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Volumn 103, Issue 13, 2011, Pages 1007-1017

Novel proteasome inhibitors to overcome bortezomib resistance

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINO 8 HYDROXYQUINOLINE; ANTINEOPLASTIC AGENT; ARSENIC TRIOXIDE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CARFILZOMIB; CEP 18770; CHLOROQUINE; CLIOQUINOL; CYCLOPHOSPHAMIDE; DEXAMETHASONE; DOXORUBICIN; LACTACYSTIN BETA LACTONE; LENALIDOMIDE; MELPHALAN; MLN 2238; MLN 9708; ONX 0912; PR 39; PREDNISONE; PROTEASOME; PROTEASOME INHIBITOR; QUINOLINE; SALINOSPORAMIDE A; THALIDOMIDE; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 79960208716     PISSN: 00278874     EISSN: 14602105     Source Type: Journal    
DOI: 10.1093/jnci/djr160     Document Type: Review
Times cited : (224)

References (95)
  • 2
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8
    • DOI 10.1038/nature01456
    • Walden H, Podgorski MS, Schulman BA. Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8. Nature. 2003;422(6929):330-334. (Pubitemid 36378362)
    • (2003) Nature , vol.422 , Issue.6929 , pp. 330-334
    • Walden, H.1    Podgorski, M.S.2    Schulman, B.A.3
  • 3
    • 14844291338 scopus 로고    scopus 로고
    • Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
    • DOI 10.1038/sj.emboj.7600552
    • Lois LM, Lima CD. Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. Embo J. 2005;24(3):439-451. (Pubitemid 40343247)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 439-451
    • Lois, L.M.1    Lima, C.D.2
  • 4
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko A, Heller H, Elias S, Ciechanover A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem. 1983;258(13):8206-8214.
    • (1983) J Biol Chem , vol.258 , Issue.13 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 6
    • 34347329214 scopus 로고    scopus 로고
    • Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging
    • DOI 10.1038/nature05902, PII NATURE05902
    • Jin J, Li X, Gygi SP, Harper JW. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature. 2007;447(7148):1135-1138. (Pubitemid 47014428)
    • (2007) Nature , vol.447 , Issue.7148 , pp. 1135-1138
    • Jin, J.1    Li, X.2    Gygi, S.P.3    Harper, J.W.4
  • 7
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • Haas AL, Bright PM. The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes. J Biol Chem. 1988;263(26):13258-13267.
    • (1988) J Biol Chem , vol.263 , Issue.26 , pp. 13258-13267
    • Haas, A.L.1    Bright, P.M.2
  • 8
    • 33644993733 scopus 로고    scopus 로고
    • Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis
    • DOI 10.1104/pp.105.067983
    • Kraft E, Stone SL, Ma L, et al. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol. 2005;139(4):1597-1611. (Pubitemid 43899804)
    • (2005) Plant Physiology , vol.139 , Issue.4 , pp. 1597-1611
    • Kraft, E.1    Stone, S.L.2    Ma, L.3    Su, N.4    Gao, Y.5    Lau, O.-S.6    Deng, X.-W.7    Callis, J.8
  • 9
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell J, Shih S, Dunn R, Hicke L. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol Cell. 1998;1(2):193-202. (Pubitemid 128378660)
    • (1998) Molecular Cell , vol.1 , Issue.2 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 11
    • 38149098408 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation
    • Zhou W, Zhu P, Wang J, et al. Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol Cell. 2008;29(1):69-80.
