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Volumn 6, Issue 3, 2002, Pages 301-324

Novel biologically based therapeutic strategies in myeloma

Author keywords

[No Author keywords available]

Indexed keywords

2 METHOXYESTRADIOL; AE 941; ARSENIC TRIOXIDE; BETA LAPACHONE; BORTEZOMIB; DEXAMETHASONE; GLUTARIMIDE DERIVATIVE; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE INHIBITOR; IMMUNOMODULATING AGENT; LENALIDOMIDE; LONAFARNIB; MYELOMA ANTIGEN; OBLIMERSEN; PACLITAXEL; PHOSPHODIESTERASE INHIBITOR; PROTEASOME INHIBITOR; PROTEIN FARNESYLTRANSFERASE INHIBITOR; S 3 AMINOPHTHALIMIDOGLUTARIMIDE; TELOMERASE; THALIDOMIDE; THALIDOMIDE DERIVATIVE; TIPIFARNIB; TUMOR ANTIGEN; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; VASCULOTROPIN; VATALANIB; ANTINEOPLASTIC AGENT;

EID: 0036760132     PISSN: 11270020     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1468-0734.2002.00082.x     Document Type: Review
Times cited : (10)

References (169)
  • 2
    • 0032929769 scopus 로고    scopus 로고
    • Total therapy with tandem transplants for newly diagnosed multiple myeloma
    • Barlogie B, Jagannath S, Desikan KR, et al. Total therapy with tandem transplants for newly diagnosed multiple myeloma. Blood, 93: 55-65, 1999.
    • (1999) Blood , vol.93 , pp. 55-65
    • Barlogie, B.1    Jagannath, S.2    Desikan, K.R.3
  • 3
    • 0032521131 scopus 로고    scopus 로고
    • The 86-kD subunit of Ku autoantigen mediates homotypic and heterotypic adhesion of multiple myeloma cells
    • Teoh G, Urashima M, Greenfield EA, et al. The 86-kD subunit of Ku autoantigen mediates homotypic and heterotypic adhesion of multiple myeloma cells. J Clin Invest, 101: 1379-1388, 1998.
    • (1998) J Clin Invest , vol.101 , pp. 1379-1388
    • Teoh, G.1    Urashima, M.2    Greenfield, E.A.3
  • 4
    • 0034544469 scopus 로고    scopus 로고
    • Ku86 variant expression and function in multiple myeloma cells is associated with increased sensitivity to DNA damage
    • Tai Y-T, Teoh G, Lin B, et al. Ku86 variant expression and function in multiple myeloma cells is associated with increased sensitivity to DNA damage. J Immunol, 165: 6347-6355, 2000.
    • (2000) J Immunol , vol.165 , pp. 6347-6355
    • Tai, Y.-T.1    Teoh, G.2    Lin, B.3
  • 5
    • 0036189567 scopus 로고    scopus 로고
    • Translocation of Ku86/Ku70 to the multiple myeloma cell membrane: Functional implications
    • Tai Y-T, Podar K, Kraeft S-K, et al. Translocation of Ku86/Ku70 to the multiple myeloma cell membrane: Functional implications. Exp Hematol, 30: 212-220, 2002.
    • (2002) Exp Hematol , vol.30 , pp. 212-220
    • Tai, Y.-T.1    Podar, K.2    Kraeft, S.-K.3
  • 6
    • 0030576534 scopus 로고    scopus 로고
    • Ku86-deficient mice exhibit severe combined immunodeficiency and defective processing of V(D)J recombination intermediates
    • Zhu C, Bogue MA, Lim DS, et al. Ku86-deficient mice exhibit severe combined immunodeficiency and defective processing of V(D)J recombination intermediates. Cell, 86: 379-389, 1996.
    • (1996) Cell , vol.86 , pp. 379-389
    • Zhu, C.1    Bogue, M.A.2    Lim, D.S.3
  • 7
    • 0032522564 scopus 로고    scopus 로고
    • Ku 80 is required for immunoglobulin isotype switching
    • Casellas R, Nussenzweig A, Wuerffel R, et al. Ku80 is required for immunoglobulin isotype switching. EMBO J 17: 2404-2411, 1998.
    • (1998) EMBO J , vol.17 , pp. 2404-2411
    • Casellas, R.1    Nussenzweig, A.2    Wuerffel, R.3
  • 8
    • 0034732239 scopus 로고    scopus 로고
    • DNA repair protein Ku80 suppresses chromosomal aberrations and malignant transformation
    • Difilippantonio MJ, Zhu J, Chen HT, et al. DNA repair protein Ku80 suppresses chromosomal aberrations and malignant transformation. Nature, 404: 510-514, 2000.
    • (2000) Nature , vol.404 , pp. 510-514
    • Difilippantonio, M.J.1    Zhu, J.2    Chen, H.T.3
  • 9
    • 0024391288 scopus 로고
    • Response of purified myeloma cells to hematopoietic growth factors
    • Anderson KC, Jones RC, Morimoto C, et al. Response of purified myeloma cells to hematopoietic growth factors. Blood, 73: 1915-1924, 1989.
    • (1989) Blood , vol.73 , pp. 1915-1924
    • Anderson, K.C.1    Jones, R.C.2    Morimoto, C.3
  • 10
    • 0026793868 scopus 로고
    • Role of interleukin-6 in the growth of myeloma derived cell lines
    • Barut BA, Zon LI, Cochran MK, et al. Role of interleukin-6 in the growth of myeloma derived cell lines. Leukemia Res, 16: 951-959, 1992.
    • (1992) Leukemia Res , vol.16 , pp. 951-959
    • Barut, B.A.1    Zon, L.I.2    Cochran, M.K.3
  • 11
    • 0026590187 scopus 로고
    • Lack of a role of interleukin-11 in the growth of multiple myeloma
    • Paul PD, Barut BA, Cochran MK, et al. Lack of a role of interleukin-11 in the growth of multiple myeloma. Leukemia Res, 16: 247-252, 1992.
    • (1992) Leukemia Res , vol.16 , pp. 247-252
    • Paul, P.D.1    Barut, B.A.2    Cochran, M.K.3
  • 12
    • 0030026437 scopus 로고    scopus 로고
    • Transforming growth factor β1: Differential effects on multiple myeloma versus normal B cells
    • Urashima M, Ogata A, Chauhan D, et al. Transforming growth factor β1: Differential effects on multiple myeloma versus normal B cells. Blood, 87: 1928-1938, 1996.
    • (1996) Blood , vol.87 , pp. 1928-1938
    • Urashima, M.1    Ogata, A.2    Chauhan, D.3
  • 13
    • 0028799055 scopus 로고
    • Oncostatin M induces association of GRB2 with Janus kinase JAK2 in multiple myeloma cells
    • Chauhan D, Kharbanda SM, Ogata A, et al. Oncostatin M induces association of GRB2 with Janus kinase JAK2 in multiple myeloma cells. J Exp Med, 182: 1801-1806, 1995.
    • (1995) J Exp Med , vol.182 , pp. 1801-1806
    • Chauhan, D.1    Kharbanda, S.M.2    Ogata, A.3
  • 14
    • 0035958517 scopus 로고    scopus 로고
    • The role of tumor necrosis factor α in the pathophysiology of multiple myeloma: Therapeutic applications
    • Hideshima T, Chauhan D, Schlossman R, et al. The role of tumor necrosis factor α in the pathophysiology of multiple myeloma: Therapeutic applications. Oncogene, 20: 4519-4527, 2001.
    • (2001) Oncogene , vol.20 , pp. 4519-4527
    • Hideshima, T.1    Chauhan, D.2    Schlossman, R.3
  • 15
    • 0035880256 scopus 로고    scopus 로고
    • Vascular endothelial growth factor triggered signaling cascades mediating multiple myeloma cell growth and migration
    • Podar K, Tai YT, Davies FE, et al. Vascular endothelial growth factor triggered signaling cascades mediating multiple myeloma cell growth and migration. Blood, 98: 428-435, 2001.
    • (2001) Blood , vol.98 , pp. 428-435
    • Podar, K.1    Tai, Y.T.2    Davies, F.E.3
  • 16
    • 0029837401 scopus 로고    scopus 로고
    • Interleukin-6 promotes multiple myeloma cell growth via phosphorylation of retinoblastoma protein
    • Urashima M, Ogata A, Chauhan D, et al. Interleukin-6 promotes multiple myeloma cell growth via phosphorylation of retinoblastoma protein. Blood, 88: 2219-2227, 1996.
    • (1996) Blood , vol.88 , pp. 2219-2227
    • Urashima, M.1    Ogata, A.2    Chauhan, D.3
  • 17
    • 0031225483 scopus 로고    scopus 로고
    • Interleukin-6 triggers cell growth via the ras dependent mitogen activated protein kinase (MAPK) cascade
    • Ogata A, Chauhan D, Teoh G, et al. Interleukin-6 triggers cell growth via the ras dependent mitogen activated protein kinase (MAPK) cascade. J Immunol, 159: 2212-2221, 1997.
    • (1997) J Immunol , vol.159 , pp. 2212-2221
    • Ogata, A.1    Chauhan, D.2    Teoh, G.3
  • 18
    • 0030948787 scopus 로고    scopus 로고
    • Blockade of MAPK signaling in interleukin-6 independent multiple myeloma cells
    • Ogata A, Chauhan D, Urashima M, et al. Blockade of MAPK signaling in interleukin-6 independent multiple myeloma cells. Clin Cancer Res, 3: 1017-1022, 1997.
    • (1997) Clin Cancer Res , vol.3 , pp. 1017-1022
    • Ogata, A.1    Chauhan, D.2    Urashima, M.3
  • 19
    • 0029994074 scopus 로고    scopus 로고
    • Therapeutic strategies for inhibition of interleukin-6 mediated multiple myeloma cell growth
    • Ogata A, Anderson KC. Therapeutic strategies for inhibition of interleukin-6 mediated multiple myeloma cell growth. Leukemia Res, 20: 303-307, 1996.
