메뉴 건너뛰기




Volumn 23, Issue 17, 2005, Pages 3971-3993

Epigenetic and chromatin modifiers as targeted therapy of hematologic malignancies

Author keywords

[No Author keywords available]

Indexed keywords

4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; 4 N ACETYLDINALINE; 5 AZA 2' DEOXYCYTIDINE; 5 AZACITIDINE; APICIDIN; AZACITIDINE; BORTEZOMIB; CYCLOHEXIMIDE; DEOXYCYTIDINE; FR 901228; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; UNCLASSIFIED DRUG; VORINOSTAT; ZEBULARINE; HISTONE DEACETYLASE; METHYLTRANSFERASE;

EID: 21244467166     PISSN: 0732183X     EISSN: None     Source Type: Journal    
DOI: 10.1200/JCO.2005.16.600     Document Type: Review
Times cited : (289)

References (303)
  • 1
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • Bird A: DNA methylation patterns and epigenetic memory. Genes Dev 16:6-21, 2002
    • (2002) Genes Dev , vol.16 , pp. 6-21
    • Bird, A.1
  • 2
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones PA, Baylin SB: The fundamental role of epigenetic events in cancer. Nat Rev Genet 3:415-428, 2002
    • (2002) Nat Rev Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 3
    • 0034176798 scopus 로고    scopus 로고
    • DNA hypermethylation in tumorigenesis: Epigenetics joins genetics
    • Baylin SB, Herman JG: DNA hypermethylation in tumorigenesis: Epigenetics joins genetics. Trends Genet 16:168-174, 2000
    • (2000) Trends Genet , vol.16 , pp. 168-174
    • Baylin, S.B.1    Herman, J.G.2
  • 4
    • 1042278765 scopus 로고    scopus 로고
    • The history of cancer epigenetics
    • Feinberg AP, Tycko B: The history of cancer epigenetics. Nat Rev Cancer 4:143-153, 2004
    • (2004) Nat Rev Cancer , vol.4 , pp. 143-153
    • Feinberg, A.P.1    Tycko, B.2
  • 5
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD: The language of covalent histone modifications. Nature 403:41-45, 2000
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 6
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD: Translating the histone code. Science 293:1074-1080, 2001
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 7
    • 1042290351 scopus 로고    scopus 로고
    • The SWI/SNF complex-Chromatin and cancer
    • Roberts CW, Orkin SH: The SWI/SNF complex-Chromatin and cancer. Nat Rev Cancer 4:133-142, 2004
    • (2004) Nat Rev Cancer , vol.4 , pp. 133-142
    • Roberts, C.W.1    Orkin, S.H.2
  • 8
    • 0347444723 scopus 로고    scopus 로고
    • MicroRNAs: Genomics, biogenesis, mechanism, and function
    • Bartel DP: MicroRNAs: Genomics, biogenesis, mechanism, and function. Cell 116:281-297, 2004
    • (2004) Cell , vol.116 , pp. 281-297
    • Bartel, D.P.1
  • 9
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein B, Kinzler KW: Cancer genes and the pathways they control. Nat Med 10:789-799, 2004
    • (2004) Nat Med , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 10
    • 4744344066 scopus 로고    scopus 로고
    • Epigenetics and cancer
    • Lund AH, van Lohuizen M: Epigenetics and cancer. Genes Dev 18:2315-2335, 2004
    • (2004) Genes Dev , vol.18 , pp. 2315-2335
    • Lund, A.H.1    van Lohuizen, M.2
  • 11
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA: The hallmarks of cancer. Cell 100:57-70, 2000
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 12
    • 0033566302 scopus 로고    scopus 로고
    • Chromatin remodeling and leukemia: New therapeutic paradigms
    • Redner RL, Wang J, Liu JM: Chromatin remodeling and leukemia: New therapeutic paradigms. Blood 94:417-428, 1999
    • (1999) Blood , vol.94 , pp. 417-428
    • Redner, R.L.1    Wang, J.2    Liu, J.M.3
  • 13
    • 0036040215 scopus 로고    scopus 로고
    • Chromatin modification, leukaemia and implications for therapy
