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Volumn 27, Issue 6, 2013, Pages 297-304

Targeting the ubiquitin proteasome system in haematological malignancies

Author keywords

Proteasome inhibitors; Ubiquitin proteasome system

Indexed keywords

BORTEZOMIB; CARFILZOMIB; DELANZOMIB; DEUBIQUITINATING ENZYME INHIBITOR; ENZYME INHIBITOR; HISTONE DEACETYLASE INHIBITOR; INHIBITOR OF APOPTOSIS PROTEIN; IPSI 101; IXAZOMIB CITRATE; LENALIDOMIDE; MELPHALAN; NEDD8 ACTIVATING ENZYME INHIBITOR; NSC 624206; OPROZOMIB; PEVONEDISTAT; PPZD 4409; PR 047; PR 924; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN FBXW7; PROTEIN MDM2; S PHASE KINASE ASSOCIATED PROTEIN 2; SALINOSPORAMIDE A; UBIQUITIN PROTEASOME SYSTEM; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E1; UBIQUITIN PROTEIN LIGASE E2; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE E3 INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84887611976     PISSN: 0268960X     EISSN: 15321681     Source Type: Journal    
DOI: 10.1016/j.blre.2013.10.002     Document Type: Article
Times cited : (61)

References (129)
  • 1
    • 84864610631 scopus 로고    scopus 로고
    • Selectivity of the ubiquitin-binding modules
    • Rahighi S., Dikic I. Selectivity of the ubiquitin-binding modules. FEBS Lett 2012, 586:2705-2710.
    • (2012) FEBS Lett , vol.586 , pp. 2705-2710
    • Rahighi, S.1    Dikic, I.2
  • 3
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4Å resolution
    • Groll M., Ditzel L., Lowe J., et al. Structure of 20S proteasome from yeast at 2.4Å resolution. Nature 1997, 386:463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3
  • 4
    • 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, 7:1062-1067.
    • (2000) Nat Struct Biol , vol.7 , pp. 1062-1067
    • Groll, M.1    Bajorek, M.2    Kohler, A.3
  • 5
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock K.L., Goldberg A.L. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu Rev Immunol 1999, 17:739-779.
    • (1999) Annu Rev Immunol , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 6
    • 79958772781 scopus 로고    scopus 로고
    • The role of the proteasome in the generation of MHC class I ligands and immune responses
    • Sijts E.J., Kloetzel P.M. The role of the proteasome in the generation of MHC class I ligands and immune responses. Cell Mol Life Sci 2011, 68:1491-1502.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 1491-1502
    • Sijts, E.J.1    Kloetzel, P.M.2
  • 9
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler H.C. Activation of the cell death program by inhibition of proteasome function. Proc Natl Acad Sci 1997, 94:855-860.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 855-860
    • Drexler, H.C.1
  • 10
    • 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., Grever M.R., Orlowski M., Dang C.V. 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    Grever, M.R.4    Orlowski, M.5    Dang, C.V.6
  • 11
    • 0025115736 scopus 로고
    • Abnormally high expression of proteasomes in human leukemic cells
    • Kumatori A., Tanaka K., Inamura N., et al. Abnormally high expression of proteasomes in human leukemic cells. Proc Natl Acad Sci 1990, 87:7071-7075.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 7071-7075
    • Kumatori, A.1    Tanaka, K.2    Inamura, N.3
  • 12
    • 33847380754 scopus 로고    scopus 로고
    • Circulating proteasome levels are an independent prognostic factor for survival in multiple myeloma
    • Jakob C., Egerer K., Liebisch P., et al. Circulating proteasome levels are an independent prognostic factor for survival in multiple myeloma. Blood 2007, 109:2100-2105.
    • (2007) Blood , vol.109 , pp. 2100-2105
    • Jakob, C.1    Egerer, K.2    Liebisch, P.3
  • 13
    • 66649101365 scopus 로고    scopus 로고
    • Proteasome enzymatic activities in plasma as risk stratification of patients with acute myeloid leukemia and advanced-stage myelodysplastic syndrome
    • Ma W., Kantarjian H., Bekele B., et al. Proteasome enzymatic activities in plasma as risk stratification of patients with acute myeloid leukemia and advanced-stage myelodysplastic syndrome. Clin Cancer Res 2009, 15:3820-3826.
    • (2009) Clin Cancer Res , vol.15 , pp. 3820-3826
    • Ma, W.1    Kantarjian, H.2    Bekele, B.3
  • 14
    • 59749086449 scopus 로고    scopus 로고
    • Proteasome proteolytic profile is linked to Bcr-Abl expression
    • Crawford L.J., Windrum P., Magill L., et al. Proteasome proteolytic profile is linked to Bcr-Abl expression. Exp Hematol 2009, 37:357-366.
    • (2009) Exp Hematol , vol.37 , pp. 357-366
    • Crawford, L.J.1    Windrum, P.2    Magill, L.3
  • 15
    • 33745728140 scopus 로고    scopus 로고
    • Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132
    • Crawford L.J., Walker B., Ovaa H., et al. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res 2006, 66:6379-6386.
    • (2006) Cancer Res , vol.66 , pp. 6379-6386
    • Crawford, L.J.1    Walker, B.2    Ovaa, H.3
  • 18
    • 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, 61:3071-3076.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 19
    • 65649154116 scopus 로고    scopus 로고
    • Myeloma cells exhibit an increase in proteasome activity and an enhanced response to proteasome inhibition in the bone marrow microenvironment in vivo
    • Edwards C.M., Lwin S.T., Fowler J.A., et al. Myeloma cells exhibit an increase in proteasome activity and an enhanced response to proteasome inhibition in the bone marrow microenvironment in vivo. Am J Hematol 2009, 84:268-272.
    • (2009) Am J Hematol , vol.84 , pp. 268-272
    • Edwards, C.M.1    Lwin, S.T.2    Fowler, J.A.3
  • 20
    • 0012433771 scopus 로고    scopus 로고
    • Effects of the proteasome inhibitor PS-341 on apoptosis and angiogenesis in orthotopic human pancreatic tumor xenografts
    • Nawrocki S.T., Bruns C.J., Harbison M.T., et al. Effects of the proteasome inhibitor PS-341 on apoptosis and angiogenesis in orthotopic human pancreatic tumor xenografts. Mol Cancer Ther 2002, 1:1243-1253.
    • (2002) Mol Cancer Ther , vol.1 , pp. 1243-1253
    • Nawrocki, S.T.1    Bruns, C.J.2    Harbison, M.T.3
  • 21
    • 33750566914 scopus 로고    scopus 로고
    • Bortezomib reduces serum dickkopf-1 and receptor activator of nuclear factor-kappaB ligand concentrations and normalises indices of bone remodelling in patients with relapsed multiple myeloma
    • Terpos E., Heath D.J., Rahemtulla A., et al. Bortezomib reduces serum dickkopf-1 and receptor activator of nuclear factor-kappaB ligand concentrations and normalises indices of bone remodelling in patients with relapsed multiple myeloma. Br J Haematol 2006, 135:688-692.
    • (2006) Br J Haematol , vol.135 , pp. 688-692
    • Terpos, E.1    Heath, D.J.2    Rahemtulla, A.3
  • 22
    • 33746786028 scopus 로고    scopus 로고
    • Bortezomib increases osteoblast activity in myeloma patients irrespective of response to treatment
    • Heider U., Kaiser M., Muller C., et al. Bortezomib increases osteoblast activity in myeloma patients irrespective of response to treatment. Eur J Haematol 2006, 77:233-238.