    • (2008) Mol Cell , vol.29 , Issue.1 , pp. 69-80
    • Zhou, W.1    Zhu, P.2    Wang, J.3
  • 13
    • 33646196532 scopus 로고    scopus 로고
    • Regulation of DNA repair by ubiquitylation
    • Huang TT, D'Andrea AD. Regulation of DNA repair by ubiquitylation. Nat Rev Mol Cell Biol. 2006;7(5):323-334.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.5 , pp. 323-334
    • Huang, T.T.1    D'Andrea, A.D.2
  • 14
    • 33645708319 scopus 로고    scopus 로고
    • Regulation of monoubiquitinated PCNA by DUB autocleavage
    • Huang TT, Nijman SM, Mirchandani KD, et al. Regulation of monoubiquitinated PCNA by DUB autocleavage. Nat Cell Biol. 2006;8(4):339-347.
    • (2006) Nat Cell Biol , vol.8 , Issue.4 , pp. 339-347
    • Huang, T.T.1    Nijman, S.M.2    Mirchandani, K.D.3
  • 15
  • 16
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalization protease
    • Baumeister W, Walz J, Zuhk F, Seemuller E. The proteasome: paradigm of a self-compartmentalization protease. Cell. 1998;92(6):367-380.
    • (1998) Cell , vol.92 , Issue.6 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhk, F.3    Seemuller, E.4
  • 17
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and elF3
    • DOI 10.1016/S0092-8674(00)81603-7
    • Glickman MH, Rubin DM, Coux O, et al. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell. 1998;94(5):615-623. (Pubitemid 28427580)
    • (1998) Cell , vol.94 , Issue.5 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 18
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
    • Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science. 1995;268(5210):533-539.
    • (1995) Science , vol.268 , Issue.5210 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 20
    • 0033766480 scopus 로고    scopus 로고
    • A gated channel into the proteasome core particle
    • Groll M, Bajorek M, Kohler A, et al. A gated channel into the proteasome core particle. Nat Struct Biol. 2000;7(11):1062-1067.
    • (2000) Nat Struct Biol , vol.7 , Issue.11 , pp. 1062-1067
    • Groll, M.1    Bajorek, M.2    Kohler, A.3
  • 23
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing
    • DOI 10.1074/jbc.272.40.25200
    • Heinemeyer W, Fischer M, Krimmer T, Stachon U, Wolf DH. The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J Biol Chem. 1997;272(40):25200-25209. (Pubitemid 27415707)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 25200-25209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 24
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • DOI 10.1016/S0092-8674(00)80171-3
    • Chen P, Hochstrasser M. Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell. 1996;86(6):961-972. (Pubitemid 26336800)
    • (1996) Cell , vol.86 , Issue.6 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 26
    • 0032514684 scopus 로고    scopus 로고
    • Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1
    • Nussbaum AK, Dick TP, Keilholz W, et al. Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1. Proc Natl Acad Sci USA. 1998;95(21):12504-12509.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.21 , pp. 12504-12509
    • Nussbaum, A.K.1    Dick, T.P.2    Keilholz, W.3
  • 30
    • 76349089770 scopus 로고    scopus 로고
    • Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions
    • Yu Y, Smith DM, Kim HM, Rodriguez V, Goldberg AL, Cheng Y. Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions. Embo J. 2010;29(3):692-702.
