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Volumn 21, Issue 6, 2007, Pages 1071-1091

Preclinical Studies of Novel Targeted Therapies

Author keywords

[No Author keywords available]

Indexed keywords

3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [4 (4' CHLORO 2 BIPHENYLYLMETHYL) 1 PIPERAZINYL] N [4 [3 DIMETHYLAMINO 1 (PHENYLTHIOMETHYL)PROPYLAMINO] 3 NITROBENZENESULFONYL]BENZAMIDE; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; ANSAMYCIN DERIVATIVE; ARRY 142886; AZD 6244; BORTEZOMIB; CD20 ANTIGEN; CD40 LIGAND; DEPSIPEPTIDE; DEXAMETHASONE; FIBROBLAST GROWTH FACTOR; FR 901228; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE; INTERLEUKIN 4; IPI 504; KD 5170; LBH 589; LENALIDOMIDE; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; NPI 0052; OBLIMERSEN; PERIFOSINE; PR 171; PROTEASOME INHIBITOR; PROTEIN KINASE B; RAPAMYCIN; TEMSIROLIMUS; TUBACIN; UNCLASSIFIED DRUG; VORINOSTAT; WNT1 PROTEIN;

EID: 35748939416     PISSN: 08898588     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.hoc.2007.08.013     Document Type: Review
Times cited : (21)

References (150)
  • 1
    • 0036884062 scopus 로고    scopus 로고
    • Molecular mechanisms of novel therapeutic approaches for multiple myeloma
    • Hideshima T., and Anderson K.C. Molecular mechanisms of novel therapeutic approaches for multiple myeloma. Nat Rev Cancer 2 (2002) 927-937
    • (2002) Nat Rev Cancer , vol.2 , pp. 927-937
    • Hideshima, T.1    Anderson, K.C.2
  • 2
    • 3242777803 scopus 로고    scopus 로고
    • Advances in biology of multiple myeloma: clinical applications
    • Hideshima T., Bergsagel P.L., Kuehl W.M., et al. Advances in biology of multiple myeloma: clinical applications. Blood 104 (2004) 607-618
    • (2004) Blood , vol.104 , pp. 607-618
    • Hideshima, T.1    Bergsagel, P.L.2    Kuehl, W.M.3
  • 3
    • 34547106018 scopus 로고    scopus 로고
    • Understanding multiple myeloma pathogenesis in the bone marrow to identify new therapeutic targets
    • Hideshima T., Mitsiades C., Tonon G., et al. Understanding multiple myeloma pathogenesis in the bone marrow to identify new therapeutic targets. Nat Rev Cancer 7 (2007) 585-598
    • (2007) Nat Rev Cancer , vol.7 , pp. 585-598
    • Hideshima, T.1    Mitsiades, C.2    Tonon, G.3
  • 4
    • 0028799055 scopus 로고
    • Oncostatin M induces association of Grb2 with Janus kinase JAK2 in multiple myeloma cells
    • Chauhan D., Kharbanda S., Ogata A., et al. Oncostatin M induces association of Grb2 with Janus kinase JAK2 in multiple myeloma cells. J Exp Med 182 (1995) 1801-1806
    • (1995) J Exp Med , vol.182 , pp. 1801-1806
    • Chauhan, D.1    Kharbanda, S.2    Ogata, A.3
  • 5
    • 0032428364 scopus 로고    scopus 로고
    • Interleukin-1 in multiple myeloma: producer cells and their role in the control of IL-6 production
    • Costes V., Portier M., Lu Z.Y., et al. Interleukin-1 in multiple myeloma: producer cells and their role in the control of IL-6 production. Br J Haematol 103 (1998) 1152-1160
    • (1998) Br J Haematol , vol.103 , pp. 1152-1160
    • Costes, V.1    Portier, M.2    Lu, Z.Y.3
  • 6
    • 0033401640 scopus 로고    scopus 로고
    • The role of interleukin-1 beta in the pathogenesis of multiple myeloma
    • Lust J.A., and Donovan K.A. The role of interleukin-1 beta in the pathogenesis of multiple myeloma. Hematol Oncol Clin North Am 13 (1999) 1117-1125
    • (1999) Hematol Oncol Clin North Am , vol.13 , pp. 1117-1125
    • Lust, J.A.1    Donovan, K.A.2
  • 7
    • 0027133422 scopus 로고
    • Adhesion of human myeloma-derived cell lines to bone marrow stromal cells stimulates IL-6 secretion
    • Uchiyama H., Barut B.A., Mohrbacher A.F., et al. Adhesion of human myeloma-derived cell lines to bone marrow stromal cells stimulates IL-6 secretion. Blood 82 (1993) 3712-3720
    • (1993) Blood , vol.82 , pp. 3712-3720
    • Uchiyama, H.1    Barut, B.A.2    Mohrbacher, A.F.3
  • 8
    • 0030041147 scopus 로고    scopus 로고
    • Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NF-kB
    • Chauhan D., Uchiyama H., Akbarali Y., et al. Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NF-kB. Blood 87 (1996) 1104-1112
    • (1996) Blood , vol.87 , pp. 1104-1112
    • Chauhan, D.1    Uchiyama, H.2    Akbarali, Y.3
  • 9
    • 0030026437 scopus 로고    scopus 로고
    • Transforming growth factor b1: Differential effects on multiple myeloma versus normal B cells
    • Urashima M., Ogata A., Chauhan D., et al. Transforming growth factor b1: Differential effects on multiple myeloma versus normal B cells. Blood 87 (1996) 1928-1938
    • (1996) Blood , vol.87 , pp. 1928-1938
    • Urashima, M.1    Ogata, A.2    Chauhan, D.3
  • 10
    • 0034655957 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and interleukin-6 in paracrine tumor-stromal cell interactions in multiple myeloma
    • Dankbar B., Padro T., Leo R., et al. Vascular endothelial growth factor and interleukin-6 in paracrine tumor-stromal cell interactions in multiple myeloma. Blood 95 (2000) 2630-2636
    • (2000) Blood , vol.95 , pp. 2630-2636
    • Dankbar, B.1    Padro, T.2    Leo, R.3
  • 11
    • 0035195019 scopus 로고    scopus 로고
    • Adherence of multiple myeloma cells to bone marrow stromal cells upregulates vascular endothelial growth factor secretion: therapeutic applications
    • Gupta D., Treon S.P., Shima Y., et al. Adherence of multiple myeloma cells to bone marrow stromal cells upregulates vascular endothelial growth factor secretion: therapeutic applications. Leukemia 15 (2001) 1950-1961
    • (2001) Leukemia , vol.15 , pp. 1950-1961
    • Gupta, D.1    Treon, S.P.2    Shima, Y.3
  • 12
    • 0031225483 scopus 로고    scopus 로고
    • Interleukin-6 triggers cell growth via the ras-dependent mitogen-activated protein kinase cascade
    • Ogata A., Chauhan D., Teoh G., et al. Interleukin-6 triggers cell growth via the ras-dependent mitogen-activated protein kinase cascade. J Immunol 159 (1997) 2212-2221
    • (1997) J Immunol , vol.159 , pp. 2212-2221
    • Ogata, A.1    Chauhan, D.2    Teoh, G.3
  • 13
    • 0030948787 scopus 로고    scopus 로고
    • Blockade of mitogen-activated protein kinase cascade signaling in interleukin-6 independent multiple myeloma cells
    • Ogata A., Chauhan D., Urashima M., et al. Blockade of mitogen-activated protein kinase cascade signaling in interleukin-6 independent multiple myeloma cells. Clin Cancer Res 3 (1997) 1017-1022
    • (1997) Clin Cancer Res , vol.3 , pp. 1017-1022
    • Ogata, A.1    Chauhan, D.2    Urashima, M.3
  • 14
    • 34548844157 scopus 로고    scopus 로고
    • Targeting MEK induces myeloma cell cytotoxicity and inhibits osteoclastogenesis
    • Tai Y.T., Fulciniti M., Hideshima T., et al. Targeting MEK induces myeloma cell cytotoxicity and inhibits osteoclastogenesis. Blood 110 (2007) 1656-1663
    • (2007) Blood , vol.110 , pp. 1656-1663
    • Tai, Y.T.1    Fulciniti, M.2    Hideshima, T.3
  • 15
    • 0032984589 scopus 로고    scopus 로고
    • Constitutive activation of STAT-3 signaling confers resistance to apoptosis in human U266 myeloma cells
    • Catlett-Falcone R., Landowski T.H., Oshiro M.M., et al. Constitutive activation of STAT-3 signaling confers resistance to apoptosis in human U266 myeloma cells. Immunity 10 (1999) 105-115
    • (1999) Immunity , vol.10 , pp. 105-115
    • Catlett-Falcone, R.1    Landowski, T.H.2    Oshiro, M.M.3
  • 16
    • 0032711250 scopus 로고    scopus 로고
    • IL-6 up-regulates mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway
    • Puthier D., Bataille R., and Amiot M. IL-6 up-regulates mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway. Eur J Immunol 29 (1999) 3945-3950
    • (1999) Eur J Immunol , vol.29 , pp. 3945-3950
    • Puthier, D.1    Bataille, R.2    Amiot, M.3
  • 17
    • 0035136846 scopus 로고    scopus 로고
    • Inhibition of STAT3 signaling leads to apoptosis of leukemic large granular lymphocytes and decreased Mcl-1 expression