    • (2006) Eur J Haematol , vol.77 , pp. 233-238
    • Heider, U.1    Kaiser, M.2    Muller, C.3
  • 23
    • 34347400592 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib affects osteoblast differentiation in vitro and in vivo in multiple myeloma patients
    • Giuliani N., Morandi F., Tagliaferri S., et al. The proteasome inhibitor bortezomib affects osteoblast differentiation in vitro and in vivo in multiple myeloma patients. Blood 2007, 110:334-338.
    • (2007) Blood , vol.110 , pp. 334-338
    • Giuliani, N.1    Morandi, F.2    Tagliaferri, S.3
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0345447210 scopus 로고    scopus 로고
    • Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy
    • Kane R.C., Bross P.F., Farrell A.T., Pazdur R. Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist 2003, 8:508-513.
    • (2003) Oncologist , vol.8 , pp. 508-513
    • Kane, R.C.1    Bross, P.F.2    Farrell, A.T.3    Pazdur, R.4
  • 28
    • 33744832401 scopus 로고    scopus 로고
    • United States Food and Drug Administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy
    • Kane R.C., Farrell A.T., Sridhara R., Pazdur R. United States Food and Drug Administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy. Clin Cancer Res 2006, 12:2955-2960.
    • (2006) Clin Cancer Res , vol.12 , pp. 2955-2960
    • Kane, R.C.1    Farrell, A.T.2    Sridhara, R.3    Pazdur, R.4
  • 29
    • 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
  • 30
    • 84862696482 scopus 로고    scopus 로고
    • Bortezomib combination therapy in multiple myeloma
    • Kapoor P., Ramakrishnan V., Rajkumar S.V. Bortezomib combination therapy in multiple myeloma. Semin Hematol 2012, 49:228-242.
    • (2012) Semin Hematol , vol.49 , pp. 228-242
    • Kapoor, P.1    Ramakrishnan, V.2    Rajkumar, S.V.3
  • 31
    • 77954125336 scopus 로고    scopus 로고
    • Peripheral neuropathy during bortezomib treatment of multiple myeloma: a review of recent studies
    • Cavaletti G., Jakubowiak A.J. Peripheral neuropathy during bortezomib treatment of multiple myeloma: a review of recent studies. Leuk Lymphoma 2010, 51:1178-1187.
    • (2010) Leuk Lymphoma , vol.51 , pp. 1178-1187
    • Cavaletti, G.1    Jakubowiak, A.J.2
  • 32
    • 84993814033 scopus 로고    scopus 로고
    • Safety and efficacy of subcutaneous formulation of bortezomib versus the conventional intravenous formulation in multiple myeloma
    • Mateos M.V., San Miguel J.F. Safety and efficacy of subcutaneous formulation of bortezomib versus the conventional intravenous formulation in multiple myeloma. Ther Adv Hematol 2012, 3:117-124.
    • (2012) Ther Adv Hematol , vol.3 , pp. 117-124
    • Mateos, M.V.1    San Miguel, J.F.2
  • 33
    • 84872806944 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic and covariate analysis of subcutaneous versus intravenous administration of bortezomib in patients with relapsed multiple myeloma
    • Moreau P., Karamanesht I.I., Domnikova N., et al. Pharmacokinetic, pharmacodynamic and covariate analysis of subcutaneous versus intravenous administration of bortezomib in patients with relapsed multiple myeloma. Clin Pharmacokinet 2012, 51:823-829.
    • (2012) Clin Pharmacokinet , vol.51 , pp. 823-829
    • Moreau, P.1    Karamanesht, I.I.2    Domnikova, N.3
  • 34
    • 84887616117 scopus 로고    scopus 로고
    • The efficacy and safety analysis of bortezomib retreatment in 76 patients with relapsed/refractory multiple myeloma
    • Lu J., Hou J., Zhang C.Y., et al. The efficacy and safety analysis of bortezomib retreatment in 76 patients with relapsed/refractory multiple myeloma. Zhonghua Xue Ye Xue Za Zhi 2013, 34:309-312.
    • (2013) Zhonghua Xue Ye Xue Za Zhi , vol.34 , pp. 309-312
    • Lu, J.1    Hou, J.2    Zhang, C.Y.3
  • 35
    • 84873990173 scopus 로고    scopus 로고
    • A prospective, international phase 2 study of bortezomib retreatment in patients with relapsed multiple myeloma
    • Petrucci M.T., Giraldo P., Corradini P., et al. A prospective, international phase 2 study of bortezomib retreatment in patients with relapsed multiple myeloma. Br J Haematol 2013, 160:649-659.
    • (2013) Br J Haematol , vol.160 , pp. 649-659
    • Petrucci, M.T.1    Giraldo, P.2    Corradini, P.3
  • 36
    • 84860749854 scopus 로고    scopus 로고
    • Effective response with bortezomib retreatment in relapsed multiple myeloma-a multicentre retrospective survey in Switzerland
    • Taverna C., Voegeli J., Trojan A., Olie R.A., von Rohr A. Effective response with bortezomib retreatment in relapsed multiple myeloma-a multicentre retrospective survey in Switzerland. Swiss Med Wkly 2012, 142:w13562.
    • (2012) Swiss Med Wkly , vol.142
    • Taverna, C.1    Voegeli, J.2    Trojan, A.3    Olie, R.A.4    von Rohr, A.5
  • 37
    • 58149235237 scopus 로고    scopus 로고
    • Utility of bortezomib retreatment in relapsed or refractory multiple myeloma patients: a multicenter case series
    • Wolf J., Richardson P.G., Schuster M., LeBlanc A., Walters I.B., Battleman D.S. Utility of bortezomib retreatment in relapsed or refractory multiple myeloma patients: a multicenter case series. Clin Adv Hematol Oncol 2008, 6:755-760.
    • (2008) Clin Adv Hematol Oncol , vol.6 , pp. 755-760
    • Wolf, J.1    Richardson, P.G.2    Schuster, M.3    LeBlanc, A.4    Walters, I.B.5    Battleman, D.S.6
  • 38
    • 34848870352 scopus 로고    scopus 로고
    • Bortezomib for the treatment of mantle cell lymphoma
    • Kane R.C., Dagher R., Farrell A., et al. Bortezomib for the treatment of mantle cell lymphoma. Clin Cancer Res 2007, 13:5291-5294.
    • (2007) Clin Cancer Res , vol.13 , pp. 5291-5294
    • Kane, R.C.1    Dagher, R.2    Farrell, A.3
  • 39
    • 84875693885 scopus 로고    scopus 로고
    • Bortezomib added to daunorubicin and cytarabine during induction therapy and to intermediate-dose cytarabine for consolidation in patients with previously untreated acute myeloid leukemia age 60 to 75years: CALGB (Alliance) study 10502
    • Attar E.C., Johnson J.L., Amrein P.C., et al. Bortezomib added to daunorubicin and cytarabine during induction therapy and to intermediate-dose cytarabine for consolidation in patients with previously untreated acute myeloid leukemia age 60 to 75years: CALGB (Alliance) study 10502. J Clin Oncol 2013, 31:923-929.
