메뉴 건너뛰기




Volumn 49, Issue 3, 2012, Pages 196-206

An Historic Perspective of Proteasome Inhibition

Author keywords

[No Author keywords available]

Indexed keywords

[4 [4 [(2,3 DIHYDRO 1H INDEN 1 YL)AMINO] 7H PYRROLO[2,3 D]PYRIMIDIN 7 YL] 2 HYDROXYCYCLOPENTYLMETHYL] SULFAMATE; ALDEHYDE; BORONIC ACID DERIVATIVE; BORTEZOMIB; CARFILZOMIB; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IXAZOMIB CITRATE; KETONE; LACTONE; MELPHALAN; PREDNISONE; PROTEASOME; PROTEASOME INHIBITOR; SALINOSPORAMIDE A; SULFONE DERIVATIVE; UBIQUITIN;

EID: 84862667721     PISSN: 00371963     EISSN: 15328686     Source Type: Journal    
DOI: 10.1053/j.seminhematol.2012.04.009     Document Type: Article
Times cited : (14)

References (115)
  • 1
    • 79959929490 scopus 로고    scopus 로고
    • Preclinical strategies to define predictive biomarkers for therapeutically relevant cancer subtypes
    • Pajic M., Scarlett C.J., Chang D.K., Sutherland R.L., Biankin A.V. Preclinical strategies to define predictive biomarkers for therapeutically relevant cancer subtypes. Hum Genet 2011, 130:93-101.
    • (2011) Hum Genet , vol.130 , pp. 93-101
    • Pajic, M.1    Scarlett, C.J.2    Chang, D.K.3    Sutherland, R.L.4    Biankin, A.V.5
  • 2
    • 79959398524 scopus 로고    scopus 로고
    • International Myeloma Working Group consensus approach to the treatment of multiple myeloma patients who are candidates for autologous stem cell transplantation
    • Cavo M., Rajkumar S.V., Palumbo A., et al. International Myeloma Working Group consensus approach to the treatment of multiple myeloma patients who are candidates for autologous stem cell transplantation. Blood 2011, 117:6063-6073.
    • (2011) Blood , vol.117 , pp. 6063-6073
    • Cavo, M.1    Rajkumar, S.V.2    Palumbo, A.3
  • 3
    • 79955552589 scopus 로고    scopus 로고
    • Multiple myeloma treatment strategies with novel agents in 2011: a European perspective
    • Ludwig H., Beksac M., Blade J., et al. Multiple myeloma treatment strategies with novel agents in 2011: a European perspective. Oncologist 2011, 16:388-403.
    • (2011) Oncologist , vol.16 , pp. 388-403
    • Ludwig, H.1    Beksac, M.2    Blade, J.3
  • 4
    • 41949130070 scopus 로고    scopus 로고
    • Improved survival in multiple myeloma and the impact of novel therapies
    • Kumar S.K., Rajkumar S.V., Dispenzieri A., et al. Improved survival in multiple myeloma and the impact of novel therapies. Blood 2008, 111:2516-2520.
    • (2008) Blood , vol.111 , pp. 2516-2520
    • Kumar, S.K.1    Rajkumar, S.V.2    Dispenzieri, A.3
  • 5
    • 78851472260 scopus 로고    scopus 로고
    • Immunoglobulin light chain amyloidosis: 2011 update on diagnosis, risk-stratification, and management
    • Gertz M.A. Immunoglobulin light chain amyloidosis: 2011 update on diagnosis, risk-stratification, and management. Am J Hematol 2011, 86:180-186.
    • (2011) Am J Hematol , vol.86 , pp. 180-186
    • Gertz, M.A.1
  • 6
    • 80053131089 scopus 로고    scopus 로고
    • Mantle cell lymphoma: the promise of new treatment options
    • Goy A., Kahl B. Mantle cell lymphoma: the promise of new treatment options. Crit Rev Oncol Hematol 2010, 80:69-86.
    • (2010) Crit Rev Oncol Hematol , vol.80 , pp. 69-86
    • Goy, A.1    Kahl, B.2
  • 8
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • M111.013284
    • Wagner S.A., Beli P., Weinert B.T., et al. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics 2011, 10. M111.013284.
    • (2011) Mol Cell Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3
  • 9
    • 23944474593 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Cell Death Differ 2005, 12:1178-1190.
    • (2005) Cell Death Differ , vol.12 , pp. 1178-1190
    • Ciechanover, A.1
  • 10
    • 0016017019 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells
    • Goldberg A.L., Dice J.F. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem 1974, 43:835-869.
    • (1974) Annu Rev Biochem , vol.43 , pp. 835-869
    • Goldberg, A.L.1    Dice, J.F.2
  • 11
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis
    • Hershko A., Ciechanover A., Heller H., Haas A.L., Rose I.A. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci U S A 1980, 77:1783-1786.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 12
    • 0019887743 scopus 로고
    • Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown
    • Hershko A., Ciechanover A., Rose I.A. Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown. J Biol Chem 1981, 256:1525-1528.
    • (1981) J Biol Chem , vol.256 , pp. 1525-1528
    • Hershko, A.1    Ciechanover, A.2    Rose, I.A.3
  • 13
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • Hough R., Pratt G., Rechsteiner M. Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J Biol Chem 1987, 262:8303-8313.
    • (1987) J Biol Chem , vol.262 , pp. 8303-8313
    • Hough, R.1    Pratt, G.2    Rechsteiner, M.3
  • 14
    • 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, 107:687-717.
    • (2007) Chem Rev , vol.107 , pp. 687-717
    • Borissenko, L.1    Groll, M.2
  • 15
    • 0020478687 scopus 로고
    • "Covalent affinity" purification of ubiquitin-activating enzyme
    • Ciechanover A., Elias S., Heller H., Hershko A. "Covalent affinity" purification of ubiquitin-activating enzyme. J Biol Chem 1982, 257:2537-2542.