    • Jones LK, Saha V: Chromatin modification, leukaemia and implications for therapy. Br J Haematol 118:714-727, 2002
    • (2002) Br J Haematol , vol.118 , pp. 714-727
    • Jones, L.K.1    Saha, V.2
  • 14
    • 0345357773 scopus 로고    scopus 로고
    • Gene silencing in cancer in association with promoter hypermethylation
    • Herman JG, Baylin SB: Gene silencing in cancer in association with promoter hypermethylation. N Engl J Med 349:2042-2054, 2003
    • (2003) N Engl J Med , vol.349 , pp. 2042-2054
    • Herman, J.G.1    Baylin, S.B.2
  • 15
    • 10344260184 scopus 로고    scopus 로고
    • CpG island methylator phenotype in cancer
    • Issa JP: CpG island methylator phenotype in cancer. Nat Rev Cancer 4:988-993, 2004
    • (2004) Nat Rev Cancer , vol.4 , pp. 988-993
    • Issa, J.P.1
  • 16
    • 0035962631 scopus 로고    scopus 로고
    • DNA methylation, methyltransferases, and cancer
    • Robertson KD: DNA methylation, methyltransferases, and cancer. Oncogene 20:3139-3155, 2001
    • (2001) Oncogene , vol.20 , pp. 3139-3155
    • Robertson, K.D.1
  • 17
    • 0344321897 scopus 로고    scopus 로고
    • Impact of aging on DNA methylation
    • Richardson B: Impact of aging on DNA methylation. Ageing Res Rev 2:245-261, 2003
    • (2003) Ageing Res Rev , vol.2 , pp. 245-261
    • Richardson, B.1
  • 18
    • 0020627846 scopus 로고
    • Hypomethylation of ras oncogenes in primary human cancers
    • Feinberg AP, Vogelstein B: Hypomethylation of ras oncogenes in primary human cancers. Biochem Biophys Res Commun 111:47-54, 1983
    • (1983) Biochem Biophys Res Commun , vol.111 , pp. 47-54
    • Feinberg, A.P.1    Vogelstein, B.2
  • 19
    • 0027239823 scopus 로고
    • bcl-2 gene hypomethylation and high-level expression in B-cell chronic lymphocytic leukemia
    • Hanada M, Delia D, Aiello A, et al: bcl-2 gene hypomethylation and high-level expression in B-cell chronic lymphocytic leukemia. Blood 82:1820-1828, 1993
    • (1993) Blood , vol.82 , pp. 1820-1828
    • Hanada, M.1    Delia, D.2    Aiello, A.3
  • 20
    • 1042263110 scopus 로고    scopus 로고
    • Promoter methylation of cyclin D2 gene in gastric carcinoma
    • Oshimo Y, Nakayama H, Ito R, et al: Promoter methylation of cyclin D2 gene in gastric carcinoma. Int J Oncol 23:1663-1670, 2003
    • (2003) Int J Oncol , vol.23 , pp. 1663-1670
    • Oshimo, Y.1    Nakayama, H.2    Ito, R.3
  • 21
    • 0037068353 scopus 로고    scopus 로고
    • DNA methylation in cancer: Too much, but also too little
    • Ehrlich M: DNA methylation in cancer: Too much, but also too little. Oncogene 21:5400-5413, 2002
    • (2002) Oncogene , vol.21 , pp. 5400-5413
    • Ehrlich, M.1
  • 22
    • 0032480226 scopus 로고    scopus 로고
    • DNA hypomethylation leads to elevated mutation rates
    • Chen RZ, Pettersson U, Beard C, et al: DNA hypomethylation leads to elevated mutation rates. Nature 395:89-93, 1998
    • (1998) Nature , vol.395 , pp. 89-93
    • Chen, R.Z.1    Pettersson, U.2    Beard, C.3
  • 23
    • 0242584449 scopus 로고    scopus 로고
    • Induction of tumors in mice by genomic hypomethylation
    • Gaudet F, Hodgson JG, Eden A: Induction of tumors in mice by genomic hypomethylation. Science 300:489-492, 2003
    • (2003) Science , vol.300 , pp. 489-492
    • Gaudet, F.1    Hodgson, J.G.2    Eden, A.3
  • 24
    • 0031017268 scopus 로고    scopus 로고
    • Methylation of the hMLH1 promoter correlates with lack of expression of hMLH1 in sporadic colon tumors and mismatch repair-defective human tumor cell lines
    • Kane MF, Loda M, Gaida GM, et al: Methylation of the hMLH1 promoter correlates with lack of expression of hMLH1 in sporadic colon tumors and mismatch repair-defective human tumor cell lines. Cancer Res 57:808-811, 1997
