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Volumn 26, Issue 3, 2012, Pages 671-704

Role of Histone Deacetylase Inhibitors in the Treatment of Lymphomas and Multiple Myeloma

Author keywords

Epigenetic therapy; Histone deacetylase inhibitors; Lymphoma; Multiple myeloma

Indexed keywords

4 PHENYLBUTYRIC ACID; 5 AZA 2' DEOXYCYTIDINE; BELINOSTAT; BORTEZOMIB; DACINOSTAT; DEPSIPEPTIDE; DEXAMETHASONE; ENTINOSTAT; HISTONE DEACETYLASE INHIBITOR; LBH 586; LENALIDOMIDE; MOCETINOSTAT; NICOTINAMIDE; PANOBINOSTAT; ROMIDEPSIN; SIRTINOL; SK 7041; TACEDINALINE; TUBACIN; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 84859955695     PISSN: 08898588     EISSN: 15581977     Source Type: Journal    
DOI: 10.1016/j.hoc.2012.01.006     Document Type: Review
Times cited : (15)

References (179)
  • 1
    • 21244467166 scopus 로고    scopus 로고
    • Epigenetic and chromatin modifiers as targeted therapy of hematologic malignancies
    • Bhalla K.N. Epigenetic and chromatin modifiers as targeted therapy of hematologic malignancies. J Clin Oncol 2005, 23(17):3971-3993.
    • (2005) J Clin Oncol , vol.23 , Issue.17 , pp. 3971-3993
    • Bhalla, K.N.1
  • 2
    • 67449110956 scopus 로고    scopus 로고
    • Epigenetic therapies reach Main Street
    • Bates S.E. Epigenetic therapies reach Main Street. Clin Cancer Res 2009, 15(12):3917.
    • (2009) Clin Cancer Res , vol.15 , Issue.12 , pp. 3917
    • Bates, S.E.1
  • 3
    • 67349222049 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as anti-neoplastic agents
    • Batty N., Malouf G.G., Issa J.P. Histone deacetylase inhibitors as anti-neoplastic agents. Cancer Lett 2009, 280(2):192-200.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 192-200
    • Batty, N.1    Malouf, G.G.2    Issa, J.P.3
  • 4
    • 40849139208 scopus 로고    scopus 로고
    • Epigenetics in cancer
    • Esteller M. Epigenetics in cancer. N Engl J Med 2008, 358(11):1148-1159.
    • (2008) N Engl J Med , vol.358 , Issue.11 , pp. 1148-1159
    • Esteller, M.1
  • 5
    • 80054720150 scopus 로고    scopus 로고
    • The biology of HDAC in cancer: the nuclear and epigenetic components
    • Hagelkruys A., Sawicka A., Rennmayr M., et al. The biology of HDAC in cancer: the nuclear and epigenetic components. Handb Exp Pharmacol 2011, 206:13-37.
    • (2011) Handb Exp Pharmacol , vol.206 , pp. 13-37
    • Hagelkruys, A.1    Sawicka, A.2    Rennmayr, M.3
  • 6
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science 2001, 293(5532):1074-1080.
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 7
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: from genomic organization to genomic regulation
    • Khorasanizadeh S. The nucleosome: from genomic organization to genomic regulation. Cell 2004, 116(2):259-272.
    • (2004) Cell , vol.116 , Issue.2 , pp. 259-272
    • Khorasanizadeh, S.1
  • 8
    • 34547683194 scopus 로고    scopus 로고
    • Phase IIb multicenter trial of vorinostat in patients with persistent, progressive, or treatment refractory cutaneous T-cell lymphoma
    • Olsen E.A., Kim Y.H., Kuzel T.M., et al. Phase IIb multicenter trial of vorinostat in patients with persistent, progressive, or treatment refractory cutaneous T-cell lymphoma. J Clin Oncol 2007, 25(21):3109-3115.
    • (2007) J Clin Oncol , vol.25 , Issue.21 , pp. 3109-3115
    • Olsen, E.A.1    Kim, Y.H.2    Kuzel, T.M.3
  • 9
    • 84860004808 scopus 로고    scopus 로고
    • Pooled analysis of two international multicenter clinical studies of romidepsin in 167 patients with cutaneous lymphoma
    • 45th American Society of Clinical Oncology Annual Meeting, Atlanta, December
    • Demierre M. Pooled analysis of two international multicenter clinical studies of romidepsin in 167 patients with cutaneous lymphoma. 45th American Society of Clinical Oncology Annual Meeting, Atlanta, December 2009.
    • (2009)
    • Demierre, M.1
  • 10
    • 79952977561 scopus 로고    scopus 로고
    • Phase 2 trial of romidepsin in patients with peripheral T-cell lymphoma
    • Piekarz R.L., Frye R., Prince H.M., et al. Phase 2 trial of romidepsin in patients with peripheral T-cell lymphoma. Blood 2011, 117(22):5827-5834.
    • (2011) Blood , vol.117 , Issue.22 , pp. 5827-5834
    • Piekarz, R.L.1    Frye, R.2    Prince, H.M.3
  • 11
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 1997, 389(6649):349-352.
    • (1997) Nature , vol.389 , Issue.6649 , pp. 349-352
    • Grunstein, M.1
  • 12
    • 0032055037 scopus 로고    scopus 로고
    • Covalent modifications of histones: expression from chromatin templates
    • Davie J.R. Covalent modifications of histones: expression from chromatin templates. Curr Opin Genet Dev 1998, 8(2):173-178.
    • (1998) Curr Opin Genet Dev , vol.8 , Issue.2 , pp. 173-178
    • Davie, J.R.1
  • 13
    • 77953133352 scopus 로고    scopus 로고
    • Emerging role of epigenetic therapies in cutaneous T-cell lymphomas
    • Zain J., Kaminetzky D., O'Connor O.A. Emerging role of epigenetic therapies in cutaneous T-cell lymphomas. Expert Rev Hematol 2010, 3(2):187-203.
    • (2010) Expert Rev Hematol , vol.3 , Issue.2 , pp. 187-203
    • Zain, J.1    Kaminetzky, D.2    O'Connor, O.A.3
  • 14
    • 28644440158 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: discovery and development as anticancer agents
    • Marks P.A., Dokmanovic M. Histone deacetylase inhibitors: discovery and development as anticancer agents. Expert Opin Investig Drugs 2005, 14(12):1497-1511.
    • (2005) Expert Opin Investig Drugs , vol.14 , Issue.12 , pp. 1497-1511
    • Marks, P.A.1    Dokmanovic, M.2
  • 15
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G., Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem 2004, 73:417-435.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 16
    • 77955176402 scopus 로고    scopus 로고
    • Targeted treatment and new agents in peripheral T-cell lymphoma
    • Zain J.M., O'Connor O. Targeted treatment and new agents in peripheral T-cell lymphoma. Int J Hematol 2010, 92(1):33-44.
    • (2010) Int J Hematol , vol.92 , Issue.1 , pp. 33-44
    • Zain, J.M.1    O'Connor, O.2
  • 17
    • 39749190600 scopus 로고    scopus 로고
    • The potential of histone deacetylase inhibitors for the treatment of multiple myeloma
    • Prince H.M., Bishton M., Harrison S. The potential of histone deacetylase inhibitors for the treatment of multiple myeloma. Leuk Lymphoma 2008, 49(3):385-387.
    • (2008) Leuk Lymphoma , vol.49 , Issue.3 , pp. 385-387
    • Prince, H.M.1    Bishton, M.2    Harrison, S.3
  • 18
    • 67449138841 scopus 로고    scopus 로고
    • Epigenetic modifiers: basic understanding and clinical development
    • Piekarz R.L., Bates S.E. Epigenetic modifiers: basic understanding and clinical development. Clin Cancer Res 2009, 15(12):3918-3926.
    • (2009) Clin Cancer Res , vol.15 , Issue.12 , pp. 3918-3926
    • Piekarz, R.L.1    Bates, S.E.2
  • 19
    • 33644836549 scopus 로고    scopus 로고
    • Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies
    • O'Connor O.A., Heaney M.L., Schwartz L., et al. Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies. J Clin Oncol 2006, 24(1):166-173.
    • (2006) J Clin Oncol , vol.24 , Issue.1 , pp. 166-173
    • O'Connor, O.A.1    Heaney, M.L.2    Schwartz, L.3
  • 20
    • 77955943626 scopus 로고    scopus 로고
    • Epigenetic therapy of lymphoma using histone deacetylase inhibitors
    • Cotto M., Cabanillas F., Tirado M., et al. Epigenetic therapy of lymphoma using histone deacetylase inhibitors. Clin Transl Oncol 2010, 12(6):401-409.
    • (2010) Clin Transl Oncol , vol.12 , Issue.6 , pp. 401-409
    • Cotto, M.1    Cabanillas, F.2    Tirado, M.3
  • 21
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: past, present and future
    • Yoo C.B., Jones P.A. Epigenetic therapy of cancer: past, present and future. Nat Rev Drug Discov 2006, 5(1):37-50.
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.1 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 22
    • 38449100788 scopus 로고    scopus 로고
    • Expression profile of class I histone deacetylases in human cancer tissues
    • Nakagawa M., Oda Y., Eguchi T., et al. Expression profile of class I histone deacetylases in human cancer tissues. Oncol Rep 2007, 18(4):769-774.
    • (2007) Oncol Rep , vol.18 , Issue.4 , pp. 769-774
    • Nakagawa, M.1    Oda, Y.2    Eguchi, T.3
  • 23
    • 70350451749 scopus 로고    scopus 로고
    • Expression of histone deacetylases in lymphoma: implication for the development of selective inhibitors
    • Gloghini A., Buglio D., Khaskhely N.M., et al. Expression of histone deacetylases in lymphoma: implication for the development of selective inhibitors. Br J Haematol 2009, 147(4):515-525.