    • (1996) Leukemia Res , vol.20 , pp. 303-307
    • Ogata, A.1    Anderson, K.C.2
  • 20
    • 0030864876 scopus 로고    scopus 로고
    • Dexamethasone induces apoptosis of multiple myeloma cells in a JNK/SAP kinase independent mechanism
    • Chauhan D, Pandey P, Ogata A, et al. Dexamethasone induces apoptosis of multiple myeloma cells in a JNK/SAP kinase independent mechanism. Oncogene, 15: 837-843, 1997.
    • (1997) Oncogene , vol.15 , pp. 837-843
    • Chauhan, D.1    Pandey, P.2    Ogata, A.3
  • 21
    • 0033581897 scopus 로고    scopus 로고
    • RAFTK/PYK-2 dependent and independent apoptosis in multiple myeloma
    • Chauhan D, Hideshima T, Pandey P, et al. RAFTK/PYK-2 dependent and independent apoptosis in multiple myeloma. Oncogene, 18: 6733-6740, 1999.
    • (1999) Oncogene , vol.18 , pp. 6733-6740
    • Chauhan, D.1    Hideshima, T.2    Pandey, P.3
  • 22
    • 15144349717 scopus 로고    scopus 로고
    • Cytochrome-c dependent and independent induction of apoptosis in multiple myeloma
    • Chauhan D, Pandey P, Ogata A, et al. Cytochrome-c dependent and independent induction of apoptosis in multiple myeloma. J Biol Chem, 272: 29995-29997, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 29995-29997
    • Chauhan, D.1    Pandey, P.2    Ogata, A.3
  • 23
    • 0035816553 scopus 로고    scopus 로고
    • Apaf-1/cytochrome c independent and Smac dependent induction of apoptosis in multiple myeloma cells
    • Chauhan D, Rosen S, Reed JR, et al. Apaf-1/cytochrome c independent and Smac dependent induction of apoptosis in multiple myeloma cells. J. Biol Cbem, 276: 24453-24456, 2001.
    • (2001) J Biol Cbem , vol.276 , pp. 24453-24456
    • Chauhan, D.1    Rosen, S.2    Reed, J.R.3
  • 24
    • 0031029911 scopus 로고    scopus 로고
    • Interleukin-6 inhibits Fas-induced apoptosis and SAP kinase activation in multiple myeloma
    • Chauhan D, Kharbanda S, Ogata A, et al. Interleukin-6 inhibits Fas-induced apoptosis and SAP kinase activation in multiple myeloma. Blood, 89: 227-234, 1997.
    • (1997) Blood , vol.89 , pp. 227-234
    • Chauhan, D.1    Kharbanda, S.2    Ogata, A.3
  • 25
    • 0031010127 scopus 로고    scopus 로고
    • Interleukin-6 overcomes p21WAF1 upregulation and G1 growth arrest induced by dexamethasone and interferon in multiple myeloma cells
    • Urashima M, Teoh G, Chauhan D, et al. Interleukin-6 overcomes p21WAF1 upregulation and G1 growth arrest induced by dexamethasone and interferon in multiple myeloma cells. Blood, 90: 279-289, 1997.
    • (1997) Blood , vol.90 , pp. 279-289
    • Urashima, M.1    Teoh, G.2    Chauhan, D.3
  • 26
    • 0034623059 scopus 로고    scopus 로고
    • SHP2 mediates the protective effect of Interleukin-6 against dexamethasone-induced apoptosis in multiple myeloma cells
    • Chauhan D, Pandey P, Hideshima T, et al. SHP2 mediates the protective effect of Interleukin-6 against dexamethasone-induced apoptosis in multiple myeloma cells. Biol Chem, 275: 27845-27850, 2000.
    • (2000) Biol Chem , vol.275 , pp. 27845-27850
    • Chauhan, D.1    Pandey, P.2    Hideshima, T.3
  • 27
    • 0035086995 scopus 로고    scopus 로고
    • Apoptosis in multiple myeloma: Therapeutic implications
    • Chauhan D, Anderson KC. Apoptosis in multiple myeloma: Therapeutic implications. Apoptosis, 6: 47-56, 2001.
    • (2001) Apoptosis , vol.6 , pp. 47-56
    • Chauhan, D.1    Anderson, K.C.2
  • 28
    • 85047699977 scopus 로고    scopus 로고
    • Identification of genes regulated by dexamethasone in multiple myeloma cells using oligonucleotide arrays
    • Chauhan D, Auclair D, Robinson EK, et al. Identification of genes regulated by dexamethasone in multiple myeloma cells using oligonucleotide arrays. Oncogene, 21: 1346-1358, 2002.
    • (2002) Oncogene , vol.21 , pp. 1346-1358
    • Chauhan, D.1    Auclair, D.2    Robinson, E.K.3
  • 29
    • 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: 5991-6000, 2001.
    • (2001) Oncogene , vol.20 , pp. 5991-6000
    • Hideshima, T.1    Nakamura, N.2    Chauhan, D.3
  • 30
    • 0032903871 scopus 로고    scopus 로고
    • Bone marrow angiogenesis and mast cell density increase simultaneously with progression of human multiple myeloma
    • Ribatti D, Vacca A, Nico B, et al. Bone marrow angiogenesis and mast cell density increase simultaneously with progression of human multiple myeloma. Br J Cancer, 79: 451-455, 1999.
    • (1999) Br J Cancer , vol.79 , pp. 451-455
    • Ribatti, D.1    Vacca, A.2    Nico, B.3
  • 31
    • 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: 3064-3073, 1999.
    • (1999) Blood , vol.93 , pp. 3064-3073
    • Vacca, A.1    Ribatti, D.2    Presta, M.3
  • 33
    • 0032748385 scopus 로고    scopus 로고
    • Antitumor activity of thalidomide in refractory multiple myeloma
    • Singhal S, Mehta J, Desikan R, et al. Antitumor activity of thalidomide in refractory multiple myeloma. N Engl J Med, 341: 1566-1571, 1999.
    • (1999) N Engl J Med , vol.341 , pp. 1566-1571
    • Singhal, S.1    Mehta, J.2    Desikan, R.3
  • 34
    • 0032708238 scopus 로고    scopus 로고
    • Thalidomide-A revival story
    • Raje N, Anderson KC. Thalidomide-A revival story. N Engl J Med, 341: 1606-1609, 1999.
    • (1999) N Engl J Med , vol.341 , pp. 1606-1609
    • Raje, N.1    Anderson, K.C.2
  • 35
    • 0032920883 scopus 로고    scopus 로고
    • Free radical mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity
    • Parman T, Wiley MJ, Wells PG. Free radical mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity. Nat Med, 5: 582-585, 1999.
    • (1999) Nat Med , vol.5 , pp. 582-585
    • Parman, T.1    Wiley, M.J.2    Wells, P.G.3
  • 36
    • 0029925419 scopus 로고    scopus 로고
    • Thalidomide selectively modulates the density of cell surface molecules involved in the adhesion cascade
    • Geitz H, Handt S, Zwingengerger K. Thalidomide selectively modulates the density of cell surface molecules involved in the adhesion cascade. Immunopharmacology, 32: 213-221, 1996.
    • (1996) Immunopharmacology , vol.32 , pp. 213-221
    • Geitz, H.1    Handt, S.2    Zwingengerger, K.3
  • 37
    • 0031985198 scopus 로고    scopus 로고
    • Multiple myeloma: Increasing evidence for a multistep transformation process
    • Hallek M, Bergsagel PL, Anderson KC. Multiple myeloma: Increasing evidence for a multistep transformation process. Blood, 91: 3-21, 1998.
    • (1998) Blood , vol.91 , pp. 3-21
    • Hallek, M.1    Bergsagel, P.L.2    Anderson, K.C.3
  • 38
    • 0033083962 scopus 로고    scopus 로고
    • Expression of vascular endothelial growth factor and its receptor in hematological malignancies
    • Bellamy W, Richter L, Frutiger Y, et al. Expression of vascular endothelial growth factor and its receptor in hematological malignancies. Cancer Res, 59: 728-733, 1999.
    • (1999) Cancer Res , vol.59 , pp. 728-733
    • Bellamy, W.1    Richter, L.2    Frutiger, Y.3
  • 39
    • 0032100486 scopus 로고    scopus 로고
    • Thalidomide costimulates primary human T lymphocytes, preferentially inducing proliferation, cytokine production, and cytotoxic responses in the CD8+ subsets
    • Haslett PAJ, Corral LG, Albert M, et al. Thalidomide costimulates primary human T lymphocytes, preferentially inducing proliferation, cytokine production, and cytotoxic responses in the CD8+ subsets. J Exp Med, 187: 1885-1892, 1998.
    • (1998) J Exp Med , vol.187 , pp. 1885-1892
    • Haslett, P.A.J.1    Corral, L.G.2    Albert, M.3
  • 40
    • 0033168605 scopus 로고    scopus 로고
    • Differential cytokine modulation and T cell activation by two distinct classes of thalidomide analogs that are potent inhibitors of TNFα
    • Corral LG, Haslet PAJ, Muller GW, et al. Differential cytokine modulation and T cell activation by two distinct classes of thalidomide analogs that are potent inhibitors of TNFα. J Immunol, 163: 380-386, 1999.
    • (1999) J Immunol , vol.163 , pp. 380-386
    • Corral, L.G.1    Haslet, P.A.J.2    Muller, G.W.3
  • 41
    • 0034331194 scopus 로고    scopus 로고
    • Thalidomide and its analogs overcome drug resistance of human multiple myeloma cells to conventional therapy
    • Hideshima T, Chauhan D, Shima Y, et al. Thalidomide and its analogs overcome drug resistance of human multiple myeloma cells to conventional therapy. Blood, 96: 2943-2950, 2000.