    • (1982) J Biol Chem , vol.257 , pp. 2537-2542
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Hershko, A.4
  • 16
    • 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, 258:8206-8214.
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 17
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • Bedford L., Lowe J., Dick L.R., Mayer R.J., Brownell J.E. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat Rev Drug Discov 2011, 10:29-46.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 18
    • 0029347062 scopus 로고
    • New insights into proteasome function: from archaebacteria to drug development
    • Goldberg A.L., Stein R., Adams J. New insights into proteasome function: from archaebacteria to drug development. Chem Biol 1995, 2:503-508.
    • (1995) Chem Biol , vol.2 , pp. 503-508
    • Goldberg, A.L.1    Stein, R.2    Adams, J.3
  • 19
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz A.L., Ciechanover A. The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu Rev Med 1999, 50:57-74.
    • (1999) Annu Rev Med , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 20
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T., Sitia R. Protein quality control in the early secretory pathway. EMBO J 2008, 27:315-327.
    • (2008) EMBO J , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 21
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004, 4:349-360.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 22
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 2004, 5:417-421.
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 23
    • 77956108780 scopus 로고    scopus 로고
    • Enhancing activity and overcoming chemoresistance in hematologic malignancies with bortezomib: preclinical mechanistic studies
    • Reddy N., Czuczman M.S. Enhancing activity and overcoming chemoresistance in hematologic malignancies with bortezomib: preclinical mechanistic studies. Ann Oncol 2010, 21:1756-1764.
    • (2010) Ann Oncol , vol.21 , pp. 1756-1764
    • Reddy, N.1    Czuczman, M.S.2
  • 24
    • 77954134911 scopus 로고    scopus 로고
    • Potential biomarkers of bortezomib activity in mantle cell lymphoma from the phase 2 PINNACLE trial
    • Goy A., Bernstein S.H., McDonald A., et al. Potential biomarkers of bortezomib activity in mantle cell lymphoma from the phase 2 PINNACLE trial. Leuk Lymphoma 2010, 51:1269-1277.
    • (2010) Leuk Lymphoma , vol.51 , pp. 1269-1277
    • Goy, A.1    Bernstein, S.H.2    McDonald, A.3
  • 25
    • 34147129816 scopus 로고    scopus 로고
    • Gene expression profiling and correlation with outcome in clinical trials of the proteasome inhibitor bortezomib
    • Mulligan G., Mitsiades C., Bryant B., et al. Gene expression profiling and correlation with outcome in clinical trials of the proteasome inhibitor bortezomib. Blood 2007, 109:3177-3188.
    • (2007) Blood , vol.109 , pp. 3177-3188
    • Mulligan, G.1    Mitsiades, C.2    Bryant, B.3
  • 26
    • 79960892918 scopus 로고    scopus 로고
    • Bortezomib plus rituximab versus rituximab alone in patients with relapsed, rituximab-naive or rituximab-sensitive, follicular lymphoma: a randomised phase 3 trial
    • Coiffier B., Osmanov E.A., Hong X., et al. Bortezomib plus rituximab versus rituximab alone in patients with relapsed, rituximab-naive or rituximab-sensitive, follicular lymphoma: a randomised phase 3 trial. Lancet Oncol 2011, 12:773-784.
    • (2011) Lancet Oncol , vol.12 , pp. 773-784
    • Coiffier, B.1    Osmanov, E.A.2    Hong, X.3
  • 27
    • 84878709726 scopus 로고    scopus 로고
    • Identification of patient subgroups demonstrating longer progression-free survival (PFS) benefit with bortezomib-rituximab versus rituximab in patients with relapsed or refractory follicular lymphoma (FL): biomarker analyses of the phase 3 LYM3001 study
    • (abstract 265)
    • Coiffier B., Li W., Henitz E.D., et al. Identification of patient subgroups demonstrating longer progression-free survival (PFS) benefit with bortezomib-rituximab versus rituximab in patients with relapsed or refractory follicular lymphoma (FL): biomarker analyses of the phase 3 LYM3001 study. Blood 2011, 118:122. (abstract 265).
    • (2011) Blood , vol.118 , pp. 122
    • Coiffier, B.1    Li, W.2    Henitz, E.D.3
  • 28
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • Nalepa G., Rolfe M., Harper J.W. Drug discovery in the ubiquitin-proteasome system. Nat Rev Drug Discov 2006, 5:596-613.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 29
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
    • Schulman B.A., Harper J.W. Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol 2009, 10:319-331.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 30
    • 0028150688 scopus 로고
    • Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes
    • Vinitsky A., Cardozo C., Sepp-Lorenzino L., Michaud C., Orlowski M. Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J Biol Chem 1994, 269:29860-29866.
    • (1994) J Biol Chem , vol.269 , pp. 29860-29866
    • Vinitsky, A.1    Cardozo, C.2    Sepp-Lorenzino, L.3    Michaud, C.4    Orlowski, M.5
  • 31
    • 0029012388 scopus 로고
    • Potent inhibitors of proteasome
    • Iqbal M., Chatterjee S., Kauer J.C., et al. Potent inhibitors of proteasome. J Med Chem 1995, 38:2276-2277.
    • (1995) J Med Chem , vol.38 , pp. 2276-2277
    • Iqbal, M.1    Chatterjee, S.2    Kauer, J.C.3
  • 32
    • 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
    • Rock K.L., Gramm C., Rothstein L., et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994, 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3
  • 33
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: from research tools to drug candidates
    • Kisselev A.F., Goldberg A.L. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 2001, 8:739-758.
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 34
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • Myung J., Kim K.B., Crews C.M. The ubiquitin-proteasome pathway and proteasome inhibitors. Med Res Rev 2001, 21:245-273.
    • (2001) Med Res Rev , vol.21 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 35
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: lessons from the first decade
    • Orlowski R.Z., Kuhn D.J. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin Cancer Res 2008, 14:1649-1657.