    • (2013) J Clin Oncol , vol.31 , pp. 923-929
    • Attar, E.C.1    Johnson, J.L.2    Amrein, P.C.3
  • 40
    • 84880944427 scopus 로고    scopus 로고
    • Phase I dose escalation study of bortezomib in combination with lenalidomide in patients with myelodysplastic syndromes (MDS) and acute myeloid leukemia (AML)
    • Attar E.C., Amrein P.C., Fraser J.W., et al. Phase I dose escalation study of bortezomib in combination with lenalidomide in patients with myelodysplastic syndromes (MDS) and acute myeloid leukemia (AML). Leuk Res 2013, 37:1016-1020.
    • (2013) Leuk Res , vol.37 , pp. 1016-1020
    • Attar, E.C.1    Amrein, P.C.2    Fraser, J.W.3
  • 41
    • 84862726260 scopus 로고    scopus 로고
    • Clinical and pharmacodynamic activity of bortezomib and decitabine in acute myeloid leukemia
    • Blum W., Schwind S., Tarighat S.S., et al. Clinical and pharmacodynamic activity of bortezomib and decitabine in acute myeloid leukemia. Blood 2012, 119:6025-6031.
    • (2012) Blood , vol.119 , pp. 6025-6031
    • Blum, W.1    Schwind, S.2    Tarighat, S.S.3
  • 42
    • 84864045203 scopus 로고    scopus 로고
    • Bortezomib with chemotherapy is highly active in advanced B-precursor acute lymphoblastic leukemia: Therapeutic Advances in Childhood Leukemia & Lymphoma (TACL) Study
    • Messinger Y.H., Gaynon P.S., Sposto R., et al. Bortezomib with chemotherapy is highly active in advanced B-precursor acute lymphoblastic leukemia: Therapeutic Advances in Childhood Leukemia & Lymphoma (TACL) Study. Blood 2012, 120:285-290.
    • (2012) Blood , vol.120 , pp. 285-290
    • Messinger, Y.H.1    Gaynon, P.S.2    Sposto, R.3
  • 43
    • 84901301291 scopus 로고    scopus 로고
    • Phase I study of azacitidine and bortezomib in adults with relapsed or refractory acute myeloid leukemia
    • Walker A.R., Klisovic R.B., Garzon R., et al. Phase I study of azacitidine and bortezomib in adults with relapsed or refractory acute myeloid leukemia. Leuk Lymphoma 2013, 10.3109/10428194.2013.833333.
    • (2013) Leuk Lymphoma
    • Walker, A.R.1    Klisovic, R.B.2    Garzon, R.3
  • 44
    • 84884209657 scopus 로고    scopus 로고
    • Effects of bortezomib on the immune system: a focus on immune regulation
    • Mohty M., Brissot E., Savani B.N., Gaugler B. Effects of bortezomib on the immune system: a focus on immune regulation. Biol Blood Marrow Transplant 2013, 19:1416-1420.
    • (2013) Biol Blood Marrow Transplant , vol.19 , pp. 1416-1420
    • Mohty, M.1    Brissot, E.2    Savani, B.N.3    Gaugler, B.4
  • 45
    • 9644262422 scopus 로고    scopus 로고
    • Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach
    • Groll M., Huber R. Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach. Biochim Biophys Acta 2004, 1695:33-44.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 33-44
    • Groll, M.1    Huber, R.2
  • 46
    • 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 D.J., Chen Q., Voorhees P.M., et al. Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma. Blood 2007, 110:3281-3290.
    • (2007) Blood , vol.110 , pp. 3281-3290
    • Kuhn, D.J.1    Chen, Q.2    Voorhees, P.M.3
  • 47
    • 34447116376 scopus 로고    scopus 로고
    • Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome
    • Demo S.D., Kirk C.J., Aujay M.A., et al. Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. Cancer Res 2007, 67:6383-6391.
    • (2007) Cancer Res , vol.67 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Aujay, M.A.3
  • 48
    • 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 O.A., Stewart A.K., 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, 15:7085-7091.
    • (2009) Clin Cancer Res , vol.15 , pp. 7085-7091
    • O'Connor, O.A.1    Stewart, A.K.2    Vallone, M.3
  • 49
    • 79956042305 scopus 로고    scopus 로고
    • Alkaline phosphatase variation during carfilzomib treatment is associated with best response in multiple myeloma patients
    • Zangari M., Aujay M., Zhan F., et al. Alkaline phosphatase variation during carfilzomib treatment is associated with best response in multiple myeloma patients. Eur J Haematol 2011, 86:484-487.
    • (2011) Eur J Haematol , vol.86 , pp. 484-487
    • Zangari, M.1    Aujay, M.2    Zhan, F.3
  • 50
    • 84865552564 scopus 로고    scopus 로고
    • An open-label, single-arm, phase 2 study of single-agent carfilzomib in patients with relapsed and/or refractory multiple myeloma who have been previously treated with bortezomib
    • Vij R., Siegel D.S., Jagannath S., et al. An open-label, single-arm, phase 2 study of single-agent carfilzomib in patients with relapsed and/or refractory multiple myeloma who have been previously treated with bortezomib. Br J Haematol 2012, 158:739-748.
    • (2012) Br J Haematol , vol.158 , pp. 739-748
    • Vij, R.1    Siegel, D.S.2    Jagannath, S.3
  • 51
    • 84867427641 scopus 로고    scopus 로고
    • An open-label single-arm pilot phase II study (PX-171-003-A0) of low-dose, single-agent carfilzomib in patients with relapsed and refractory multiple myeloma
    • Jagannath S., Vij R., Stewart A.K., et al. An open-label single-arm pilot phase II study (PX-171-003-A0) of low-dose, single-agent carfilzomib in patients with relapsed and refractory multiple myeloma. Clin Lymphoma Myeloma Leuk 2012, 12:310-318.
    • (2012) Clin Lymphoma Myeloma Leuk , vol.12 , pp. 310-318
    • Jagannath, S.1    Vij, R.2    Stewart, A.K.3
  • 52
    • 84877089105 scopus 로고    scopus 로고
    • Phase Ib dose-escalation study (PX-171-006) of carfilzomib, lenalidomide, and low-dose dexamethasone in relapsed or progressive multiple myeloma
    • Niesvizky R., Martin T.G., Bensinger W.I., et al. Phase Ib dose-escalation study (PX-171-006) of carfilzomib, lenalidomide, and low-dose dexamethasone in relapsed or progressive multiple myeloma. Clin Cancer Res 2013, 19:2248-2256.
    • (2013) Clin Cancer Res , vol.19 , pp. 2248-2256
    • Niesvizky, R.1    Martin, T.G.2    Bensinger, W.I.3
  • 53
    • 84867295563 scopus 로고    scopus 로고
    • A phase 2 study of single-agent carfilzomib (PX-171-003-A1) in patients with relapsed and refractory multiple myeloma
    • Siegel D.S., Martin T., Wang M., et al. A phase 2 study of single-agent carfilzomib (PX-171-003-A1) in patients with relapsed and refractory multiple myeloma. Blood 2012, 120:2817-2825.
    • (2012) Blood , vol.120 , pp. 2817-2825
    • Siegel, D.S.1    Martin, T.2    Wang, M.3
  • 54
    • 84887007753 scopus 로고    scopus 로고
    • Integrated safety profile of single-agent carfilzomib: experience from 526 patients enrolled in 4 phase 2 clinical studies
    • Siegel D., Martin T., Nooka A., et al. Integrated safety profile of single-agent carfilzomib: experience from 526 patients enrolled in 4 phase 2 clinical studies. Haematologica 2013, 10.3324/haematol.2013.089334.