    • (2000) Blood , vol.96 , pp. 2943-2950
    • Hideshima, T.1    Chauhan, D.2    Shima, Y.3
  • 42
    • 0035195019 scopus 로고    scopus 로고
    • Adhesion of human multiple myeloma cell lines to bone marrow stromal cells stimulates vascular endothelial growth factor secretion: Therapeutic applications
    • Gupta D, Treon SP, Shima Y, et al. Adhesion of human multiple myeloma cell lines to bone marrow stromal cells stimulates vascular endothelial growth factor secretion: Therapeutic applications. Leukemia, 15: 1950-1961, 2001.
    • (2001) Leukemia , vol.15 , pp. 1950-1961
    • Gupta, D.1    Treon, S.P.2    Shima, Y.3
  • 43
    • 0035412366 scopus 로고    scopus 로고
    • Thalidomide and immunomodulatory derivatives augment natural killer cell cytotoxicity in multiple myeloma
    • Davies FE, Lentzsch S, Young G, et al. Thalidomide and immunomodulatory derivatives augment natural killer cell cytotoxicity in multiple myeloma. Blood, 98: 210-216, 2001.
    • (2001) Blood , vol.98 , pp. 210-216
    • Davies, F.E.1    Lentzsch, S.2    Young, G.3
  • 44
    • 0034999619 scopus 로고    scopus 로고
    • Tumor cell expression of CD59 is associated with resistance to CD20 serotherapy in B cell malignancies
    • Treon SP, Mitsiades C, Mitsiades N, et al. Tumor cell expression of CD59 is associated with resistance to CD20 serotherapy in B cell malignancies. J Immunotherapy, 24: 263-271, 2001.
    • (2001) J Immunotherapy , vol.24 , pp. 263-271
    • Treon, S.P.1    Mitsiades, C.2    Mitsiades, N.3
  • 45
    • 0036839013 scopus 로고    scopus 로고
    • Immunomodulatory derivative of thalidomide CC-5013 overcomes drug resistance and is well tolerated in patients with relapsed multiple myeloma
    • in press
    • Richardson PG, Schlossman RL, Weller E, et al. Immunomodulatory derivative of thalidomide CC-5013 overcomes drug resistance and is well tolerated in patients with relapsed multiple myeloma. Blood, in press, 2002.
    • (2002) Blood
    • Richardson, P.G.1    Schlossman, R.L.2    Weller, E.3
  • 46
    • 0037089554 scopus 로고    scopus 로고
    • S-3-amino-phthalimido-glutarimide inhibits angiogenesis and growth of B-cell neoplasias in mice
    • Lentzsch S, Rogers MS, LeBlanc R, et al. S-3-amino-phthalimido-glutarimide inhibits angiogenesis and growth of B-cell neoplasias in mice. Cancer Res, 62: 2300-2305, 2002.
    • (2002) Cancer Res , vol.62 , pp. 2300-2305
    • Lentzsch, S.1    Rogers, M.S.2    LeBlanc, R.3
  • 47
    • 0029807944 scopus 로고    scopus 로고
    • How proteolysis drives the cell cycle
    • King RW, Deshaies RJ, Peters JM, et al. How proteolysis drives the cell cycle. Science, 274: 1652-1659, 1996.
    • (1996) Science , vol.274 , pp. 1652-1659
    • King, R.W.1    Deshaies, R.J.2    Peters, J.M.3
  • 48
    • 0032481131 scopus 로고    scopus 로고
    • Prostate carcinoma death resulting from inhibition of proteasome activity is independent of functional Bcl-2 and p53
    • Herrmann JL, Briones F, Brisbay S, et al. Prostate carcinoma death resulting from inhibition of proteasome activity is independent of functional Bcl-2 and p53. Oncogene, 17: 2889-2899, 1998.
    • (1998) Oncogene , vol.17 , pp. 2889-2899
    • Herrmann, J.L.1    Briones, F.2    Brisbay, S.3
  • 49
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway. Involvement in tumor survival and progression
    • Li B, Dou Q. Bax degradation by the ubiquitin/proteasome-dependent pathway. Involvement in tumor survival and progression. Proc Natl Acad Sci USA, 97: 3850-3855, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3850-3855
    • Li, B.1    Dou, Q.2
  • 50
    • 0027980321 scopus 로고
    • The ubiquitin proteasome pathway is required for processing the NFκB precursor protein and the activation of NFκB
    • Palombella VJ, Rando OJ, Goldberg AL, et al. The ubiquitin proteasome pathway is required for processing the NFκB precursor protein and the activation of NFκB. Cell, 78: 773-785, 1994.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3
  • 52
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski RZ, Eswara JR, Lafond-Walker A, et al. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res, 58: 4342-4348, 1998.
    • (1998) Cancer Res , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3
  • 53
    • 0032885416 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 in cancer therapy
    • Teicher BA, Ara G, Herbst R, et al. The proteasome inhibitor PS-341 in cancer therapy. Clin Cancer Res, 5: 2638-2645, 1999.
    • (1999) Clin Cancer Res , vol.5 , pp. 2638-2645
    • Teicher, B.A.1    Ara, G.2    Herbst, R.3
  • 54
    • 0002561874 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 is effective as a anti-angiogenic agent in the treatment of human pancreatic carcinoma via inhibition of NFκB and subsequent inhibition of vascular endothelial growth factor production
    • Harbison MT, Bruns CJ, Bold RJ, et al. Proteasome inhibitor PS-341 is effective as a anti-angiogenic agent in the treatment of human pancreatic carcinoma via inhibition of NFκB and subsequent inhibition of vascular endothelial growth factor production. Proc Am Assoc Cancer Res, 41: 71, 2000.
    • (2000) Proc Am Assoc Cancer Res , vol.41 , pp. 71
    • Harbison, M.T.1    Bruns, C.J.2    Bold, R.J.3
  • 55
    • 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: 3071-3076, 2001.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 56
    • 0030041147 scopus 로고    scopus 로고
    • Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NFkB
    • Chauhan D, Uchiyama H, Akbarali Y, et al. Multiple myeloma cell adhesion-induced interleukin-6 expression in bone marrow stromal cells involves activation of NFkB. Blood, 87: 1104-1112, 1996.
    • (1996) Blood , vol.87 , pp. 1104-1112
    • Chauhan, D.1    Uchiyama, H.2    Akbarali, Y.3
  • 57
    • 0003216241 scopus 로고    scopus 로고
    • Phase II study of PS-341, a novel proteasome inhibitor, alone or in combination with dexamethasone in patients with multiple myeloma who have relapsed following frontline therapy and are refractory to their most recent therapy
    • Richardson PG, Berenson J, Irwin D, et al. Phase II study of PS-341, a novel proteasome inhibitor, alone or in combination with dexamethasone in patients with multiple myeloma who have relapsed following frontline therapy and are refractory to their most recent therapy. Blood, 98: 774a, 2002.
    • (2002) Blood , vol.98
    • Richardson, P.G.1    Berenson, J.2    Irwin, D.3
  • 58
    • 18544367201 scopus 로고    scopus 로고
    • NF-κB as a therapeutic target in multiple myeloma
    • in press
    • Hideshima T, Chauhan D, Richardson P, et al. NF-κB as a therapeutic target in multiple myeloma. J Biol Chem, in press, 2002.
    • (2002) J Biol Chem
    • Hideshima, T.1    Chauhan, D.2    Richardson, P.3
  • 59
    • 0023227925 scopus 로고
    • Production of lymphotoxin, a bone resorbing cytokine, by cultured human myeloma cells
    • Garrett R, Durie B, Nedwin G, et al. Production of lymphotoxin, a bone resorbing cytokine, by cultured human myeloma cells. N Engl J Med, 317: 526-532, 1987.
    • (1987) N Engl J Med , vol.317 , pp. 526-532
    • Garrett, R.1    Durie, B.2    Nedwin, G.3
  • 60
    • 0024419152 scopus 로고
    • Production of cytokines by bone marrow cells obtained from patients with multiple myeloma
    • Lichtenstein A, Berenson J, Norman D, et al. Production of cytokines by bone marrow cells obtained from patients with multiple myeloma. Blood, 74: 1266-1273, 1989.
    • (1989) Blood , vol.74 , pp. 1266-1273
    • Lichtenstein, A.1    Berenson, J.2    Norman, D.3
  • 61
    • 0032589103 scopus 로고    scopus 로고
    • Expression of interleukin-1β and tumor necrosis factor α in plasma cells from patients with multiple myeloma
    • Sati H, Greaves M, Apperley J, et al. Expression of interleukin-1β and tumor necrosis factor α in plasma cells from patients with multiple myeloma. Br J Haematol, 104: 350-357, 1999.
    • (1999) Br J Haematol , vol.104 , pp. 350-357
    • Sati, H.1    Greaves, M.2    Apperley, J.3
  • 62
    • 0033868516 scopus 로고    scopus 로고
    • High producer haplotypes of tumor necrosis factor α and lymphotoxin are associated with an increased risk of myeloma and have an improved progression free survival after treatment
    • Davies FE, Rollinson S, Rawstron A, et al. High producer haplotypes of tumor necrosis factor α and lymphotoxin are associated with an increased risk of myeloma and have an improved progression free survival after treatment. J Clin Oncol, 18: 2843-2851, 2000.
    • (2000) J Clin Oncol , vol.18 , pp. 2843-2851
    • Davies, F.E.1    Rollinson, S.2    Rawstron, A.3
  • 63
    • 0024355425 scopus 로고
    • A multiple cytokine and second messenger responsive element in the enhancer of the human interleukin-6 gene: Similarities with c-fos gene regulation
    • Ray A, Sassone-Corsi S, Sehgal P. A multiple cytokine and second messenger responsive element in the enhancer of the human interleukin-6 gene: Similarities with c-fos gene regulation. Mol Cell Biol, 9: 5537-5547, 1989.