    • (2008) Clin Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 36
    • 0031021991 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway as a therapeutic area
    • Rolfe M., Chiu M.I., Pagano M. The ubiquitin-mediated proteolytic pathway as a therapeutic area. J Mol Med (Berl) 1997, 75:5-17.
    • (1997) J Mol Med (Berl) , vol.75 , pp. 5-17
    • Rolfe, M.1    Chiu, M.I.2    Pagano, M.3
  • 37
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis
    • Delic J., Masdehors P., Omura S., et al. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis. Br J Cancer 1998, 77:1103-1107.
    • (1998) Br J Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1    Masdehors, P.2    Omura, S.3
  • 38
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski R.Z., Eswara J.R., Lafond-Walker A., et al. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res 1998, 58:4342-4348.
    • (1998) Cancer Res , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3
  • 39
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway
    • Mitch W.E., Goldberg A.L. Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N Engl J Med 1996, 335:1897-1905.
    • (1996) N Engl J Med , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 40
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994, 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 41
    • 13144294030 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B activation in vitro and in vivo: role of 26S proteasome
    • Grisham M.B., Palombella V.J., Elliott P.J., et al. Inhibition of NF-kappa B activation in vitro and in vivo: role of 26S proteasome. Methods Enzymol 1999, 300:345-363.
    • (1999) Methods Enzymol , vol.300 , pp. 345-363
    • Grisham, M.B.1    Palombella, V.J.2    Elliott, P.J.3
  • 42
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: a novel class of potent and effective antitumor agents
    • Adams J., Palombella V.J., Sausville E.A., et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res 1999, 59:2615-2622.
    • (1999) Cancer Res , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 43
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools-proteasome inhibitors offer therapeutic promise
    • Goldberg A.L., Rock K. Not just research tools-proteasome inhibitors offer therapeutic promise. Nat Med 2002, 8:338-340.
    • (2002) Nat Med , vol.8 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 44
    • 0032539702 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids
    • Adams J., Behnke M., Chen S., et al. Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg Med Chem Lett 1998, 8:333-338.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 333-338
    • Adams, J.1    Behnke, M.2    Chen, S.3
  • 46
    • 2942692143 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor bortezomib in patients with advanced solid tumors with observations in androgen-independent prostate cancer
    • Papandreou C.N., Daliani D.D., Nix D., et al. Phase I trial of the proteasome inhibitor bortezomib in patients with advanced solid tumors with observations in androgen-independent prostate cancer. J Clin Oncol 2004, 22:2108-2121.
    • (2004) J Clin Oncol , vol.22 , pp. 2108-2121
    • Papandreou, C.N.1    Daliani, D.D.2    Nix, D.3
  • 47
    • 0037111832 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor PS-341 in patients with refractory hematologic malignancies
    • Orlowski R.Z., Stinchcombe T.E., Mitchell B.S., et al. Phase I trial of the proteasome inhibitor PS-341 in patients with refractory hematologic malignancies. J Clin Oncol 2002, 20:4420-4427.
    • (2002) J Clin Oncol , vol.20 , pp. 4420-4427
    • Orlowski, R.Z.1    Stinchcombe, T.E.2    Mitchell, B.S.3
  • 48
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D., Dikic I. Targeting the ubiquitin system in cancer therapy. Nature 2009, 458:438-444.
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 49
    • 47149085982 scopus 로고    scopus 로고
    • P21 and p27: roles in carcinogenesis and drug resistance
    • Abukhdeir A.M., Park B.H. P21 and p27: roles in carcinogenesis and drug resistance. Expert Rev Mol Med 2008, 10:e19.
    • (2008) Expert Rev Mol Med , vol.10
    • Abukhdeir, A.M.1    Park, B.H.2
  • 50
    • 61649094981 scopus 로고    scopus 로고
    • Bortezomib in patients with relapsed or refractory mantle cell lymphoma: updated time-to-event analyses of the multicenter phase 2 PINNACLE study
    • Goy A., Bernstein S.H., Kahl B.S., et al. Bortezomib in patients with relapsed or refractory mantle cell lymphoma: updated time-to-event analyses of the multicenter phase 2 PINNACLE study. Ann Oncol 2009, 20:520-525.
    • (2009) Ann Oncol , vol.20 , pp. 520-525
    • Goy, A.1    Bernstein, S.H.2    Kahl, B.S.3
  • 51
    • 0036217332 scopus 로고    scopus 로고
    • Proteasome inhibition: a novel approach to cancer therapy
    • Adams J. Proteasome inhibition: a novel approach to cancer therapy. Trends Mol Med 2002, 8:S49-S54.
    • (2002) Trends Mol Med , vol.8
    • Adams, J.1
  • 52
    • 26844452967 scopus 로고    scopus 로고
    • Preclinical evaluation of the proteasome inhibitor bortezomib in cancer therapy
    • Boccadoro M., Morgan G., Cavenagh J. Preclinical evaluation of the proteasome inhibitor bortezomib in cancer therapy. Cancer Cell Int 2005, 5:18.
    • (2005) Cancer Cell Int , vol.5 , pp. 18
    • Boccadoro, M.1    Morgan, G.2    Cavenagh, J.3
  • 53
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy T.A., Smith P.G., Milhollen M.A., et al. An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 2009, 458:732-736.
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3
  • 54
    • 79952841638 scopus 로고    scopus 로고
    • The NEDD8 conjugation pathway and its relevance in cancer biology and therapy
    • Soucy T.A., Dick L.R., Smith P.G., Milhollen M.A., Brownell J.E. The NEDD8 conjugation pathway and its relevance in cancer biology and therapy. Genes Cancer 2010, 1:708-716.
    • (2010) Genes Cancer , vol.1 , pp. 708-716
    • Soucy, T.A.1    Dick, L.R.2    Smith, P.G.3    Milhollen, M.A.4    Brownell, J.E.5
  • 55
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB
    • Baldwin A.S. Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB. J Clin Invest 2001, 107:241-246.