    • (2010) Embo J. , vol.29 , Issue.3 , pp. 692-702
    • Yu, Y.1    Smith, D.M.2    Kim, H.M.3    Rodriguez, V.4    Goldberg, A.L.5    Cheng, Y.6
  • 31
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • DOI 10.1074/jbc.273.4.1982
    • Kisselev AF, Akopian TN, Goldberg AL. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J Biol Chem. 1998;273(4):1982-1989. (Pubitemid 28069243)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 32
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • DOI 10.1074/jbc.272.3.1791
    • Akopian TN, Kisselev AF, Goldberg AL. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J Biol Chem. 1997;272(3):1791-1798. (Pubitemid 27043269)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.3 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 34
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan JA, Dodson G, Duggleby HJ, et al. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature. 1995;378(6555):416-419.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3
  • 35
    • 0025771623 scopus 로고
    • A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC
    • Glynne R, Powis SH, Beck S, Kelly A, Kerr LA, Trowsdale J. A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC. Nature. 1991;353(6342):357-360. (Pubitemid 21912511)
    • (1991) Nature , vol.353 , Issue.6342 , pp. 357-360
    • Glynne, R.1    Powis, S.H.2    Beck, S.3    Kelly, A.4    Kerr, L.-A.5    Trowsdale, J.6
  • 36
    • 0026040535 scopus 로고
    • Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene
    • Martinez CK, Monaco JJ. Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene. Nature. 1991;353(6345):664-667. (Pubitemid 21912585)
    • (1991) Nature , vol.353 , Issue.6345 , pp. 664-667
    • Martinez, C.K.1    Monaco, J.J.2
  • 37
    • 0029878931 scopus 로고    scopus 로고
    • Identification of MECL-1 (LMP-10) as the third IFN-γ-inducible proteasome subunit
    • Nandi D, Jiang H, Monaco JJ. Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit. J Immunol. 1996;156(7):2361-2364. (Pubitemid 26091557)
    • (1996) Journal of Immunology , vol.156 , Issue.7 , pp. 2361-2364
    • Nandi, D.1    Jiang, H.2    Monaco, J.J.3
  • 39
    • 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, Voorhees PM, Orlowski M, Orlowski RZ. 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(19):4667-4676.
    • (2009) Blood , vol.113 , Issue.19 , pp. 4667-4676
    • Kuhn, D.J.1    Hunsucker, S.A.2    Chen, Q.3    Voorhees, P.M.4    Orlowski, M.5    Orlowski, R.Z.6
  • 40
    • 38749115417 scopus 로고    scopus 로고
    • Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits
    • DOI 10.1002/cncr.23224
    • Busse A, Kraus M, Na IK, et al. Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits. Cancer. 2008;112(3):659-670. (Pubitemid 351186207)
    • (2008) Cancer , vol.112 , Issue.3 , pp. 659-670
    • Busse, A.1    Kraus, M.2    Na, I.-K.3    Rietz, A.4    Scheibenbogen, C.5    Driessen, C.6    Blau, I.W.7    Thiel, E.8    Keilholz, U.9
  • 41
    • 70350708810 scopus 로고    scopus 로고
    • Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome
    • Parlati F, Lee SJ, Aujay M, et al. Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome. Blood. 2009;114(16):3439-3447.
    • (2009) Blood , vol.114 , Issue.16 , pp. 3439-3447
    • Parlati, F.1    Lee, S.J.2    Aujay, M.3
  • 45
    • 33645731530 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system stress sensitizes ovarian cancer to proteasome inhibitor-induced apoptosis
    • Bazzaro M, Lee MK, Zoso A, et al. Ubiquitin-proteasome system stress sensitizes ovarian cancer to proteasome inhibitor-induced apoptosis. Cancer Res. 2006;66(7):3754-3763.
    • (2006) Cancer Res , vol.66 , Issue.7 , pp. 3754-3763
    • Bazzaro, M.1    Lee, M.K.2    Zoso, A.3
  • 46
    • 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(7):3071-3076. (Pubitemid 32691956)
    • (2001) Cancer Research , vol.61 , Issue.7 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5    Adams, J.6    Anderson, K.C.7
  • 48
    • 33644845743 scopus 로고    scopus 로고
    • Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome
    • DOI 10.1016/j.str.2005.11.019, PII S0969212606000694
    • Groll M, Berkers CR, Ploegh HL, Ovaa H. Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome. Structure. 2006;14(3):451-456. (Pubitemid 43363478)
    • (2006) Structure , vol.14 , Issue.3 , pp. 451-456
    • Groll, M.1    Berkers, C.R.2    Ploegh, H.L.3    Ovaa, H.4
  • 49
    • 33646137808 scopus 로고    scopus 로고
    • Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding
    • Groll M, Huber R, Potts BC. Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding. J Am Chem Soc. 2006;128(15):5136-5141.