    • Epling-Burnette P.K., Liu J.H., Catlett-Falcone R., et al. Inhibition of STAT3 signaling leads to apoptosis of leukemic large granular lymphocytes and decreased Mcl-1 expression. J Clin Invest 107 (2001) 351-362
    • (2001) J Clin Invest , vol.107 , pp. 351-362
    • Epling-Burnette, P.K.1    Liu, J.H.2    Catlett-Falcone, R.3
  • 18
    • 15144349717 scopus 로고    scopus 로고
    • Cytochrome-c dependent and independent induction of apoptosis in multiple myeloma cells
    • Chauhan D., Pandey P., Ogata A., et al. Cytochrome-c dependent and independent induction of apoptosis in multiple myeloma cells. J Biol Chem 272 (1997) 29995-29997
    • (1997) J Biol Chem , vol.272 , pp. 29995-29997
    • Chauhan, D.1    Pandey, P.2    Ogata, A.3
  • 19
    • 0035816553 scopus 로고    scopus 로고
    • Apaf-1/cytochrome c independent and Smac dependent induction of apoptosis in multiple myeloma cells
    • Chauhan D., Hideshima T., Rosen S., et al. Apaf-1/cytochrome c independent and Smac dependent induction of apoptosis in multiple myeloma cells. J Biol Chem 276 (2001) 24453-24456
    • (2001) J Biol Chem , vol.276 , pp. 24453-24456
    • Chauhan, D.1    Hideshima, T.2    Rosen, S.3
  • 20
    • 0035921689 scopus 로고    scopus 로고
    • Biologic sequelae of interleukin-6 induced PI3-K/Akt signaling in multiple myeloma
    • Hideshima T., Nakamura N., Chauhan D., et al. Biologic sequelae of interleukin-6 induced PI3-K/Akt signaling in multiple myeloma. Oncogene 20 (2001) 5991-6000
    • (2001) Oncogene , vol.20 , pp. 5991-6000
    • Hideshima, T.1    Nakamura, N.2    Chauhan, D.3
  • 21
    • 85047699977 scopus 로고    scopus 로고
    • Identification of genes regulated by dexamethasone in multiple myeloma cells using oligonucleotide arrays
    • Chauhan D., Auclair D., Robinson E.K., et al. Identification of genes regulated by dexamethasone in multiple myeloma cells using oligonucleotide arrays. Oncogene 21 (2002) 1346-1358
    • (2002) Oncogene , vol.21 , pp. 1346-1358
    • Chauhan, D.1    Auclair, D.2    Robinson, E.K.3
  • 22
    • 0038542892 scopus 로고    scopus 로고
    • Identification of genes regulated by 2-methoxyestradiol (2ME2) in multiple myeloma cells using oligonucleotide arrays
    • Chauhan D., Li G., Auclair D., et al. Identification of genes regulated by 2-methoxyestradiol (2ME2) in multiple myeloma cells using oligonucleotide arrays. Blood 101 (2003) 3606-3614
    • (2003) Blood , vol.101 , pp. 3606-3614
    • Chauhan, D.1    Li, G.2    Auclair, D.3
  • 23
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1
    • Iwakoshi N.N., Lee A.H., Vallabhajosyula P., et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat Immunol 4 (2003) 321-329
    • (2003) Nat Immunol , vol.4 , pp. 321-329
    • Iwakoshi, N.N.1    Lee, A.H.2    Vallabhajosyula, P.3
  • 24
    • 34047136169 scopus 로고    scopus 로고
    • The differentiation and stress response factor XBP-1 drives multiple myeloma pathogenesis
    • Carrasco D.R., Sukhdeo K., Protopopov M., et al. The differentiation and stress response factor XBP-1 drives multiple myeloma pathogenesis. Cancer Cell 11 (2007) 349-360
    • (2007) Cancer Cell , vol.11 , pp. 349-360
    • Carrasco, D.R.1    Sukhdeo, K.2    Protopopov, M.3
  • 25
    • 0030057701 scopus 로고    scopus 로고
    • Soluble interleukin-6 receptor as a prognostic factor in multiple myeloma
    • Pulkki K., Pelliniemi T.T., Rajamaki A., et al. Soluble interleukin-6 receptor as a prognostic factor in multiple myeloma. Br J Haematol 92 (1996) 370-374
    • (1996) Br J Haematol , vol.92 , pp. 370-374
    • Pulkki, K.1    Pelliniemi, T.T.2    Rajamaki, A.3
  • 26
    • 0029914360 scopus 로고    scopus 로고
    • Soluble interleukin-6 receptor (sIL-6R), a new prognostic factor in multiple myeloma
    • Kyrtsonis M.C., Dedoussis G., Zervas C., et al. Soluble interleukin-6 receptor (sIL-6R), a new prognostic factor in multiple myeloma. Br J Haematol 93 (1996) 398-400
    • (1996) Br J Haematol , vol.93 , pp. 398-400
    • Kyrtsonis, M.C.1    Dedoussis, G.2    Zervas, C.3
  • 27
    • 0032525085 scopus 로고    scopus 로고
    • The prognostic value of soluble interleukin-6 receptor in patients with multiple myeloma
    • Stasi R., Brunetti M., Parma A., et al. The prognostic value of soluble interleukin-6 receptor in patients with multiple myeloma. Cancer 82 (1998) 1860-1866
    • (1998) Cancer , vol.82 , pp. 1860-1866
    • Stasi, R.1    Brunetti, M.2    Parma, A.3
  • 28
    • 0036162098 scopus 로고    scopus 로고
    • Predicting long-term (≥ 5 years) event-free survival in multiple myeloma patients following planned tandem autotransplants
    • Tricot G., Spencer T., Sawyer J., et al. Predicting long-term (≥ 5 years) event-free survival in multiple myeloma patients following planned tandem autotransplants. Br J Haematol 116 (2002) 211-217
    • (2002) Br J Haematol , vol.116 , pp. 211-217
    • Tricot, G.1    Spencer, T.2    Sawyer, J.3
  • 29
    • 0036782532 scopus 로고    scopus 로고
    • The IL-6 receptor super-antagonist Sant7 enhances antiproliferative and apoptotic effects induced by dexamethasone and zoledronic acid on multiple myeloma cells
    • Tassone P., Galea E., Forciniti S., et al. The IL-6 receptor super-antagonist Sant7 enhances antiproliferative and apoptotic effects induced by dexamethasone and zoledronic acid on multiple myeloma cells. Int J Oncol 21 (2002) 867-873
    • (2002) Int J Oncol , vol.21 , pp. 867-873
    • Tassone, P.1    Galea, E.2    Forciniti, S.3
  • 30
    • 20344385768 scopus 로고    scopus 로고
    • Combination therapy with IL-6 receptor super-antagonist Sant7 and dexamethasone induces antitumor effects in a novel SCID-hu in vivo model of human multiple myeloma
    • Tassone P., Neri P., Burger R., et al. Combination therapy with IL-6 receptor super-antagonist Sant7 and dexamethasone induces antitumor effects in a novel SCID-hu in vivo model of human multiple myeloma. Clin Cancer Res 11 (2005) 4251-4258
    • (2005) Clin Cancer Res , vol.11 , pp. 4251-4258
    • Tassone, P.1    Neri, P.2    Burger, R.3
  • 31
    • 12144290914 scopus 로고    scopus 로고
    • Inhibition of the insulin-like growth factor receptor-1 tyrosine kinase activity as a therapeutic strategy for multiple myeloma, other hematologic malignancies, and solid tumors
    • Mitsiades C.S., Mitsiades N.S., McMullan C.J., et al. Inhibition of the insulin-like growth factor receptor-1 tyrosine kinase activity as a therapeutic strategy for multiple myeloma, other hematologic malignancies, and solid tumors. Cancer Cell 5 (2004) 221-230
    • (2004) Cancer Cell , vol.5 , pp. 221-230
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 32
    • 16544395386 scopus 로고    scopus 로고
    • Insulin-like growth factors and neoplasia
    • Pollak M.N. Insulin-like growth factors and neoplasia. Novartis Found Symp 262 (2004) 84-98
    • (2004) Novartis Found Symp , vol.262 , pp. 84-98
    • Pollak, M.N.1
  • 33
    • 0036892647 scopus 로고    scopus 로고
    • Serum insulinlike growth factor is not elevated in patients with multiple myeloma but is still a prognostic factor
    • Standal T., Borset M., Lenhoff S., et al. Serum insulinlike growth factor is not elevated in patients with multiple myeloma but is still a prognostic factor. Blood 100 (2002) 3925-3929
    • (2002) Blood , vol.100 , pp. 3925-3929
    • Standal, T.1    Borset, M.2    Lenhoff, S.3
  • 34
    • 0031181228 scopus 로고    scopus 로고
    • A role for insulin-like growth factor in the regulation of IL-6-responsive human myeloma cell line growth
    • Jelinek D.F., Witzig T.E., and Arendt B.K. A role for insulin-like growth factor in the regulation of IL-6-responsive human myeloma cell line growth. J Immunol 159 (1997) 487-496
    • (1997) J Immunol , vol.159 , pp. 487-496
    • Jelinek, D.F.1    Witzig, T.E.2    Arendt, B.K.3
  • 35
    • 0036625066 scopus 로고    scopus 로고
    • Insulinlike growth factor-I signaling in multiple myeloma: downstream elements, functional correlates, and pathway cross-talk