    • (2001) J Clin Invest , vol.107 , pp. 241-246
    • Baldwin, A.S.1
  • 56
    • 0028049074 scopus 로고
    • The NF-kappa B transcription factor and cancer: high expression of NF-kappa B- and I kappa B-related proteins in tumor cell lines
    • Bours V., Dejardin E., Goujon-Letawe F., Merville M.P., Castronovo V. The NF-kappa B transcription factor and cancer: high expression of NF-kappa B- and I kappa B-related proteins in tumor cell lines. Biochem Pharmacol 1994, 47:145-149.
    • (1994) Biochem Pharmacol , vol.47 , pp. 145-149
    • Bours, V.1    Dejardin, E.2    Goujon-Letawe, F.3    Merville, M.P.4    Castronovo, V.5
  • 57
    • 0029666234 scopus 로고    scopus 로고
    • The NF-kappaB transcription factor in oncogenesis
    • Sharma H.W., Narayanan R. The NF-kappaB transcription factor in oncogenesis. Anticancer Res 1996, 16:589-596.
    • (1996) Anticancer Res , vol.16 , pp. 589-596
    • Sharma, H.W.1    Narayanan, R.2
  • 58
    • 18544367201 scopus 로고    scopus 로고
    • NF-kappa B as a therapeutic target in multiple myeloma
    • Hideshima T., Chauhan D., Richardson P., et al. NF-kappa B as a therapeutic target in multiple myeloma. J Biol Chem 2002, 277:16639-16647.
    • (2002) J Biol Chem , vol.277 , pp. 16639-16647
    • Hideshima, T.1    Chauhan, D.2    Richardson, P.3
  • 59
    • 79953782203 scopus 로고    scopus 로고
    • NF-kappaB addiction and its role in cancer: 'one size does not fit all'
    • Chaturvedi M.M., Sung B., Yadav V.R., Kannappan R., Aggarwal B.B. NF-kappaB addiction and its role in cancer: 'one size does not fit all'. Oncogene 2011, 30:1615-1630.
    • (2011) Oncogene , vol.30 , pp. 1615-1630
    • Chaturvedi, M.M.1    Sung, B.2    Yadav, V.R.3    Kannappan, R.4    Aggarwal, B.B.5
  • 60
    • 34547660308 scopus 로고    scopus 로고
    • Promiscuous mutations activate the noncanonical NF-kappaB pathway in multiple myeloma
    • Keats J.J., Fonseca R., Chesi M., et al. Promiscuous mutations activate the noncanonical NF-kappaB pathway in multiple myeloma. Cancer Cell 2007, 12:131-144.
    • (2007) Cancer Cell , vol.12 , pp. 131-144
    • Keats, J.J.1    Fonseca, R.2    Chesi, M.3
  • 61
    • 67650398258 scopus 로고    scopus 로고
    • Differential efficacy of bortezomib plus chemotherapy within molecular subtypes of diffuse large B cell lymphoma
    • Dunleavy K., Pittaluga S., Czuczman M.S., et al. Differential efficacy of bortezomib plus chemotherapy within molecular subtypes of diffuse large B cell lymphoma. Blood 2009, 113:6069-6076.
    • (2009) Blood , vol.113 , pp. 6069-6076
    • Dunleavy, K.1    Pittaluga, S.2    Czuczman, M.S.3
  • 62
    • 79952154013 scopus 로고    scopus 로고
    • Bortezomib plus CHOP-rituximab for previously untreated diffuse large B-cell lymphoma and mantle cell lymphoma
    • Ruan J., Martin P., Furman R.R., et al. Bortezomib plus CHOP-rituximab for previously untreated diffuse large B-cell lymphoma and mantle cell lymphoma. J Clin Oncol 2011, 29:690-697.
    • (2011) J Clin Oncol , vol.29 , pp. 690-697
    • Ruan, J.1    Martin, P.2    Furman, R.R.3
  • 63
    • 84878689886 scopus 로고    scopus 로고
    • PYRAMID and LYM2034: Targeted randomized phase II studies of bortezomib with or without immunochemotherapy in newly diagnosed nongerminal center B-cell-like (GCB) diffuse large B-cell lymphoma (DLBCL), including rapid prospective non-GCB subtype identification
    • TPS226 (abstract TPS226)
    • Leonard J.P., Reeves J., Ferhanoglu B., et al. PYRAMID and LYM2034: Targeted randomized phase II studies of bortezomib with or without immunochemotherapy in newly diagnosed nongerminal center B-cell-like (GCB) diffuse large B-cell lymphoma (DLBCL), including rapid prospective non-GCB subtype identification. J Clin Oncol 2011, 29. TPS226 (abstract TPS226).
    • (2011) J Clin Oncol , vol.29
    • Leonard, J.P.1    Reeves, J.2    Ferhanoglu, B.3
  • 64
    • 77955729630 scopus 로고    scopus 로고
    • Combination therapy of bortezomib with novel targeted agents: an emerging treatment strategy
    • Wright J.J. Combination therapy of bortezomib with novel targeted agents: an emerging treatment strategy. Clin Cancer Res 2010, 16:4094-4104.
    • (2010) Clin Cancer Res , vol.16 , pp. 4094-4104
    • Wright, J.J.1
  • 66
    • 0034037622 scopus 로고    scopus 로고
    • Proteasome inhibition measurements: clinical application
    • Lightcap E.S., McCormack T.A., Pien C.S., et al. Proteasome inhibition measurements: clinical application. Clin Chem 2000, 46:673-683.
    • (2000) Clin Chem , vol.46 , pp. 673-683
    • Lightcap, E.S.1    McCormack, T.A.2    Pien, C.S.3
  • 67
    • 0036023407 scopus 로고    scopus 로고
    • A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies
    • Aghajanian C., Soignet S., Dizon D.S., et al. A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies. Clin Cancer Res 2002, 8:2505-2511.