    • (2013) Haematologica
    • Siegel, D.1    Martin, T.2    Nooka, A.3
  • 55
    • 84883472160 scopus 로고    scopus 로고
    • U.S. Food and Drug Administration approval: carfilzomib for the treatment of multiple myeloma
    • Herndon T.M., Deisseroth A., Kaminskas E., et al. U.S. Food and Drug Administration approval: carfilzomib for the treatment of multiple myeloma. Clin Cancer Res 2013, 19:4559-4563.
    • (2013) Clin Cancer Res , vol.19 , pp. 4559-4563
    • Herndon, T.M.1    Deisseroth, A.2    Kaminskas, E.3
  • 56
    • 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
  • 57
    • 80051691845 scopus 로고    scopus 로고
    • In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells
    • Chauhan D., Tian Z., Zhou B., et al. In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells. Clin Cancer Res 2011, 17:5311-5321.
    • (2011) Clin Cancer Res , vol.17 , pp. 5311-5321
    • Chauhan, D.1    Tian, Z.2    Zhou, B.3
  • 58
    • 82555189384 scopus 로고    scopus 로고
    • Antitumor activity of the investigational proteasome inhibitor MLN9708 in mouse models of B-cell and plasma cell malignancies
    • Lee E.C., Fitzgerald M., Bannerman B., et al. Antitumor activity of the investigational proteasome inhibitor MLN9708 in mouse models of B-cell and plasma cell malignancies. Clin Cancer Res 2011, 17:7313-7323.
    • (2011) Clin Cancer Res , vol.17 , pp. 7313-7323
    • Lee, E.C.1    Fitzgerald, M.2    Bannerman, B.3
  • 59
    • 20044397059 scopus 로고    scopus 로고
    • Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor
    • Macherla V.R., Mitchell S.S., Manam R.R., et al. Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor. J Med Chem 2005, 48:3684-3687.
    • (2005) J Med Chem , vol.48 , pp. 3684-3687
    • Macherla, V.R.1    Mitchell, S.S.2    Manam, R.R.3
  • 60
    • 27644562277 scopus 로고    scopus 로고
    • A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from bortezomib
    • Chauhan D., Catley L., Li G., et al. A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from bortezomib. Cancer Cell 2005, 8:407-419.
    • (2005) Cancer Cell , vol.8 , pp. 407-419
    • Chauhan, D.1    Catley, L.2    Li, G.3
  • 61
    • 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 A.V., Palladino M.A., Lloyd G.K., Potts B.C., Chauhan D., Anderson K.C. Pharmacodynamic and efficacy studies of the novel proteasome inhibitor NPI-0052 (marizomib) in a human plasmacytoma xenograft murine model. Br J Haematol 2010, 149:550-559.
    • (2010) Br J Haematol , vol.149 , 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
  • 62
    • 38949125853 scopus 로고    scopus 로고
    • Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma
    • Chauhan D., Singh A., Brahmandam M., et al. Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma. Blood 2008, 111:1654-1664.
    • (2008) Blood , vol.111 , pp. 1654-1664
    • Chauhan, D.1    Singh, A.2    Brahmandam, M.3
  • 63
    • 77949315484 scopus 로고    scopus 로고
    • Combination of novel proteasome inhibitor NPI-0052 and lenalidomide trigger in vitro and in vivo synergistic cytotoxicity in multiple myeloma
    • Chauhan D., Singh A.V., Ciccarelli B., Richardson P.G., Palladino M.A., Anderson K.C. Combination of novel proteasome inhibitor NPI-0052 and lenalidomide trigger in vitro and in vivo synergistic cytotoxicity in multiple myeloma. Blood 2010, 115:834-845.
    • (2010) Blood , vol.115 , pp. 834-845
    • Chauhan, D.1    Singh, A.V.2    Ciccarelli, B.3    Richardson, P.G.4    Palladino, M.A.5    Anderson, K.C.6
  • 64
    • 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, 111:2765-2775.
    • (2008) Blood , vol.111 , pp. 2765-2775
    • Piva, R.1    Ruggeri, B.2    Williams, M.3
  • 65
    • 39749143840 scopus 로고    scopus 로고
    • Discovery of a potent, selective, and orally active proteasome inhibitor for the treatment of cancer
    • Dorsey B.D., Iqbal M., Chatterjee S., et al. Discovery of a potent, selective, and orally active proteasome inhibitor for the treatment of cancer. J Med Chem 2008, 51:1068-1072.
    • (2008) J Med Chem , vol.51 , pp. 1068-1072
    • Dorsey, B.D.1    Iqbal, M.2    Chatterjee, S.3
  • 66
    • 75149157969 scopus 로고    scopus 로고
    • The proteasome inhibitor CEP-18770 enhances the anti-myeloma activity of bortezomib and melphalan
    • Sanchez E., Li M., Steinberg J.A., et al. The proteasome inhibitor CEP-18770 enhances the anti-myeloma activity of bortezomib and melphalan. Br J Haematol 2010, 148:569-581.
    • (2010) Br J Haematol , vol.148 , pp. 569-581
    • Sanchez, E.1    Li, M.2    Steinberg, J.A.3
  • 67
    • 84872109533 scopus 로고    scopus 로고
    • A first in human phase I study of the proteasome inhibitor CEP-18770 in patients with advanced solid tumours and multiple myeloma
    • Gallerani E., Zucchetti M., Brunelli D., et al. A first in human phase I study of the proteasome inhibitor CEP-18770 in patients with advanced solid tumours and multiple myeloma. Eur J Cancer 2013, 49:290-296.
    • (2013) Eur J Cancer , vol.49 , pp. 290-296
    • Gallerani, E.1    Zucchetti, M.2    Brunelli, D.3
  • 68
    • 65649139708 scopus 로고    scopus 로고
    • Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR-047)
    • Zhou H.J., Aujay M.A., Bennett M.K., et al. Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR-047). J Med Chem 2009, 52:3028-3038.
    • (2009) J Med Chem , vol.52 , pp. 3028-3038
    • Zhou, H.J.1    Aujay, M.A.2    Bennett, M.K.3
  • 69
    • 77953264178 scopus 로고    scopus 로고
    • Selective inhibition of chymotrypsin-like activity of the immunoproteasome and constitutive proteasome in Waldenstrom macroglobulinemia
    • Roccaro A.M., Sacco A., Aujay M., et al. Selective inhibition of chymotrypsin-like activity of the immunoproteasome and constitutive proteasome in Waldenstrom macroglobulinemia. Blood 2010, 115:4051-4060.
    • (2010) Blood , vol.115 , pp. 4051-4060
    • Roccaro, A.M.1    Sacco, A.2    Aujay, M.3
  • 70
    • 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 A.V., Aujay M., et al. A novel orally active proteasome inhibitor ONX 0912 triggers in vitro and in vivo cytotoxicity in multiple myeloma. Blood 2010, 116:4906-4915.
    • (2010) Blood , vol.116 , pp. 4906-4915
    • Chauhan, D.1    Singh, A.V.2    Aujay, M.3
  • 71
    • 38749115417 scopus 로고    scopus 로고
    • Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits
    • Busse A., Kraus M., Na I.K., et al. Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits. Cancer 2008, 112:659-670.
    • (2008) Cancer , vol.112 , pp. 659-670
    • Busse, A.1    Kraus, M.2    Na, I.K.3
  • 72
    • 84887608620 scopus 로고    scopus 로고
    • Higher ratio immune vs. constitutive proteasome level as novel indicator of sensitivity of pediatric acute leukemia cells to proteasome inhibitors
    • Niewerth D., Franke N.E., Jansen G., et al. Higher ratio immune vs. constitutive proteasome level as novel indicator of sensitivity of pediatric acute leukemia cells to proteasome inhibitors. Haematologica 2013, 10.3324/haematol.2013.092411.