    • (2009) Br J Haematol , vol.147 , Issue.4 , pp. 515-525
    • Gloghini, A.1    Buglio, D.2    Khaskhely, N.M.3
  • 24
    • 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 2003, 100(8):4389-4394.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.8 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3
  • 25
    • 44949234487 scopus 로고    scopus 로고
    • The aggresome pathway as a target for therapy in hematologic malignancies
    • Simms-Waldrip T., Rodriguez-Gonzalez A., Lin T., et al. The aggresome pathway as a target for therapy in hematologic malignancies. Mol Genet Metab 2008, 94(3):283-286.
    • (2008) Mol Genet Metab , vol.94 , Issue.3 , pp. 283-286
    • Simms-Waldrip, T.1    Rodriguez-Gonzalez, A.2    Lin, T.3
  • 26
    • 0032169858 scopus 로고    scopus 로고
    • ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex
    • Wang J., Hoshino T., Redner R.L., et al. ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex. Proc Natl Acad Sci U S A 1998, 95(18):10860-10865.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.18 , pp. 10860-10865
    • Wang, J.1    Hoshino, T.2    Redner, R.L.3
  • 27
    • 0031724804 scopus 로고    scopus 로고
    • ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors
    • Lutterbach B., Westendorf J.J., Linggi B., et al. ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors. Mol Cell Biol 1998, 18(12):7176-7184.
    • (1998) Mol Cell Biol , vol.18 , Issue.12 , pp. 7176-7184
    • Lutterbach, B.1    Westendorf, J.J.2    Linggi, B.3
  • 28
    • 0031723957 scopus 로고    scopus 로고
    • Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO
    • Gelmetti V., Zhang J., Fanelli M., et al. Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO. Mol Cell Biol 1998, 18(12):7185-7191.
    • (1998) Mol Cell Biol , vol.18 , Issue.12 , pp. 7185-7191
    • Gelmetti, V.1    Zhang, J.2    Fanelli, M.3
  • 29
    • 0033634946 scopus 로고    scopus 로고
    • Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers
    • Lin R.J., Evans R.M. Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers. Mol Cell 2000, 5(5):821-830.
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 821-830
    • Lin, R.J.1    Evans, R.M.2
  • 30
    • 0033638969 scopus 로고    scopus 로고
    • Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation
    • Minucci S., Maccarana M., Cioce M., et al. Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation. Mol Cell 2000, 5(5):811-820.
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 811-820
    • Minucci, S.1    Maccarana, M.2    Cioce, M.3
  • 31
    • 57849096553 scopus 로고    scopus 로고
    • The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance
    • Villagra A., Cheng F., Wang H.W., et al. The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance. Nat Immunol 2009, 10(1):92-100.
    • (2009) Nat Immunol , vol.10 , Issue.1 , pp. 92-100
    • Villagra, A.1    Cheng, F.2    Wang, H.W.3
  • 32
    • 74449093175 scopus 로고    scopus 로고
    • Histone deacetylases and the immunological network: implications in cancer and inflammation
    • Villagra A., Sotomayor E.M., Seto E. Histone deacetylases and the immunological network: implications in cancer and inflammation. Oncogene 2010, 29(2):157-173.
    • (2010) Oncogene , vol.29 , Issue.2 , pp. 157-173
    • Villagra, A.1    Sotomayor, E.M.2    Seto, E.3
  • 33
    • 50049108874 scopus 로고    scopus 로고
    • Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma
    • Marquard L., Gjerdrum L.M., Christensen I.J., et al. Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma. Histopathology 2008, 53(3):267-277.
    • (2008) Histopathology , vol.53 , Issue.3 , pp. 267-277
    • Marquard, L.1    Gjerdrum, L.M.2    Christensen, I.J.3
  • 34
    • 25844488336 scopus 로고    scopus 로고
    • Aberrant DNA methylation in cutaneous malignancies
    • van Doorn R., Gruis N.A., Willemze R., et al. Aberrant DNA methylation in cutaneous malignancies. Semin Oncol 2005, 32(5):479-487.
    • (2005) Semin Oncol , vol.32 , Issue.5 , pp. 479-487
    • van Doorn, R.1    Gruis, N.A.2    Willemze, R.3
  • 35
    • 21244458051 scopus 로고    scopus 로고
    • Epigenetic profiling of cutaneous T-cell lymphoma: promoter hypermethylation of multiple tumor suppressor genes including BCL7a, PTPRG, and p73
    • van Doorn R., Zoutman W.H., Dijkman R., et al. Epigenetic profiling of cutaneous T-cell lymphoma: promoter hypermethylation of multiple tumor suppressor genes including BCL7a, PTPRG, and p73. J Clin Oncol 2005, 23(17):3886-3896.
    • (2005) J Clin Oncol , vol.23 , Issue.17 , pp. 3886-3896
    • van Doorn, R.1    Zoutman, W.H.2    Dijkman, R.3
  • 36
    • 33845996135 scopus 로고    scopus 로고
    • Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL)
    • Duvic M., Talpur R., Ni X., et al. Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL). Blood 2007, 109(1):31-39.
    • (2007) Blood , vol.109 , Issue.1 , pp. 31-39
    • Duvic, M.1    Talpur, R.2    Ni, X.3
  • 37
    • 51649126841 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor panobinostat induces clinical responses with associated alterations in gene expression profiles in cutaneous T-cell lymphoma
    • Ellis L., Pan Y., Smyth G.K., et al. Histone deacetylase inhibitor panobinostat induces clinical responses with associated alterations in gene expression profiles in cutaneous T-cell lymphoma. Clin Cancer Res 2008, 14(14):4500-4510.
    • (2008) Clin Cancer Res , vol.14 , Issue.14 , pp. 4500-4510
    • Ellis, L.1    Pan, Y.2    Smyth, G.K.3
  • 38
    • 72649091422 scopus 로고    scopus 로고
    • Laboratory correlates for a phase II trial of romidepsin in cutaneous and peripheral T-cell lymphoma
    • Bates S.E., Zhan Z., Steadman K., et al. Laboratory correlates for a phase II trial of romidepsin in cutaneous and peripheral T-cell lymphoma. Br J Haematol 2010, 148(2):256-267.
    • (2010) Br J Haematol , vol.148 , Issue.2 , pp. 256-267
    • Bates, S.E.1    Zhan, Z.2    Steadman, K.3
  • 39
    • 77950644059 scopus 로고    scopus 로고
    • Vorinostat interferes with the signaling transduction pathway of T-cell receptor and synergizes with phosphoinositide-3 kinase inhibitors in cutaneous T-cell lymphoma
    • Wozniak M.B., Villuendas R., Bischoff J.R., et al. Vorinostat interferes with the signaling transduction pathway of T-cell receptor and synergizes with phosphoinositide-3 kinase inhibitors in cutaneous T-cell lymphoma. Haematologica 2010, 95(4):613-621.
    • (2010) Haematologica , vol.95 , Issue.4 , pp. 613-621
    • Wozniak, M.B.1    Villuendas, R.2    Bischoff, J.R.3
  • 40
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A., Littman D.R. Signal transduction by lymphocyte antigen receptors. Cell 1994, 76(2):263-274.
    • (1994) Cell , vol.76 , Issue.2 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 41
    • 77956321374 scopus 로고    scopus 로고
    • Update on the molecular pathogenesis and clinical treatment of mantle cell lymphoma (MCL): minutes of the 9th European MCL Network Conference
    • Dreyling M., Hoster E., Bea S., et al. Update on the molecular pathogenesis and clinical treatment of mantle cell lymphoma (MCL): minutes of the 9th European MCL Network Conference. Leuk Lymphoma 2010, 51(9):1612-1622.
    • (2010) Leuk Lymphoma , vol.51 , Issue.9 , pp. 1612-1622
    • Dreyling, M.1    Hoster, E.2    Bea, S.3
  • 42
    • 67449127082 scopus 로고    scopus 로고
    • Clinical studies of histone deacetylase inhibitors
    • Prince H.M., Bishton M.J., Harrison S.J. Clinical studies of histone deacetylase inhibitors. Clin Cancer Res 2009, 15(12):3958-3969.
    • (2009) Clin Cancer Res , vol.15 , Issue.12 , pp. 3958-3969
    • Prince, H.M.1    Bishton, M.J.2    Harrison, S.J.3
  • 43
    • 0038243177 scopus 로고    scopus 로고
    • Mutations of the BCL6 proto-oncogene disrupt its negative autoregulation in diffuse large B-cell lymphoma
    • Pasqualucci L., Migliazza A., Basso K., et al. Mutations of the BCL6 proto-oncogene disrupt its negative autoregulation in diffuse large B-cell lymphoma. Blood 2003, 101(8):2914-2923.
    • (2003) Blood , vol.101 , Issue.8 , pp. 2914-2923
    • Pasqualucci, L.1    Migliazza, A.2    Basso, K.3
  • 44
    • 0034598746 scopus 로고    scopus 로고
    • Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling
    • Alizadeh A.A., Eisen M.B., Davis R.E., et al. Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling. Nature 2000, 403(6769):503-511.
    • (2000) Nature , vol.403 , Issue.6769 , pp. 503-511
    • Alizadeh, A.A.1    Eisen, M.B.2    Davis, R.E.3
  • 45
    • 27244431774 scopus 로고    scopus 로고
    • Targeting histones and proteasomes: new strategies for the treatment of lymphoma
    • O'Connor O.A. Targeting histones and proteasomes: new strategies for the treatment of lymphoma. J Clin Oncol 2005, 23(26):6429-6436.
    • (2005) J Clin Oncol , vol.23 , Issue.26 , pp. 6429-6436
    • O'Connor, O.A.1
  • 46
    • 0037077227 scopus 로고    scopus 로고
    • Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor
    • Lemercier C., Brocard M.P., Puvion-Dutilleul F., et al. Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor. J Biol Chem 2002, 277(24):22045-22052.