    • (1989) Mol Cell Biol , vol.9 , pp. 5537-5547
    • Ray, A.1    Sassone-Corsi, S.2    Sehgal, P.3
  • 64
    • 0034119907 scopus 로고    scopus 로고
    • NFκB regulates VCAM-1 expression on fibroblast-like synoviocytes
    • Li P, Sanz I, O'Keefe RJ, et al. NFκB regulates VCAM-1 expression on fibroblast-like synoviocytes. J Immunol, 164: 5990-5997, 2000.
    • (2000) J Immunol , vol.164 , pp. 5990-5997
    • Li, P.1    Sanz, I.2    O'Keefe, R.J.3
  • 65
    • 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 T, et al. Vascular endothelial growth factor and interleukin-6 in paracrine tumor stromal cell interactions in multiple myeloma. Blood, 95: 2630-2636, 2000.
    • (2000) Blood , vol.95 , pp. 2630-2636
    • Dankbar, B.1    Padro, T.2    Leo, T.3
  • 66
    • 18544377343 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with β1 integrin- and phosphatidylinositol 3-kinase-dependent PKCα activation
    • Podar K, Tai YT, Lin BK, et al. Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with β1 integrin- and phosphatidylinositol 3-kinase-dependent PKCα activation. J Biol Chem, 277: 7875-7881, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 7875-7881
    • Podar, K.1    Tai, Y.T.2    Lin, B.K.3
  • 67
    • 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: 5019-5026, 2002.
    • (2002) Cancer Res , vol.62 , pp. 5019-5026
    • Lin, B.1    Podar, K.2    Gupta, D.3
  • 68
    • 0011763774 scopus 로고    scopus 로고
    • 2-Methoxyestradiol inhibits growth of multiple myeloma cells in the bone marrow microenvironment
    • in press
    • Chauhan D, Catley L, Hideshima T, et al. 2-Methoxyestradiol inhibits growth of multiple myeloma cells in the bone marrow microenvironment. Blood, in press 2002.
    • (2002) Blood
    • Chauhan, D.1    Catley, L.2    Hideshima, T.3
  • 69
    • 0035038845 scopus 로고    scopus 로고
    • History of the development of arsenic derivatives in cancer therapy
    • Waxman S, Anderson KC. History of the development of arsenic derivatives in cancer therapy. Oncologist, 6 (Suppl. 2): 3-10, 2001.
    • (2001) Oncologist , vol.6 , Issue.SUPPL. 2 , pp. 3-10
    • Waxman, S.1    Anderson, K.C.2
  • 70
    • 0033105268 scopus 로고    scopus 로고
    • Arsenic trioxide and melarsoprol induce apoptosis in plasma cell lines and in plasma cells from myeloma patients
    • Rousselot P, Labaume S, Marolleau J-P, et al. Arsenic trioxide and melarsoprol induce apoptosis in plasma cell lines and in plasma cells from myeloma patients. Cancer Res, 59: 1041-1048, 1999.
    • (1999) Cancer Res , vol.59 , pp. 1041-1048
    • Rousselot, P.1    Labaume, S.2    Marolleau, J.-P.3
  • 71
    • 0034212785 scopus 로고    scopus 로고
    • Arsenic trioxide-mediated growth inhibition in MC/CAR myeloma cells via cell cycle arrest in association with induction of cyclin-dependent kinase inhibitor, p21, and apoptosis
    • Park WH, Seol JG, Kim ES, et al. Arsenic trioxide-mediated growth inhibition in MC/CAR myeloma cells via cell cycle arrest in association with induction of cyclin-dependent kinase inhibitor, p21, and apoptosis. Cancer Res, 60: 3065-3071, 2000.
    • (2000) Cancer Res , vol.60 , pp. 3065-3071
    • Park, W.H.1    Seol, J.G.2    Kim, E.S.3
  • 72
    • 0035133852 scopus 로고    scopus 로고
    • Co-biomodulation with arsenic trioxide in multiple myeloma
    • Gallagher RE. Co-biomodulation with arsenic trioxide in multiple myeloma. Leuk Res, 25: 237-239, 2001.
    • (2001) Leuk Res , vol.25 , pp. 237-239
    • Gallagher, R.E.1
  • 73
    • 0001560010 scopus 로고    scopus 로고
    • Pharmacologic concentrations of arsenic trioxide induces growth inhibition and apoptosis in malignant lymphocytes and multiple myeloma cells
    • PART 1
    • Chen G-Q, Zhu XH, Shen Y-L, et al. Pharmacologic concentrations of arsenic trioxide induces growth inhibition and apoptosis in malignant lymphocytes and multiple myeloma cells. Blood, 92 (Suppl. 1, Part 1): 638a, 1998.
    • (1998) Blood , vol.92 , Issue.SUPPL. 1
    • Chen, G.-Q.1    Zhu, X.H.2    Shen, Y.-L.3
  • 75
    • 0036690367 scopus 로고    scopus 로고
    • Arsenic trioxide inhibits growth of human multiple myeloma cells in the bone marrow microenvironment
    • Hayashi T, Hideshima T, Akiyama M, et al. Arsenic trioxide inhibits growth of human multiple myeloma cells in the bone marrow microenvironment. Mol Cancer, 1: 851-860.
    • Mol Cancer , vol.1 , pp. 851-860
    • Hayashi, T.1    Hideshima, T.2    Akiyama, M.3
  • 76
    • 0035030143 scopus 로고    scopus 로고
    • Arsenic trioxide: An emerging therapy for multiple myeloma
    • Munshi NC. Arsenic trioxide: An emerging therapy for multiple myeloma. Oncologist, 6 (Suppl. 2): 17-21, 2001.
    • (2001) Oncologist , vol.6 , Issue.SUPPL. 2 , pp. 17-21
    • Munshi, N.C.1
  • 78
    • 0034663032 scopus 로고    scopus 로고
    • Arsenic trioxide induces dose- and time-dependent apoptosis of endothelium and may exert an antileukemic effect via inhibition of angiogenesis
    • Roboz GJ, Dias S, Lam G, et al. Arsenic trioxide induces dose- and time-dependent apoptosis of endothelium and may exert an antileukemic effect via inhibition of angiogenesis. Blood, 96: 1525-1530, 2000.
    • (2000) Blood , vol.96 , pp. 1525-1530
    • Roboz, G.J.1    Dias, S.2    Lam, G.3
  • 79
    • 0033572313 scopus 로고    scopus 로고
    • Arsenic trioxide causes selective necrosis in solid murine tumors by vascular shutdown
    • Lew YS, Brown SL, Griffin RJ, et al. Arsenic trioxide causes selective necrosis in solid murine tumors by vascular shutdown. Cancer Res, 59: 6033-6037, 1999.
    • (1999) Cancer Res , vol.59 , pp. 6033-6037
    • Lew, Y.S.1    Brown, S.L.2    Griffin, R.J.3
  • 81
    • 0035437189 scopus 로고    scopus 로고
    • Ascorbic acid enhances arsenic trioxide-induced cytotoxicity in multiple myeloma cells
    • Grad JM, Bahlis NJ, Reis I, et al. Ascorbic acid enhances arsenic trioxide-induced cytotoxicity in multiple myeloma cells. Blood, 98: 805-813, 2001.
    • (2001) Blood , vol.98 , pp. 805-813
    • Grad, J.M.1    Bahlis, N.J.2    Reis, I.3
  • 82
    • 0001321540 scopus 로고    scopus 로고
    • Enhanced cytotoxicity to arsenic trioxide in resistant multiple myeloma by butathione sulfoxime (BSO)
    • Gartenhaus RB, Prachand S, Gordon LI. Enhanced cytotoxicity to arsenic trioxide in resistant multiple myeloma by butathione sulfoxime (BSO). Blood, 96 (Suppl. 11): 758a-759a, 2000.
    • (2000) Blood , vol.96 , Issue.SUPPL. 11
    • Gartenhaus, R.B.1    Prachand, S.2    Gordon, L.I.3
  • 83
    • 0032933610 scopus 로고    scopus 로고
    • Malignant cells can be sensitized to undergo growth inhibition and apoptosis by arsenic trioxide through modulation of the glutathione redox system
    • Dai J, Weinberg RS, Waxman S, et al. Malignant cells can be sensitized to undergo growth inhibition and apoptosis by arsenic trioxide through modulation of the glutathione redox system. Blood, 93: 268-277, 1999.
    • (1999) Blood , vol.93 , pp. 268-277
    • Dai, J.1    Weinberg, R.S.2    Waxman, S.3
  • 85
    • 0035437171 scopus 로고    scopus 로고
    • TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: Therapeutic applications
    • Mitsiades CS, Treon SP, Mitsiades N, et al. TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: Therapeutic applications. Blood, 98: 795-804, 2001.
    • (2001) Blood , vol.98 , pp. 795-804
    • Mitsiades, C.S.1    Treon, S.P.2    Mitsiades, N.3
  • 86
    • 0037085796 scopus 로고    scopus 로고
    • Intracellular regulation of tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human multiple myeloma cells
    • Mitsiades N, Mitsiades CS, Poulaki V, et al. Intracellular regulation of tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human multiple myeloma cells. Blood, 99: 2162-2178, 2002.
    • (2002) Blood , vol.99 , pp. 2162-2178
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 87
    • 0034895563 scopus 로고    scopus 로고
    • Concepts in the use of TRAIL/Apo2L: An emerging biotherapy for myeloma and other neoplasias
    • Mitsiades N, Mitsiades CS, Poulaki V, et al. Concepts in the use of TRAIL/Apo2L: An emerging biotherapy for myeloma and other neoplasias. Expert Opin Invest Drugs, 10: 1521-1530, 2001.
    • (2001) Expert Opin Invest Drugs , vol.10 , pp. 1521-1530
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 88
    • 0035207897 scopus 로고    scopus 로고
    • Neovastat, a naturally occurring multifunctional antiangiogenic drug, in phase III clinical trials
    • Falardeau P, Champague P, Poyet P, et al. Neovastat, a naturally occurring multifunctional antiangiogenic drug, in phase III clinical trials. Semin Oncol, 28: 620-625, 2001.