    • Qiang Y.W., Kopantzev E., and Rudikoff S. Insulinlike growth factor-I signaling in multiple myeloma: downstream elements, functional correlates, and pathway cross-talk. Blood 99 (2002) 4138-4146
    • (2002) Blood , vol.99 , pp. 4138-4146
    • Qiang, Y.W.1    Kopantzev, E.2    Rudikoff, S.3
  • 36
    • 0037158513 scopus 로고    scopus 로고
    • Activation of NF-kB and upregulation of intracellular anti-apoptotic proteins via the IGF-1/Akt signaling in human multiple myeloma cells: therapeutic implications
    • Mitsiades C.S., Mitsiades N., Poulaki V., et al. Activation of NF-kB and upregulation of intracellular anti-apoptotic proteins via the IGF-1/Akt signaling in human multiple myeloma cells: therapeutic implications. Oncogene 21 (2002) 5673-5683
    • (2002) Oncogene , vol.21 , pp. 5673-5683
    • Mitsiades, C.S.1    Mitsiades, N.2    Poulaki, V.3
  • 37
    • 0037484893 scopus 로고    scopus 로고
    • The IGF/IGF-1R system is a major therapeutic target for multiple myeloma, other hematologic malignancies and solid tumors
    • Mitsiades C.S., Mitsiades N., Kung A.L., et al. The IGF/IGF-1R system is a major therapeutic target for multiple myeloma, other hematologic malignancies and solid tumors. Blood 100 (2002) 170a
    • (2002) Blood , vol.100
    • Mitsiades, C.S.1    Mitsiades, N.2    Kung, A.L.3
  • 38
    • 0141731299 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 induces adhesion and migration in human multiple myeloma cells via activation of beta1-integrin and phosphatidylinositol 3'-kinase/AKT signaling
    • Tai Y.T., Podar K., Catley L., et al. Insulin-like growth factor-1 induces adhesion and migration in human multiple myeloma cells via activation of beta1-integrin and phosphatidylinositol 3'-kinase/AKT signaling. Cancer Res 63 (2003) 5850-5858
    • (2003) Cancer Res , vol.63 , pp. 5850-5858
    • Tai, Y.T.1    Podar, K.2    Catley, L.3
  • 39
    • 0037458621 scopus 로고    scopus 로고
    • Essential role of caveolae in interleukin-6- and insulin-like growth factor I-triggered Akt-1-mediated survival of multiple myeloma cells
    • Podar K., Tai Y.T., Cole C.E., et al. Essential role of caveolae in interleukin-6- and insulin-like growth factor I-triggered Akt-1-mediated survival of multiple myeloma cells. J Biol Chem 278 (2003) 5794-5801
    • (2003) J Biol Chem , vol.278 , pp. 5794-5801
    • Podar, K.1    Tai, Y.T.2    Cole, C.E.3
  • 41
    • 13544255403 scopus 로고    scopus 로고
    • The pathophysiological role of VEGF in hematological malignancies: therapeutic implications
    • Podar K., and Anderson K.C. The pathophysiological role of VEGF in hematological malignancies: therapeutic implications. Blood 105 (2005) 1383-1395
    • (2005) Blood , vol.105 , pp. 1383-1395
    • Podar, K.1    Anderson, K.C.2
  • 42
    • 0035880256 scopus 로고    scopus 로고
    • Vascular endothelial growth factor triggers signaling cascades mediating multiple myeloma cell growth and migration
    • Podar K., Tai Y.T., Davies F.E., et al. Vascular endothelial growth factor triggers signaling cascades mediating multiple myeloma cell growth and migration. Blood 98 (2001) 428-435
    • (2001) Blood , vol.98 , pp. 428-435
    • Podar, K.1    Tai, Y.T.2    Davies, F.E.3
  • 43
    • 18544377343 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with beta 1 integrin- and phosphatidylinositol 3-kinase-dependent PKC alpha activation
    • Podar K., Tai Y.T., Lin B.K., et al. Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with beta 1 integrin- and phosphatidylinositol 3-kinase-dependent PKC alpha activation. J Biol Chem 277 (2002) 7875-7881
    • (2002) J Biol Chem , vol.277 , pp. 7875-7881
    • Podar, K.1    Tai, Y.T.2    Lin, B.K.3
  • 44
    • 0036731996 scopus 로고    scopus 로고
    • The vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584 inhibits growth and migration of multiple myeloma cells in the bone marrow microenvironment
    • Lin B., Podar K., Gupta D., et al. The vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584 inhibits growth and migration of multiple myeloma cells in the bone marrow microenvironment. Cancer Res 62 (2002) 5019-5026
    • (2002) Cancer Res , vol.62 , pp. 5019-5026
    • Lin, B.1    Podar, K.2    Gupta, D.3
  • 45
    • 11144354204 scopus 로고    scopus 로고
    • GW654652, the pan-inhibitor of VEGF receptors, blocks the growth and migration of multiple myeloma cells in the bone marrow microenvironment
    • Podar K., Catley L.P., Tai Y.T., et al. GW654652, the pan-inhibitor of VEGF receptors, blocks the growth and migration of multiple myeloma cells in the bone marrow microenvironment. Blood 103 (2004) 3474-3479
    • (2004) Blood , vol.103 , pp. 3474-3479
    • Podar, K.1    Catley, L.P.2    Tai, Y.T.3
  • 46
    • 5644225628 scopus 로고    scopus 로고
    • Caveolin-1 is required for vascular endothelial growth factor-triggered multiple myeloma cell migration and is targeted by bortezomib
    • Podar K., Shringarpure R., Tai Y.T., et al. Caveolin-1 is required for vascular endothelial growth factor-triggered multiple myeloma cell migration and is targeted by bortezomib. Cancer Res 64 (2004) 7500-7506
    • (2004) Cancer Res , vol.64 , pp. 7500-7506
    • Podar, K.1    Shringarpure, R.2    Tai, Y.T.3
  • 47
    • 6944253220 scopus 로고    scopus 로고
    • VEGF induces MCL-1 upregulation and protects multiple myeloma cells against apoptosis
    • Le Gouill S., Podar K., Amiot M., et al. VEGF induces MCL-1 upregulation and protects multiple myeloma cells against apoptosis. Blood 104 (2004) 2886-2892
    • (2004) Blood , vol.104 , pp. 2886-2892
    • Le Gouill, S.1    Podar, K.2    Amiot, M.3
  • 48
    • 33845882259 scopus 로고    scopus 로고
    • The small-molecule VEGF receptor inhibitor pazopanib (GW786034B) targets both tumor and endothelial cells in multiple myeloma
    • Podar K., Tonon G., Sattler M., et al. The small-molecule VEGF receptor inhibitor pazopanib (GW786034B) targets both tumor and endothelial cells in multiple myeloma. Proc Natl Acad Sci U S A 103 (2006) 19478-19483
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19478-19483
    • Podar, K.1    Tonon, G.2    Sattler, M.3
  • 49
    • 0033134764 scopus 로고    scopus 로고
    • Bone marrow neovascularization, plasma cell angiogenic potential, and matrix metalloproteinase-2 secretion parallel progression of human multiple myeloma
    • Vacca A., Ribatti D., Presta M., et al. Bone marrow neovascularization, plasma cell angiogenic potential, and matrix metalloproteinase-2 secretion parallel progression of human multiple myeloma. Blood 93 (1999) 3064-3073
    • (1999) Blood , vol.93 , pp. 3064-3073
    • Vacca, A.1    Ribatti, D.2    Presta, M.3
  • 50
    • 0038446643 scopus 로고    scopus 로고
    • Paracrine interactions of basic fibroblast growth factor and interleukin-6 in multiple myeloma
    • Bisping G., Leo R., Wenning D., et al. Paracrine interactions of basic fibroblast growth factor and interleukin-6 in multiple myeloma. Blood 101 (2003) 2775-2783
    • (2003) Blood , vol.101 , pp. 2775-2783
    • Bisping, G.1    Leo, R.2    Wenning, D.3
  • 51
    • 0032212243 scopus 로고    scopus 로고
    • The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts
    • Chesi M., Nardini E., Lim R.S.C., et al. The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts. Blood 92 (1998) 3025-3034
    • (1998) Blood , vol.92 , pp. 3025-3034
    • Chesi, M.1    Nardini, E.2    Lim, R.S.C.3
  • 52
    • 0030922231 scopus 로고    scopus 로고
    • Frequent translocation t(4;14)(p16.3;q32.3) in multiple myeloma: association with increased expression and activating mutations of fibroblast growth factor receptor 3
    • Chesi M., Nardini E., Brents L.A., et al. Frequent translocation t(4;14)(p16.3;q32.3) in multiple myeloma: association with increased expression and activating mutations of fibroblast growth factor receptor 3. Nat Genet 16 (1997) 260-264
    • (1997) Nat Genet , vol.16 , pp. 260-264
    • Chesi, M.1    Nardini, E.2    Brents, L.A.3
  • 53
    • 0037441747 scopus 로고    scopus 로고
    • In multiple myeloma, t(4;14)(p16;q32) is an adverse prognostic factor irrespective of FGFR3 expression