    • (2002) Clin Cancer Res , vol.8 , pp. 2505-2511
    • Aghajanian, C.1    Soignet, S.2    Dizon, D.S.3
  • 68
    • 5644250621 scopus 로고    scopus 로고
    • A phase 2 study of two doses of bortezomib in relapsed or refractory myeloma
    • Jagannath S., Barlogie B., Berenson J., et al. A phase 2 study of two doses of bortezomib in relapsed or refractory myeloma. Br J Haematol 2004, 127:165-172.
    • (2004) Br J Haematol , vol.127 , pp. 165-172
    • Jagannath, S.1    Barlogie, B.2    Berenson, J.3
  • 69
    • 0037973279 scopus 로고    scopus 로고
    • A phase 2 study of bortezomib in relapsed, refractory myeloma
    • Richardson P.G., Barlogie B., Berenson J., et al. A phase 2 study of bortezomib in relapsed, refractory myeloma. N Engl J Med 2003, 348:2609-2617.
    • (2003) N Engl J Med , vol.348 , pp. 2609-2617
    • Richardson, P.G.1    Barlogie, B.2    Berenson, J.3
  • 70
    • 33750625445 scopus 로고    scopus 로고
    • Multicenter phase II study of bortezomib in patients with relapsed or refractory mantle cell lymphoma
    • Fisher R.I., Bernstein S.H., Kahl B.S., et al. Multicenter phase II study of bortezomib in patients with relapsed or refractory mantle cell lymphoma. J Clin Oncol 2006, 24:4867-4874.
    • (2006) J Clin Oncol , vol.24 , pp. 4867-4874
    • Fisher, R.I.1    Bernstein, S.H.2    Kahl, B.S.3
  • 71
    • 20044376092 scopus 로고    scopus 로고
    • Phase II clinical experience with the novel proteasome inhibitor bortezomib in patients with indolent non-Hodgkin's lymphoma and mantle cell lymphoma
    • O'Connor O.A., Wright J., Moskowitz C., et al. Phase II clinical experience with the novel proteasome inhibitor bortezomib in patients with indolent non-Hodgkin's lymphoma and mantle cell lymphoma. J Clin Oncol 2005, 23:676-684.
    • (2005) J Clin Oncol , vol.23 , pp. 676-684
    • O'Connor, O.A.1    Wright, J.2    Moskowitz, C.3
  • 72
    • 79960934028 scopus 로고    scopus 로고
    • Efficacy and safety of once-weekly and twice-weekly bortezomib in patients with relapsed systemic AL amyloidosis: results of a phase 1/2 study
    • Reece D.E., Hegenbart U., Sanchorawala V., et al. Efficacy and safety of once-weekly and twice-weekly bortezomib in patients with relapsed systemic AL amyloidosis: results of a phase 1/2 study. Blood 2011, 118:865-873.
    • (2011) Blood , vol.118 , pp. 865-873
    • Reece, D.E.1    Hegenbart, U.2    Sanchorawala, V.3
  • 73
    • 34250630491 scopus 로고    scopus 로고
    • Multicenter clinical trial of bortezomib in relapsed/refractory Waldenstrom's macroglobulinemia: results of WMCTG trial 03-248
    • Treon S.P., Hunter Z.R., Matous J., et al. Multicenter clinical trial of bortezomib in relapsed/refractory Waldenstrom's macroglobulinemia: results of WMCTG trial 03-248. Clin Cancer Res 2007, 13:3320-3325.
    • (2007) Clin Cancer Res , vol.13 , pp. 3320-3325
    • Treon, S.P.1    Hunter, Z.R.2    Matous, J.3
  • 74
    • 28444436266 scopus 로고    scopus 로고
    • Risk factors and kinetics of thrombocytopenia associated with bortezomib for relapsed, refractory multiple myeloma
    • Lonial S., Waller E.K., Richardson P.G., et al. Risk factors and kinetics of thrombocytopenia associated with bortezomib for relapsed, refractory multiple myeloma. Blood 2005, 106:3777-3784.
    • (2005) Blood , vol.106 , pp. 3777-3784
    • Lonial, S.1    Waller, E.K.2    Richardson, P.G.3
  • 75
    • 52649096895 scopus 로고    scopus 로고
    • Characterisation of haematological profiles and low risk of thromboembolic events with bortezomib in patients with relapsed multiple myeloma
    • Lonial S., Richardson P.G., San M.J., et al. Characterisation of haematological profiles and low risk of thromboembolic events with bortezomib in patients with relapsed multiple myeloma. Br J Haematol 2008, 143:222-229.
    • (2008) Br J Haematol , vol.143 , pp. 222-229
    • Lonial, S.1    Richardson, P.G.2    San, M.J.3
  • 76
    • 31444440714 scopus 로고    scopus 로고
    • Normal hematopoietic stem cell function in mice following treatment with bortezomib
    • Fitzgerald M., Fraser C., Webb I., et al. Normal hematopoietic stem cell function in mice following treatment with bortezomib. Biol Blood Marrow Transplant 2003, 9:121.
    • (2003) Biol Blood Marrow Transplant , vol.9 , pp. 121
    • Fitzgerald, M.1    Fraser, C.2    Webb, I.3
  • 77
    • 70349260793 scopus 로고    scopus 로고
    • Mobilization in myeloma revisited: IMWG consensus perspectives on stem cell collection following initial therapy with thalidomide-, lenalidomide-, or bortezomib-containing regimens
    • Kumar S., Giralt S., Stadtmauer E.A., et al. Mobilization in myeloma revisited: IMWG consensus perspectives on stem cell collection following initial therapy with thalidomide-, lenalidomide-, or bortezomib-containing regimens. Blood 2009, 114:1729-1735.
    • (2009) Blood , vol.114 , pp. 1729-1735
    • Kumar, S.1    Giralt, S.2    Stadtmauer, E.A.3
  • 78
    • 35148873640 scopus 로고    scopus 로고
    • Use of bortezomib as induction therapy prior to stem cell transplantation in frontline treatment of multiple myeloma: impact on stem cell harvesting and engraftment
    • Oakervee H., Popat R., Cavenagh J.D. Use of bortezomib as induction therapy prior to stem cell transplantation in frontline treatment of multiple myeloma: impact on stem cell harvesting and engraftment. Leuk Lymphoma 2007, 48:1910-1921.