    • (1997) Cancer Res , vol.57 , pp. 808-811
    • Kane, M.F.1    Loda, M.2    Gaida, G.M.3
  • 25
    • 13144266670 scopus 로고    scopus 로고
    • Incidence and functional consequences of hMLH1 promoter hypermethylation in colorectal carcinoma
    • Herman JG, Umar A, Polyak K, et al: Incidence and functional consequences of hMLH1 promoter hypermethylation in colorectal carcinoma. Proc Natl Acad Sci U S A 95:6870-6875, 1998
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6870-6875
    • Herman, J.G.1    Umar, A.2    Polyak, K.3
  • 26
    • 0033587747 scopus 로고    scopus 로고
    • CpG island methylator phenotype in colorectal cancer
    • Toyota M, Ahuja N, Ohe-Toyota M, et al: CpG island methylator phenotype in colorectal cancer. Proc Natl Acad Sci U S A 96:8681-8686, 1999
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8681-8686
    • Toyota, M.1    Ahuja, N.2    Ohe-Toyota, M.3
  • 27
    • 0033229890 scopus 로고    scopus 로고
    • Aberrant methylation in gastric cancer associated with the CpG island methylator phenotype
    • Toyota M, Ahuja N, Suzuki H, et al: Aberrant methylation in gastric cancer associated with the CpG island methylator phenotype. Cancer Res 59:5438-5442, 1999
    • (1999) Cancer Res , vol.59 , pp. 5438-5442
    • Toyota, M.1    Ahuja, N.2    Suzuki, H.3
  • 28
    • 0034795045 scopus 로고    scopus 로고
    • Promoter methylation of the DNA repair gene MGMT in astrocytomas is frequently associated with G:C → A:T mutations of the TP53 tumor suppressor gene
    • Nakamura M, Watanabe T, Yonekawa Y, et al: Promoter methylation of the DNA repair gene MGMT in astrocytomas is frequently associated with G:C → A:T mutations of the TP53 tumor suppressor gene. Carcinogenesis 22:1715-1719, 2001
    • (2001) Carcinogenesis , vol.22 , pp. 1715-1719
    • Nakamura, M.1    Watanabe, T.2    Yonekawa, Y.3
  • 29
    • 19244370208 scopus 로고    scopus 로고
    • Inactivation of the DNA repair gene O6-methylguanine-DNA methyltransferase by promoter hypermethylation is associated with G to A mutations in K-ras in colorectal tumorigenesis
    • Esteller M, Toyota M, Sanchez-Cespedes M, et al: Inactivation of the DNA repair gene O6-methylguanine-DNA methyltransferase by promoter hypermethylation is associated with G to A mutations in K-ras in colorectal tumorigenesis. Cancer Res 60:2368-2371, 2000
    • (2000) Cancer Res , vol.60 , pp. 2368-2371
    • Esteller, M.1    Toyota, M.2    Sanchez-Cespedes, M.3
  • 30
    • 0036243106 scopus 로고    scopus 로고
    • High level of microsatellite instability but not hypermethylation of mismatch repair genes in therapy-related and secondary acute myeloid leukaemia and myelodysplastic syndrome
    • Sheikhha MH, Tobal K, Liu Yin JA, et al: High level of microsatellite instability but not hypermethylation of mismatch repair genes in therapy-related and secondary acute myeloid leukaemia and myelodysplastic syndrome. Br J Haematol 117:359-365, 2002
    • (2002) Br J Haematol , vol.117 , pp. 359-365
    • Sheikhha, M.H.1    Tobal, K.2    Liu Yin, J.A.3
  • 31
    • 0035895208 scopus 로고    scopus 로고
    • Loss of imprinting of the insulin-like growth factor II gene occurs by biallelic methylation in a core region of H19-associated CTCF-binding sites in colorectal cancer
    • Nakagawa H, Chadwick RB, Peltomaki P, et al: Loss of imprinting of the insulin-like growth factor II gene occurs by biallelic methylation in a core region of H19-associated CTCF-binding sites in colorectal cancer. Proc Natl Acad Sci U S A 98:591-596, 2001
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 591-596