    • (2013) Haematologica
    • Niewerth, D.1    Franke, N.E.2    Jansen, G.3
  • 73
    • 78650348146 scopus 로고    scopus 로고
    • PR-924, a selective inhibitor of the immunoproteasome subunit LMP-7, blocks multiple myeloma cell growth both in vitro and in vivo
    • Singh A.V., Bandi M., Aujay M.A., et al. PR-924, a selective inhibitor of the immunoproteasome subunit LMP-7, blocks multiple myeloma cell growth both in vitro and in vivo. Br J Haematol 2011, 152:155-163.
    • (2011) Br J Haematol , vol.152 , pp. 155-163
    • Singh, A.V.1    Bandi, M.2    Aujay, M.A.3
  • 74
    • 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., Voorhees P.M., Orlowski M., Orlowski R.Z. 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    Voorhees, P.M.4    Orlowski, M.5    Orlowski, R.Z.6
  • 75
    • 77950421253 scopus 로고    scopus 로고
    • The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma
    • Xu G.W., Ali M., Wood T.E., et al. The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma. Blood 2010, 115:2251-2259.
    • (2010) Blood , vol.115 , pp. 2251-2259
    • Xu, G.W.1    Ali, M.2    Wood, T.E.3
  • 76
    • 34548188010 scopus 로고    scopus 로고
    • UBE1L2, a novel E1 enzyme specific for ubiquitin
    • Pelzer C., Kassner I., Matentzoglu K., et al. UBE1L2, a novel E1 enzyme specific for ubiquitin. J Biol Chem 2007, 282:23010-23014.
    • (2007) J Biol Chem , vol.282 , pp. 23010-23014
    • Pelzer, C.1    Kassner, I.2    Matentzoglu, K.3
  • 77
    • 35148886143 scopus 로고    scopus 로고
    • Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics
    • Yang Y., Kitagaki J., Dai R.M., et al. Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics. Cancer Res 2007, 67:9472-9481.
    • (2007) Cancer Res , vol.67 , pp. 9472-9481
    • Yang, Y.1    Kitagaki, J.2    Dai, R.M.3
  • 78
    • 84858978749 scopus 로고    scopus 로고
    • Identification and mechanistic studies of a novel ubiquitin E1 inhibitor
    • Ungermannova D., Parker S.J., Nasveschuk C.G., et al. Identification and mechanistic studies of a novel ubiquitin E1 inhibitor. J Biomol Screen 2012, 17:421-434.
    • (2012) J Biomol Screen , vol.17 , pp. 421-434
    • Ungermannova, D.1    Parker, S.J.2    Nasveschuk, C.G.3
  • 79
    • 84862269352 scopus 로고    scopus 로고
    • Initial testing of the investigational NEDD8-activating enzyme inhibitor MLN4924 by the pediatric preclinical testing program
    • Smith M.A., Maris J.M., Gorlick R., et al. Initial testing of the investigational NEDD8-activating enzyme inhibitor MLN4924 by the pediatric preclinical testing program. Pediatr Blood Cancer 2012, 59:246-253.
    • (2012) Pediatr Blood Cancer , vol.59 , pp. 246-253
    • Smith, M.A.1    Maris, J.M.2    Gorlick, R.3
  • 80
    • 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 M.A., 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, 116:1515-1523.
    • (2010) Blood , vol.116 , pp. 1515-1523
    • Milhollen, M.A.1    Traore, T.2    Adams-Duffy, J.3
  • 81
    • 77952558703 scopus 로고    scopus 로고
    • Inhibition of NEDD8-activating enzyme: a novel approach for the treatment of acute myeloid leukemia
    • Swords R.T., Kelly K.R., Smith P.G., et al. Inhibition of NEDD8-activating enzyme: a novel approach for the treatment of acute myeloid leukemia. Blood 2010, 115:3796-3800.
    • (2010) Blood , vol.115 , pp. 3796-3800
    • Swords, R.T.1    Kelly, K.R.2    Smith, P.G.3
  • 82
    • 84862637714 scopus 로고    scopus 로고
    • Molecular and cellular effects of NEDD8-activating enzyme inhibition in myeloma
    • McMillin D.W., Jacobs H.M., Delmore J.E., et al. Molecular and cellular effects of NEDD8-activating enzyme inhibition in myeloma. Mol Cancer Ther 2012, 11:942-951.
    • (2012) Mol Cancer Ther , vol.11 , pp. 942-951
    • McMillin, D.W.1    Jacobs, H.M.2    Delmore, J.E.3
  • 83
    • 77950579617 scopus 로고    scopus 로고
    • The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines
    • David Y., Ziv T., Admon A., Navon A. The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem 2010, 285:8595-8604.
    • (2010) J Biol Chem , vol.285 , pp. 8595-8604
    • David, Y.1    Ziv, T.2    Admon, A.3    Navon, A.4
  • 84
    • 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, 23:3597-3602.
    • (2004) Oncogene , vol.23 , pp. 3597-3602
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 85
    • 0034890050 scopus 로고    scopus 로고
    • Expression and localization of the CDC34 ubiquitin-conjugating enzyme in pediatric acute lymphoblastic leukemia
    • Eliseeva E., Pati D., Diccinanni M.B., et al. Expression and localization of the CDC34 ubiquitin-conjugating enzyme in pediatric acute lymphoblastic leukemia. Cell Growth Differ 2001, 12:427-433.
    • (2001) Cell Growth Differ , vol.12 , pp. 427-433
    • Eliseeva, E.1    Pati, D.2    Diccinanni, M.B.3
  • 86
    • 79959656754 scopus 로고    scopus 로고
    • An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme
    • Ceccarelli D.F., Tang X., Pelletier B., et al. An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme. Cell 2011, 145:1075-1087.
    • (2011) Cell , vol.145 , pp. 1075-1087
    • Ceccarelli, D.F.1    Tang, X.2    Pelletier, B.3
  • 87
    • 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, 120:1668-1677.
    • (2012) Blood , vol.120 , pp. 1668-1677
    • Pulvino, M.1    Liang, Y.2    Oleksyn, D.3
  • 88
    • 77957891990 scopus 로고    scopus 로고
    • In vitro transformation of primary human CD34+ cells by AML fusion oncogenes: early gene expression profiling reveals possible drug target in AML
    • Abdul-Nabi A.M., Yassin E.R., Varghese N., Deshmukh H., Yaseen N.R. In vitro transformation of primary human CD34+ cells by AML fusion oncogenes: early gene expression profiling reveals possible drug target in AML. PLoS One 2010, 5:e12464.
    • (2010) PLoS One , vol.5
    • Abdul-Nabi, A.M.1    Yassin, E.R.2    Varghese, N.3    Deshmukh, H.4    Yaseen, N.R.5
  • 89
    • 71049193131 scopus 로고    scopus 로고
    • Frequency and prognostic significance of murine double minute protein-2 overexpression and p53 gene mutations in childhood acute lymphoblastic leukemia
    • Hendy O.M., Elghannam D.M., El-Sharnouby J.A., Goda E.F., El-Ashry R., Al-Tonbary Y. Frequency and prognostic significance of murine double minute protein-2 overexpression and p53 gene mutations in childhood acute lymphoblastic leukemia. Hematology 2009, 14:335-340.