    • (2007) Leuk Lymphoma , vol.48 , pp. 1910-1921
    • Oakervee, H.1    Popat, R.2    Cavenagh, J.D.3
  • 79
    • 33746010219 scopus 로고    scopus 로고
    • Frequency, characteristics, and reversibility of peripheral neuropathy during treatment of advanced multiple myeloma with bortezomib
    • Richardson P.G., Briemberg H., Jagannath S., et al. Frequency, characteristics, and reversibility of peripheral neuropathy during treatment of advanced multiple myeloma with bortezomib. J Clin Oncol 2006, 24:3113-3120.
    • (2006) J Clin Oncol , vol.24 , pp. 3113-3120
    • Richardson, P.G.1    Briemberg, H.2    Jagannath, S.3
  • 80
    • 84859632261 scopus 로고    scopus 로고
    • Management of treatment-emergent peripheral neuropathy in multiple myeloma
    • Richardson P.G., Delforge M., Beksac M., et al. Management of treatment-emergent peripheral neuropathy in multiple myeloma. Leukemia 2012, 26:595-608.
    • (2012) Leukemia , vol.26 , pp. 595-608
    • Richardson, P.G.1    Delforge, M.2    Beksac, M.3
  • 81
    • 83955165140 scopus 로고    scopus 로고
    • Response and resistance to NF-kappaB inhibitors in mouse models of lung adenocarcinoma
    • Xue W., Meylan E., Oliver T.G., et al. Response and resistance to NF-kappaB inhibitors in mouse models of lung adenocarcinoma. Cancer Discov 2011, 1:236-247.
    • (2011) Cancer Discov , vol.1 , pp. 236-247
    • Xue, W.1    Meylan, E.2    Oliver, T.G.3
  • 82
    • 20444433230 scopus 로고    scopus 로고
    • Bortezomib or high-dose dexamethasone for relapsed multiple myeloma
    • Richardson P.G., Sonneveld P., Schuster M.W., et al. Bortezomib or high-dose dexamethasone for relapsed multiple myeloma. N Engl J Med 2005, 352:2487-2498.
    • (2005) N Engl J Med , vol.352 , pp. 2487-2498
    • Richardson, P.G.1    Sonneveld, P.2    Schuster, M.W.3
  • 83
    • 50449086728 scopus 로고    scopus 로고
    • Bortezomib plus melphalan and prednisone for initial treatment of multiple myeloma
    • San Miguel J.F., Schlag R., Khuageva N.K., et al. Bortezomib plus melphalan and prednisone for initial treatment of multiple myeloma. N Engl J Med 2008, 359:906-917.
    • (2008) N Engl J Med , vol.359 , pp. 906-917
    • San Miguel, J.F.1    Schlag, R.2    Khuageva, N.K.3
  • 84
    • 84858791957 scopus 로고    scopus 로고
    • Continued overall survival benefit after 5 years' follow-up with bortezomib-melphalan-prednisone (VMP) versus melphalan-prednisone (MP) in patients with previously untreated multiple myeloma, and no increased risk of second primary malignancies: final results of the phase 3 VISTA trial
    • (abstract 476)
    • San Miguel J.F., Schlag R., Khuageva N.K., et al. Continued overall survival benefit after 5 years' follow-up with bortezomib-melphalan-prednisone (VMP) versus melphalan-prednisone (MP) in patients with previously untreated multiple myeloma, and no increased risk of second primary malignancies: final results of the phase 3 VISTA trial. Blood 2011, 118:221-222. (abstract 476).
    • (2011) Blood , vol.118 , pp. 221-222
    • San Miguel, J.F.1    Schlag, R.2    Khuageva, N.K.3
  • 85
    • 78650303860 scopus 로고    scopus 로고
    • Bortezomib with thalidomide plus dexamethasone compared with thalidomide plus dexamethasone as induction therapy before, and consolidation therapy after, double autologous stem-cell transplantation in newly diagnosed multiple myeloma: a randomised phase 3 study
    • Cavo M., Tacchetti P., Patriarca F., et al. Bortezomib with thalidomide plus dexamethasone compared with thalidomide plus dexamethasone as induction therapy before, and consolidation therapy after, double autologous stem-cell transplantation in newly diagnosed multiple myeloma: a randomised phase 3 study. Lancet 2010, 376:2075-2085.
    • (2010) Lancet , vol.376 , pp. 2075-2085
    • Cavo, M.1    Tacchetti, P.2    Patriarca, F.3
  • 86
    • 78049488759 scopus 로고    scopus 로고
    • Bortezomib plus dexamethasone is superior to vincristine plus doxorubicin plus dexamethasone as induction treatment prior to autologous stem-cell transplantation in newly diagnosed multiple myeloma: results of the IFM 2005-01 phase III trial
    • Harousseau J.L., Attal M., Avet-Loiseau H., et al. Bortezomib plus dexamethasone is superior to vincristine plus doxorubicin plus dexamethasone as induction treatment prior to autologous stem-cell transplantation in newly diagnosed multiple myeloma: results of the IFM 2005-01 phase III trial. J Clin Oncol 2010, 28:4621-4629.
    • (2010) J Clin Oncol , vol.28 , pp. 4621-4629
    • Harousseau, J.L.1    Attal, M.2    Avet-Loiseau, H.3
  • 87
    • 79956001465 scopus 로고    scopus 로고
    • Consensus recommendations for standard investigative workup: report of the International Myeloma Workshop Consensus Panel 3
    • Dimopoulos M., Kyle R., Fermand J.P., et al. Consensus recommendations for standard investigative workup: report of the International Myeloma Workshop Consensus Panel 3. Blood 2011, 117:4701-4705.