    • (2001) Semin Oncol , vol.28 , pp. 620-625
    • Falardeau, P.1    Champague, P.2    Poyet, P.3
  • 89
    • 0036211156 scopus 로고    scopus 로고
    • Antiangiogenic and antimetastatic properties of Neovastat (AE-941), an orally active extract derived from cartilage tissue
    • Dupont E, Falardeau P, Mousa SA, et al. Antiangiogenic and antimetastatic properties of Neovastat (AE-941), an orally active extract derived from cartilage tissue. Clin Exp Metastasis, 19: 145-153, 2002.
    • (2002) Clin Exp Metastasis , vol.19 , pp. 145-153
    • Dupont, E.1    Falardeau, P.2    Mousa, S.A.3
  • 90
    • 0035060804 scopus 로고    scopus 로고
    • Matrix proteinase inhibition by AE-941, a multifunctional antiangiogenic compound
    • Gingras D, Renaud A, Mousseau N, et al. Matrix proteinase inhibition by AE-941, a multifunctional antiangiogenic compound. Anticancer Res, 21: 145-155, 2001.
    • (2001) Anticancer Res , vol.21 , pp. 145-155
    • Gingras, D.1    Renaud, A.2    Mousseau, N.3
  • 91
    • 0036554985 scopus 로고    scopus 로고
    • The antiangiogenic agent neovastat (AE-941) inhibits vascular endothelial growth factormediated biological effects
    • Beliveau R, Gingras D, Kruger EA, et al. The antiangiogenic agent neovastat (AE-941) inhibits vascular endothelial growth factormediated biological effects. Clin Cancer Res, 8: 1242-1250, 2002.
    • (2002) Clin Cancer Res , vol.8 , pp. 1242-1250
    • Beliveau, R.1    Gingras, D.2    Kruger, E.A.3
  • 92
    • 0036479614 scopus 로고    scopus 로고
    • The effect of Neovastat (AE-941) on an experimental metastatic bone tumor model
    • Weber MH, Lee J, Orr FW. The effect of Neovastat (AE-941) on an experimental metastatic bone tumor model. Int J Oncol, 20: 299-303, 2002.
    • (2002) Int J Oncol , vol.20 , pp. 299-303
    • Weber, M.H.1    Lee, J.2    Orr, F.W.3
  • 93
    • 0036668668 scopus 로고    scopus 로고
    • Neovastat (AE-941) in refractory renal cell carcinoma patients: Report of a Phase II trial with two dose levels
    • in press
    • Batist G, Patenaude F, Champagne P, et al. Neovastat (AE-941) in refractory renal cell carcinoma patients: Report of a Phase II trial with two dose levels. Ann Oncol, in press, 2002.
    • (2002) Ann Oncol
    • Batist, G.1    Patenaude, F.2    Champagne, P.3
  • 94
    • 0031787643 scopus 로고    scopus 로고
    • Expression of Bcl-2 family of proteins in fresh myeloma cells
    • Harada N, Hata H, Yoshida M, et al. Expression of Bcl-2 family of proteins in fresh myeloma cells. Leukemia, 12: 1817-1820, 1998.
    • (1998) Leukemia , vol.12 , pp. 1817-1820
    • Harada, N.1    Hata, H.2    Yoshida, M.3
  • 95
    • 0026527344 scopus 로고
    • Expression of bcl-2 gene in human multiple myeloma cell lines and normal plasma cells
    • Pettersson M, Jernberg-Wiklund H, Larsson LG, et al. Expression of bcl-2 gene in human multiple myeloma cell lines and normal plasma cells. Blood, 79: 495-502, 1992.
    • (1992) Blood , vol.79 , pp. 495-502
    • Pettersson, M.1    Jernberg-Wiklund, H.2    Larsson, L.G.3
  • 96
    • 0031957034 scopus 로고    scopus 로고
    • bcl-2 expression in plasma cells from neoplastic gammopathies and reactive plasmacytosis: A comparative study
    • Miguel-Garcia A, Orero T, Matutes E, et al. bcl-2 expression in plasma cells from neoplastic gammopathies and reactive plasmacytosis: A comparative study. Haematologica, 83: 298-304, 1998.
    • (1998) Haematologica , vol.83 , pp. 298-304
    • Miguel-Garcia, A.1    Orero, T.2    Matutes, E.3
  • 97
    • 0028596130 scopus 로고
    • The oncoprotein phenotype of plasma cells from patients with multiple myeloma
    • Brown RD, Pope B, Luo XF, et al. The oncoprotein phenotype of plasma cells from patients with multiple myeloma. Leuk Lymphoma, 16: 147-156, 1994.
    • (1994) Leuk Lymphoma , vol.16 , pp. 147-156
    • Brown, R.D.1    Pope, B.2    Luo, X.F.3
  • 98
    • 0025995589 scopus 로고
    • Normal and neoplastic human plasma cells express bcl-2 antigen
    • Hamilton MS, Barker HF, Ball J, et al. Normal and neoplastic human plasma cells express bcl-2 antigen. Leukemia, 5: 768-771, 1991.
    • (1991) Leukemia , vol.5 , pp. 768-771
    • Hamilton, M.S.1    Barker, H.F.2    Ball, J.3
  • 99
    • 0011789930 scopus 로고    scopus 로고
    • Bcl-2 protein expression is not related to short survival in multiple myeloma
    • Ong F, van Nieuwkoop JA, de Groot-Swings GM, et al. Bcl-2 protein expression is not related to short survival in multiple myeloma. Leukemia, 12: 220-229, 1998.
    • (1998) Leukemia , vol.12 , pp. 220-229
    • Ong, F.1    Van Nieuwkoop, J.A.2    De Groot-Swings, G.M.3
  • 100
    • 0028886023 scopus 로고
    • Response to interferon therapy in patients with multiple myeloma correlates with expression of the Bcl-2 oncoprotein
    • Sangfelt O, Osterborg A, Grander D, et al. Response to interferon therapy in patients with multiple myeloma correlates with expression of the Bcl-2 oncoprotein. Int J Cancer, 63: 190-192, 1995.
    • (1995) Int J Cancer , vol.63 , pp. 190-192
    • Sangfelt, O.1    Osterborg, A.2    Grander, D.3
  • 101
    • 0031847918 scopus 로고    scopus 로고
    • Bcl-2 overexpression is associated with resistance to dexamethasone, but not melphalan, in multiple myeloma cells
    • Gazitt Y, Fey V, Thomas C, et al. Bcl-2 overexpression is associated with resistance to dexamethasone, but not melphalan, in multiple myeloma cells. Int J Oncol, 13: 397-405, 1998.
    • (1998) Int J Oncol , vol.13 , pp. 397-405
    • Gazitt, Y.1    Fey, V.2    Thomas, C.3
  • 102
    • 0026721173 scopus 로고
    • Therapeutic application of oligonucleotides
    • Crooke ST. Therapeutic application of oligonucleotides. Ann Rev Pharmacol Toxicol, 32: 329-376, 1992.
    • (1992) Ann Rev Pharmacol Toxicol , vol.32 , pp. 329-376
    • Crooke, S.T.1
  • 106
    • 0011782475 scopus 로고
    • Analysis of RAS oncogene mutations in human lymphoid malignancies
    • Neri A, Knowles DM, Greco A, et al. Analysis of RAS oncogene mutations in human lymphoid malignancies. Proc Natl Acad Sci USA, 86: 9268-9272, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.86 , pp. 9268-9272
    • Neri, A.1    Knowles, D.M.2    Greco, A.3
  • 107
    • 0029819604 scopus 로고    scopus 로고
    • Activating mutations of N- and K-ras in multiple myeloma show distinct clinical associations: Analysis of the Eastern Cooperative Oncology Group Phase III trial
    • Liu P, Quam L, Billadeau D, et al. Activating mutations of N- and K-ras in multiple myeloma show distinct clinical associations: Analysis of the Eastern Cooperative Oncology Group Phase III trial. Blood, 88: 2699-2706, 1996.
    • (1996) Blood , vol.88 , pp. 2699-2706
    • Liu, P.1    Quam, L.2    Billadeau, D.3
  • 108
    • 0026747866 scopus 로고
    • Isoprenoid addition to Ras is the critical modification for its membrane association and transforming activity
    • Kato K, Cox AD, Hisaka MM, et al. Isoprenoid addition to Ras is the critical modification for its membrane association and transforming activity. Proc Natl Acad Sci USA, 89: 6403-6407, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6403-6407
    • Kato, K.1    Cox, A.D.2    Hisaka, M.M.3
  • 109
    • 0030749464 scopus 로고    scopus 로고
    • Inhibition of Ras prenylation: A novel approach to cancer chemotherapy
    • Sebti SM, Hamilton AD. Inhibition of Ras prenylation: A novel approach to cancer chemotherapy. Pharmacol Therapeutics, 74: 103-114, 1997.
    • (1997) Pharmacol Therapeutics , vol.74 , pp. 103-114
    • Sebti, S.M.1    Hamilton, A.D.2
  • 110
    • 0034905234 scopus 로고    scopus 로고
    • Synergy of the protein farnesyltransferase inhibitor SCH66336 and cisplatin in human cancer cell lines
    • Adjei AA, Davis JN, Bruzek LM, et al. Synergy of the protein farnesyltransferase inhibitor SCH66336 and cisplatin in human cancer cell lines. Clin Cancer Res, 7: 1438-1445, 2001.
    • (2001) Clin Cancer Res , vol.7 , pp. 1438-1445
    • Adjei, A.A.1    Davis, J.N.2    Bruzek, L.M.3
  • 111
    • 0035383789 scopus 로고    scopus 로고
    • Clinical and biologic activity of the farnesyltransferase inhibitor R115777 in adults with refractory and relapsed acute leukemias: A phase I clinical-laboratory correlative trial
    • Karp JE, Lancet JE, Kaufmann SH, et al. Clinical and biologic activity of the farnesyltransferase inhibitor R115777 in adults with refractory and relapsed acute leukemias: a phase I clinical-laboratory correlative trial. Blood, 97: 3361-3369, 2001.