    • (2002) J Biol Chem , vol.277 , Issue.24 , pp. 22045-22052
    • Lemercier, C.1    Brocard, M.P.2    Puvion-Dutilleul, F.3
  • 47
    • 38949165127 scopus 로고    scopus 로고
    • Constitutively activated STAT3 promotes cell proliferation and survival in the activated B-cell subtype of diffuse large B-cell lymphomas
    • Ding B.B., Yu J.J., Yu R.Y., et al. Constitutively activated STAT3 promotes cell proliferation and survival in the activated B-cell subtype of diffuse large B-cell lymphomas. Blood 2008, 111(3):1515-1523.
    • (2008) Blood , vol.111 , Issue.3 , pp. 1515-1523
    • Ding, B.B.1    Yu, J.J.2    Yu, R.Y.3
  • 48
    • 0037097818 scopus 로고    scopus 로고
    • The role of cytokines in classical Hodgkin lymphoma
    • Skinnider B.F., Mak T.W. The role of cytokines in classical Hodgkin lymphoma. Blood 2002, 99(12):4283-4297.
    • (2002) Blood , vol.99 , Issue.12 , pp. 4283-4297
    • Skinnider, B.F.1    Mak, T.W.2
  • 49
    • 20444374404 scopus 로고    scopus 로고
    • From Hodgkin disease to Hodgkin lymphoma: biologic insights and therapeutic potential
    • Re D., Thomas R.K., Behringer K., et al. From Hodgkin disease to Hodgkin lymphoma: biologic insights and therapeutic potential. Blood 2005, 105(12):4553-4560.
    • (2005) Blood , vol.105 , Issue.12 , pp. 4553-4560
    • Re, D.1    Thomas, R.K.2    Behringer, K.3
  • 50
    • 0035992266 scopus 로고    scopus 로고
    • The role of interleukin 13 in classical Hodgkin lymphoma
    • Skinnider B.F., Kapp U., Mak T.W. The role of interleukin 13 in classical Hodgkin lymphoma. Leuk Lymphoma 2002, 43(6):1203-1210.
    • (2002) Leuk Lymphoma , vol.43 , Issue.6 , pp. 1203-1210
    • Skinnider, B.F.1    Kapp, U.2    Mak, T.W.3
  • 51
    • 0033591689 scopus 로고    scopus 로고
    • Interleukin 13 is secreted by and stimulates the growth of Hodgkin and Reed-Sternberg cells
    • Kapp U., Yeh W.C., Patterson B., et al. Interleukin 13 is secreted by and stimulates the growth of Hodgkin and Reed-Sternberg cells. J Exp Med 1999, 189(12):1939-1946.
    • (1999) J Exp Med , vol.189 , Issue.12 , pp. 1939-1946
    • Kapp, U.1    Yeh, W.C.2    Patterson, B.3
  • 52
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan Z.L., Guan Y.J., Chatterjee D., et al. Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 2005, 307(5707):269-273.
    • (2005) Science , vol.307 , Issue.5707 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3
  • 53
    • 51649092609 scopus 로고    scopus 로고
    • Vorinostat inhibits STAT6-mediated TH2 cytokine and TARC production and induces cell death in Hodgkin lymphoma cell lines
    • Buglio D., Georgakis G.V., Hanabuchi S., et al. Vorinostat inhibits STAT6-mediated TH2 cytokine and TARC production and induces cell death in Hodgkin lymphoma cell lines. Blood 2008, 112(4):1424-1433.
    • (2008) Blood , vol.112 , Issue.4 , pp. 1424-1433
    • Buglio, D.1    Georgakis, G.V.2    Hanabuchi, S.3
  • 54
    • 0029764293 scopus 로고    scopus 로고
    • Induction of MAGE genes in lymphoid cells by the demethylating agent 5-aza-2'-deoxycytidine
    • Shichijo S., Yamada A., Sagawa K., et al. Induction of MAGE genes in lymphoid cells by the demethylating agent 5-aza-2'-deoxycytidine. Jpn J Cancer Res 1996, 87(7):751-756.
    • (1996) Jpn J Cancer Res , vol.87 , Issue.7 , pp. 751-756
    • Shichijo, S.1    Yamada, A.2    Sagawa, K.3
  • 55
    • 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 2004, 101(2):540-545.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.2 , pp. 540-545
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 56
    • 1842830815 scopus 로고    scopus 로고
    • Microarray profiling of the effects of histone deacetylase inhibitors on gene expression in cancer cell lines
    • Gray S.G., Qian C.N., Furge K., et al. Microarray profiling of the effects of histone deacetylase inhibitors on gene expression in cancer cell lines. Int J Oncol 2004, 24(4):773-795.
    • (2004) Int J Oncol , vol.24 , Issue.4 , pp. 773-795
    • Gray, S.G.1    Qian, C.N.2    Furge, K.3
  • 57
    • 54849407184 scopus 로고    scopus 로고
    • In vivo anti-myeloma activity and modulation of gene expression profile induced by valproic acid, a histone deacetylase inhibitor
    • Neri P., Tagliaferri P., Di Martino M.T., et al. In vivo anti-myeloma activity and modulation of gene expression profile induced by valproic acid, a histone deacetylase inhibitor. Br J Haematol 2008, 143(4):520-531.
    • (2008) Br J Haematol , vol.143 , Issue.4 , pp. 520-531
    • Neri, P.1    Tagliaferri, P.2    Di Martino, M.T.3
  • 58
    • 33947726288 scopus 로고    scopus 로고
    • Valproic acid induces non-apoptotic cell death mechanisms in multiple myeloma cell lines
    • Schwartz C., Palissot V., Aouali N., et al. Valproic acid induces non-apoptotic cell death mechanisms in multiple myeloma cell lines. Int J Oncol 2007, 30(3):573-582.
    • (2007) Int J Oncol , vol.30 , Issue.3 , pp. 573-582
    • Schwartz, C.1    Palissot, V.2    Aouali, N.3
  • 59
    • 0034770423 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors increase p21(WAF1) and induce apoptosis of human myeloma cell lines independent of decreased IL-6 receptor expression
    • Lavelle D., Westside Division, Chicago, et al. Histone deacetylase inhibitors increase p21(WAF1) and induce apoptosis of human myeloma cell lines independent of decreased IL-6 receptor expression. Am J Hematol 2001, 68(3):170-178.
    • (2001) Am J Hematol , vol.68 , Issue.3 , pp. 170-178
    • Lavelle, D.1    Westside, D.2    Chicago3
  • 60
    • 33644554220 scopus 로고    scopus 로고
    • The effects of the histone deacetylase inhibitor valproic acid on cell cycle, growth suppression and apoptosis in multiple myeloma
    • Kaiser M., Zavrski I., Sterz J., et al. The effects of the histone deacetylase inhibitor valproic acid on cell cycle, growth suppression and apoptosis in multiple myeloma. Haematologica 2006, 91(2):248-251.
    • (2006) Haematologica , vol.91 , Issue.2 , pp. 248-251
    • Kaiser, M.1    Zavrski, I.2    Sterz, J.3
  • 61
    • 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 2006, 66(11):5781-5789.
    • (2006) Cancer Res , vol.66 , Issue.11 , pp. 5781-5789
    • Maiso, P.1    Carvajal-Vergara, X.2    Ocio, E.M.3
  • 62
    • 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 2004, 125(2):156-161.
    • (2004) Br J Haematol , vol.125 , Issue.2 , pp. 156-161
    • Khan, S.B.1    Maududi, T.2    Barton, K.3
  • 63
    • 34548125345 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor ITF2357 has anti-leukemic activity in vitro and in vivo and inhibits IL-6 and VEGF production by stromal cells
    • Golay J., Cuppini L., Leoni F., et al. The histone deacetylase inhibitor ITF2357 has anti-leukemic activity in vitro and in vivo and inhibits IL-6 and VEGF production by stromal cells. Leukemia 2007, 21(9):1892-1900.
    • (2007) Leukemia , vol.21 , Issue.9 , pp. 1892-1900
    • Golay, J.1    Cuppini, L.2    Leoni, F.3
  • 64
    • 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 2003, 102(7):2615-2622.
    • (2003) Blood , vol.102 , Issue.7 , pp. 2615-2622
    • Catley, L.1    Weisberg, E.2    Tai, Y.T.3
  • 65
    • 49849084681 scopus 로고    scopus 로고
    • KD5170, a novel mercaptoketone-based histone deacetylase inhibitor, exerts antimyeloma effects by DNA damage and mitochondrial signaling
    • Feng R., Ma H., Hassig C.A., et al. KD5170, a novel mercaptoketone-based histone deacetylase inhibitor, exerts antimyeloma effects by DNA damage and mitochondrial signaling. Mol Cancer Ther 2008, 7(6):1494-1505.
    • (2008) Mol Cancer Ther , vol.7 , Issue.6 , pp. 1494-1505
    • Feng, R.1    Ma, H.2    Hassig, C.A.3
  • 66
    • 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 2006, 108(10):3441-3449.
    • (2006) Blood , vol.108 , Issue.10 , pp. 3441-3449
    • Catley, L.1    Weisberg, E.2    Kiziltepe, T.3
  • 67
    • 6944226365 scopus 로고    scopus 로고
    • Apoptosis of multiple myeloma
    • Oancea M., Mani A., Hussein M.A., et al. Apoptosis of multiple myeloma. Int J Hematol 2004, 80(3):224-231.
    • (2004) Int J Hematol , vol.80 , Issue.3 , pp. 224-231
    • Oancea, M.1    Mani, A.2    Hussein, M.A.3
  • 68
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nat Rev Cancer 2002, 2(6):420-430.
    • (2002) Nat Rev Cancer , vol.2 , Issue.6 , pp. 420-430
    • Ashkenazi, A.1
  • 69
    • 28544437352 scopus 로고    scopus 로고
    • Growth factors and antiapoptotic signaling pathways in multiple myeloma
    • van de Donk N.W., Lokhorst H.M., Bloem A.C. Growth factors and antiapoptotic signaling pathways in multiple myeloma. Leukemia 2005, 19(12):2177-2185.