    • (2009) Hematology , vol.14 , pp. 335-340
    • Hendy, O.M.1    Elghannam, D.M.2    El-Sharnouby, J.A.3    Goda, E.F.4    El-Ashry, R.5    Al-Tonbary, Y.6
  • 90
    • 84891606259 scopus 로고    scopus 로고
    • MDM2 phenotypic and genotypic profiling, respective to TP53 genetic status, in diffuse large B-cell lymphoma patients treated with rituximab-CHOP immunochemotherapy
    • Xu-Monette Z.Y., Moller M.B., Tzankov A., et al. MDM2 phenotypic and genotypic profiling, respective to TP53 genetic status, in diffuse large B-cell lymphoma patients treated with rituximab-CHOP immunochemotherapy. Blood 2013, 10.1182/blood-2012-12-473702.
    • (2013) Blood
    • Xu-Monette, Z.Y.1    Moller, M.B.2    Tzankov, A.3
  • 91
    • 77649274289 scopus 로고    scopus 로고
    • HDM4 is overexpressed in mantle cell lymphoma and its inhibition induces p21 expression and apoptosis
    • Liang M., Han X., Vadhan-Raj S., et al. HDM4 is overexpressed in mantle cell lymphoma and its inhibition induces p21 expression and apoptosis. Mod Pathol 2010, 23:381-391.
    • (2010) Mod Pathol , vol.23 , pp. 381-391
    • Liang, M.1    Han, X.2    Vadhan-Raj, S.3
  • 92
    • 0030921866 scopus 로고    scopus 로고
    • MDM2 protein overexpression promotes proliferation and survival of multiple myeloma cells
    • Teoh G., Urashima M., Ogata A., et al. MDM2 protein overexpression promotes proliferation and survival of multiple myeloma cells. Blood 1997, 90:1982-1992.
    • (1997) Blood , vol.90 , pp. 1982-1992
    • Teoh, G.1    Urashima, M.2    Ogata, A.3
  • 93
    • 84875359668 scopus 로고    scopus 로고
    • Targeting p53 by small molecules in haematological malignancies
    • (23-8722-6-23)
    • Saha M.N., Qiu L., Chang H. Targeting p53 by small molecules in haematological malignancies. J Hematol Oncol 2013, 6. (23-8722-6-23).
    • (2013) J Hematol Oncol , vol.6
    • Saha, M.N.1    Qiu, L.2    Chang, H.3
  • 94
    • 79955799680 scopus 로고    scopus 로고
    • Activation of the p53 pathway by the MDM2 inhibitor nutlin-3a overcomes BCL2 overexpression in a preclinical model of diffuse large B-cell lymphoma associated with t(14;18)(q32;q21)
    • Drakos E., Singh R.R., Rassidakis G.Z., et al. Activation of the p53 pathway by the MDM2 inhibitor nutlin-3a overcomes BCL2 overexpression in a preclinical model of diffuse large B-cell lymphoma associated with t(14;18)(q32;q21). Leukemia 2011, 25:856-867.
    • (2011) Leukemia , vol.25 , pp. 856-867
    • Drakos, E.1    Singh, R.R.2    Rassidakis, G.Z.3
  • 95
    • 84859782521 scopus 로고    scopus 로고
    • MDM2 inhibitor nutlin-3a induces apoptosis and senescence in cutaneous T-cell lymphoma: role of p53
    • Manfe V., Biskup E., Johansen P., et al. MDM2 inhibitor nutlin-3a induces apoptosis and senescence in cutaneous T-cell lymphoma: role of p53. J Invest Dermatol 2012, 132:1487-1496.
    • (2012) J Invest Dermatol , vol.132 , pp. 1487-1496
    • Manfe, V.1    Biskup, E.2    Johansen, P.3
  • 96
    • 77957174185 scopus 로고    scopus 로고
    • Molecular mechanisms of nutlin-induced apoptosis in multiple myeloma: evidence for p53-transcription-dependent and -independent pathways
    • Saha M.N., Jiang H., Chang H. Molecular mechanisms of nutlin-induced apoptosis in multiple myeloma: evidence for p53-transcription-dependent and -independent pathways. Cancer Biol Ther 2010, 10:567-578.
    • (2010) Cancer Biol Ther , vol.10 , pp. 567-578
    • Saha, M.N.1    Jiang, H.2    Chang, H.3
  • 97
    • 84873710768 scopus 로고    scopus 로고
    • Initial testing of the MDM2 inhibitor RG7112 by the Pediatric Preclinical Testing Program
    • Carol H., Reynolds C.P., Kang M.H., et al. Initial testing of the MDM2 inhibitor RG7112 by the Pediatric Preclinical Testing Program. Pediatr Blood Cancer 2013, 60:633-641.
    • (2013) Pediatr Blood Cancer , vol.60 , pp. 633-641
    • Carol, H.1    Reynolds, C.P.2    Kang, M.H.3
  • 98
    • 77956563054 scopus 로고    scopus 로고
    • The novel tryptamine derivative JNJ-26854165 induces wild-type p53- and E2F1-mediated apoptosis in acute myeloid and lymphoid leukemias
    • Kojima K., Burks J.K., Arts J., Andreeff M. The novel tryptamine derivative JNJ-26854165 induces wild-type p53- and E2F1-mediated apoptosis in acute myeloid and lymphoid leukemias. Mol Cancer Ther 2010, 9:2545-2557.
    • (2010) Mol Cancer Ther , vol.9 , pp. 2545-2557
    • Kojima, K.1    Burks, J.K.2    Arts, J.3    Andreeff, M.4
  • 99
    • 53049095963 scopus 로고    scopus 로고
    • Inhibition of the p53 E3 ligase HDM-2 induces apoptosis and DNA damage-independent p53 phosphorylation in mantle cell lymphoma
    • Jones R.J., Chen Q., Voorhees P.M., et al. Inhibition of the p53 E3 ligase HDM-2 induces apoptosis and DNA damage-independent p53 phosphorylation in mantle cell lymphoma. Clin Cancer Res 2008, 14:5416-5425.
    • (2008) Clin Cancer Res , vol.14 , pp. 5416-5425
    • Jones, R.J.1    Chen, Q.2    Voorhees, P.M.3
  • 100
    • 80054105519 scopus 로고    scopus 로고
    • HDM-2 inhibition suppresses expression of ribonucleotide reductase subunit M2, and synergistically enhances gemcitabine-induced cytotoxicity in mantle cell lymphoma
    • Jones R.J., Baladandayuthapani V., Neelapu S., et al. HDM-2 inhibition suppresses expression of ribonucleotide reductase subunit M2, and synergistically enhances gemcitabine-induced cytotoxicity in mantle cell lymphoma. Blood 2011, 118:4140-4149.
    • (2011) Blood , vol.118 , pp. 4140-4149
    • Jones, R.J.1    Baladandayuthapani, V.2    Neelapu, S.3
  • 101
    • 84866270528 scopus 로고    scopus 로고
    • HDM2 antagonist MI-219 (spiro-oxindole), but not Nutlin-3 (cis-imidazoline), regulates p53 through enhanced HDM2 autoubiquitination and degradation in human malignant B-cell lymphomas
    • Sosin A.M., Burger A.M., Siddiqi A., Abrams J., Mohammad R.M., Al-Katib A.M. HDM2 antagonist MI-219 (spiro-oxindole), but not Nutlin-3 (cis-imidazoline), regulates p53 through enhanced HDM2 autoubiquitination and degradation in human malignant B-cell lymphomas. J Hematol Oncol 2012, 5:57.