    • (2006) J Am Chem Soc , vol.128 , Issue.15 , pp. 5136-5141
    • Groll, M.1    Huber, R.2    Potts, B.C.3
  • 50
    • 33947659939 scopus 로고    scopus 로고
    • 20S proteasome and its inhibitors: Crystallographic knowledge for drug development
    • DOI 10.1021/cr0502504
    • Borissenko L, Groll M. 20S proteasome and its inhibitors: crystallographic knowledge for drug development. Chem Rev. 2007;107(3):687-717. (Pubitemid 46502369)
    • (2007) Chemical Reviews , vol.107 , Issue.3 , pp. 687-717
    • Borissenko, L.1    Groll, M.2
  • 52
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • DOI 10.1016/S1535-6108(04)00120-5, PII S1535610804001205
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell. 2004;5(5):417-421. (Pubitemid 38610244)
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 417-421
    • Adams, J.1
  • 54
    • 50449086728 scopus 로고    scopus 로고
    • Bortezomib plus melphalan and prednisone for initial treatment of multiple myeloma
    • San Miguel JF, Schlag R, Khuageva NK, et al. Bortezomib plus melphalan and prednisone for initial treatment of multiple myeloma. N Engl J Med. 2008;359(9):906-917.
    • (2008) N Engl J Med , vol.359 , Issue.9 , pp. 906-917
    • San Miguel, J.F.1    Schlag, R.2    Khuageva, N.K.3
  • 55
    • 77954618168 scopus 로고    scopus 로고
    • Lenalidomide, bortezomib, and dexamethasone combination therapy in patients with newly diagnosed multiple myeloma
    • Richardson PG, Weller E, Lonial S, et al. Lenalidomide, bortezomib, and dexamethasone combination therapy in patients with newly diagnosed multiple myeloma. Blood. 2010;116(5):679-686.
    • (2010) Blood , vol.116 , Issue.5 , pp. 679-686
    • Richardson, P.G.1    Weller, E.2    Lonial, S.3
  • 56
    • 78650993336 scopus 로고    scopus 로고
    • Bortezomib-melphalan-prednisone-thalidomide followed by maintenance with bortezomib-thalidomide compared with bortezomib-melphalan-prednisone for initial treatment of multiple myeloma: A randomized controlled trial
    • Palumbo A, Bringhen S, Rossi D, et al. Bortezomib-melphalan-prednisone- thalidomide followed by maintenance with bortezomib-thalidomide compared with bortezomib-melphalan-prednisone for initial treatment of multiple myeloma: a randomized controlled trial. J Clin Oncol. 2010;28(34):5101-5109.
    • (2010) J Clin Oncol. , vol.28 , Issue.34 , pp. 5101-5109
    • Palumbo, A.1    Bringhen, S.2    Rossi, D.3
  • 57
    • 77954660886 scopus 로고    scopus 로고
    • Bortezomib, dexamethasone, cyclophosphamide and lenalidomide combination for newly diagnosed multiple myeloma: Phase 1 results from the multicenter EVOLUTION study
    • Kumar SK, Flinn I, Noga SJ, et al. Bortezomib, dexamethasone, cyclophosphamide and lenalidomide combination for newly diagnosed multiple myeloma: phase 1 results from the multicenter EVOLUTION study. Leukemia. 2010;24(7):1350-1356.
    • (2010) Leukemia , vol.24 , Issue.7 , pp. 1350-1356
    • Kumar, S.K.1    Flinn, I.2    Noga, S.J.3
  • 59
    • 77955714026 scopus 로고    scopus 로고
    • Primary therapy with single agent bortezomib as induction, maintenance and re-induction in patients with high-risk myeloma: Results of the ECOG E2A02 trial
    • Dispenzieri A, Jacobus S, Vesole DH, Callandar N, Fonseca R, Greipp PR. Primary therapy with single agent bortezomib as induction, maintenance and re-induction in patients with high-risk myeloma: results of the ECOG E2A02 trial. Leukemia. 2010;24(8):1406-1411.