    • (2005) Leukemia , vol.19 , Issue.12 , pp. 2177-2185
    • van de Donk, N.W.1    Lokhorst, H.M.2    Bloem, A.C.3
  • 70
    • 34250029013 scopus 로고    scopus 로고
    • Membrane expression of DR4, DR5 and caspase-8 levels, but not Mcl-1, determine sensitivity of human myeloma cells to Apo2L/TRAIL
    • Gomez-Benito M., Martinez-Lorenzo M.J., Anel A., et al. Membrane expression of DR4, DR5 and caspase-8 levels, but not Mcl-1, determine sensitivity of human myeloma cells to Apo2L/TRAIL. Exp Cell Res 2007, 313(11):2378-2388.
    • (2007) Exp Cell Res , vol.313 , Issue.11 , pp. 2378-2388
    • Gomez-Benito, M.1    Martinez-Lorenzo, M.J.2    Anel, A.3
  • 71
    • 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 2003, 101(10):4055-4062.
    • (2003) Blood , vol.101 , Issue.10 , pp. 4055-4062
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 72
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao Y., Gao Z., Marks P.A., et al. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci U S A 2004, 101(52):18030-18035.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.52 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3
  • 73
    • 45949083938 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) induces apoptosis or autophagy-associated cell death in chondrosarcoma cell lines
    • Yamamoto S., Tanaka K., Sakimura R., et al. Suberoylanilide hydroxamic acid (SAHA) induces apoptosis or autophagy-associated cell death in chondrosarcoma cell lines. Anticancer Res 2008, 28(3A):1585-1591.
    • (2008) Anticancer Res , vol.28 , Issue.3 A , pp. 1585-1591
    • Yamamoto, S.1    Tanaka, K.2    Sakimura, R.3
  • 74
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 1999, 286(5446):1888-1893.
    • (1999) Science , vol.286 , Issue.5446 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 75
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett E.J., Bence N.F., Jayakumar R., et al. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 2005, 17(3):351-365.
    • (2005) Mol Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3
  • 76
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000, 10(12):524-530.
    • (2000) Trends Cell Biol , vol.10 , Issue.12 , pp. 524-530
    • Kopito, R.R.1
  • 77
    • 20844435806 scopus 로고    scopus 로고
    • Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma
    • Hideshima T., Bradner J.E., Wong J., et al. Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma. Proc Natl Acad Sci U S A 2005, 102(24):8567-8572.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.24 , pp. 8567-8572
    • Hideshima, T.1    Bradner, J.E.2    Wong, J.3
  • 78
    • 37849005468 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor valproic acid inhibits proliferation and induces apoptosis in KM3 cells via downregulating VEGF receptor
    • Dong X.F., Song Q., Li L.Z., et al. Histone deacetylase inhibitor valproic acid inhibits proliferation and induces apoptosis in KM3 cells via downregulating VEGF receptor. Neuro Endocrinol Lett 2007, 28(6):775-780.
    • (2007) Neuro Endocrinol Lett , vol.28 , Issue.6 , pp. 775-780
    • Dong, X.F.1    Song, Q.2    Li, L.Z.3
  • 79
    • 67349232016 scopus 로고    scopus 로고
    • Valproic acid exerts anti-tumor as well as anti-angiogenic effects on myeloma
    • Kitazoe K., Abe M., Hiasa M., et al. Valproic acid exerts anti-tumor as well as anti-angiogenic effects on myeloma. Int J Hematol 2009, 89(1):45-57.
    • (2009) Int J Hematol , vol.89 , Issue.1 , pp. 45-57
    • Kitazoe, K.1    Abe, M.2    Hiasa, M.3
  • 80
    • 49649122294 scopus 로고    scopus 로고
    • Epigenetic silencing of the tetraspanin CD9 during disease progression in multiple myeloma cells and correlation with survival
    • De Bruyne E., Bos T.J., Asosingh K., et al. Epigenetic silencing of the tetraspanin CD9 during disease progression in multiple myeloma cells and correlation with survival. Clin Cancer Res 2008, 14(10):2918-2926.
    • (2008) Clin Cancer Res , vol.14 , Issue.10 , pp. 2918-2926
    • De Bruyne, E.1    Bos, T.J.2    Asosingh, K.3
  • 81
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: is transcription the primary target?
    • Johnstone R.W., Licht J.D. Histone deacetylase inhibitors in cancer therapy: is transcription the primary target?. Cancer Cell 2003, 4(1):13-18.
    • (2003) Cancer Cell , vol.4 , Issue.1 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 82
    • 12444321545 scopus 로고    scopus 로고
    • Phase I clinical trial of histone deacetylase inhibitor: suberoylanilide hydroxamic acid administered intravenously
    • Kelly W.K., Richon V.M., O'Connor O., et al. Phase I clinical trial of histone deacetylase inhibitor: suberoylanilide hydroxamic acid administered intravenously. Clin Cancer Res 2003, 9(10 Pt 1):3578-3588.
    • (2003) Clin Cancer Res , vol.9 , Issue.10 PART 1 , pp. 3578-3588
    • Kelly, W.K.1    Richon, V.M.2    O'Connor, O.3
  • 83
    • 0036301281 scopus 로고    scopus 로고
    • Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms
    • Sandor V., Bakke S., Robey R.W., et al. Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms. Clin Cancer Res 2002, 8(3):718-728.
    • (2002) Clin Cancer Res , vol.8 , Issue.3 , pp. 718-728
    • Sandor, V.1    Bakke, S.2    Robey, R.W.3
  • 84
    • 51649110503 scopus 로고    scopus 로고
    • Phase 1 study of the oral isotype specific histone deacetylase inhibitor MGCD0103 in leukemia
    • Garcia-Manero G., Assouline S., Cortes J., et al. Phase 1 study of the oral isotype specific histone deacetylase inhibitor MGCD0103 in leukemia. Blood 2008, 112(4):981-989.
    • (2008) Blood , vol.112 , Issue.4 , pp. 981-989
    • Garcia-Manero, G.1    Assouline, S.2    Cortes, J.3
  • 85
    • 34247860871 scopus 로고    scopus 로고
    • Vorinostat for treatment of cutaneous manifestations of advanced primary cutaneous T-cell lymphoma
    • Mann B.S., Johnson J.R., He K., et al. Vorinostat for treatment of cutaneous manifestations of advanced primary cutaneous T-cell lymphoma. Clin Cancer Res 2007, 13(8):2318-2322.
    • (2007) Clin Cancer Res , vol.13 , Issue.8 , pp. 2318-2322
    • Mann, B.S.1    Johnson, J.R.2    He, K.3
  • 86
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane A.A., Chabner B.A. Histone deacetylase inhibitors in cancer therapy. J Clin Oncol 2009, 27(32):5459-5468.
    • (2009) J Clin Oncol , vol.27 , Issue.32 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 87
    • 77953434862 scopus 로고    scopus 로고
    • Romidepsin (Istodax) for cutaneous T-cell lymphoma
    • Romidepsin (Istodax) for cutaneous T-cell lymphoma. Med Lett Drugs Ther 2010, 52(1339):42-43.
    • (2010) Med Lett Drugs Ther , vol.52 , Issue.1339 , pp. 42-43
  • 88
    • 34548515727 scopus 로고    scopus 로고
    • Mechanisms of HDAC inhibitor-induced thrombocytopenia
    • Matsuoka H., Unami A., Fujimura T., et al. Mechanisms of HDAC inhibitor-induced thrombocytopenia. Eur J Pharmacol 2007, 571(2-3):88-96.
    • (2007) Eur J Pharmacol , vol.571 , Issue.2-3 , pp. 88-96
    • Matsuoka, H.1    Unami, A.2    Fujimura, T.3
  • 89
    • 33746080897 scopus 로고    scopus 로고
    • Challenges of evaluating the cardiac effects of anticancer agents
    • Bates S.E., Rosing D.R., Fojo T., et al. Challenges of evaluating the cardiac effects of anticancer agents. Clin Cancer Res 2006, 12(13):3871-3874.
    • (2006) Clin Cancer Res , vol.12 , Issue.13 , pp. 3871-3874
    • Bates, S.E.1    Rosing, D.R.2    Fojo, T.3
  • 90
    • 34548276036 scopus 로고    scopus 로고
    • Molecularly targeted oncology therapeutics and prolongation of the QT interval
    • Strevel E.L., Ing D.J., Siu L.L. Molecularly targeted oncology therapeutics and prolongation of the QT interval. J Clin Oncol 2007, 25(22):3362-3371.
    • (2007) J Clin Oncol , vol.25 , Issue.22 , pp. 3362-3371
    • Strevel, E.L.1    Ing, D.J.2    Siu, L.L.3
  • 91
    • 33745683507 scopus 로고    scopus 로고
    • Cardiac studies in patients treated with depsipeptide, FK228, in a phase II trial for T-cell lymphoma
    • Piekarz R.L., Frye A.R., Wright J.J., et al. Cardiac studies in patients treated with depsipeptide, FK228, in a phase II trial for T-cell lymphoma. Clin Cancer Res 2006, 12(12):3762-3773.
    • (2006) Clin Cancer Res , vol.12 , Issue.12 , pp. 3762-3773
    • Piekarz, R.L.1    Frye, A.R.2    Wright, J.J.3
  • 92
    • 33746035691 scopus 로고    scopus 로고
    • Cardiotoxicity of histone deacetylase inhibitor depsipeptide in patients with metastatic neuroendocrine tumors
    • Shah M.H., Binkley P., Chan K., et al. Cardiotoxicity of histone deacetylase inhibitor depsipeptide in patients with metastatic neuroendocrine tumors. Clin Cancer Res 2006, 12(13):3997-4003.