    • (2001) Blood , vol.97 , pp. 3361-3369
    • Karp, J.E.1    Lancet, J.E.2    Kaufmann, S.H.3
  • 112
    • 0021229959 scopus 로고
    • β-lapachone: Synthesis of derivatives and activities in tumor models
    • Schaffner-Sabba K, Schmidt-Ruppin KH, Wehrli W, et al. β-lapachone: Synthesis of derivatives and activities in tumor models. J Med Chem, 27: 990-994, 1984.
    • (1984) J Med Chem , vol.27 , pp. 990-994
    • Schaffner-Sabba, K.1    Schmidt-Ruppin, K.H.2    Wehrli, W.3
  • 113
    • 0033539487 scopus 로고    scopus 로고
    • Potent inhibition of tumor survival in vivo by β-lapachone plus taxol: Combining drugs imposes different artificial checkpoints
    • Li CJ, Li Y-Z, Pinto AV, et al. Potent inhibition of tumor survival in vivo by β-lapachone plus taxol: Combining drugs imposes different artificial checkpoints. Proc Natl Acad Sci USA, 96: 13369-13374, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13369-13374
    • Li, C.J.1    Li, Y.-Z.2    Pinto, A.V.3
  • 114
    • 18444383960 scopus 로고    scopus 로고
    • β-lapachone, a novel plant product overcomes drug resistance in human multiple myeloma cells
    • in press
    • Gupta D, Podar K, Lin B, et al. β-lapachone, a novel plant product overcomes drug resistance in human multiple myeloma cells. Exp Hem, in press, 2002.
    • (2002) Exp Hem
    • Gupta, D.1    Podar, K.2    Lin, B.3
  • 115
    • 0033045065 scopus 로고    scopus 로고
    • Release of mitochondrial cytochrome c in both apoptosis and necrosis induced by β-lapachone in human carcinoma cells
    • Li Y-Z, Li CJ, Pinto AV, et al. Release of mitochondrial cytochrome c in both apoptosis and necrosis induced by β-lapachone in human carcinoma cells. Mol Med, 5: 232-239, 1999.
    • (1999) Mol Med , vol.5 , pp. 232-239
    • Li, Y.-Z.1    Li, C.J.2    Pinto, A.V.3
  • 116
    • 0030982641 scopus 로고    scopus 로고
    • The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase
    • Pratt WB. The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase. Ann Rev Pharmacol Toxicol, 37: 297-326, 1997.
    • (1997) Ann Rev Pharmacol Toxicol , vol.37 , pp. 297-326
    • Pratt, W.B.1
  • 117
    • 0031054517 scopus 로고    scopus 로고
    • The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Rafkinase
    • Stancato LF, Silverstein AM, Owens-Grillo JK, et al. The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Rafkinase. J Biol Chem, 272: 4013-4020, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 4013-4020
    • Stancato, L.F.1    Silverstein, A.M.2    Owens-Grillo, J.K.3
  • 118
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
    • Lewis J, Devin A, Miller A, et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem, 275: 10519-10526, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3
  • 119
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P, Saleh A, Nakazawa A, et al. Negative regulation of cytochrome c-mediated oligomerization of apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J, 19: 4310-4322, 2000.
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3
  • 120
    • 79960970524 scopus 로고    scopus 로고
    • The HSP90 molecular chaperone as a novel therapeutic target in hematological malignancies
    • Mitsiades CS, Mitsiades N, Poulaki V, et al. The HSP90 molecular chaperone as a novel therapeutic target in hematological malignancies. Blood, 98: 377a, 2001.
    • (2001) Blood , vol.98
    • Mitsiades, C.S.1    Mitsiades, N.2    Poulaki, V.3
  • 121
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Workman P, Maloney A. HSP90 as a new therapeutic target for cancer therapy: The story unfolds. Expert Opin Biol Ther, 2: 3-24, 2002.
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Workman, P.1    Maloney, A.2
  • 122
    • 0033566643 scopus 로고    scopus 로고
    • Desipeptide (FR901228): A novel therapeutic agent with selective, in vitro activity against human B-cell chronic lymphocytic leukemia cells
    • Byrd JC, Shinn C, Ravi R, et al. Desipeptide (FR901228): A novel therapeutic agent with selective, in vitro activity against human B-cell chronic lymphocytic leukemia cells. Blood, 94: 1401-1408, 1999.
    • (1999) Blood , vol.94 , pp. 1401-1408
    • Byrd, J.C.1    Shinn, C.2    Ravi, R.3
  • 123
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhoff TW, Rifkind RA, et al. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci USA, 97: 10014-10019, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3
  • 124
    • 0035132140 scopus 로고    scopus 로고
    • Histone deacetylase-targeted treatment restores retinoic acid signaling and differentiation in acute myeloid leukemia
    • Ferrara FF, Fazi F, Bianchini A, et al. Histone deacetylase-targeted treatment restores retinoic acid signaling and differentiation in acute myeloid leukemia. Cancer Res, 61: 2-7, 2001.
    • (2001) Cancer Res , vol.61 , pp. 2-7
    • Ferrara, F.F.1    Fazi, F.2    Bianchini, A.3
  • 125
    • 79960971567 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) induces growth arrest and apoptosis in multiple myeloma (MM) and Waldenstrom's Macroglobulinemia (WM) cell lines and patient tumor cells
    • Mitsiades N, Mitsiades CS, Poulaki V, et al. The histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) induces growth arrest and apoptosis in multiple myeloma (MM) and Waldenstrom's Macroglobulinemia (WM) cell lines and patient tumor cells. Blood, 98: 376a, 2001.
    • (2001) Blood , vol.98
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 126
    • 0035262502 scopus 로고    scopus 로고
    • Telomerase: Biology and phase I trials
    • Kelland LR. Telomerase: Biology and phase I trials. Lancet Oncol, 2: 95-102, 2001.
    • (2001) Lancet Oncol , vol.2 , pp. 95-102
    • Kelland, L.R.1
  • 127
    • 0030931491 scopus 로고    scopus 로고
    • Telomere shortening and tumor formation by mouse cells lacking telomerase RNA
    • Blasco MA, Lee HW, Hande MP, et al. Telomere shortening and tumor formation by mouse cells lacking telomerase RNA. Cell, 91: 25-34, 1997.
    • (1997) Cell , vol.91 , pp. 25-34
    • Blasco, M.A.1    Lee, H.W.2    Hande, M.P.3
  • 128
    • 0033568462 scopus 로고    scopus 로고
    • Telomere shortening and apoptosis in telomerase-inhibited human tumor cells
    • Zhang X, Mar V, Zhou W, et al. Telomere shortening and apoptosis in telomerase-inhibited human tumor cells. Genes Dev, 13: 2388-2399, 1999.
    • (1999) Genes Dev , vol.13 , pp. 2388-2399
    • Zhang, X.1    Mar, V.2    Zhou, W.3
  • 129
    • 0033455559 scopus 로고    scopus 로고
    • Inhibition of human telomerase in immortal human cells leads to progressive telomere shortening and cell death
    • Herbert B-S, Pitts AE, Baker SE, et al. Inhibition of human telomerase in immortal human cells leads to progressive telomere shortening and cell death. Proc Natl Acad Sci USA, 96: 14726-14781, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14726-14781
    • Herbert, B.-S.1    Pitts, A.E.2    Baker, S.E.3
  • 130
    • 0037148329 scopus 로고    scopus 로고
    • Telomerase inhibition, oligonucleotides, and clinical trials
    • Corey DR. Telomerase inhibition, oligonucleotides, and clinical trials. Oncogene, 21: 631-637, 2002.
    • (2002) Oncogene , vol.21 , pp. 631-637
    • Corey, D.R.1
  • 131
    • 0037148567 scopus 로고    scopus 로고
    • Oligonucleotide N3′→P5′ phosphoramidates as efficient telomerase inhibitors
    • Shea-Herbert B, Pongracz K, Shay JW, et al. Oligonucleotide N3′→P5′ phosphoramidates as efficient telomerase inhibitors. Oncogene, 21: 638-642, 2002.
    • (2002) Oncogene , vol.21 , pp. 638-642
    • Shea-Herbert, B.1    Pongracz, K.2    Shay, J.W.3
  • 132
    • 0036241599 scopus 로고    scopus 로고
    • A G-Quadruplex-interactive potent small-molecule inhibitor of telomerase exhibiting in vitro and in vivo antitumor activity
    • Gowan SM, Harrison JR, Patterson L, et al. A G-Quadruplex-interactive potent small-molecule inhibitor of telomerase exhibiting in vitro and in vivo antitumor activity. Mol Pharmacol, 61: 1154-1162, 2002.
    • (2002) Mol Pharmacol , vol.61 , pp. 1154-1162
    • Gowan, S.M.1    Harrison, J.R.2    Patterson, L.3
  • 133
    • 0002162095 scopus 로고    scopus 로고
    • Strategies to improve the outcome of stem cell transplantation in multiple myeloma
    • Green AR (ed). Macmillan, Hampshire, England
    • Anderson KC. Strategies to improve the outcome of stem cell transplantation in multiple myeloma. In: European Haematology Association Educational Book, Green AR (ed). Macmillan, Hampshire, England, pp. 42-45, 2000.
    • (2000) European Haematology Association Educational Book , pp. 42-45
    • Anderson, K.C.1
  • 134
    • 0000612742 scopus 로고    scopus 로고
    • Multiple myeloma: New insights and therapeutic approaches
    • Schechter GP, Berliner N, Telen MJ (eds). Publisher, Publisher City
    • Anderson KC. Multiple myeloma: New insights and therapeutic approaches. In: American Society of Hematology Education Book, Schechter GP, Berliner N, Telen MJ (eds). Publisher, Publisher City, pp. 159-165, 2000.