    • Keats J.J., Reiman T., Maxwell C.A., et al. In multiple myeloma, t(4;14)(p16;q32) is an adverse prognostic factor irrespective of FGFR3 expression. Blood 101 (2003) 1520-1529
    • (2003) Blood , vol.101 , pp. 1520-1529
    • Keats, J.J.1    Reiman, T.2    Maxwell, C.A.3
  • 54
    • 22044440001 scopus 로고    scopus 로고
    • Immunohistochemistry accurately predicts FGFR3 aberrant expression and t(4;14) in multiple myeloma
    • Chang H., Stewart A.K., Qi X.Y., et al. Immunohistochemistry accurately predicts FGFR3 aberrant expression and t(4;14) in multiple myeloma. Blood 106 (2005) 353-355
    • (2005) Blood , vol.106 , pp. 353-355
    • Chang, H.1    Stewart, A.K.2    Qi, X.Y.3
  • 55
    • 15944378835 scopus 로고    scopus 로고
    • CHIR-258, a novel, multitargeted tyrosine kinase inhibitor for the potential treatment of t(4;14) multiple myeloma
    • Trudel S., Li Z.H., Wei E., et al. CHIR-258, a novel, multitargeted tyrosine kinase inhibitor for the potential treatment of t(4;14) multiple myeloma. Blood 105 (2005) 2941-2948
    • (2005) Blood , vol.105 , pp. 2941-2948
    • Trudel, S.1    Li, Z.H.2    Wei, E.3
  • 56
    • 33646555792 scopus 로고    scopus 로고
    • The inhibitory anti-FGFR3 antibody, PRO-001, is cytotoxic to t(4;14) multiple myeloma cells
    • Trudel S., Stewart A.K., Rom E., et al. The inhibitory anti-FGFR3 antibody, PRO-001, is cytotoxic to t(4;14) multiple myeloma cells. Blood 107 (2006) 4039-4046
    • (2006) Blood , vol.107 , pp. 4039-4046
    • Trudel, S.1    Stewart, A.K.2    Rom, E.3
  • 57
    • 1942456800 scopus 로고    scopus 로고
    • Inhibition of fibroblast growth factor receptor 3 induces differentiation and apoptosis in t(4;14) myeloma
    • Trudel S., Ely S., Farooqi Y., et al. Inhibition of fibroblast growth factor receptor 3 induces differentiation and apoptosis in t(4;14) myeloma. Blood 103 (2004) 3521-3528
    • (2004) Blood , vol.103 , pp. 3521-3528
    • Trudel, S.1    Ely, S.2    Farooqi, Y.3
  • 58
    • 31744438381 scopus 로고    scopus 로고
    • FGFR3 as a therapeutic target of the small molecule inhibitor PKC412 in hematopoietic malignancies
    • Chen J., Lee B.H., Williams I.R., et al. FGFR3 as a therapeutic target of the small molecule inhibitor PKC412 in hematopoietic malignancies. Oncogene 24 (2005) 8259-8267
    • (2005) Oncogene , vol.24 , pp. 8259-8267
    • Chen, J.1    Lee, B.H.2    Williams, I.R.3
  • 59
    • 11144355586 scopus 로고    scopus 로고
    • BAFF and APRIL protect myeloma cells from apoptosis induced by interleukin 6 deprivation and dexamethasone
    • Moreaux J., Legouffe E., Jourdan E., et al. BAFF and APRIL protect myeloma cells from apoptosis induced by interleukin 6 deprivation and dexamethasone. Blood 103 (2004) 3148-3157
    • (2004) Blood , vol.103 , pp. 3148-3157
    • Moreaux, J.1    Legouffe, E.2    Jourdan, E.3
  • 60
    • 0942298590 scopus 로고    scopus 로고
    • Expression of BCMA, TACI, and BAFF-R in multiple myeloma: a mechanism for growth and survival
    • Novak A.J., Darce J.R., Arendt B.K., et al. Expression of BCMA, TACI, and BAFF-R in multiple myeloma: a mechanism for growth and survival. Blood 103 (2004) 689-694
    • (2004) Blood , vol.103 , pp. 689-694
    • Novak, A.J.1    Darce, J.R.2    Arendt, B.K.3
  • 61
    • 33746122751 scopus 로고    scopus 로고
    • Role of B-cell-activating factor in adhesion and growth of human multiple myeloma cells in the bone marrow microenvironment
    • Tai Y.T., Li X.F., Breitkreutz I., et al. Role of B-cell-activating factor in adhesion and growth of human multiple myeloma cells in the bone marrow microenvironment. Cancer Res 66 (2006) 6675-6682
    • (2006) Cancer Res , vol.66 , pp. 6675-6682
    • Tai, Y.T.1    Li, X.F.2    Breitkreutz, I.3
  • 62
    • 11144355390 scopus 로고    scopus 로고
    • Illegitimate WNT signaling promotes proliferation of multiple myeloma cells
    • Derksen P.W., Tjin E., Meijer H.P., et al. Illegitimate WNT signaling promotes proliferation of multiple myeloma cells. Proc Natl Acad Sci U S A 101 (2004) 6122-6127
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6122-6127
    • Derksen, P.W.1    Tjin, E.2    Meijer, H.P.3
  • 63
    • 34250678970 scopus 로고    scopus 로고
    • Targeting the beta-catenin/TCF transcriptional complex in the treatment of multiple myeloma
    • Sukhdeo K., Mani M., Zhang Y., et al. Targeting the beta-catenin/TCF transcriptional complex in the treatment of multiple myeloma. Proc Natl Acad Sci U S A 104 (2007) 7516-7521
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7516-7521
    • Sukhdeo, K.1    Mani, M.2    Zhang, Y.3
  • 64
    • 9144240010 scopus 로고    scopus 로고
    • DKK1, a negative regulator of Wnt signaling, is a target of the beta-catenin/TCF pathway
    • Niida A., Hiroko T., Kasai M., et al. DKK1, a negative regulator of Wnt signaling, is a target of the beta-catenin/TCF pathway. Oncogene 23 (2004) 8520-8526
    • (2004) Oncogene , vol.23 , pp. 8520-8526
    • Niida, A.1    Hiroko, T.2    Kasai, M.3
  • 65
    • 0346363760 scopus 로고    scopus 로고
    • The role of the Wnt-signaling antagonist DKK1 in the development of osteolytic lesions in multiple myeloma
    • Tian E., Zhan F., Walker R., et al. The role of the Wnt-signaling antagonist DKK1 in the development of osteolytic lesions in multiple myeloma. N Engl J Med 349 (2003) 2483-2494
    • (2003) N Engl J Med , vol.349 , pp. 2483-2494
    • Tian, E.1    Zhan, F.2    Walker, R.3
  • 66
    • 33847397091 scopus 로고    scopus 로고
    • Antibody-based inhibition of DKK1 suppresses tumor-induced bone resorption and multiple myeloma growth in vivo
    • Yaccoby S., Ling W., Zhan F., et al. Antibody-based inhibition of DKK1 suppresses tumor-induced bone resorption and multiple myeloma growth in vivo. Blood 109 (2007) 2106-2111
    • (2007) Blood , vol.109 , pp. 2106-2111
    • Yaccoby, S.1    Ling, W.2    Zhan, F.3
  • 67
    • 0037082449 scopus 로고    scopus 로고
    • CD40 activation induces p53-dependent vascular endothelial growth factor secretion in human multiple myeloma cells
    • Tai Y.T., Podar K., Gupta D., et al. CD40 activation induces p53-dependent vascular endothelial growth factor secretion in human multiple myeloma cells. Blood 99 (2002) 1419-1427
    • (2002) Blood , vol.99 , pp. 1419-1427
    • Tai, Y.T.1    Podar, K.2    Gupta, D.3
  • 68
    • 0038784379 scopus 로고    scopus 로고
    • CD40 induces human multiple myeloma cell migration via phosphatidylinositol 3-kinase/AKT/NF-kappa B signaling
    • Tai Y.T., Podar K., Mitsiades N., et al. CD40 induces human multiple myeloma cell migration via phosphatidylinositol 3-kinase/AKT/NF-kappa B signaling. Blood 101 (2003) 2762-2769
    • (2003) Blood , vol.101 , pp. 2762-2769
    • Tai, Y.T.1    Podar, K.2    Mitsiades, N.3
  • 69
    • 6944247322 scopus 로고    scopus 로고
    • Mechanisms by which SGN-40, a humanized anti-CD40 antibody, induces cytotoxicity in human multiple myeloma cells: clinical implications
    • Tai Y.T., Catley L.P., Mitsiades C.S., et al. Mechanisms by which SGN-40, a humanized anti-CD40 antibody, induces cytotoxicity in human multiple myeloma cells: clinical implications. Cancer Res 64 (2004) 2846-2852
    • (2004) Cancer Res , vol.64 , pp. 2846-2852
    • Tai, Y.T.1    Catley, L.P.2    Mitsiades, C.S.3
  • 70
    • 19944430437 scopus 로고    scopus 로고
    • Molecular mechanisms whereby immunomodulatory drugs activate natural killer cells: clinical application
    • Hayashi T., Hideshima T., Akiyama M., et al. Molecular mechanisms whereby immunomodulatory drugs activate natural killer cells: clinical application. Br J Haematol 128 (2005) 192-203
    • (2005) Br J Haematol , vol.128 , pp. 192-203
    • Hayashi, T.1    Hideshima, T.2    Akiyama, M.3
  • 71
    • 29244488561 scopus 로고    scopus 로고
    • Immunomodulatory drug lenalidomide (CC-5013, IMiD3) augments anti-CD40 SGN-40-induced cytotoxicity in human multiple myeloma: clinical implications