    • (2006) Clin Cancer Res , vol.12 , Issue.13 , pp. 3997-4003
    • Shah, M.H.1    Binkley, P.2    Chan, K.3
  • 93
    • 34347358543 scopus 로고    scopus 로고
    • Valproic acid monotherapy leads to CR in a patient with refractory diffuse large B cell lymphoma
    • Zain J., Rotter A., Weiss L., et al. Valproic acid monotherapy leads to CR in a patient with refractory diffuse large B cell lymphoma. Leuk Lymphoma 2007, 48(6):1216-1218.
    • (2007) Leuk Lymphoma , vol.48 , Issue.6 , pp. 1216-1218
    • Zain, J.1    Rotter, A.2    Weiss, L.3
  • 94
    • 80054045887 scopus 로고    scopus 로고
    • Inhibitory effect of VPA on multiple myeloma U266 cell proliferation and regulation of histone acetylation
    • [in Chinese]
    • Zhu Y.F., Ye B.G., Shen J.Z., et al. Zhongguo Shi Yan Xue Ye Xue Za Zhi 2010, 18(3):638-641. [in Chinese].
    • (2010) Zhongguo Shi Yan Xue Ye Xue Za Zhi , vol.18 , Issue.3 , pp. 638-641
    • Zhu, Y.F.1    Ye, B.G.2    Shen, J.Z.3
  • 95
    • 71849117270 scopus 로고    scopus 로고
    • Potential efficacy of the oral histone deacetylase inhibitor vorinostat in a phase I trial in follicular and mantle cell lymphoma
    • Watanabe T., Kato H., Kobayashi Y., et al. Potential efficacy of the oral histone deacetylase inhibitor vorinostat in a phase I trial in follicular and mantle cell lymphoma. Cancer Sci 2010, 101(1):196-200.
    • (2010) Cancer Sci , vol.101 , Issue.1 , pp. 196-200
    • Watanabe, T.1    Kato, H.2    Kobayashi, Y.3
  • 96
    • 43049092663 scopus 로고    scopus 로고
    • Phase II trial of oral vorinostat (suberoylanilide hydroxamic acid) in relapsed diffuse large-B-cell lymphoma
    • Crump M., Coiffier B., Jacobsen E.D., et al. Phase II trial of oral vorinostat (suberoylanilide hydroxamic acid) in relapsed diffuse large-B-cell lymphoma. Ann Oncol 2008, 19(5):964-969.
    • (2008) Ann Oncol , vol.19 , Issue.5 , pp. 964-969
    • Crump, M.1    Coiffier, B.2    Jacobsen, E.D.3
  • 97
    • 77749333564 scopus 로고    scopus 로고
    • Phase 2 study of suberoylanilide hydroxamic acid (SAHA) in relapsed or refractory indolent non-Hodgkin lymphoma: a California Cancer Consortium Study
    • [abstract: 18515]
    • Kirshbaum M., Zain J., Popplewell L., et al. Phase 2 study of suberoylanilide hydroxamic acid (SAHA) in relapsed or refractory indolent non-Hodgkin lymphoma: a California Cancer Consortium Study. J Clin Oncol 2007, 25(18S). [abstract: 18515].
    • (2007) J Clin Oncol , vol.25 , Issue.18 S
    • Kirshbaum, M.1    Zain, J.2    Popplewell, L.3
  • 98
    • 49349104503 scopus 로고    scopus 로고
    • A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia
    • Gimsing P., Hansen M., Knudsen L.M., et al. A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia. Eur J Haematol 2008, 81(3):170-176.
    • (2008) Eur J Haematol , vol.81 , Issue.3 , pp. 170-176
    • Gimsing, P.1    Hansen, M.2    Knudsen, L.M.3
  • 99
    • 79959611523 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic properties of an oral formulation of the histone deacetylase inhibitor belinostat (PXD101)
    • Steele N.L., Plumb J.A., Vidal L., et al. Pharmacokinetic and pharmacodynamic properties of an oral formulation of the histone deacetylase inhibitor belinostat (PXD101). Cancer Chemother Pharmacol 2011, 67(6):1273-1279.
    • (2011) Cancer Chemother Pharmacol , vol.67 , Issue.6 , pp. 1273-1279
    • Steele, N.L.1    Plumb, J.A.2    Vidal, L.3
  • 100
    • 84859939412 scopus 로고    scopus 로고
    • Preliminary results of an ongoing phase I trial of oral belinostat a novel histone deacetylase inhibitor in patients with lymphoid malignancies
    • (ASH abstract book 3710)
    • Zain J. Preliminary results of an ongoing phase I trial of oral belinostat a novel histone deacetylase inhibitor in patients with lymphoid malignancies. Blood 2011, (ASH abstract book 3710).
    • (2011) Blood
    • Zain, J.1
  • 101
    • 78651374215 scopus 로고    scopus 로고
    • Phase 1 analysis of the safety and pharmacodynamics of the novel broad spectrum HDACi PCI-24781 in relapsed and refractory lymphoma
    • [abstract: 2726]
    • Evans A. Phase 1 analysis of the safety and pharmacodynamics of the novel broad spectrum HDACi PCI-24781 in relapsed and refractory lymphoma. Blood 2009, 114. [abstract: 2726].
    • (2009) Blood , vol.114
    • Evans, A.1
  • 102
    • 58149382688 scopus 로고    scopus 로고
    • Classification of lymphoid neoplasms: the microscope as a tool for disease discovery
    • Jaffe E.S., Harris N.L., Stein H., et al. Classification of lymphoid neoplasms: the microscope as a tool for disease discovery. Blood 2008, 112(12):4384-4399.
    • (2008) Blood , vol.112 , Issue.12 , pp. 4384-4399
    • Jaffe, E.S.1    Harris, N.L.2    Stein, H.3
  • 103
    • 20844443468 scopus 로고    scopus 로고
    • WHO-EORTC classification for cutaneous lymphomas
    • Willemze R., Jaffe E.S., Burg G., et al. WHO-EORTC classification for cutaneous lymphomas. Blood 2005, 105(10):3768-3785.
    • (2005) Blood , vol.105 , Issue.10 , pp. 3768-3785
    • Willemze, R.1    Jaffe, E.S.2    Burg, G.3
  • 104
    • 51649091675 scopus 로고    scopus 로고
    • International peripheral T-cell and natural killer/T-cell lymphoma study: pathology findings and clinical outcomes
    • Vose J., Armitage J., Weisenburger D. International peripheral T-cell and natural killer/T-cell lymphoma study: pathology findings and clinical outcomes. J Clin Oncol 2008, 26(25):4124-4130.
    • (2008) J Clin Oncol , vol.26 , Issue.25 , pp. 4124-4130
    • Vose, J.1    Armitage, J.2    Weisenburger, D.3
  • 105
    • 73949149251 scopus 로고    scopus 로고
    • Phase II multi-institutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma
    • Piekarz R.L., Frye R., Turner M., et al. Phase II multi-institutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma. J Clin Oncol 2009, 27(32):5410-5417.
    • (2009) J Clin Oncol , vol.27 , Issue.32 , pp. 5410-5417
    • Piekarz, R.L.1    Frye, R.2    Turner, M.3
  • 106
    • 78951475688 scopus 로고    scopus 로고
    • Final results from a pivotal, multicenter, international, open-label, phase 2 study of romidepsin in progressive or relapsed peripheral T-Cell lymphoma (PTCL) following prior systemic therapy
    • (ASH abstract book)
    • Coiffier B. Final results from a pivotal, multicenter, international, open-label, phase 2 study of romidepsin in progressive or relapsed peripheral T-Cell lymphoma (PTCL) following prior systemic therapy. Blood 2010, 114:116. (ASH abstract book).
    • (2010) Blood , vol.114 , pp. 116
    • Coiffier, B.1
  • 107
    • 78651360000 scopus 로고    scopus 로고
    • Final results of a phase 2 trial of belinostat in patients with recurrent or refractory peripheral or cutaneous T cell lymphomas
    • [abstract: 920]
    • Pohlman B. Final results of a phase 2 trial of belinostat in patients with recurrent or refractory peripheral or cutaneous T cell lymphomas. Blood 2009, [abstract: 920].
    • (2009) Blood
    • Pohlman, B.1
  • 108
    • 0036144131 scopus 로고    scopus 로고
    • Quantifying skin disease burden in mycosis fungoides-type cutaneous T-cell lymphomas: the severity-weighted assessment tool (SWAT)
    • Stevens S.R., Ke M.S., Parry E.J., et al. Quantifying skin disease burden in mycosis fungoides-type cutaneous T-cell lymphomas: the severity-weighted assessment tool (SWAT). Arch Dermatol 2002, 138(1):42-48.
    • (2002) Arch Dermatol , vol.138 , Issue.1 , pp. 42-48
    • Stevens, S.R.1    Ke, M.S.2    Parry, E.J.3
  • 110
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report
    • Piekarz R.L., Robey R., Sandor V., et al. Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report. Blood 2001, 98(9):2865-2868.
    • (2001) Blood , vol.98 , Issue.9 , pp. 2865-2868
    • Piekarz, R.L.1    Robey, R.2    Sandor, V.3
  • 111
    • 77954879663 scopus 로고    scopus 로고
    • Final results from a multicenter, international, pivotal study of romidepsin in refractory cutaneous T-cell lymphoma
    • Whittaker S.J., Demierre M.F., Kim E.J., et al. Final results from a multicenter, international, pivotal study of romidepsin in refractory cutaneous T-cell lymphoma. J Clin Oncol 2010, 28(29):4485-4491.
    • (2010) J Clin Oncol , vol.28 , Issue.29 , pp. 4485-4491
    • Whittaker, S.J.1    Demierre, M.F.2    Kim, E.J.3
  • 112
    • 0035863468 scopus 로고    scopus 로고
    • Pivotal phase III trial of two dose levels of denileukin diftitox for the treatment of cutaneous T-cell lymphoma
    • Olsen E., Duvic M., Frankel A., et al. Pivotal phase III trial of two dose levels of denileukin diftitox for the treatment of cutaneous T-cell lymphoma. J Clin Oncol 2001, 19(2):376-388.