    • (2010) Leukemia , vol.24 , Issue.8 , pp. 1406-1411
    • Dispenzieri, A.1    Jacobus, S.2    Vesole, D.H.3    Callandar, N.4    Fonseca, R.5    Greipp, P.R.6
  • 60
    • 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(6):2489-2499.
    • (2008) Blood , vol.112 , Issue.6 , pp. 2489-2499
    • Oerlemans, R.1    Franke, N.E.2    Assaraf, Y.G.3
  • 61
    • 67049107847 scopus 로고    scopus 로고
    • Different mutants of PSMB5 confer varying bortezomib resistance in T lymphoblastic lymphoma/leukemia cells derived from the Jurkat cell line
    • Lu S, Yang J, Chen Z, et al. Different mutants of PSMB5 confer varying bortezomib resistance in T lymphoblastic lymphoma/leukemia cells derived from the Jurkat cell line. Exp Hematol. 2009;37(7):831-837.
    • (2009) Exp Hematol , vol.37 , Issue.7 , pp. 831-837
    • Lu, S.1    Yang, J.2    Chen, Z.3
  • 62
    • 77954978455 scopus 로고    scopus 로고
    • Effect of noncompetitive proteasome inhibition on bortezomib resistance
    • Li X, Wood TE, Sprangers R, et al. Effect of noncompetitive proteasome inhibition on bortezomib resistance. J Natl Cancer Inst. 2010;102(14):1069-1082.
    • (2010) J Natl Cancer Inst. , vol.102 , Issue.14 , pp. 1069-1082
    • Li, X.1    Wood, T.E.2    Sprangers, R.3
  • 63
    • 28844435438 scopus 로고    scopus 로고
    • No evidence of mutations of the PSMB5 (beta-5 subunit of proteasome) in a case of myeloma with clinical resistance to Bortezomib [1]
    • DOI 10.1016/j.leukres.2005.06.014, PII S0145212605002560
    • Politou M, Karadimitris A, Terpos E, Kotsianidis I, Apperley JF, Rahemtulla A. No evidence of mutations of the PSMB5 (beta-5 subunit of proteasome) in a case of myeloma with clinical resistance to Bortezomib. Leuk Res. 2006;30(2):240-241. (Pubitemid 41773346)
    • (2006) Leukemia Research , vol.30 , Issue.2 , pp. 240-241
    • Politou, M.1    Karadimitris, A.2    Terpos, E.3    Kotsianidis, I.4    Apperley, J.F.5    Rahemtulla, A.6
  • 66
    • 77950238258 scopus 로고    scopus 로고
    • Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer
    • Kupperman E, Lee EC, Cao Y, et al. Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer. Cancer Res. 2010;70(5):1970- 1980.
    • (2010) Cancer Res. , vol.70 , Issue.5 , pp. 1970-1980
    • Kupperman, E.1    Lee, E.C.2    Cao, Y.3
  • 67
    • 75149157969 scopus 로고    scopus 로고
    • The proteasome inhibitor CEP-18770 enhances the anti-myeloma activity of bortezomib and melphalan
    • Sanchez E, Li M, Steinberg JA, et al. The proteasome inhibitor CEP-18770 enhances the anti-myeloma activity of bortezomib and melphalan. Br J Haematol. 2010;148(4):569-581.
    • (2010) Br J Haematol , vol.148 , Issue.4 , pp. 569-581
    • Sanchez, E.1    Li, M.2    Steinberg, J.A.3
  • 68
    • 41949110089 scopus 로고    scopus 로고
    • CEP-18770: A novel, orally active proteasome inhibitor with a tumor-selective pharmacologic profile competitive with bortezomib
    • Piva R, Ruggeri B, Williams M, et al. CEP-18770: a novel, orally active proteasome inhibitor with a tumor-selective pharmacologic profile competitive with bortezomib. Blood. 2008;111(5):2765-2775.