    • (2000) American Society of Hematology Education Book , pp. 159-165
    • Anderson, K.C.1
  • 135
    • 20244374668 scopus 로고    scopus 로고
    • + donor lymphocytes for treatment of relapse after allogeneic bone marrow transplant
    • + donor lymphocytes for treatment of relapse after allogeneic bone marrow transplant. Blood, 91: 3671-3680, 1998.
    • (1998) Blood , vol.91 , pp. 3671-3680
    • Alyea, E.P.1    Soiffer, R.J.2    Canning, C.3
  • 136
    • 0030815867 scopus 로고    scopus 로고
    • Donor lymphocyte infusions are effective in relapsed multiple myeloma after allogeneic bone marrow transplantation
    • Lokhorst HM, Schattenberg JJ, Cornelissen JJ, et al. Donor lymphocyte infusions are effective in relapsed multiple myeloma after allogeneic bone marrow transplantation. Blood, 90: 4206-4211, 1997.
    • (1997) Blood , vol.90 , pp. 4206-4211
    • Lokhorst, H.M.1    Schattenberg, J.J.2    Cornelissen, J.J.3
  • 137
    • 0035883066 scopus 로고    scopus 로고
    • T-cell depleted allogeneic bone marrow transplantation followed by donor lymphocyte infusion in patients with multiple myeloma: Induction of graft-versus-myeloma effect
    • Alyea EP, Weller E, Schlossman RL, et al. T-cell depleted allogeneic bone marrow transplantation followed by donor lymphocyte infusion in patients with multiple myeloma: Induction of graft-versus-myeloma effect. Blood, 98: 934-939, 2001.
    • (2001) Blood , vol.98 , pp. 934-939
    • Alyea, E.P.1    Weller, E.2    Schlossman, R.L.3
  • 138
    • 0011791417 scopus 로고    scopus 로고
    • T-cell depleted allogeneic bone marrow transplantation followed by donor lymphocyte infusion in patients with multiple myeloma: Reduced transplant related toxicity with preservation of graft-versus-myeloma effect
    • University of Alberta, Canada
    • Alyea EP, Weller E, Schlossman RL, et al. T-cell depleted allogeneic bone marrow transplantation followed by donor lymphocyte infusion in patients with multiple myeloma: Reduced transplant related toxicity with preservation of graft-versus-myeloma effect. VIIIth International Myeloma Workshop Abstract Book, University of Alberta, Canada, p. 154, 2001.
    • (2001) VIIIth International Myeloma Workshop Abstract Book , pp. 154
    • Alyea, E.P.1    Weller, E.2    Schlossman, R.L.3
  • 139
    • 0033642858 scopus 로고    scopus 로고
    • Conversion to full donor chimerism following donor lymphocyte infusion is associated with disease response in patients with multiple myeloma
    • Orsini E, Alyea EP, Chillemi A, et al. Conversion to full donor chimerism following donor lymphocyte infusion is associated with disease response in patients with multiple myeloma. Biol Blood Marrow Transplant, 6: 375-386, 2000.
    • (2000) Biol Blood Marrow Transplant , vol.6 , pp. 375-386
    • Orsini, E.1    Alyea, E.P.2    Chillemi, A.3
  • 140
    • 0034019523 scopus 로고    scopus 로고
    • Changes in T cell receptor repertoire associated with graft-versus-tumor effect and graftversus-host disease in patients with relapsed multiple myeloma after donor lymphocyte infusion
    • Orsini E, Alyea EP, Schlossman R, et al. Changes in T cell receptor repertoire associated with graft-versus-tumor effect and graftversus-host disease in patients with relapsed multiple myeloma after donor lymphocyte infusion. Bone Marrow Transplant, 25: 623-632, 2000.
    • (2000) Bone Marrow Transplant , vol.25 , pp. 623-632
    • Orsini, E.1    Alyea, E.P.2    Schlossman, R.3
  • 141
    • 79960970875 scopus 로고    scopus 로고
    • Nonmyeloablative conditioning with low dose intravenous busulfan and fludarabine is safe and sufficient to obtain allogeneic stem cell engraftment in patients with hematological malignancies
    • Alyea EP, Neuberg Donna Canning C, et al. Nonmyeloablative conditioning with low dose intravenous busulfan and fludarabine is safe and sufficient to obtain allogeneic stem cell engraftment in patients with hematological malignancies. Blood, 98: 185a, 2001.
    • (2001) Blood , vol.98
    • Alyea, E.P.1    Neuberg Donna Canning, C.2
  • 142
    • 4243831866 scopus 로고    scopus 로고
    • Identification of target antigens associated with graft-vs-myeloma response after allogeneic bone marrow transplantation and donor lymphocyte infusion
    • Bellucci R, Wu CJ, Munshi NC, et al. Identification of target antigens associated with graft-vs-myeloma response after allogeneic bone marrow transplantation and donor lymphocyte infusion. Blood, 98: 405a, 2001.
    • (2001) Blood , vol.98
    • Bellucci, R.1    Wu, C.J.2    Munshi, N.C.3
  • 143
    • 0027496486 scopus 로고
    • Monoclonal antibody purged bone marrow transplantation therapy for multiple myeloma
    • Anderson KC, Andersen J, Soiffer R, et al. Monoclonal antibody purged bone marrow transplantation therapy for multiple myeloma. Blood, 82: 2568-2576, 1993.
    • (1993) Blood , vol.82 , pp. 2568-2576
    • Anderson, K.C.1    Andersen, J.2    Soiffer, R.3
  • 144
    • 0028962288 scopus 로고
    • Monoclonal antibody-purged bone marrow transplantation therapy for multiple myeloma
    • Seiden MV, Schlossman R, Andersen J, et al. Monoclonal antibody-purged bone marrow transplantation therapy for multiple myeloma. Leuk Lymphoma, 17: 87-93, 1995.
    • (1995) Leuk Lymphoma , vol.17 , pp. 87-93
    • Seiden, M.V.1    Schlossman, R.2    Andersen, J.3
  • 145
    • 0000551812 scopus 로고    scopus 로고
    • + selected versus unselected autologous peripheral blood progenitor cell transplantation in multiple myeloma
    • + selected versus unselected autologous peripheral blood progenitor cell transplantation in multiple myeloma. Blood, 93: 1-13, 1999.
    • (1999) Blood , vol.93 , pp. 1-13
    • Vesico, R.1    Schiller, G.2    Stewart, K.3
  • 146
    • 0035449067 scopus 로고    scopus 로고
    • Purging of autologous peripheral blood stem cells using CD34 selection does not improve overall or progression free survival following high dose chemotherapy for multiple myeloma: Results of a multi-center randomized controlled trial
    • Stewart AK, Vesico R, Schiller G, et al. Purging of autologous peripheral blood stem cells using CD34 selection does not improve overall or progression free survival following high dose chemotherapy for multiple myeloma: Results of a multi-center randomized controlled trial. J Clin Oncol, 19: 3771-3779, 2001.
    • (2001) J Clin Oncol , vol.19 , pp. 3771-3779
    • Stewart, A.K.1    Vesico, R.2    Schiller, G.3
  • 147
    • 17444405911 scopus 로고    scopus 로고
    • Adenovirus vector based purging of multiple myeloma cells
    • Teoh G, Chen L, Urashima M, et al. Adenovirus vector based purging of multiple myeloma cells. Blood, 92: 4591-4601, 1998.
    • (1998) Blood , vol.92 , pp. 4591-4601
    • Teoh, G.1    Chen, L.2    Urashima, M.3
  • 148
    • 0034995643 scopus 로고    scopus 로고
    • A pilot study of combined immunotherapy with autologous adoptive tumour-specific T-cell transfer, vaccination with CD40-activated malignant B cells and interleukin-2
    • Schultze JL, Anderson KC, Gilleece MH, et al. A pilot study of combined immunotherapy with autologous adoptive tumour-specific T-cell transfer, vaccination with CD40-activated malignant B cells and interleukin-2. Br J Haematol, 113: 455-460, 2001.
    • (2001) Br J Haematol , vol.113 , pp. 455-460
    • Schultze, J.L.1    Anderson, K.C.2    Gilleece, M.H.3
  • 149
    • 0031469361 scopus 로고    scopus 로고
    • CD40-activated human B cells: An alternative source of highly efficient antigen presenting cells to generate autologous antigen-specific T cells for adoptive immunotherapy
    • Schultze JL, Michalak S, Seamon MJ, et al. CD40-activated human B cells: An alternative source of highly efficient antigen presenting cells to generate autologous antigen-specific T cells for adoptive immunotherapy. J Clin Invest, 100: 2757-2765, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 2757-2765
    • Schultze, J.L.1    Michalak, S.2    Seamon, M.J.3
  • 150
    • 0036565877 scopus 로고    scopus 로고
    • Human primary and memory cytotoxic T lymphocyte responses are efficiently induced by means of CD40-activated B cells as antigen-presenting cells: Potential for clinical application
    • Von Bergwelt-Baildon MS, Vonderheide RH, Maecker B, et al. Human primary and memory cytotoxic T lymphocyte responses are efficiently induced by means of CD40-activated B cells as antigen-presenting cells: Potential for clinical application. Blood, 99: 3319-3325, 2002.
    • (2002) Blood , vol.99 , pp. 3319-3325
    • Von Bergwelt-Baildon, M.S.1    Vonderheide, R.H.2    Maecker, B.3
  • 151
    • 4244101939 scopus 로고    scopus 로고
    • Tumor rejection antigen 1 (GRP94) expression is induced by CD40 ligand activation of multiple myeloma cells and mediates allogeneic T cell reactivity
    • Teoh G, Tai YT, Greenfield EA, et al. Tumor rejection antigen 1 (GRP94) expression is induced by CD40 ligand activation of multiple myeloma cells and mediates allogeneic T cell reactivity. Blood, 92 (Suppl. 1): 101a, 1998.