    • Tai Y.T., Li X.F., Catley L., et al. Immunomodulatory drug lenalidomide (CC-5013, IMiD3) augments anti-CD40 SGN-40-induced cytotoxicity in human multiple myeloma: clinical implications. Cancer Res 65 (2005) 11712-11720
    • (2005) Cancer Res , vol.65 , pp. 11712-11720
    • Tai, Y.T.1    Li, X.F.2    Catley, L.3
  • 72
    • 0036140240 scopus 로고    scopus 로고
    • CD20-directed serotherapy in patients with multiple myeloma: biologic considerations and therapeutic applications
    • Treon S.P., Pilarski L.M., Belch A.R., et al. CD20-directed serotherapy in patients with multiple myeloma: biologic considerations and therapeutic applications. J Immunother 25 (2002) 72-81
    • (2002) J Immunother , vol.25 , pp. 72-81
    • Treon, S.P.1    Pilarski, L.M.2    Belch, A.R.3
  • 73
    • 35748984055 scopus 로고    scopus 로고
    • Killing of drug-sensitive and resistant myeloma cells and disruption of their bone marrow stromal interaction by HuLuc63, a novel humanized anti-CS1 monoclonal antibody
    • Tai Y.-T., Song W., Li X.-F., et al. Killing of drug-sensitive and resistant myeloma cells and disruption of their bone marrow stromal interaction by HuLuc63, a novel humanized anti-CS1 monoclonal antibody. Blood 108 (2006) 990a
    • (2006) Blood , vol.108
    • Tai, Y.-T.1    Song, W.2    Li, X.-F.3
  • 74
    • 18244406798 scopus 로고    scopus 로고
    • Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib
    • Berkers C.R., Verdoes M., Lichtman E., et al. Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib. Nat Methods 2 (2005) 357-362
    • (2005) Nat Methods , vol.2 , pp. 357-362
    • Berkers, C.R.1    Verdoes, M.2    Lichtman, E.3
  • 75
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kB and I kB proteins: new discoveries and insights
    • Baldwin Jr. A.S. The NF-kB and I kB proteins: new discoveries and insights. Annu Rev Immunol 14 (1996) 649-683
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 76
    • 0027332498 scopus 로고
    • The IkB proteins: multifunctional regulators of Rel NF-kB transcription factors
    • Beg A.A., and Baldwin Jr. A.S. The IkB proteins: multifunctional regulators of Rel NF-kB transcription factors. Genes Dev 7 (1993) 2064-2070
    • (1993) Genes Dev , vol.7 , pp. 2064-2070
    • Beg, A.A.1    Baldwin Jr., A.S.2
  • 77
    • 0032575379 scopus 로고    scopus 로고
    • Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate
    • Zandi E., Chen Y., and Karin M. Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate. Science 281 (1998) 1360-1363
    • (1998) Science , vol.281 , pp. 1360-1363
    • Zandi, E.1    Chen, Y.2    Karin, M.3
  • 78
    • 0030613551 scopus 로고    scopus 로고
    • The IkB kinase complex (IKK) contains two kinase subunits, IKKa and IKKb, necessary for IkB phosphorylation and NF-kB activation
    • Zandi E., Rothwarf D.M., Delhase M., et al. The IkB kinase complex (IKK) contains two kinase subunits, IKKa and IKKb, necessary for IkB phosphorylation and NF-kB activation. Cell 91 (1997) 243-252
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3
  • 79
    • 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 61 (2001) 3071-3076
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 80
    • 0242496212 scopus 로고    scopus 로고
    • Molecular sequelae of proteasome inhibition in human multiple myeloma cells
    • Mitsiades N., Mitsiades C.S., Poulaki V., et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci U S A 99 (2002) 14374-14379
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14374-14379
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 81
    • 0037443551 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: therapeutic applications
    • Mitsiades N., Mitsiades C.S., Richardson P.G., et al. The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: therapeutic applications. Blood 101 (2003) 2377-2380
    • (2003) Blood , vol.101 , pp. 2377-2380
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 82
    • 0037441760 scopus 로고    scopus 로고
    • Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341
    • Hideshima T., Mitsiades C., Akiyama M., et al. Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341. Blood 101 (2003) 1530-1534
    • (2003) Blood , vol.101 , pp. 1530-1534
    • Hideshima, T.1    Mitsiades, C.2    Akiyama, M.3
  • 83
    • 0043193876 scopus 로고    scopus 로고
    • Proteasome inhibitors disrupt the unfolded protein response in myeloma cells
    • Lee A.H., Iwakoshi N.N., Anderson K.C., et al. Proteasome inhibitors disrupt the unfolded protein response in myeloma cells. Proc Natl Acad Sci U S A 100 (2003) 9946-9951
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9946-9951
    • Lee, A.H.1    Iwakoshi, N.N.2    Anderson, K.C.3
  • 84
    • 0346122900 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 abrogates IL-6 triggered signaling cascades via caspase-dependent downregulation of gp130 in multiple myeloma
    • Hideshima T., Chauhan D., Hayashi T., et al. Proteasome inhibitor PS-341 abrogates IL-6 triggered signaling cascades via caspase-dependent downregulation of gp130 in multiple myeloma. Oncogene 22 (2003) 8386-8393
    • (2003) Oncogene , vol.22 , pp. 8386-8393
    • Hideshima, T.1    Chauhan, D.2    Hayashi, T.3
  • 85
    • 0035958517 scopus 로고    scopus 로고
    • Role of TNF-a in the pathophysiology of human multiple myeloma: therapeutic applications
    • Hideshima T., Chauhan D., Schlossman R.L., et al. Role of TNF-a in the pathophysiology of human multiple myeloma: therapeutic applications. Oncogene 20 (2001) 4519-4527
    • (2001) Oncogene , vol.20 , pp. 4519-4527
    • Hideshima, T.1    Chauhan, D.2    Schlossman, R.L.3
  • 86
    • 18544367201 scopus 로고    scopus 로고
    • NF-kB as a therapeutic target in multiple myeloma
    • Hideshima T., Chauhan D., Richardson P., et al. NF-kB as a therapeutic target in multiple myeloma. J Biol Chem 277 (2002) 16639-16647
    • (2002) J Biol Chem , vol.277 , pp. 16639-16647
    • Hideshima, T.1    Chauhan, D.2    Richardson, P.3
  • 87
    • 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 77 (2006) 233-238
    • (2006) Eur J Haematol , vol.77 , pp. 233-238
    • Heider, U.1    Kaiser, M.2    Muller, C.3
  • 88
    • 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 110 (2007) 334-338
    • (2007) Blood , vol.110 , pp. 334-338
    • Giuliani, N.1    Morandi, F.2    Tagliaferri, S.3
  • 89
    • 34548133601 scopus 로고    scopus 로고
    • Bortezomib inhibits human osteoclastogenesis
    • von Metzler I., Krebbel H., Hecht M., et al. Bortezomib inhibits human osteoclastogenesis. Leukemia 21 (2007) 2025-2034
    • (2007) Leukemia , vol.21 , pp. 2025-2034
    • von Metzler, I.1    Krebbel, H.2    Hecht, M.3
  • 90
    • 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 8 (2005) 407-419
    • (2005) Cancer Cell , vol.8 , pp. 407-419
    • Chauhan, D.1    Catley, L.2    Li, G.3
  • 91
    • 34347375499 scopus 로고    scopus 로고
    • NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells
    • Miller C.P., Ban K., Dujka M.E., et al. NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells. Blood 110 (2007) 267-277
    • (2007) Blood , vol.110 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3
  • 92
    • 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 67 (2007) 6383-6391
    • (2007) Cancer Res , vol.67 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Aujay, M.A.3
  • 93
    • 35748970136 scopus 로고    scopus 로고
    • Multicenter phase I studies to evaluate the safety, tolerability, and clinical response to intensive dosing with the proteasome Inhibitor PR-171 in patients with relapsed or refractory hematological malignancies
    • O'Connor O.A., Orlowski R.Z., Alsina M., et al. Multicenter phase I studies to evaluate the safety, tolerability, and clinical response to intensive dosing with the proteasome Inhibitor PR-171 in patients with relapsed or refractory hematological malignancies. Blood 108 (2006) 687a
    • (2006) Blood , vol.108
    • O'Connor, O.A.1    Orlowski, R.Z.2    Alsina, M.3