    • (2011) Blood , vol.117 , pp. 4701-4705
    • Dimopoulos, M.1    Kyle, R.2    Fermand, J.P.3
  • 88
    • 79956039754 scopus 로고    scopus 로고
    • Consensus recommendations for risk stratification in multiple myeloma: report of the International Myeloma Workshop Consensus Panel 2
    • Munshi N.C., Anderson K.C., Bergsagel P.L., et al. Consensus recommendations for risk stratification in multiple myeloma: report of the International Myeloma Workshop Consensus Panel 2. Blood 2011, 117:4696-4700.
    • (2011) Blood , vol.117 , pp. 4696-4700
    • Munshi, N.C.1    Anderson, K.C.2    Bergsagel, P.L.3
  • 89
    • 79955977910 scopus 로고    scopus 로고
    • Consensus recommendations for the uniform reporting of clinical trials: report of the International Myeloma Workshop Consensus Panel 1
    • Rajkumar S.V., Harousseau J.L., Durie B., et al. Consensus recommendations for the uniform reporting of clinical trials: report of the International Myeloma Workshop Consensus Panel 1. Blood 2011, 117:4691-4695.
    • (2011) Blood , vol.117 , pp. 4691-4695
    • Rajkumar, S.V.1    Harousseau, J.L.2    Durie, B.3
  • 90
    • 78049528598 scopus 로고    scopus 로고
    • Mechanisms of peripheral neuropathy associated with bortezomib and vincristine in patients with newly diagnosed multiple myeloma: a prospective analysis of data from the HOVON-65/GMMG-HD4 trial
    • Broyl A., Corthals S.L., Jongen J.L., et al. Mechanisms of peripheral neuropathy associated with bortezomib and vincristine in patients with newly diagnosed multiple myeloma: a prospective analysis of data from the HOVON-65/GMMG-HD4 trial. Lancet Oncol 2010, 11:1057-1065.
    • (2010) Lancet Oncol , vol.11 , pp. 1057-1065
    • Broyl, A.1    Corthals, S.L.2    Jongen, J.L.3
  • 91
    • 80355125798 scopus 로고    scopus 로고
    • Genetic factors underlying the risk of bortezomib induced peripheral neuropathy in multiple myeloma patients
    • Corthals S.L., Kuiper R., Johnson D.C., et al. Genetic factors underlying the risk of bortezomib induced peripheral neuropathy in multiple myeloma patients. Haematologica 2011, 96:1728-1732.
    • (2011) Haematologica , vol.96 , pp. 1728-1732
    • Corthals, S.L.1    Kuiper, R.2    Johnson, D.C.3
  • 92
    • 74949121208 scopus 로고    scopus 로고
    • VMP (bortezomib, melphalan, and prednisone) is active and well tolerated in newly diagnosed patients with multiple myeloma with moderately impaired renal function, and results in reversal of renal impairment: cohort analysis of the phase III VISTA study
    • Dimopoulos M.A., Richardson P.G., Schlag R., et al. VMP (bortezomib, melphalan, and prednisone) is active and well tolerated in newly diagnosed patients with multiple myeloma with moderately impaired renal function, and results in reversal of renal impairment: cohort analysis of the phase III VISTA study. J Clin Oncol 2009, 27:6086-6093.
    • (2009) J Clin Oncol , vol.27 , pp. 6086-6093
    • Dimopoulos, M.A.1    Richardson, P.G.2    Schlag, R.3
  • 93
    • 42349108452 scopus 로고    scopus 로고
    • Efficacy and safety of bortezomib in patients with renal impairment: results from the APEX phase 3 study
    • San-Miguel J.F., Richardson P.G., Sonneveld P., et al. Efficacy and safety of bortezomib in patients with renal impairment: results from the APEX phase 3 study. Leukemia 2008, 22:842-849.
    • (2008) Leukemia , vol.22 , pp. 842-849
    • San-Miguel, J.F.1    Richardson, P.G.2    Sonneveld, P.3
  • 94
    • 79954426340 scopus 로고    scopus 로고
    • Fewer bone disease events, improvement in bone remodeling, and evidence of bone healing with bortezomib plus melphalan-prednisone vs. melphalan-prednisone in the phase III VISTA trial in multiple myeloma
    • Delforge M., Terpos E., Richardson P.G., et al. Fewer bone disease events, improvement in bone remodeling, and evidence of bone healing with bortezomib plus melphalan-prednisone vs. melphalan-prednisone in the phase III VISTA trial in multiple myeloma. Eur J Haematol 2011, 86:372-384.
    • (2011) Eur J Haematol , vol.86 , pp. 372-384
    • Delforge, M.1    Terpos, E.2    Richardson, P.G.3
  • 95
    • 77649237033 scopus 로고    scopus 로고
    • Building on bortezomib: second-generation proteasome inhibitors as anti-cancer therapy
    • Dick L.R., Fleming P.E. Building on bortezomib: second-generation proteasome inhibitors as anti-cancer therapy. Drug Discov Today 2010, 15:243-249.
    • (2010) Drug Discov Today , vol.15 , pp. 243-249
    • Dick, L.R.1    Fleming, P.E.2
  • 96
    • 77950238258 scopus 로고    scopus 로고
    • Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer
    • Kupperman E., Lee E.C., Cao Y., et al. Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer. Cancer Res 2010, 70:1970-1980.
    • (2010) Cancer Res , vol.70 , pp. 1970-1980
    • Kupperman, E.1    Lee, E.C.2    Cao, Y.3
  • 97
    • 79955461011 scopus 로고    scopus 로고
    • Subcutaneous versus intravenous administration of bortezomib in patients with relapsed multiple myeloma: a randomised, phase 3, non-inferiority study
    • Moreau P., Pylypenko H., Grosicki S., et al. Subcutaneous versus intravenous administration of bortezomib in patients with relapsed multiple myeloma: a randomised, phase 3, non-inferiority study. Lancet Oncol 2011, 12:431-440.