    • (2001) J Clin Oncol , vol.19 , Issue.2 , pp. 376-388
    • Olsen, E.1    Duvic, M.2    Frankel, A.3
  • 114
    • 38949146399 scopus 로고    scopus 로고
    • A phase 1 pharmacokinetic and pharmacodynamic study of the histone deacetylase inhibitor belinostat in patients with advanced solid tumors
    • Steele N.L., Plumb J.A., Vidal L., et al. A phase 1 pharmacokinetic and pharmacodynamic study of the histone deacetylase inhibitor belinostat in patients with advanced solid tumors. Clin Cancer Res 2008, 14(3):804-810.
    • (2008) Clin Cancer Res , vol.14 , Issue.3 , pp. 804-810
    • Steele, N.L.1    Plumb, J.A.2    Vidal, L.3
  • 115
    • 67651177148 scopus 로고    scopus 로고
    • Phase II trial of oral panobinostat (LBH589) in patients with refractory cutaneous T cell lymphoma (CTCL)
    • [abstract: 8555]
    • Duvic M. Phase II trial of oral panobinostat (LBH589) in patients with refractory cutaneous T cell lymphoma (CTCL). J Clin Oncol 2008, 26(Suppl). [abstract: 8555].
    • (2008) J Clin Oncol , vol.26 , Issue.SUPPL.
    • Duvic, M.1
  • 116
    • 81855220397 scopus 로고    scopus 로고
    • Care of the adult Hodgkin lymphoma survivor
    • Thompson C.A., Mauck K., Havyer R., et al. Care of the adult Hodgkin lymphoma survivor. Am J Med 2011, 124(12):1106-1112.
    • (2011) Am J Med , vol.124 , Issue.12 , pp. 1106-1112
    • Thompson, C.A.1    Mauck, K.2    Havyer, R.3
  • 117
    • 67650874081 scopus 로고    scopus 로고
    • Cancer statistics, 2009
    • Jemal A., Siegel R., Ward E., et al. Cancer statistics, 2009. CA Cancer J Clin 2009, 59(4):225-249.
    • (2009) CA Cancer J Clin , vol.59 , Issue.4 , pp. 225-249
    • Jemal, A.1    Siegel, R.2    Ward, E.3
  • 118
    • 0141927874 scopus 로고    scopus 로고
    • Progressive disease following autologous transplantation in patients with chemosensitive relapsed or primary refractory Hodgkin's disease or aggressive non-Hodgkin's lymphoma
    • Kewalramani T., Nimer S.D., Zelenetz A.D., et al. Progressive disease following autologous transplantation in patients with chemosensitive relapsed or primary refractory Hodgkin's disease or aggressive non-Hodgkin's lymphoma. Bone Marrow Transplant 2003, 32(7):673-679.
    • (2003) Bone Marrow Transplant , vol.32 , Issue.7 , pp. 673-679
    • Kewalramani, T.1    Nimer, S.D.2    Zelenetz, A.D.3
  • 119
    • 78651366533 scopus 로고    scopus 로고
    • Vorinostat in relapsed or refractory Hodgkin lymphoma: SWOG 0517
    • [abstract: 2574]
    • Kirshbaum M. Vorinostat in relapsed or refractory Hodgkin lymphoma: SWOG 0517. Blood 2007, 110. [abstract: 2574].
    • (2007) Blood , vol.110
    • Kirshbaum, M.1
  • 120
    • 79953719767 scopus 로고    scopus 로고
    • Final analysis: phase II study of oral panobinostat in relapsed/refractory Hodgkin lymphoma in patients following autologous stem cell transplant
    • [abstract: 419], (ASH abstract book) 2010
    • Sureda A. Final analysis: phase II study of oral panobinostat in relapsed/refractory Hodgkin lymphoma in patients following autologous stem cell transplant. Blood 2010, 116. [abstract: 419], (ASH abstract book) 2010.
    • (2010) Blood , vol.116
    • Sureda, A.1
  • 121
    • 45249087368 scopus 로고    scopus 로고
    • Isotype-selective HDAC-inhibitor MGCD0103 decreases serum TARC concentrations and produces clinical responses in heavily pretreated patients with relapsed classical HL
    • [abstract: 2566]
    • Younes A. Isotype-selective HDAC-inhibitor MGCD0103 decreases serum TARC concentrations and produces clinical responses in heavily pretreated patients with relapsed classical HL. Blood 2007, 110. [abstract: 2566].
    • (2007) Blood , vol.110
    • Younes, A.1
  • 122
    • 39749103428 scopus 로고    scopus 로고
    • Phase I trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) in patients with advanced multiple myeloma
    • Richardson P., Mitsiades C., Colson K., et al. Phase I trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) in patients with advanced multiple myeloma. Leuk Lymphoma 2008, 49(3):502-507.
    • (2008) Leuk Lymphoma , vol.49 , Issue.3 , pp. 502-507
    • Richardson, P.1    Mitsiades, C.2    Colson, K.3
  • 123
    • 78650992102 scopus 로고    scopus 로고
    • Phase 2 trial of the histone deacetylase inhibitor romidepsin for the treatment of refractory multiple myeloma
    • Niesvizky R., Ely S., Mark T., et al. Phase 2 trial of the histone deacetylase inhibitor romidepsin for the treatment of refractory multiple myeloma. Cancer 2011, 117(2):336-342.
    • (2011) Cancer , vol.117 , Issue.2 , pp. 336-342
    • Niesvizky, R.1    Ely, S.2    Mark, T.3
  • 124
    • 0037852202 scopus 로고    scopus 로고
    • The proteasome: structure, function, and role in the cell
    • Adams J. The proteasome: structure, function, and role in the cell. Cancer Treat Rev 2003, 29(Suppl 1):3-9.
    • (2003) Cancer Treat Rev , vol.29 , Issue.SUPPL. 1 , pp. 3-9
    • Adams, J.1
  • 125
    • 77955871803 scopus 로고    scopus 로고
    • Histone deacetylases are critical targets of bortezomib-induced cytotoxicity in multiple myeloma
    • Kikuchi J., Wada T., Shimizu R., et al. Histone deacetylases are critical targets of bortezomib-induced cytotoxicity in multiple myeloma. Blood 2010, 116(3):406-417.
    • (2010) Blood , vol.116 , Issue.3 , pp. 406-417
    • Kikuchi, J.1    Wada, T.2    Shimizu, R.3
  • 126
    • 2542523228 scopus 로고    scopus 로고
    • Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors
    • Pei X.Y., Dai Y., Grant S. Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors. Clin Cancer Res 2004, 10(11):3839-3852.
    • (2004) Clin Cancer Res , vol.10 , Issue.11 , pp. 3839-3852
    • Pei, X.Y.1    Dai, Y.2    Grant, S.3
  • 127
    • 34848873093 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, PXD101, potentiates bortezomib-induced anti-multiple myeloma effect by induction of oxidative stress and DNA damage
    • Feng R., Oton A., Mapara M.Y., et al. The histone deacetylase inhibitor, PXD101, potentiates bortezomib-induced anti-multiple myeloma effect by induction of oxidative stress and DNA damage. Br J Haematol 2007, 139(3):385-397.
    • (2007) Br J Haematol , vol.139 , Issue.3 , pp. 385-397
    • Feng, R.1    Oton, A.2    Mapara, M.Y.3
  • 128
    • 53049110009 scopus 로고    scopus 로고
    • Myc regulates aggresome formation, the induction of Noxa, and apoptosis in response to the combination of bortezomib and SAHA
    • Nawrocki S.T., Carew J.S., Maclean K.H., et al. Myc regulates aggresome formation, the induction of Noxa, and apoptosis in response to the combination of bortezomib and SAHA. Blood 2008, 112(7):2917-2926.
    • (2008) Blood , vol.112 , Issue.7 , pp. 2917-2926
    • Nawrocki, S.T.1    Carew, J.S.2    Maclean, K.H.3
  • 129
    • 79953235225 scopus 로고    scopus 로고
    • Vorinostat combined with bortezomib in patients with relapsed or relapsed and refractory multiple myeloma: update on the Vantage Study Program
    • (ASH meeting abstract # 1952)
    • Siegel D.S., Jagannath S., Hajek R., et al. Vorinostat combined with bortezomib in patients with relapsed or relapsed and refractory multiple myeloma: update on the Vantage Study Program. Blood 2010, 116(21). (ASH meeting abstract # 1952).
    • (2010) Blood , vol.116 , Issue.21
    • Siegel, D.S.1    Jagannath, S.2    Hajek, R.3
  • 130
    • 77954678294 scopus 로고    scopus 로고
    • Vorinostat plus bortezomib for the treatment of relapsed/refractory multiple myeloma: a case series illustrating utility in clinical practice
    • Mazumder A., Vesole D.H., Jagannath S. Vorinostat plus bortezomib for the treatment of relapsed/refractory multiple myeloma: a case series illustrating utility in clinical practice. Clin Lymphoma Myeloma Leuk 2010, 10(2):149-151.
    • (2010) Clin Lymphoma Myeloma Leuk , vol.10 , Issue.2 , pp. 149-151
    • Mazumder, A.1    Vesole, D.H.2    Jagannath, S.3
  • 131
    • 77955270038 scopus 로고    scopus 로고
    • Combined proteasome and histone deacetylase inhibition: a promising synergy for patients with relapsed/refractory multiple myeloma
    • Jagannath S., Dimopoulos M.A., Lonial S. Combined proteasome and histone deacetylase inhibition: a promising synergy for patients with relapsed/refractory multiple myeloma. Leuk Res 2010, 34(9):1111-1118.
