.2    Matsumoto, M.3


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