    • (2011) Lancet Oncol , vol.12 , pp. 431-440
    • Moreau, P.1    Pylypenko, H.2    Grosicki, S.3
  • 98
    • 79951494668 scopus 로고    scopus 로고
    • Initial genome sequencing and analysis of multiple myeloma
    • Chapman M.A., Lawrence M.S., Keats J.J., et al. Initial genome sequencing and analysis of multiple myeloma. Nature 2011, 471:467-472.
    • (2011) Nature , vol.471 , pp. 467-472
    • Chapman, M.A.1    Lawrence, M.S.2    Keats, J.J.3
  • 99
    • 79953814654 scopus 로고    scopus 로고
    • RNAi screen of the druggable genome identifies modulators of proteasome inhibitor sensitivity in myeloma including CDK5
    • Zhu Y.X., Tiedemann R., Shi C.X., et al. RNAi screen of the druggable genome identifies modulators of proteasome inhibitor sensitivity in myeloma including CDK5. Blood 2011, 117:3847-3857.
    • (2011) Blood , vol.117 , pp. 3847-3857
    • Zhu, Y.X.1    Tiedemann, R.2    Shi, C.X.3
  • 102
    • 54249154593 scopus 로고    scopus 로고
    • The UPS: a promising target for breast cancer treatment
    • Sato K., Rajendra E., Ohta T. The UPS: a promising target for breast cancer treatment. BMC Biochem 2008, 9(Suppl 1):S2.
    • (2008) BMC Biochem , vol.9 , Issue.SUPPL. 1
    • Sato, K.1    Rajendra, E.2    Ohta, T.3
  • 103
    • 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 D.J., Hunsucker S.A., 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, 113:4667-4676.
    • (2009) Blood , vol.113 , pp. 4667-4676
    • Kuhn, D.J.1    Hunsucker, S.A.2    Chen, Q.3
  • 104
    • 0036017391 scopus 로고    scopus 로고
    • Protein degradation and the generation of MHC class I-presented peptides
    • Rock K.L., York I.A., Saric T., Goldberg A.L. Protein degradation and the generation of MHC class I-presented peptides. Adv Immunol 2002, 80:1-70.
    • (2002) Adv Immunol , vol.80 , pp. 1-70
    • Rock, K.L.1    York, I.A.2    Saric, T.3    Goldberg, A.L.4
  • 105
    • 77956624118 scopus 로고    scopus 로고
    • The NF-kappaB signaling in cystic fibrosis lung disease: pathophysiology and therapeutic potential
    • Bodas M., Vij N. The NF-kappaB signaling in cystic fibrosis lung disease: pathophysiology and therapeutic potential. Discov Med 2010, 9:346-356.
    • (2010) Discov Med , vol.9 , pp. 346-356
    • Bodas, M.1    Vij, N.2
  • 106
    • 0347987907 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiovascular diseases-a hypothesis extended
    • Herrmann J., Ciechanover A., Lerman L.O., Lerman A. The ubiquitin-proteasome system in cardiovascular diseases-a hypothesis extended. Cardiovasc Res 2004, 61:11-21.
    • (2004) Cardiovasc Res , vol.61 , pp. 11-21
    • Herrmann, J.1    Ciechanover, A.2    Lerman, L.O.3    Lerman, A.4
  • 107
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman N.L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol 2009, 118:329-347.
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 108
    • 54249104026 scopus 로고    scopus 로고
    • The ubiquitin system, disease, and drug discovery
    • Petroski M.D. The ubiquitin system, disease, and drug discovery. BMC Biochem 2008, 9(Suppl 1):S7.
    • (2008) BMC Biochem , vol.9 , Issue.SUPPL. 1
    • Petroski, M.D.1
  • 109
    • 0024210542 scopus 로고
    • A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation
    • Ganoth D., Leshinsky E., Eytan E., Hershko A. A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation. J Biol Chem 1988, 263:12412-12419.
    • (1988) J Biol Chem , vol.263 , pp. 12412-12419
    • Ganoth, D.1    Leshinsky, E.2    Eytan, E.3    Hershko, A.4
  • 110
    • 0019508071 scopus 로고
    • Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system
    • Ciechanover A., Heller H., Katz-Etzion R., Hershko A. Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system. Proc Natl Acad Sci U S A 1981, 78:761-765.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 761-765
    • Ciechanover, A.1    Heller, H.2    Katz-Etzion, R.3    Hershko, A.4
  • 111
    • 0019731397 scopus 로고
    • A multicatalytic protease complex from pituitary that forms enkephalin and enkephalin containing peptides
    • Orlowski M., Wilk S. A multicatalytic protease complex from pituitary that forms enkephalin and enkephalin containing peptides. Biochem Biophys Res Commun 1981, 101:814-822.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 814-822
    • Orlowski, M.1    Wilk, S.2
  • 112
    • 0020674228 scopus 로고
    • Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex
    • Wilk S., Orlowski M. Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex. J Neurochem 1983, 40:842-849.
    • (1983) J Neurochem , vol.40 , pp. 842-849
    • Wilk, S.1    Orlowski, M.2
  • 113
    • 0024285837 scopus 로고
    • Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)
    • Arrigo A.P., Tanaka K., Goldberg A.L., Welch W.J. Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature 1988, 331:192-194.
    • (1988) Nature , vol.331 , pp. 192-194
    • Arrigo, A.P.1    Tanaka, K.2    Goldberg, A.L.3    Welch, W.J.4
  • 114
    • 0024413057 scopus 로고
    • ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin
    • Eytan E., Ganoth D., Armon T., Hershko A. ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. Proc Natl Acad Sci U S A 1989, 86:7751-7755.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 7751-7755
    • Eytan, E.1    Ganoth, D.2    Armon, T.3    Hershko, A.4
  • 115
    • 0024285838 scopus 로고
    • Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase
    • Falkenburg P.E., Haass C., Kloetzel P.M., et al. Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase. Nature 1988, 331:190-192.
    • (1988) Nature , vol.331 , pp. 190-192
    • Falkenburg, P.E.1    Haass, C.2    Kloetzel, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.