    • Nakagawa, H.1    Chadwick, R.B.2    Peltomaki, P.3
  • 32
    • 0033945861 scopus 로고    scopus 로고
    • DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
    • Rountree MR, Bachman KE, Baylin SB: DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet 25:269-277, 2000
    • (2000) Nat Genet , vol.25 , pp. 269-277
    • Rountree, M.R.1    Bachman, K.E.2    Baylin, S.B.3
  • 33
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan X, Ng HH, Johnson CA, et al: Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393:386-389, 1998
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3
  • 34
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters
    • Robertson KD, Ait-Si-Ali S, Yokochi T, et al: DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat Genet 25:338-342, 2000
    • (2000) Nat Genet , vol.25 , pp. 338-342
    • Robertson, K.D.1    Ait-Si-Ali, S.2    Yokochi, T.3
  • 35
    • 0033988813 scopus 로고    scopus 로고
    • DNA methyltransferase Dnmt1 associates with histone deacetylase activity
    • Fuks F, Burgers WA, Brehm A, et al: DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat Genet 24:88-91, 2000
    • (2000) Nat Genet , vol.24 , pp. 88-91
    • Fuks, F.1    Burgers, W.A.2    Brehm, A.3
  • 36
    • 0036607452 scopus 로고    scopus 로고
    • DNA methyltransferases get connected to chromatin
    • Burgers WA, Fuks F, Kouzarides T: DNA methyltransferases get connected to chromatin. Trends Genet 18:275-277, 2002
    • (2002) Trends Genet , vol.18 , pp. 275-277
    • Burgers, W.A.1    Fuks, F.2    Kouzarides, T.3
  • 37
    • 0038527642 scopus 로고    scopus 로고
    • Methyltransferase recruitment and DNA hypermethylation of target promoters by an oncogenic transcription factor
    • Di Croce L, Raker VA, Corsaro M, et al: Methyltransferase recruitment and DNA hypermethylation of target promoters by an oncogenic transcription factor. Science 295:1079-1082, 2002
    • (2002) Science , vol.295 , pp. 1079-1082
    • Di Croce, L.1    Raker, V.A.2    Corsaro, M.3
  • 38
    • 0032890965 scopus 로고    scopus 로고
    • The DNA methylation paradox
    • Jones PA: The DNA methylation paradox. Trends Genet 15:34-37, 1999
    • (1999) Trends Genet , vol.15 , pp. 34-37
    • Jones, P.A.1
  • 39
    • 0030710153 scopus 로고    scopus 로고
    • How does DNA methylation repress transcription?
    • Kass SU, Pruss D, Wolffe AP: How does DNA methylation repress transcription? Trends Genet 13:444-449, 1997
    • (1997) Trends Genet , vol.13 , pp. 444-449
    • Kass, S.U.1    Pruss, D.2    Wolffe, A.P.3
  • 40
    • 0035890665 scopus 로고    scopus 로고
    • Altered chromatin structure associated with methylation-induced gene silencing in cancer cells: Correlation of accessibility, methylation, MeCP2 binding and acetylation
    • Nguyen CT, Gonzales FA, Jones PA: Altered chromatin structure associated with methylation-induced gene silencing in cancer cells: Correlation of accessibility, methylation, MeCP2 binding and acetylation. Nucleic Acids Res 29:4598-4606, 2001
    • (2001) Nucleic Acids Res , vol.29 , pp. 4598-4606
    • Nguyen, C.T.1    Gonzales, F.A.2    Jones, P.A.3
  • 41
    • 9144271660 scopus 로고    scopus 로고
    • Silencing effect of CpG island hypermethylation and histone modifications on O6-methylguanine-DNA methyltransferase (MGMT) gene expression in human cancer
    • Nakagawachi T, Soejima H, Urano T, et al: Silencing effect of CpG island hypermethylation and histone modifications on O6-methylguanine-DNA methyltransferase (MGMT) gene expression in human cancer. Oncogene 22:8835-8844, 2003
    • (2003) Oncogene , vol.22 , pp. 8835-8844
    • Nakagawachi, T.1    Soejima, H.2    Urano, T.3