    • (2008) Blood , vol.111 , Issue.5 , pp. 2765-2775
    • Piva, R.1    Ruggeri, B.2    Williams, M.3
  • 71
    • 72549116835 scopus 로고    scopus 로고
    • A phase 1 dose escalation study of the safety and pharmacokinetics of the novel proteasome inhibitor carfilzomib (PR-171) in patients with hematologic malignancies
    • O'Connor OA, Stewart AK, Vallone M, et al. A phase 1 dose escalation study of the safety and pharmacokinetics of the novel proteasome inhibitor carfilzomib (PR-171) in patients with hematologic malignancies. Clin Cancer Res. 2009;15(22):7085-7091.
    • (2009) Clin Cancer Res , vol.15 , Issue.22 , pp. 7085-7091
    • O'Connor, O.A.1    Stewart, A.K.2    Vallone, M.3
  • 73
    • 65649139708 scopus 로고    scopus 로고
    • Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR-047)
    • Zhou HJ, Aujay MA, Bennett MK, et al. Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR-047). J Med Chem. 2009;52(9):3028-3038.
    • (2009) J Med Chem , vol.52 , Issue.9 , pp. 3028-3038
    • Zhou, H.J.1    Aujay, M.A.2    Bennett, M.K.3
  • 74
    • 78649755360 scopus 로고    scopus 로고
    • A novel orally active proteasome inhibitor ONX 0912 trigger 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 trigger in vitro and in vivo cytotoxicity in multiple myeloma. Blood. 2010;116(23):4906-4915.
    • (2010) Blood , vol.116 , Issue.23 , pp. 4906-4915
    • Chauhan, D.1    Singh, A.V.2    Aujay, M.3
  • 75
    • 0037455147 scopus 로고    scopus 로고
    • Salinosporamide A: A highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora
    • DOI 10.1002/anie.200390115
    • Feling RH, Buchanan GO, Mincer TJ, Kauffman CA, Jensen PR, Fenical W. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus salinospora. Angew Chem Int Ed Engl. 2003;42(3):355-357. (Pubitemid 36176323)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.3 , pp. 355-357
    • Feling, R.H.1    Buchanan, G.O.2    Mincer, T.J.3    Kauffman, C.A.4    Jensen, P.R.5    Fenical, W.6
  • 76
    • 77951682116 scopus 로고    scopus 로고
    • Pharmacodynamic and efficacy studies of the novel proteasome inhibitor NPI-0052 (marizomib) in a human plasmacytoma xenograft murine model
    • Singh AV, Palladino MA, Lloyd GK, Potts BC, Chauhan D, Anderson KC. Pharmacodynamic and efficacy studies of the novel proteasome inhibitor NPI-0052 (marizomib) in a human plasmacytoma xenograft murine model. Br J Haematol. 2010;149(4):550-559.
    • (2010) Br J Haematol. , vol.149 , Issue.4 , pp. 550-559
    • Singh, A.V.1    Palladino, M.A.2    Lloyd, G.K.3    Potts, B.C.4    Chauhan, D.5    Anderson, K.C.6
  • 77
    • 34347375499 scopus 로고    scopus 로고
    • NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells
    • DOI 10.1182/blood-2006-03-013128
    • Miller CP, Ban K, Dujka ME, et al. NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells. Blood. 2007;110(1):267-277. (Pubitemid 47026844)
    • (2007) Blood , vol.110 , Issue.1 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3    McConkey, D.J.4    Munsell, M.5    Palladino, M.6    Chandra, J.7
  • 78
    • 79960214124 scopus 로고    scopus 로고
    • Phase 1 clinical trial of NPI-0052 a novel proteasome inhibitor in patients with multiple myeloma
    • Orlando FL: American Society of Hematology, Abstract 2770
    • Richardson P, Hofmeister C, Zimmerman T, et al. Phase 1 clinical trial of NPI-0052, a novel proteasome inhibitor in patients with multiple myeloma. In: Orlando, FL: American Society of Hematology Annual Meeting; 2010. Abstract 2770.