    • (2012) J Hematol Oncol , vol.5 , pp. 57
    • Sosin, A.M.1    Burger, A.M.2    Siddiqi, A.3    Abrams, J.4    Mohammad, R.M.5    Al-Katib, A.M.6
  • 102
    • 62549108186 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins in haematological malignancies
    • Fulda S. Inhibitor of apoptosis proteins in haematological malignancies. Leukemia 2009, 23:467-476.
    • (2009) Leukemia , vol.23 , pp. 467-476
    • Fulda, S.1
  • 103
    • 1542608418 scopus 로고    scopus 로고
    • Inhibition of survivin expression suppresses the growth of aggressive non-Hodgkin's lymphoma
    • Ansell S.M., Arendt B.K., Grote D.M., et al. Inhibition of survivin expression suppresses the growth of aggressive non-Hodgkin's lymphoma. Leukemia 2004, 18:616-623.
    • (2004) Leukemia , vol.18 , pp. 616-623
    • Ansell, S.M.1    Arendt, B.K.2    Grote, D.M.3
  • 104
    • 84863154799 scopus 로고    scopus 로고
    • Initial testing (stage 1) of LCL161, a SMAC mimetic, by the Pediatric Preclinical Testing Program
    • Houghton P.J., Kang M.H., Reynolds C.P., et al. Initial testing (stage 1) of LCL161, a SMAC mimetic, by the Pediatric Preclinical Testing Program. Pediatr Blood Cancer 2012, 58:636-639.
    • (2012) Pediatr Blood Cancer , vol.58 , pp. 636-639
    • Houghton, P.J.1    Kang, M.H.2    Reynolds, C.P.3
  • 105
    • 84862776560 scopus 로고    scopus 로고
    • The Smac mimetic RMT5265.2HCL induces apoptosis in EBV and HTLV-I associated lymphoma cells by inhibiting XIAP and promoting the mitochondrial release of cytochrome C and Smac
    • Ramachandiran S., Cain J., Liao A., et al. The Smac mimetic RMT5265.2HCL induces apoptosis in EBV and HTLV-I associated lymphoma cells by inhibiting XIAP and promoting the mitochondrial release of cytochrome C and Smac. Leuk Res 2012, 36:784-790.
    • (2012) Leuk Res , vol.36 , pp. 784-790
    • Ramachandiran, S.1    Cain, J.2    Liao, A.3
  • 106
    • 80755140040 scopus 로고    scopus 로고
    • Deregulated apoptosis signaling in core-binding factor leukemia differentiates clinically relevant, molecular marker-independent subgroups
    • Luck S.C., Russ A.C., Botzenhardt U., et al. Deregulated apoptosis signaling in core-binding factor leukemia differentiates clinically relevant, molecular marker-independent subgroups. Leukemia 2011, 25:1728-1738.
    • (2011) Leukemia , vol.25 , pp. 1728-1738
    • Luck, S.C.1    Russ, A.C.2    Botzenhardt, U.3
  • 107
    • 70350450612 scopus 로고    scopus 로고
    • Phase I/II trial of AEG35156 X-linked inhibitor of apoptosis protein antisense oligonucleotide combined with idarubicin and cytarabine in patients with relapsed or primary refractory acute myeloid leukemia
    • Schimmer A.D., Estey E.H., Borthakur G., et al. Phase I/II trial of AEG35156 X-linked inhibitor of apoptosis protein antisense oligonucleotide combined with idarubicin and cytarabine in patients with relapsed or primary refractory acute myeloid leukemia. J Clin Oncol 2009, 27:4741-4746.
    • (2009) J Clin Oncol , vol.27 , pp. 4741-4746
    • Schimmer, A.D.1    Estey, E.H.2    Borthakur, G.3
  • 108
    • 4143117855 scopus 로고    scopus 로고
    • Elevated S-phase kinase-associated protein 2 protein expression in acute myelogenous leukemia: its association with constitutive phosphorylation of phosphatase and tensin homologue protein and poor prognosis
    • Min Y.H., Cheong J.W., Lee M.H., et al. Elevated S-phase kinase-associated protein 2 protein expression in acute myelogenous leukemia: its association with constitutive phosphorylation of phosphatase and tensin homologue protein and poor prognosis. Clin Cancer Res 2004, 10:5123-5130.
    • (2004) Clin Cancer Res , vol.10 , pp. 5123-5130
    • Min, Y.H.1    Cheong, J.W.2    Lee, M.H.3
  • 109
    • 20244376911 scopus 로고    scopus 로고
    • BCR-ABL induces the expression of Skp2 through the PI3K pathway to promote p27Kip1 degradation and proliferation of chronic myelogenous leukemia cells
    • Andreu E.J., Lledo E., Poch E., et al. BCR-ABL induces the expression of Skp2 through the PI3K pathway to promote p27Kip1 degradation and proliferation of chronic myelogenous leukemia cells. Cancer Res 2005, 65:3264-3272.
    • (2005) Cancer Res , vol.65 , pp. 3264-3272
    • Andreu, E.J.1    Lledo, E.2    Poch, E.3
  • 110
    • 34249652414 scopus 로고    scopus 로고
    • CKS1B, overexpressed in aggressive disease, regulates multiple myeloma growth and survival through SKP2- and p27Kip1-dependent and -independent mechanisms
    • Zhan F., Colla S., Wu X., et al. CKS1B, overexpressed in aggressive disease, regulates multiple myeloma growth and survival through SKP2- and p27Kip1-dependent and -independent mechanisms. Blood 2007, 109:4995-5001.
    • (2007) Blood , vol.109 , pp. 4995-5001
    • Zhan, F.1    Colla, S.2    Wu, X.3
  • 111
    • 47149092405 scopus 로고    scopus 로고
    • Targeting the p27 E3 ligase SCF(Skp2) results in p27- and Skp2-mediated cell-cycle arrest and activation of autophagy
    • Chen Q., Xie W., Kuhn D.J., et al. Targeting the p27 E3 ligase SCF(Skp2) results in p27- and Skp2-mediated cell-cycle arrest and activation of autophagy. Blood 2008, 111:4690-4699.
    • (2008) Blood , vol.111 , pp. 4690-4699
    • Chen, Q.1    Xie, W.2    Kuhn, D.J.3
  • 112
    • 84881192827 scopus 로고    scopus 로고
    • Pharmacological inactivation of Skp2 SCF ubiquitin ligase restricts cancer stem cell traits and cancer progression
    • Chan C.H., Morrow J.K., Li C.F., et al. Pharmacological inactivation of Skp2 SCF ubiquitin ligase restricts cancer stem cell traits and cancer progression. Cell 2013, 154:556-568.
    • (2013) Cell , vol.154 , pp. 556-568
    • Chan, C.H.1    Morrow, J.K.2    Li, C.F.3
  • 113
    • 84886546357 scopus 로고    scopus 로고
    • Inhibitors of SCF-Skp2/Cks1 E3 ligase block estrogen-induced growth stimulation and degradation of nuclear p27kip1: therapeutic potential for endometrial cancer
    • Pavlides S.C., Huang K.T., Reid D.A., et al. Inhibitors of SCF-Skp2/Cks1 E3 ligase block estrogen-induced growth stimulation and degradation of nuclear p27kip1: therapeutic potential for endometrial cancer. Endocrinology 2013, 10.1210/en.2013-1757.