  • 94
    • 0034331194 scopus 로고    scopus 로고
    • Thalidomide and its analogues overcome drug resistance of human multiple myeloma cells to conventional therapy
    • Hideshima T., Chauhan D., Shima Y., et al. Thalidomide and its analogues overcome drug resistance of human multiple myeloma cells to conventional therapy. Blood 96 (2000) 2943-2950
    • (2000) Blood , vol.96 , pp. 2943-2950
    • Hideshima, T.1    Chauhan, D.2    Shima, Y.3
  • 95
    • 10744231369 scopus 로고    scopus 로고
    • Immunomodulatory drug costimulates T cells via the B7-CD28 pathway
    • LeBlanc R., Hideshima T., Catley L.P., et al. Immunomodulatory drug costimulates T cells via the B7-CD28 pathway. Blood 103 (2004) 1787-1790
    • (2004) Blood , vol.103 , pp. 1787-1790
    • LeBlanc, R.1    Hideshima, T.2    Catley, L.P.3
  • 96
    • 0035412366 scopus 로고    scopus 로고
    • Thalidomide and immunomodulatory derivatives augment natural killer cell cytotoxicity in multiple myeloma
    • Davies F.E., Raje N., Hideshima T., et al. Thalidomide and immunomodulatory derivatives augment natural killer cell cytotoxicity in multiple myeloma. Blood 98 (2001) 210-216
    • (2001) Blood , vol.98 , pp. 210-216
    • Davies, F.E.1    Raje, N.2    Hideshima, T.3
  • 97
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden J.E., Peart M.J., and Johnstone R.W. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 5 (2006) 769-784
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 98
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin M.S., Donigian J.R., Cohen A., et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188-193
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3
  • 99
    • 20544471104 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in programmed cell death and cancer therapy
    • Marks P.A., and Jiang X. Histone deacetylase inhibitors in programmed cell death and cancer therapy. Cell Cycle 4 (2005) 549-551
    • (2005) Cell Cycle , vol.4 , pp. 549-551
    • Marks, P.A.1    Jiang, X.2
  • 100
    • 28644440158 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: discovery and development as anticancer agents
    • Marks P.A., and Dokmanovic M. Histone deacetylase inhibitors: discovery and development as anticancer agents. Expert Opin Investig Drugs 14 (2005) 1497-1511
    • (2005) Expert Opin Investig Drugs , vol.14 , pp. 1497-1511
    • Marks, P.A.1    Dokmanovic, M.2
  • 101
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin R.J., Nagy L., Inoue S., et al. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391 (1998) 811-814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3
  • 102
    • 0035755974 scopus 로고    scopus 로고
    • Histone deacetylases and cancer: causes and therapies
    • Marks P., Rifkind R.A., Richon V.M., et al. Histone deacetylases and cancer: causes and therapies. Nat Rev Cancer 1 (2001) 194-202
    • (2001) Nat Rev Cancer , vol.1 , pp. 194-202
    • Marks, P.1    Rifkind, R.A.2    Richon, V.M.3
  • 103
    • 0037589018 scopus 로고    scopus 로고
    • Molecular sequelae of histone deacetylase inhibition in human malignant B cells
    • Mitsiades N., Mitsiades C.S., Richardson P.G., et al. Molecular sequelae of histone deacetylase inhibition in human malignant B cells. Blood 101 (2003) 4055-4062
    • (2003) Blood , vol.101 , pp. 4055-4062
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 104
    • 0034706893 scopus 로고    scopus 로고
    • Activation of the p21WAF1/CIP1 promoter independent of p53 by the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) through the Sp1 sites
    • Huang L., Sowa Y., Sakai T., et al. Activation of the p21WAF1/CIP1 promoter independent of p53 by the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) through the Sp1 sites. Oncogene 19 (2000) 5712-5719
    • (2000) Oncogene , vol.19 , pp. 5712-5719
    • Huang, L.1    Sowa, Y.2    Sakai, T.3
  • 105
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon V.M., Sandhoff T.W., Rifkind R.A., et al. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci U S A 97 (2000) 10014-10019
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3
  • 106
    • 9144220841 scopus 로고    scopus 로고
    • Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications
    • Mitsiades C.S., Mitsiades N.S., McMullan C.J., et al. Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications. Proc Natl Acad Sci U S A 101 (2004) 540-545
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 540-545
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 107
    • 23244459828 scopus 로고    scopus 로고
    • Interactive effects of HDAC inhibitors and TRAIL on apoptosis are associated with changes in mitochondrial functions and expressions of cell cycle regulatory genes in multiple myeloma
    • Fandy T.E., Shankar S., Ross D.D., et al. Interactive effects of HDAC inhibitors and TRAIL on apoptosis are associated with changes in mitochondrial functions and expressions of cell cycle regulatory genes in multiple myeloma. Neoplasia 7 (2005) 646-657
    • (2005) Neoplasia , vol.7 , pp. 646-657
    • Fandy, T.E.1    Shankar, S.2    Ross, D.D.3
  • 108
    • 10744229917 scopus 로고    scopus 로고
    • N-hydroxy-3-phenyl-2-propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: discovery of (2E)-N-hydroxy-3-[4-[[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide (NVP-LAQ824)
    • Remiszewski S.W., Sambucetti L.C., Bair K.W., et al. N-hydroxy-3-phenyl-2-propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: discovery of (2E)-N-hydroxy-3-[4-[[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide (NVP-LAQ824). J Med Chem 46 (2003) 4609-4624
    • (2003) J Med Chem , vol.46 , pp. 4609-4624
    • Remiszewski, S.W.1    Sambucetti, L.C.2    Bair, K.W.3
  • 109
    • 9144225360 scopus 로고    scopus 로고
    • Selective growth inhibition of tumor cells by a novel histone deacetylase inhibitor, NVP-LAQ824
    • Atadja P., Gao L., Kwon P., et al. Selective growth inhibition of tumor cells by a novel histone deacetylase inhibitor, NVP-LAQ824. Cancer Res 64 (2004) 689-695
    • (2004) Cancer Res , vol.64 , pp. 689-695
    • Atadja, P.1    Gao, L.2    Kwon, P.3
  • 110
    • 33846225576 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors deplete enhancer of zeste 2 and associated polycomb repressive complex 2 proteins in human acute leukemia cells
    • Fiskus W., Pranpat M., Balasis M., et al. Histone deacetylase inhibitors deplete enhancer of zeste 2 and associated polycomb repressive complex 2 proteins in human acute leukemia cells. Mol Cancer Ther 5 (2006) 3096-3104
    • (2006) Mol Cancer Ther , vol.5 , pp. 3096-3104
    • Fiskus, W.1    Pranpat, M.2    Balasis, M.3
  • 111
    • 11144358387 scopus 로고    scopus 로고
    • Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells
    • Guo F., Sigua C., Tao J., et al. Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells. Cancer Res 64 (2004) 2580-2589
    • (2004) Cancer Res , vol.64 , pp. 2580-2589
    • Guo, F.1    Sigua, C.2    Tao, J.3
  • 112
    • 30044434594 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide
    • Rosato R.R., Maggio S.C., Almenara J.A., et al. The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide. Mol Pharmacol 69 (2006) 216-225
    • (2006) Mol Pharmacol , vol.69 , pp. 216-225
    • Rosato, R.R.1    Maggio, S.C.2    Almenara, J.A.3
  • 113
    • 11144334135 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor NVP-LAQ824 has significant activity against myeloid leukemia cells in vitro and in vivo
    • Weisberg E., Catley L., Kujawa J., et al. Histone deacetylase inhibitor NVP-LAQ824 has significant activity against myeloid leukemia cells in vitro and in vivo. Leukemia 18 (2004) 1951-1963
    • (2004) Leukemia , vol.18 , pp. 1951-1963
    • Weisberg, E.1    Catley, L.2    Kujawa, J.3
  • 114
    • 4644364508 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584
    • Qian D.Z., Wang X., Kachhap S.K., et al. The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584. Cancer Res 64 (2004) 6626-6634