    • (2010) Leuk Res , vol.34 , Issue.9 , pp. 1111-1118
    • Jagannath, S.1    Dimopoulos, M.A.2    Lonial, S.3
  • 132
    • 34250767283 scopus 로고    scopus 로고
    • 5-Azacytidine, a DNA methyltransferase inhibitor, induces ATR-mediated DNA double-strand break responses, apoptosis, and synergistic cytotoxicity with doxorubicin and bortezomib against multiple myeloma cells
    • Kiziltepe T., Hideshima T., Catley L., et al. 5-Azacytidine, a DNA methyltransferase inhibitor, induces ATR-mediated DNA double-strand break responses, apoptosis, and synergistic cytotoxicity with doxorubicin and bortezomib against multiple myeloma cells. Mol Cancer Ther 2007, 6(6):1718-1727.
    • (2007) Mol Cancer Ther , vol.6 , Issue.6 , pp. 1718-1727
    • Kiziltepe, T.1    Hideshima, T.2    Catley, L.3
  • 133
    • 56449128746 scopus 로고    scopus 로고
    • New drugs in multiple myeloma: mechanisms of action and phase I/II clinical findings
    • Ocio E.M., Mateos M.V., Maiso P., et al. New drugs in multiple myeloma: mechanisms of action and phase I/II clinical findings. Lancet Oncol 2008, 9(12):1157-1165.
    • (2008) Lancet Oncol , vol.9 , Issue.12 , pp. 1157-1165
    • Ocio, E.M.1    Mateos, M.V.2    Maiso, P.3
  • 134
    • 0037276902 scopus 로고    scopus 로고
    • The interaction of histone deacetylase inhibitors and DNA methyltransferase inhibitors in the treatment of human cancer cells
    • Zhu W.G., Otterson G.A. The interaction of histone deacetylase inhibitors and DNA methyltransferase inhibitors in the treatment of human cancer cells. Curr Med Chem Anticancer Agents 2003, 3(3):187-199.
    • (2003) Curr Med Chem Anticancer Agents , vol.3 , Issue.3 , pp. 187-199
    • Zhu, W.G.1    Otterson, G.A.2
  • 135
    • 84859993255 scopus 로고    scopus 로고
    • Regulation of Bim expression by IGF-1 in the 5T33MM murine model for multiple myeloma
    • (ASH abstract book)
    • De Bruyne E. Regulation of Bim expression by IGF-1 in the 5T33MM murine model for multiple myeloma. Blood 2007, 110:3512. (ASH abstract book).
    • (2007) Blood , vol.110 , pp. 3512
    • De Bruyne, E.1
  • 136
    • 26844453345 scopus 로고    scopus 로고
    • Perspectives for combination therapy to overcome drug-resistant multiple myeloma
    • Catley L., Tai Y.T., Chauhan D., et al. Perspectives for combination therapy to overcome drug-resistant multiple myeloma. Drug Resist Updat 2005, 8(4):205-218.
    • (2005) Drug Resist Updat , vol.8 , Issue.4 , pp. 205-218
    • Catley, L.1    Tai, Y.T.2    Chauhan, D.3
  • 137
    • 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 2005, 7(7):646-657.
    • (2005) Neoplasia , vol.7 , Issue.7 , pp. 646-657
    • Fandy, T.E.1    Shankar, S.2    Ross, D.D.3
  • 138
    • 33644486735 scopus 로고    scopus 로고
    • Interactive effects of histone deacetylase inhibitors and TRAIL on apoptosis in human leukemia cells: involvement of both death receptor and mitochondrial pathways
    • Shankar S., Singh T.R., Fandy T.E., et al. Interactive effects of histone deacetylase inhibitors and TRAIL on apoptosis in human leukemia cells: involvement of both death receptor and mitochondrial pathways. Int J Mol Med 2005, 16(6):1125-1138.
    • (2005) Int J Mol Med , vol.16 , Issue.6 , pp. 1125-1138
    • Shankar, S.1    Singh, T.R.2    Fandy, T.E.3
  • 139
    • 74549173443 scopus 로고    scopus 로고
    • Romidepsin and belinostat synergize the antineoplastic effect of bortezomib in mantle cell lymphoma
    • Paoluzzi L., Scotto L., Marchi E., et al. Romidepsin and belinostat synergize the antineoplastic effect of bortezomib in mantle cell lymphoma. Clin Cancer Res 2010, 16(2):554-565.
    • (2010) Clin Cancer Res , vol.16 , Issue.2 , pp. 554-565
    • Paoluzzi, L.1    Scotto, L.2    Marchi, E.3
  • 140
    • 38049126172 scopus 로고    scopus 로고
    • Synergistic interaction of the histone deacetylase inhibitor SAHA with the proteasome inhibitor bortezomib in mantle cell lymphoma
    • Heider U., von Metzler I., Kaiser M., et al. Synergistic interaction of the histone deacetylase inhibitor SAHA with the proteasome inhibitor bortezomib in mantle cell lymphoma. Eur J Haematol 2008, 80(2):133-142.
    • (2008) Eur J Haematol , vol.80 , Issue.2 , pp. 133-142
    • Heider, U.1    von Metzler, I.2    Kaiser, M.3
  • 141
    • 38949105902 scopus 로고    scopus 로고
    • Interactions between bortezomib and romidepsin and belinostat in chronic lymphocytic leukemia cells
    • Dai Y., Chen S., Kramer L.B., et al. Interactions between bortezomib and romidepsin and belinostat in chronic lymphocytic leukemia cells. Clin Cancer Res 2008, 14(2):549-558.
    • (2008) Clin Cancer Res , vol.14 , Issue.2 , pp. 549-558
    • Dai, Y.1    Chen, S.2    Kramer, L.B.3
  • 142
    • 77953937449 scopus 로고    scopus 로고
    • The pan-HDAC inhibitor vorinostat potentiates the activity of the proteasome inhibitor carfilzomib in human DLBCL cells in vitro and in vivo
    • Dasmahapatra G., Lembersky D., Kramer L., et al. The pan-HDAC inhibitor vorinostat potentiates the activity of the proteasome inhibitor carfilzomib in human DLBCL cells in vitro and in vivo. Blood 2010, 115(22):4478-4487.
    • (2010) Blood , vol.115 , Issue.22 , pp. 4478-4487
    • Dasmahapatra, G.1    Lembersky, D.2    Kramer, L.3
  • 143
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J., Nikolaev A.Y., Imai S., et al. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 2001, 107(2):137-148.
    • (2001) Cell , vol.107 , Issue.2 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3
  • 144
    • 84859986964 scopus 로고    scopus 로고
    • DNA methylation is involved in malignancy and is seen, in progression, in more than 80% of all solid tumours. Methylation is one of the main physiological processes to induce silencing of gene expression
    • (ASH meeting abstract # 3733)
    • Amengual J. DNA methylation is involved in malignancy and is seen, in progression, in more than 80% of all solid tumours. Methylation is one of the main physiological processes to induce silencing of gene expression. Blood 2011, (ASH meeting abstract # 3733).
    • (2011) Blood
    • Amengual, J.1
  • 145
    • 78651346762 scopus 로고    scopus 로고
    • Phase I trial of oral vorinostat in combination with bexarotene in advanced cutaneous T-cell lymphoma
    • [abstract 0270]
    • Dummer R. Phase I trial of oral vorinostat in combination with bexarotene in advanced cutaneous T-cell lymphoma. Haematologica 2008, 93(sl):110. [abstract 0270].
    • (2008) Haematologica , vol.93 , Issue.SL , pp. 110
    • Dummer, R.1
  • 146
    • 84858118209 scopus 로고    scopus 로고
    • Combination of epigenetic agents synergistically reverse the malignant phenotype in models of T-cell lymphoma
    • (ASH meeting abstract # 2727)
    • Marchi E. Combination of epigenetic agents synergistically reverse the malignant phenotype in models of T-cell lymphoma. Blood 2011, (ASH meeting abstract # 2727).
    • (2011) Blood
    • Marchi, E.1
  • 147
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
    • Gregoretti I.V., Lee Y.M., Goodson H.V. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol 2004, 338(1):17-31.
    • (2004) J Mol Biol , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 148
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C., Guardiola A., Shao R., et al. HDAC6 is a microtubule-associated deacetylase. Nature 2002, 417(6887):455-458.
    • (2002) Nature , vol.417 , Issue.6887 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 149
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • Gao L., Cueto M.A., Asselbergs F., et al. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem 2002, 277(28):25748-25755.
    • (2002) J Biol Chem , vol.277 , Issue.28 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3
  • 150
    • 0037925520 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2
    • Kramer O.H., Zhu P., Ostendorff H.P., et al. The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2. EMBO J 2003, 22(13):3411-3420.
    • (2003) EMBO J , vol.22 , Issue.13 , pp. 3411-3420
    • Kramer, O.H.1    Zhu, P.2    Ostendorff, H.P.3
  • 151
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden J.E., Peart M.J., Johnstone R.W. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 2006, 5(9):769-784.
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 152
    • 0142179154 scopus 로고    scopus 로고
    • Identification of novel isoform-selective inhibitors within class I histone deacetylases
    • Hu E., Dul E., Sung C.M., et al. Identification of novel isoform-selective inhibitors within class I histone deacetylases. J Pharmacol Exp Ther 2003, 307(2):720-728.
    • (2003) J Pharmacol Exp Ther , vol.307 , Issue.2 , pp. 720-728
    • Hu, E.1    Dul, E.2    Sung, C.M.3
  • 153
    • 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 2002, 62(17):4916-4921.
    • (2002) Cancer Res , vol.62 , Issue.17 , pp. 4916-4921
    • Furumai, R.1    Matsuyama, A.2    Kobashi, N.3
  • 154
    • 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 2004, 64(7):2580-2589.
    • (2004) Cancer Res , vol.64 , Issue.7 , pp. 2580-2589
    • Guo, F.1    Sigua, C.2    Tao, J.3
  • 155
    • 13444306459 scopus 로고    scopus 로고
    • Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells
    • Nebbioso A., Clarke N., Voltz E., et al. Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells. Nat Med 2005, 11(1):77-84.
    • (2005) Nat Med , vol.11 , Issue.1 , pp. 77-84
    • Nebbioso, A.1    Clarke, N.2    Voltz, E.3
  • 156
    • 0028927607 scopus 로고
    • The Fas death factor
    • Nagata S., Golstein P. The Fas death factor. Science 1995, 267(5203):1449-1456.