    • (2013) Endocrinology
    • Pavlides, S.C.1    Huang, K.T.2    Reid, D.A.3
  • 114
    • 84882353683 scopus 로고    scopus 로고
    • High-throughput screening AlphaScreen Assay for identification of small-molecule inhibitors of ubiquitin E3 ligase SCFSkp2-Cks1
    • Ungermannova D., Lee J., Zhang G., Dallmann H.G., McHenry C.S., Liu X. High-throughput screening AlphaScreen Assay for identification of small-molecule inhibitors of ubiquitin E3 ligase SCFSkp2-Cks1. J Biomol Screen 2013, 18:910-920.
    • (2013) J Biomol Screen , vol.18 , pp. 910-920
    • Ungermannova, D.1    Lee, J.2    Zhang, G.3    Dallmann, H.G.4    McHenry, C.S.5    Liu, X.6
  • 115
    • 84871569969 scopus 로고    scopus 로고
    • Specific small molecule inhibitors of Skp2-mediated p27 degradation
    • Wu L., Grigoryan A.V., Li Y., Hao B., Pagano M., Cardozo T.J. Specific small molecule inhibitors of Skp2-mediated p27 degradation. Chem Biol 2012, 19:1515-1524.
    • (2012) Chem Biol , vol.19 , pp. 1515-1524
    • Wu, L.1    Grigoryan, A.V.2    Li, Y.3    Hao, B.4    Pagano, M.5    Cardozo, T.J.6
  • 116
    • 45149123052 scopus 로고    scopus 로고
    • Control of hematopoietic stem cell quiescence by the E3 ubiquitin ligase Fbw7
    • Thompson B.J., Jankovic V., Gao J., et al. Control of hematopoietic stem cell quiescence by the E3 ubiquitin ligase Fbw7. J Exp Med 2008, 205:1395-1408.
    • (2008) J Exp Med , vol.205 , pp. 1395-1408
    • Thompson, B.J.1    Jankovic, V.2    Gao, J.3
  • 117
    • 35148842479 scopus 로고    scopus 로고
    • FBXW7/hCDC4 is a general tumor suppressor in human cancer
    • Akhoondi S., Sun D., von der Lehr N., et al. FBXW7/hCDC4 is a general tumor suppressor in human cancer. Cancer Res 2007, 67:9006-9012.
    • (2007) Cancer Res , vol.67 , pp. 9006-9012
    • Akhoondi, S.1    Sun, D.2    von der Lehr, N.3
  • 118
    • 34547820257 scopus 로고    scopus 로고
    • The SCFFBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia
    • Thompson B.J., Buonamici S., Sulis M.L., et al. The SCFFBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia. J Exp Med 2007, 204:1825-1835.
    • (2007) J Exp Med , vol.204 , pp. 1825-1835
    • Thompson, B.J.1    Buonamici, S.2    Sulis, M.L.3
  • 119
    • 34547780475 scopus 로고    scopus 로고
    • FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to gamma-secretase inhibitors
    • O'Neil J., Grim J., Strack P., et al. FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to gamma-secretase inhibitors. J Exp Med 2007, 204:1813-1824.
    • (2007) J Exp Med , vol.204 , pp. 1813-1824
    • O'Neil, J.1    Grim, J.2    Strack, P.3
  • 120
    • 84879364450 scopus 로고    scopus 로고
    • The ubiquitin ligase FBXW7 modulates leukemia-initiating cell activity by regulating MYC stability
    • King B., Trimarchi T., Reavie L., et al. The ubiquitin ligase FBXW7 modulates leukemia-initiating cell activity by regulating MYC stability. Cell 2013, 153:1552-1566.
    • (2013) Cell , vol.153 , pp. 1552-1566
    • King, B.1    Trimarchi, T.2    Reavie, L.3
  • 121
    • 84876434253 scopus 로고    scopus 로고
    • Regulation of c-Myc ubiquitination controls chronic myelogenous leukemia initiation and progression
    • Reavie L., Buckley S.M., Loizou E., et al. Regulation of c-Myc ubiquitination controls chronic myelogenous leukemia initiation and progression. Cancer Cell 2013, 23:362-375.
    • (2013) Cancer Cell , vol.23 , pp. 362-375
    • Reavie, L.1    Buckley, S.M.2    Loizou, E.3
  • 122
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M., Huang X., Lill J.R., et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010, 463:103-107.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3
  • 123
    • 79953072934 scopus 로고    scopus 로고
    • Bcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis
    • Sun H., Kapuria V., Peterson L.F., et al. Bcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis. Blood 2011, 117:3151-3162.
    • (2011) Blood , vol.117 , pp. 3151-3162
    • Sun, H.1    Kapuria, V.2    Peterson, L.F.3
  • 124
    • 76449094879 scopus 로고    scopus 로고
    • The therapeutic potential of deubiquitinating enzyme inhibitors
    • Colland F. The therapeutic potential of deubiquitinating enzyme inhibitors. Biochem Soc Trans 2010, 38:137-143.
    • (2010) Biochem Soc Trans , vol.38 , pp. 137-143
    • Colland, F.1
  • 125
    • 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, 22:345-358.
    • (2012) Cancer Cell , vol.22 , pp. 345-358
    • Chauhan, D.1    Tian, Z.2    Nicholson, B.3
  • 126
    • 84887609779 scopus 로고    scopus 로고
    • Phase 2 dose-expansion study (PX-171-006) of carfilzomib, lenalidomide and low-dose dexamethasone in relapsed or progressive multiple myeloma
    • Wang M., Martin T., Bensinger W., et al. Phase 2 dose-expansion study (PX-171-006) of carfilzomib, lenalidomide and low-dose dexamethasone in relapsed or progressive multiple myeloma. Blood 2013, 10.1182/blood-2013-07-511170.
    • (2013) Blood
    • Wang, M.1    Martin, T.2    Bensinger, W.3
  • 127
    • 84863713771 scopus 로고    scopus 로고
    • Flat-dosing versus BSA-based dosing for MLN9708, an investigational proteasome inhibitor: population pharmacokinetic (PK) analysis of pooled data from 4 Phase-1 studies
    • Gupta N., Saleh M., Venkatakrishna K. Flat-dosing versus BSA-based dosing for MLN9708, an investigational proteasome inhibitor: population pharmacokinetic (PK) analysis of pooled data from 4 Phase-1 studies. Blood 2011, 118:1433.
    • (2011) Blood , vol.118 , pp. 1433
    • Gupta, N.1    Saleh, M.2    Venkatakrishna, K.3
  • 128
    • 84857919694 scopus 로고    scopus 로고
    • Phase 1 clinical evaluation of twice-weekly marizomib (NPI-0052), a novel proteasome inhibitor, in patients with relapsed/refractory multiple myeloma (MM)
    • Richardson P.G., Spencer A., Cannell P., et al. Phase 1 clinical evaluation of twice-weekly marizomib (NPI-0052), a novel proteasome inhibitor, in patients with relapsed/refractory multiple myeloma (MM). Blood 2011, 118:302.
    • (2011) Blood , vol.118 , pp. 302
    • Richardson, P.G.1    Spencer, A.2    Cannell, P.3
  • 129
    • 84886873220 scopus 로고    scopus 로고
    • A Phase 1b dose-escalation study of split-dose oprozomib (ONX0912) in patients with hematologic malignancies
    • Savona M., Berdeja J., Lee S. A Phase 1b dose-escalation study of split-dose oprozomib (ONX0912) in patients with hematologic malignancies. Blood 2012, 120:203.
    • (2012) Blood , vol.120 , pp. 203
    • Savona, M.1    Berdeja, J.2    Lee, S.3


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