    • (1998) Blood , vol.92 , Issue.SUPPL. 1
    • Teoh, G.1    Tai, Y.T.2    Greenfield, E.A.3
  • 152
    • 0033558252 scopus 로고    scopus 로고
    • Muc-1 core protein is expressed on multiple myeloma cells and is induced by dexamethasone
    • Treon SP, Mollick JA, Urashima M, et al. Muc-1 core protein is expressed on multiple myeloma cells and is induced by dexamethasone. Blood, 93: 1287-1298, 1999.
    • (1999) Blood , vol.93 , pp. 1287-1298
    • Treon, S.P.1    Mollick, J.A.2    Urashima, M.3
  • 153
    • 0035884392 scopus 로고    scopus 로고
    • The epithelial tumor antigen MUC1 is expressed in hematological malignancies and is recognized by MUC1-specific cytotoxic T-lymphocytes
    • Brossart P, Schneider A, Dill P, et al. The epithelial tumor antigen MUC1 is expressed in hematological malignancies and is recognized by MUC1-specific cytotoxic T-lymphocytes. Cancer Res, 61: 6846-6850, 2001.
    • (2001) Cancer Res , vol.61 , pp. 6846-6850
    • Brossart, P.1    Schneider, A.2    Dill, P.3
  • 154
    • 0034646220 scopus 로고    scopus 로고
    • Activation of antitumor cytotoxic T lymphocytes by fusions of human dendritic cells and breast carcinoma cells
    • Gong J, Avigan D, Chen D, et al. Activation of antitumor cytotoxic T lymphocytes by fusions of human dendritic cells and breast carcinoma cells. Proc Natl Acad Sci USA, 97: 2715-2718, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2715-2718
    • Gong, J.1    Avigan, D.2    Chen, D.3
  • 155
    • 0034254702 scopus 로고    scopus 로고
    • Fusions of human ovarian carcinoma cells with autologous or allogeneic dendritic cells induce antitumor immunity
    • Gong J, Nikrui N, Chen D, et al. Fusions of human ovarian carcinoma cells with autologous or allogeneic dendritic cells induce antitumor immunity. J Immunol, 165: 1705-1711, 2000.
    • (2000) J Immunol , vol.165 , pp. 1705-1711
    • Gong, J.1    Nikrui, N.2    Chen, D.3
  • 156
    • 0035181956 scopus 로고    scopus 로고
    • Vaccination with allogeneic dendritic cells fused to carcinoma cells induces antitumor immunity in MUC1 transgenic mice
    • Tanaka Y, Koido S, Chen D, et al. Vaccination with allogeneic dendritic cells fused to carcinoma cells induces antitumor immunity in MUC1 transgenic mice. Clin Immunol, 101: 192-200, 2001.
    • (2001) Clin Immunol , vol.101 , pp. 192-200
    • Tanaka, Y.1    Koido, S.2    Chen, D.3
  • 157
    • 0033106274 scopus 로고    scopus 로고
    • Bone marrow and peripheral blood dendritic cells from patients with multiple myeloma are phenotypically and functionally normal despite the detection of Kaposi's sarcoma herpes virus gene sequences
    • Raje N, Gong J, Chauhan D, et al. Bone marrow and peripheral blood dendritic cells from patients with multiple myeloma are phenotypically and functionally normal despite the detection of Kaposi's sarcoma herpes virus gene sequences. Blood, 93: 1487-1495, 1999.
    • (1999) Blood , vol.93 , pp. 1487-1495
    • Raje, N.1    Gong, J.2    Chauhan, D.3
  • 158
    • 0036529823 scopus 로고    scopus 로고
    • Immunization against murine multiple myeloma with fusions of dendritic and plasmacytoma cells is potentiated by interleukin 12
    • Gong J, Koido S, Chen D, et al. Immunization against murine multiple myeloma with fusions of dendritic and plasmacytoma cells is potentiated by interleukin 12. Blood, 99: 2512-2517, 2002.
    • (2002) Blood , vol.99 , pp. 2512-2517
    • Gong, J.1    Koido, S.2    Chen, D.3
  • 159
    • 0034125194 scopus 로고    scopus 로고
    • Immunoglobulin framework-derived peptides function as cytotoxic T cell epitopes expressed commonly in B cell malignancies
    • Trojan A, Schultze JL, Witzens M, et al. Immunoglobulin framework-derived peptides function as cytotoxic T cell epitopes expressed commonly in B cell malignancies. Nat Med, 6: 667-672, 2000.
    • (2000) Nat Med , vol.6 , pp. 667-672
    • Trojan, A.1    Schultze, J.L.2    Witzens, M.3
  • 160
    • 0033151591 scopus 로고    scopus 로고
    • The telomerase catalytic subunit is a widely expressed tumor-associated antigen recognized by cytotoxic T lymphocytes
    • Vonderheide RH, Hahn WC, Schultze JL, et al. The telomerase catalytic subunit is a widely expressed tumor-associated antigen recognized by cytotoxic T lymphocytes. Immunity, 10: 673-679, 1999.
    • (1999) Immunity , vol.10 , pp. 673-679
    • Vonderheide, R.H.1    Hahn, W.C.2    Schultze, J.L.3
  • 161
    • 4243807215 scopus 로고    scopus 로고
    • Targeting universal tumor antigens with cytotoxic T cells: Potential of CYP1B1 for broadly applicable antigen-specific immunotherapy
    • Maecker B, Sherr DH, Shen C, et al. Targeting universal tumor antigens with cytotoxic T cells: Potential of CYP1B1 for broadly applicable antigen-specific immunotherapy. Blood, 94 (Suppl. 1): 43a, 1999.
    • (1999) Blood , vol.94 , Issue.SUPPL. 1
    • Maecker, B.1    Sherr, D.H.2    Shen, C.3
  • 162
    • 0027987119 scopus 로고
    • Anti-CD38-blocked ricin: An immunotoxin for the treatment of multiple myeloma
    • Goldmacher VS, Bourret LA, Levine BA, et al. Anti-CD38-blocked ricin: An immunotoxin for the treatment of multiple myeloma. Blood, 84: 3017-3025, 1994.
    • (1994) Blood , vol.84 , pp. 3017-3025
    • Goldmacher, V.S.1    Bourret, L.A.2    Levine, B.A.3
  • 163
    • 7344239852 scopus 로고    scopus 로고
    • Anti-B4 blocked ricin: A phase II trial of 7 day continuous infusion in patients with multiple myeloma
    • Grossbard ML, Fidias P, Kinsella J, et al. Anti-B4 blocked ricin: A phase II trial of 7 day continuous infusion in patients with multiple myeloma. Br J Haematol, 102: 509-515, 1998.
    • (1998) Br J Haematol , vol.102 , pp. 509-515
    • Grossbard, M.L.1    Fidias, P.2    Kinsella, J.3
  • 164
    • 0033792783 scopus 로고    scopus 로고
    • Immunotherapeutic strategies for the treatment of plasma cells malignancies
    • Treon SP, Raje N, Anderson KC. Immunotherapeutic strategies for the treatment of plasma cells malignancies. Semin Oncol, 27: 598-613, 2000.
    • (2000) Semin Oncol , vol.27 , pp. 598-613
    • Treon, S.P.1    Raje, N.2    Anderson, K.C.3
  • 165
    • 0033996882 scopus 로고    scopus 로고
    • Treatment of multiple myeloma by antibody mediated immunotherapy and induction of myeloma selective antigens
    • Treon SP, Shima Y, Grossbard ML, et al. Treatment of multiple myeloma by antibody mediated immunotherapy and induction of myeloma selective antigens. Ann Oncol, 11 (Suppl. 1): 107-111, 2000.
    • (2000) Ann Oncol , vol.11 , Issue.SUPPL. 1 , pp. 107-111
    • Treon, S.P.1    Shima, Y.2    Grossbard, M.L.3
  • 166
    • 0034468110 scopus 로고    scopus 로고
    • The use of rituximab in the treatment of malignant and nonmalignant plasma cell disorders
    • Treon SP, Anderson KC. The use of rituximab in the treatment of malignant and nonmalignant plasma cell disorders. Semin Oncol, 27: 79-85, 2000.
    • (2000) Semin Oncol , vol.27 , pp. 79-85
    • Treon, S.P.1    Anderson, K.C.2
  • 167
    • 0036140240 scopus 로고    scopus 로고
    • CD20-directed serotherapy in patients with multiple myeloma: Biologic considerations and therapeutic applications
    • Treon SP, Pilarski LM, Belch AR, et al. CD20-directed serotherapy in patients with multiple myeloma: Biologic considerations and therapeutic applications. J Immunother, 25: 72-81, 2002.
    • (2002) J Immunother , vol.25 , pp. 72-81
    • Treon, S.P.1    Pilarski, L.M.2    Belch, A.R.3
  • 168
    • 0034330930 scopus 로고    scopus 로고
    • Elevated soluble MUC-1 levels and decreased anti-MUC-1 antibody levels in patients with multiple myeloma
    • Treon SP, Maimonis P, Bua D, et al. Elevated soluble MUC-1 levels and decreased anti-MUC-1 antibody levels in patients with multiple myeloma. Blood, 96: 3147-3153, 2000.
    • (2000) Blood , vol.96 , pp. 3147-3153
    • Treon, S.P.1    Maimonis, P.2    Bua, D.3
  • 169
    • 0034999927 scopus 로고    scopus 로고
    • CD20-directed antibody-mediated immunotherapy induces responses and facilitates hematological recovery in patients with Waldenstrom's Macroglobulinemia
    • Treon SP, Agus DB, Link B, et al. CD20-directed antibody-mediated immunotherapy induces responses and facilitates hematological recovery in patients with Waldenstrom's Macroglobulinemia. J Immunother, 24: 272-279, 2001.
    • (2001) J Immunother , vol.24 , pp. 272-279
    • Treon, S.P.1    Agus, D.B.2    Link, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.