    • (1995) Science , vol.267 , Issue.5203 , pp. 1449-1456
    • Nagata, S.1    Golstein, P.2
  • 157
    • 49849103540 scopus 로고    scopus 로고
    • Characterisation of the novel apoptotic and therapeutic activities of the histone deacetylase inhibitor romidepsin
    • Newbold A., Lindemann R.K., Cluse L.A., et al. Characterisation of the novel apoptotic and therapeutic activities of the histone deacetylase inhibitor romidepsin. Mol Cancer Ther 2008, 7(5):1066-1079.
    • (2008) Mol Cancer Ther , vol.7 , Issue.5 , pp. 1066-1079
    • Newbold, A.1    Lindemann, R.K.2    Cluse, L.A.3
  • 158
    • 34249941680 scopus 로고    scopus 로고
    • Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma
    • Lindemann R.K., Newbold A., Whitecross K.F., et al. Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma. Proc Natl Acad Sci U S A 2007, 104(19):8071-8076.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.19 , pp. 8071-8076
    • Lindemann, R.K.1    Newbold, A.2    Whitecross, K.F.3
  • 159
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science 1998, 281(5381):1312-1316.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 160
    • 0032807406 scopus 로고    scopus 로고
    • The modular nature of apoptotic signaling proteins
    • Hofmann K. The modular nature of apoptotic signaling proteins. Cell Mol Life Sci 1999, 55(8-9):1113-1128.
    • (1999) Cell Mol Life Sci , vol.55 , Issue.8-9 , pp. 1113-1128
    • Hofmann, K.1
  • 161
    • 0042090495 scopus 로고    scopus 로고
    • Novel mechanisms of apoptosis induced by histone deacetylase inhibitors
    • Peart M.J., Tainton K.M., Ruefli A.A., et al. Novel mechanisms of apoptosis induced by histone deacetylase inhibitors. Cancer Res 2003, 63(15):4460-4471.
    • (2003) Cancer Res , vol.63 , Issue.15 , pp. 4460-4471
    • Peart, M.J.1    Tainton, K.M.2    Ruefli, A.A.3
  • 162
    • 0035048449 scopus 로고    scopus 로고
    • Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes
    • Kim M.S., Kwon H.J., Lee Y.M., et al. Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. Nat Med 2001, 7(4):437-443.
    • (2001) Nat Med , vol.7 , Issue.4 , pp. 437-443
    • Kim, M.S.1    Kwon, H.J.2    Lee, Y.M.3
  • 163
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation
    • Jeong J.W., Bae M.K., Ahn M.Y., et al. Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. Cell 2002, 111(5):709-720.
    • (2002) Cell , vol.111 , Issue.5 , pp. 709-720
    • Jeong, J.W.1    Bae, M.K.2    Ahn, M.Y.3
  • 164
    • 34447509697 scopus 로고    scopus 로고
    • Vorinostat: a new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma
    • Duvic M., Vu J. Vorinostat: a new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma. Expert Opin Investig Drugs 2007, 16(7):1111-1120.
    • (2007) Expert Opin Investig Drugs , vol.16 , Issue.7 , pp. 1111-1120
    • Duvic, M.1    Vu, J.2
  • 165
    • 14844353574 scopus 로고    scopus 로고
    • Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors
    • Peart M.J., Smyth G.K., van Laar R.K., et al. Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors. Proc Natl Acad Sci U S A 2005, 102(10):3697-3702.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.10 , pp. 3697-3702
    • Peart, M.J.1    Smyth, G.K.2    van Laar, R.K.3
  • 166
    • 33645230001 scopus 로고    scopus 로고
    • Acetylation of p53 at lysine 373/382 by the histone deacetylase inhibitor depsipeptide induces expression of p21(Waf1/Cip1)
    • Zhao Y., Lu S., Wu L., et al. Acetylation of p53 at lysine 373/382 by the histone deacetylase inhibitor depsipeptide induces expression of p21(Waf1/Cip1). Mol Cell Biol 2006, 26(7):2782-2790.
    • (2006) Mol Cell Biol , vol.26 , Issue.7 , pp. 2782-2790
    • Zhao, Y.1    Lu, S.2    Wu, L.3
  • 167
    • 20744449274 scopus 로고    scopus 로고
    • Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NF-kappaB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP downregulation, and c-Jun N-terminal kinase 1 activation
    • Dai Y., Rahmani M., Dent P., et al. Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NF-kappaB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP downregulation, and c-Jun N-terminal kinase 1 activation. Mol Cell Biol 2005, 25(13):5429-5444.
    • (2005) Mol Cell Biol , vol.25 , Issue.13 , pp. 5429-5444
    • Dai, Y.1    Rahmani, M.2    Dent, P.3
  • 168
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S., Wagner T., Heinzel T., et al. Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int J Biochem Cell Biol 2009, 41(1):185-198.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.1 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3
  • 169
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • Bereshchenko O.R., Gu W., Dalla-Favera R. Acetylation inactivates the transcriptional repressor BCL6. Nat Genet 2002, 32(4):606-613.
    • (2002) Nat Genet , vol.32 , Issue.4 , pp. 606-613
    • Bereshchenko, O.R.1    Gu, W.2    Dalla-Favera, R.3
  • 170
    • 80053192714 scopus 로고    scopus 로고
    • Disruption of IkappaB kinase (IKK)-mediated RelA serine 536 phosphorylation sensitizes human multiple myeloma cells to histone deacetylase (HDAC) inhibitors
    • Dai Y., Chen S., Wang L., et al. Disruption of IkappaB kinase (IKK)-mediated RelA serine 536 phosphorylation sensitizes human multiple myeloma cells to histone deacetylase (HDAC) inhibitors. J Biol Chem 2011, 286(39):34036-34050.
    • (2011) J Biol Chem , vol.286 , Issue.39 , pp. 34036-34050
    • Dai, Y.1    Chen, S.2    Wang, L.3
  • 171
    • 27644586649 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors radiosensitize human melanoma cells by suppressing DNA repair activity
    • Munshi A., Kurland J.F., Nishikawa T., et al. Histone deacetylase inhibitors radiosensitize human melanoma cells by suppressing DNA repair activity. Clin Cancer Res 2005, 11(13):4912-4922.
    • (2005) Clin Cancer Res , vol.11 , Issue.13 , pp. 4912-4922
    • Munshi, A.1    Kurland, J.F.2    Nishikawa, T.3
  • 172
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis
    • Cohen H.Y., Lavu S., Bitterman K.J., et al. Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis. Mol Cell 2004, 13(5):627-638.
    • (2004) Mol Cell , vol.13 , Issue.5 , pp. 627-638
    • Cohen, H.Y.1    Lavu, S.2    Bitterman, K.J.3
  • 173
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs J.J., Murphy P.J., Gaillard S., et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell 2005, 18(5):601-607.
    • (2005) Mol Cell , vol.18 , Issue.5 , pp. 601-607
    • Kovacs, J.J.1    Murphy, P.J.2    Gaillard, S.3
  • 174
    • 34047097863 scopus 로고    scopus 로고
    • FK228 inhibits Hsp90 chaperone function in K562 cells via hyperacetylation of Hsp70
    • Wang Y., Wang S.Y., Zhang X.H., et al. FK228 inhibits Hsp90 chaperone function in K562 cells via hyperacetylation of Hsp70. Biochem Biophys Res Commun 2007, 356(4):998-1003.
    • (2007) Biochem Biophys Res Commun , vol.356 , Issue.4 , pp. 998-1003
    • Wang, Y.1    Wang, S.Y.2    Zhang, X.H.3
  • 175
    • 25144496594 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases alter kinetochore assembly by disrupting pericentromeric heterochromatin
    • Robbins A.R., Jablonski S.A., Yen T.J., et al. Inhibitors of histone deacetylases alter kinetochore assembly by disrupting pericentromeric heterochromatin. Cell Cycle 2005, 4(5):717-726.
    • (2005) Cell Cycle , vol.4 , Issue.5 , pp. 717-726
    • Robbins, A.R.1    Jablonski, S.A.2    Yen, T.J.3
  • 176
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli A.A., Ausserlechner M.J., Bernhard D., et al. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc Natl Acad Sci U S A 2001, 98(19):10833-10838.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.19 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3
  • 177
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
    • Butler L.M., Zhou X., Xu W.S., et al. The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc Natl Acad Sci U S A 2002, 99(18):11700-11705.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.18 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3
  • 178
    • 0035132573 scopus 로고    scopus 로고
    • Induction of MAGE-3 expression in lung and esophageal cancer cells
    • [discussion: 301-2]
    • Weiser T.S., Ohnmacht G.A., Guo Z.S., et al. Induction of MAGE-3 expression in lung and esophageal cancer cells. Ann Thorac Surg 2001, 71(1):295-301. [discussion: 301-2].
    • (2001) Ann Thorac Surg , vol.71 , Issue.1 , pp. 295-301
    • Weiser, T.S.1    Ohnmacht, G.A.2    Guo, Z.S.3
  • 179
    • 0035126974 scopus 로고    scopus 로고
    • Sequential 5-Aza-2 deoxycytidine-depsipeptide FR901228 treatment induces apoptosis preferentially in cancer cells and facilitates their recognition by cytolytic T lymphocytes specific for NY-ESO-1
    • Weiser T.S., Guo Z.S., Ohnmacht G.A., et al. Sequential 5-Aza-2 deoxycytidine-depsipeptide FR901228 treatment induces apoptosis preferentially in cancer cells and facilitates their recognition by cytolytic T lymphocytes specific for NY-ESO-1. J Immunother 2001, 24(2):151-161.
    • (2001) J Immunother , vol.24 , Issue.2 , pp. 151-161
    • Weiser, T.S.1    Guo, Z.S.2    Ohnmacht, G.A.3


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