    • (2004) Cancer Res , vol.64 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3
  • 115
    • 0141593496 scopus 로고    scopus 로고
    • NVP-LAQ824 is a potent novel histone deacetylase inhibitor with significant activity against multiple myeloma
    • Catley L., Weisberg E., Tai Y.T., et al. NVP-LAQ824 is a potent novel histone deacetylase inhibitor with significant activity against multiple myeloma. Blood 102 (2003) 2615-2622
    • (2003) Blood , vol.102 , pp. 2615-2622
    • Catley, L.1    Weisberg, E.2    Tai, Y.T.3
  • 116
    • 20844444898 scopus 로고    scopus 로고
    • Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3
    • George P., Bali P., Annavarapu S., et al. Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood 105 (2005) 1768-1776
    • (2005) Blood , vol.105 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3
  • 117
    • 33745888156 scopus 로고    scopus 로고
    • Combined effects of novel tyrosine kinase inhibitor AMN107 and histone deacetylase inhibitor LBH589 against Bcr-Abl-expressing human leukemia cells
    • Fiskus W., Pranpat M., Bali P., et al. Combined effects of novel tyrosine kinase inhibitor AMN107 and histone deacetylase inhibitor LBH589 against Bcr-Abl-expressing human leukemia cells. Blood 108 (2006) 645-652
    • (2006) Blood , vol.108 , pp. 645-652
    • Fiskus, W.1    Pranpat, M.2    Bali, P.3
  • 118
    • 33845741562 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer
    • Geng L., Cuneo K.C., Fu A., et al. Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer. Cancer Res 66 (2006) 11298-11304
    • (2006) Cancer Res , vol.66 , pp. 11298-11304
    • Geng, L.1    Cuneo, K.C.2    Fu, A.3
  • 119
    • 33947242973 scopus 로고    scopus 로고
    • Abrogation of MAPK and Akt signaling by AEE788 synergistically potentiates histone deacetylase inhibitor-induced apoptosis through reactive oxygen species generation
    • Yu C., Friday B.B., Lai J.P., et al. Abrogation of MAPK and Akt signaling by AEE788 synergistically potentiates histone deacetylase inhibitor-induced apoptosis through reactive oxygen species generation. Clin Cancer Res 13 (2007) 1140-1148
    • (2007) Clin Cancer Res , vol.13 , pp. 1140-1148
    • Yu, C.1    Friday, B.B.2    Lai, J.P.3
  • 120
    • 31544464120 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with histone deacetylase inhibitors: the hydroxamic acid derivative LBH589
    • Qian D.Z., Kato Y., Shabbeer S., et al. Targeting tumor angiogenesis with histone deacetylase inhibitors: the hydroxamic acid derivative LBH589. Clin Cancer Res 12 (2006) 634-642
    • (2006) Clin Cancer Res , vol.12 , pp. 634-642
    • Qian, D.Z.1    Kato, Y.2    Shabbeer, S.3
  • 121
    • 33745258655 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor LBH589 is a potent antimyeloma agent that overcomes drug resistance
    • Maiso P., Carvajal-Vergara X., Ocio E.M., et al. The histone deacetylase inhibitor LBH589 is a potent antimyeloma agent that overcomes drug resistance. Cancer Res 66 (2006) 5781-5789
    • (2006) Cancer Res , vol.66 , pp. 5781-5789
    • Maiso, P.1    Carvajal-Vergara, X.2    Ocio, E.M.3
  • 122
    • 33751172982 scopus 로고    scopus 로고
    • Aggresome induction by proteasome inhibitor bortezomib and alpha-tubulin hyperacetylation by tubulin deacetylase (TDAC) inhibitor LBH589 are synergistic in myeloma cells
    • Catley L., Weisberg E., Kiziltepe T., et al. Aggresome induction by proteasome inhibitor bortezomib and alpha-tubulin hyperacetylation by tubulin deacetylase (TDAC) inhibitor LBH589 are synergistic in myeloma cells. Blood 108 (2006) 3441-3449
    • (2006) Blood , vol.108 , pp. 3441-3449
    • Catley, L.1    Weisberg, E.2    Kiziltepe, T.3
  • 123
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty S.J., Koeller K.M., Wong J.C., et al. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc Natl Acad Sci U S A 100 (2003) 4389-4394
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3
  • 124
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: aggravating aggresomes
    • Garcia-Mata R., Gao Y.S., and Sztul E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 3 (2002) 388-396
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 125
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y., Kovacs J.J., McLaurin A., et al. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115 (2003) 727-738
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3
  • 126
    • 20844435806 scopus 로고    scopus 로고
    • Small molecule inhibition of proteasome and aggresome function induces synergistic anti-tumor activity in multiple myeloma
    • Hideshima H., Bradner J.E., Wong J., et al. Small molecule inhibition of proteasome and aggresome function induces synergistic anti-tumor activity in multiple myeloma. Proc Natl Acad Sci USA 102 (2005) 8567-8572
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8567-8572
    • Hideshima, H.1    Bradner, J.E.2    Wong, J.3
  • 127
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases
    • Furumai R., Matsuyama A., Kobashi N., et al. FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res 62 (2002) 4916-4921
    • (2002) Cancer Res , vol.62 , pp. 4916-4921
    • Furumai, R.1    Matsuyama, A.2    Kobashi, N.3
  • 128
    • 2042505684 scopus 로고    scopus 로고
    • Analysis of histone deacetylase inhibitor, depsipeptide (FR901228), effect on multiple myeloma
    • Khan S.B., Maududi T., Barton K., et al. Analysis of histone deacetylase inhibitor, depsipeptide (FR901228), effect on multiple myeloma. Br J Haematol 125 (2004) 156-161
    • (2004) Br J Haematol , vol.125 , pp. 156-161
    • Khan, S.B.1    Maududi, T.2    Barton, K.3
  • 129
    • 1642453460 scopus 로고    scopus 로고
    • Pharmacodynamic response and inhibition of growth of human tumor xenografts by the novel histone deacetylase inhibitor PXD101
    • Plumb J.A., Finn P.W., Williams R.J., et al. Pharmacodynamic response and inhibition of growth of human tumor xenografts by the novel histone deacetylase inhibitor PXD101. Mol Cancer Ther 2 (2003) 721-728
    • (2003) Mol Cancer Ther , vol.2 , pp. 721-728
    • Plumb, J.A.1    Finn, P.W.2    Williams, R.J.3
  • 130
    • 34548138147 scopus 로고    scopus 로고
    • A novel, mercaptoketone-based HDAC inhibitor, KD5170 exerts marked inhibition of osteoclast formation and anti-Myeloma activity in vitro
    • Feng R., Hager J.H., Hassig C.A., et al. A novel, mercaptoketone-based HDAC inhibitor, KD5170 exerts marked inhibition of osteoclast formation and anti-Myeloma activity in vitro. Blood 108 (2006) 991a
    • (2006) Blood , vol.108
    • Feng, R.1    Hager, J.H.2    Hassig, C.A.3
  • 131
    • 33846208233 scopus 로고    scopus 로고
    • STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90alpha and beta in multiple myeloma cells, which critically contribute to tumor-cell survival
    • Chatterjee M., Jain S., Stuhmer T., et al. STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90alpha and beta in multiple myeloma cells, which critically contribute to tumor-cell survival. Blood 109 (2007) 720-728
    • (2007) Blood , vol.109 , pp. 720-728
    • Chatterjee, M.1    Jain, S.2    Stuhmer, T.3
  • 132
    • 31544436323 scopus 로고    scopus 로고
    • Antimyeloma activity of heat shock protein-90 inhibition
    • Mitsiades C.S., Mitsiades N.S., McMullan C.J., et al. Antimyeloma activity of heat shock protein-90 inhibition. Blood 107 (2006) 1092-1100
    • (2006) Blood , vol.107 , pp. 1092-1100
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 133
    • 34948890040 scopus 로고    scopus 로고
    • Heat shock protein inhibition is associated with activation of the unfolded protein response (UPR) pathway in myeloma plasma cells
    • Davenport E.L., Moore H.E., Dunlop A.S., et al. Heat shock protein inhibition is associated with activation of the unfolded protein response (UPR) pathway in myeloma plasma cells. Blood 110 (2007) 2641-2649
    • (2007) Blood , vol.110 , pp. 2641-2649