    • (2010) Annual Meeting
    • Richardson, P.1    Hofmeister, C.2    Zimmerman, T.3
  • 79
    • 0029129210 scopus 로고
    • Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: Comparative mapping of the locus for the human peptide antibiotic FALL-39
    • Gudmundsson GH, Magnusson KP, Chowdhary BP, Johansson M, Andersson L, Boman HG. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. Proc Natl Acad Sci USA. 1995;92(15):7085-7089.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.15 , pp. 7085-7089
    • Gudmundsson, G.H.1    Magnusson, K.P.2    Chowdhary, B.P.3    Johansson, M.4    Andersson, L.5    Boman, H.G.6
  • 81
    • 0042848726 scopus 로고    scopus 로고
    • Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity
    • DOI 10.1021/bi034784f
    • Gaczynska M, Osmulski PA, Gao Y, Post MJ, Simons M. Proline-and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry. 2003;42(29):8663-8670. (Pubitemid 36899808)
    • (2003) Biochemistry , vol.42 , Issue.29 , pp. 8663-8670
    • Gaczynska, M.1    Osmulski, P.A.2    Gao, Y.3    Post, M.J.4    Simons, M.5
  • 82
    • 46049107832 scopus 로고    scopus 로고
    • TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors
    • DOI 10.1021/bi8005913
    • Sprangers R, Li X, Mao X, Rubinstein JL, Schimmer AD, Kay LE. TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors. Biochemistry. 2008;47(26):6727-6734. (Pubitemid 351898927)
    • (2008) Biochemistry , vol.47 , Issue.26 , pp. 6727-6734
    • Sprangers, R.1    Li, X.2    Mao, X.3    Rubinstein, J.L.4    Schimmer, A.D.5    Kay, L.E.6
  • 83
    • 0015207395 scopus 로고
    • Prophylactic value of clioquinol against travellers' diarrhoea
    • Richards DA. Prophylactic value of clioquinol against travellers' diarrhoea. Lancet. 1971;1(7688):44-45.
    • (1971) Lancet , vol.1 , Issue.7688 , pp. 44-45
    • Richards, D.A.1
  • 84
    • 0014661451 scopus 로고
    • Trial of clioquinol in cholera
    • Woodward WE, Rahman AS. Trial of clioquinol in cholera. Lancet. 1969;2(7614):270.
    • (1969) Lancet , vol.2 , Issue.7614 , pp. 270
    • Woodward, W.E.1    Rahman, A.S.2
  • 85
    • 0015937048 scopus 로고
    • Relation between subacute myelo-optic neuropathy (S.M.O.N.) and clioquinol: Nationwide survey
    • Nakae K, Yamamoto S, Shigematsu I, Kono R. Relation between subacute myelo-optic neuropathy (S.M.O.N.) and clioquinol: nationwide survey. Lancet. 1973;1(7796):171-173.
    • (1973) Lancet , vol.1 , Issue.7796 , pp. 171-173
    • Nakae, K.1    Yamamoto, S.2    Shigematsu, I.3    Kono, R.4
  • 87
    • 62549083952 scopus 로고    scopus 로고
    • Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma
    • Mao X, Li X, Sprangers R, et al. Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma. Leukemia. 2009;23(3):585-590.