    • Davenport, E.L.1    Moore, H.E.2    Dunlop, A.S.3
  • 134
    • 33751258297 scopus 로고    scopus 로고
    • Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90
    • Sydor J.R., Normant E., Pien C.S., et al. Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc Natl Acad Sci U S A 103 (2006) 17408-17413
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17408-17413
    • Sydor, J.R.1    Normant, E.2    Pien, C.S.3
  • 135
    • 0034548453 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase/AKT kinase pathway in multiple myeloma plasma cells: roles in cytokine-dependent survival and proliferative responses
    • Tu Y., Gardner A., and Lichtenstein A. The phosphatidylinositol 3-kinase/AKT kinase pathway in multiple myeloma plasma cells: roles in cytokine-dependent survival and proliferative responses. Cancer Res 60 (2000) 6763-6770
    • (2000) Cancer Res , vol.60 , pp. 6763-6770
    • Tu, Y.1    Gardner, A.2    Lichtenstein, A.3
  • 136
    • 33646577479 scopus 로고    scopus 로고
    • Perifosine, an oral bioactive novel alkylphospholipid, inhibits Akt and induces in vitro and in vivo cytotoxicity in human multiple myeloma cells
    • Hideshima T., Catley L., Yasui H., et al. Perifosine, an oral bioactive novel alkylphospholipid, inhibits Akt and induces in vitro and in vivo cytotoxicity in human multiple myeloma cells. Blood 107 (2006) 4053-4062
    • (2006) Blood , vol.107 , pp. 4053-4062
    • Hideshima, T.1    Catley, L.2    Yasui, H.3
  • 137
    • 33846243705 scopus 로고    scopus 로고
    • Edelfosine and perifosine induce selective apoptosis in multiple myeloma by recruitment of death receptors and downstream signaling molecules into lipid rafts
    • Gajate C., and Mollinedo F. Edelfosine and perifosine induce selective apoptosis in multiple myeloma by recruitment of death receptors and downstream signaling molecules into lipid rafts. Blood 109 (2007) 711-719
    • (2007) Blood , vol.109 , pp. 711-719
    • Gajate, C.1    Mollinedo, F.2
  • 138
    • 34548181762 scopus 로고    scopus 로고
    • Inhibition of Akt induces significant downregulation of survivin and cytotoxicity in human multiple myeloma cells
    • Hideshima T., Catley L., Raje N., et al. Inhibition of Akt induces significant downregulation of survivin and cytotoxicity in human multiple myeloma cells. Br J Haematol 138 (2007) 783-791
    • (2007) Br J Haematol , vol.138 , pp. 783-791
    • Hideshima, T.1    Catley, L.2    Raje, N.3
  • 139
    • 0037013205 scopus 로고    scopus 로고
    • Signal pathways involved in activation of p70S6K and phosphorylation of 4E-BP1 following exposure of multiple myeloma tumor cells to interleukin-6
    • Shi Y., Hsu J.H., Hu L., et al. Signal pathways involved in activation of p70S6K and phosphorylation of 4E-BP1 following exposure of multiple myeloma tumor cells to interleukin-6. J Biol Chem 277 (2002) 15712-15720
    • (2002) J Biol Chem , vol.277 , pp. 15712-15720
    • Shi, Y.1    Hsu, J.H.2    Hu, L.3
  • 140
    • 0037179847 scopus 로고    scopus 로고
    • Role of the phosphatidylinositol 3-kinase/Akt and mTOR/P70S6-kinase pathways in the proliferation and apoptosis in multiple myeloma
    • Pene F., Claessens Y.E., Muller O., et al. Role of the phosphatidylinositol 3-kinase/Akt and mTOR/P70S6-kinase pathways in the proliferation and apoptosis in multiple myeloma. Oncogene 21 (2002) 6587-6597
    • (2002) Oncogene , vol.21 , pp. 6587-6597
    • Pene, F.1    Claessens, Y.E.2    Muller, O.3
  • 141
    • 17444440115 scopus 로고    scopus 로고
    • Rapamycin sensitizes multiple myeloma cells to apoptosis induced by dexamethasone
    • Stromberg T., Dimberg A., Hammarberg A., et al. Rapamycin sensitizes multiple myeloma cells to apoptosis induced by dexamethasone. Blood 103 (2004) 3138-3147
    • (2004) Blood , vol.103 , pp. 3138-3147
    • Stromberg, T.1    Dimberg, A.2    Hammarberg, A.3
  • 142
    • 0036735346 scopus 로고    scopus 로고
    • Enhanced sensitivity of multiple myeloma cells containing PTEN mutations to CCI-779
    • Shi Y., Gera J., Hu L., et al. Enhanced sensitivity of multiple myeloma cells containing PTEN mutations to CCI-779. Cancer Res 62 (2002) 5027-5034
    • (2002) Cancer Res , vol.62 , pp. 5027-5034
    • Shi, Y.1    Gera, J.2    Hu, L.3
  • 143
    • 10244260355 scopus 로고    scopus 로고
    • Combination of the mTOR inhibitor rapamycin and Revlimid™(CC-5013) has synergistic activity in multiple myeloma
    • Raje N., Kumar S., Hideshima T., et al. Combination of the mTOR inhibitor rapamycin and Revlimid™(CC-5013) has synergistic activity in multiple myeloma. Blood 104 (2004) 4188-4193
    • (2004) Blood , vol.104 , pp. 4188-4193
    • Raje, N.1    Kumar, S.2    Hideshima, T.3
  • 144
    • 10244229652 scopus 로고    scopus 로고
    • In vivo antitumor effects of the mTOR inhibitor CCI-779 against human multiple myeloma cells in a xenograft model
    • Frost P., Moatamed F., Hoang B., et al. In vivo antitumor effects of the mTOR inhibitor CCI-779 against human multiple myeloma cells in a xenograft model. Blood 104 (2004) 4181-4187
    • (2004) Blood , vol.104 , pp. 4181-4187
    • Frost, P.1    Moatamed, F.2    Hoang, B.3
  • 145
    • 34147104488 scopus 로고    scopus 로고
    • AKT activity regulates the ability of mTOR inhibitors to prevent angiogenesis and VEGF expression in multiple myeloma cells
    • Frost P., Shi Y., Hoang B., et al. AKT activity regulates the ability of mTOR inhibitors to prevent angiogenesis and VEGF expression in multiple myeloma cells. Oncogene 26 (2007) 2255-2262
    • (2007) Oncogene , vol.26 , pp. 2255-2262
    • Frost, P.1    Shi, Y.2    Hoang, B.3
  • 146
    • 2942666279 scopus 로고    scopus 로고
    • G3139, a Bcl-2 antisense oligodeoxynucleotide, induces clinical responses in VAD refractory myeloma
    • van de Donk N.W., de Weerdt O., Veth G., et al. G3139, a Bcl-2 antisense oligodeoxynucleotide, induces clinical responses in VAD refractory myeloma. Leukemia 18 (2004) 1078-1084
    • (2004) Leukemia , vol.18 , pp. 1078-1084
    • van de Donk, N.W.1    de Weerdt, O.2    Veth, G.3
  • 147
    • 23044452536 scopus 로고    scopus 로고
    • Phase II study of G3139, a Bcl-2 antisense oligonucleotide, in combination with dexamethasone and thalidomide in relapsed multiple myeloma patients
    • Badros A.Z., Goloubeva O., Rapoport A.P., et al. Phase II study of G3139, a Bcl-2 antisense oligonucleotide, in combination with dexamethasone and thalidomide in relapsed multiple myeloma patients. J Clin Oncol 23 (2005) 4089-4099
    • (2005) J Clin Oncol , vol.23 , pp. 4089-4099
    • Badros, A.Z.1    Goloubeva, O.2    Rapoport, A.P.3
  • 148
    • 34250770481 scopus 로고    scopus 로고
    • ABT-737, an inhibitor of Bcl-2 family proteins, is a potent inducer of apoptosis in multiple myeloma cells
    • Kline M.P., Rajkumar S.V., Timm M.M., et al. ABT-737, an inhibitor of Bcl-2 family proteins, is a potent inducer of apoptosis in multiple myeloma cells. Leukemia 21 (2007) 1549-1560
    • (2007) Leukemia , vol.21 , pp. 1549-1560
    • Kline, M.P.1    Rajkumar, S.V.2    Timm, M.M.3
  • 149
    • 34147142477 scopus 로고    scopus 로고
    • A novel Bcl-2/Bcl-X(L)/Bcl-w inhibitor ABT-737 as therapy in multiple myeloma
    • Chauhan D., Velankar M., Brahmandam M., et al. A novel Bcl-2/Bcl-X(L)/Bcl-w inhibitor ABT-737 as therapy in multiple myeloma. Oncogene 26 (2007) 2374-2380
    • (2007) Oncogene , vol.26 , pp. 2374-2380
    • Chauhan, D.1    Velankar, M.2    Brahmandam, M.3
  • 150
    • 33846884216 scopus 로고    scopus 로고
    • The Bcl-2 family protein inhibitor, ABT-737, has substantial antimyeloma activity and shows synergistic effect with dexamethasone and melphalan
    • Trudel S., Stewart A.K., Li Z., et al. The Bcl-2 family protein inhibitor, ABT-737, has substantial antimyeloma activity and shows synergistic effect with dexamethasone and melphalan. Clin Cancer Res 13 (2007) 621-629
    • (2007) Clin Cancer Res , vol.13 , pp. 621-629
    • Trudel, S.1    Stewart, A.K.2    Li, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.