    • (2009) Leukemia , vol.23 , Issue.3 , pp. 585-590
    • Mao, X.1    Li, X.2    Sprangers, R.3
  • 89
    • 33847746963 scopus 로고    scopus 로고
    • Clioquinol, a therapeutic agent for alzheimer's disease, has proteasome-inhibitory, androgen receptor-suppressing, apoptosis-inducing, and antitumor activities in human prostate cancer cells and xenografts
    • DOI 10.1158/0008-5472.CAN-06-3546
    • Chen D, Cui QC, Yang H, et al. Clioquinol, a therapeutic agent for Alzheimer's disease, has proteasome-inhibitory, androgen receptor-suppressing, apoptosis-inducing, and antitumor activities in human prostate cancer cells and xenografts. Cancer Res. 2007;67(4):1636-1644. (Pubitemid 46383389)
    • (2007) Cancer Research , vol.67 , Issue.4 , pp. 1636-1644
    • Chen, D.1    Cui, Q.C.2    Yang, H.3    Barrea, R.A.4    Sarkar, F.H.5    Sheng, S.6    Yan, B.7    Reddy, G.P.V.8    Dou, Q.P.9
  • 90
    • 84901648175 scopus 로고    scopus 로고
    • Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells
    • Daniel KG, Chen D, Orlu S, Cui QC, Miller FR, Dou QP. Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells. Breast Cancer Res. 2005;7(6):R897-R908.
    • (2005) Breast Cancer Res , vol.7 , Issue.6
    • Daniel, K.G.1    Chen, D.2    Orlu, S.3    Cui, Q.C.4    Miller, F.R.5    Dou, Q.P.6
  • 91
    • 77449146289 scopus 로고    scopus 로고
    • Metal ionophores-an emerging class of anticancer drugs
    • Ding WQ, Lind SE. Metal ionophores-an emerging class of anticancer drugs. IUBMB Life. 2009;61(11):1013-1018.
    • (2009) IUBMB Life , vol.61 , Issue.11 , pp. 1013-1018
    • Ding, W.Q.1    Lind, S.E.2
  • 92
    • 0037036523 scopus 로고    scopus 로고
    • Concentrations of Fe, Cu and Zn in breast tissue: A synchrotron XRF study
    • DOI 10.1088/0031-9155/47/13/310, PII S0031915502351418
    • Geraki K, Farquharson MJ, Bradley DA. Concentrations of Fe, Cu and Zn in breast tissue: a synchrotron XRF study. Phys Med Biol. 2002;47(13):2327-2339. (Pubitemid 34812209)
    • (2002) Physics in Medicine and Biology , vol.47 , Issue.13 , pp. 2327-2339
    • Geraki, K.1    Farquharson, M.J.2    Bradley, D.A.3
  • 93
    • 0024586132 scopus 로고
    • Use of the copper/zinc ratio in the diagnosis of lung cancer
    • DOI 10.1002/1097-0142(19890215)63:4<726::AID-CNCR2820630421>3.0. CO;2-P
    • Diez M, Cerdan FJ, Arroyo M, Balibrea JL. Use of the copper/zinc ratio in the diagnosis of lung cancer. Cancer. 1989;63(4):726-730. (Pubitemid 19050277)
    • (1989) Cancer , vol.63 , Issue.4 , pp. 726-730
    • Diez, M.1    Cerdan, F.J.2    Arroyo, M.3    Balibrea, J.L.4
  • 94
    • 0027448830 scopus 로고
    • Quantitative analysis of copper, zinc and copper/zinc ratio in selected human brain tumors
    • DOI 10.1007/BF01324697
    • Yoshida D, Ikeda Y, Nakazawa S. Quantitative analysis of copper, zinc and copper/zinc ratio in selected human brain tumors. J Neurooncol. 1993;16(2):109-115. (Pubitemid 23304718)
    • (1993) Journal of Neuro-Oncology , vol.16 , Issue.2 , pp. 109-115
    • Yoshida, D.1    Ikeda, Y.2    Nakazawa, S.3
  • 95
    • 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(11):2251-2259.
    • (2010) Blood , vol.115 , Issue.11 , pp. 2251-2259
    • Xu, G.W.1    Ali, M.2    Wood, T.E.3


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