  • 42
    • 3042742922 scopus 로고    scopus 로고
    • Enhanced antitumor activity of a combination of MBD2-antisense electrotransfer gene therapy and bleomycin electrochemotherapy
    • Ivanov MA, Lamrihi B, Szyf M, et al: Enhanced antitumor activity of a combination of MBD2-antisense electrotransfer gene therapy and bleomycin electrochemotherapy. J Gene Med 5:893-899, 2003
    • (2003) J Gene Med , vol.5 , pp. 893-899
    • Ivanov, M.A.1    Lamrihi, B.2    Szyf, M.3
  • 43
    • 0037603586 scopus 로고    scopus 로고
    • Deficiency of Mbd2 suppresses intestinal tumorigenesis
    • Sansom OJ, Berger J, Bishop SM, et al: Deficiency of Mbd2 suppresses intestinal tumorigenesis. Nat Genet 34:145-147, 2003
    • (2003) Nat Genet , vol.34 , pp. 145-147
    • Sansom, O.J.1    Berger, J.2    Bishop, S.M.3
  • 44
    • 0027769876 scopus 로고
    • A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano M, Hannon GJ, Beach D: A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature 366:704-707, 1993
    • (1993) Nature , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.J.2    Beach, D.3
  • 45
    • 0028787221 scopus 로고
    • CDKN2 gene silencing in lung cancer by DNA hypermethylation and kinetics of p16INK4 protein induction by 5-aza 2′deoxycytidine
    • Otterson GA, Khleif SN, Chen W, et al: CDKN2 gene silencing in lung cancer by DNA hypermethylation and kinetics of p16INK4 protein induction by 5-aza 2′deoxycytidine. Oncogene 11:1211-1216, 1995
    • (1995) Oncogene , vol.11 , pp. 1211-1216
    • Otterson, G.A.1    Khleif, S.N.2    Chen, W.3
  • 46
    • 0343953594 scopus 로고    scopus 로고
    • Hypermethylation can selectively silence individual p16ink4A alleles in neoplasia
    • Myohanen SK, Baylin SB, Herman JG: Hypermethylation can selectively silence individual p16ink4A alleles in neoplasia. Cancer Res 58:591-593, 1998
    • (1998) Cancer Res , vol.58 , pp. 591-593
    • Myohanen, S.K.1    Baylin, S.B.2    Herman, J.G.3
  • 47
    • 0028152397 scopus 로고
    • Cytidine methylation of regulatory sequences near the pi-class glutathione S-transferase gene accompanies human prostatic carcinogenesis
    • Lee WH, Morton RA, Epstein JI, et al: Cytidine methylation of regulatory sequences near the pi-class glutathione S-transferase gene accompanies human prostatic carcinogenesis. Proc Natl Acad Sci U S A 91:11733-11737, 1994
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 11733-11737
    • Lee, W.H.1    Morton, R.A.2    Epstein, J.I.3
  • 48
    • 0033545329 scopus 로고    scopus 로고
    • Detailed methylation analysis of the glutathione S-transferase pi (GSTP1) gene in prostate cancer
    • Millar DS, Ow KK, Paul CL, et al: Detailed methylation analysis of the glutathione S-transferase pi (GSTP1) gene in prostate cancer. Oncogene 18:1313-1324, 1999
    • (1999) Oncogene , vol.18 , pp. 1313-1324
    • Millar, D.S.1    Ow, K.K.2    Paul, C.L.3
  • 49
    • 0030925099 scopus 로고    scopus 로고
    • Extensive DNA methylation spanning the Rb promoter in retinoblastoma tumors
    • Stirzaker C, Millar DS, Paul CL, et al: Extensive DNA methylation spanning the Rb promoter in retinoblastoma tumors. Cancer Res 57:2229-2237, 1997
    • (1997) Cancer Res , vol.57 , pp. 2229-2237
    • Stirzaker, C.1    Millar, D.S.2    Paul, C.L.3
  • 50
    • 0033179375 scopus 로고    scopus 로고
    • Concurrent DNA hypermethylation of multiple genes in acute myeloid leukemia
    • Melki JR, Vincent PC, Clark SJ: Concurrent DNA hypermethylation of multiple genes in acute myeloid leukemia. Cancer Res 59:3730-3740, 1999
    • (1999) Cancer Res , vol.59 , pp. 3730-3740
    • Melki, J.R.1    Vincent, P.C.2    Clark, S.J.3
  • 51
    • 0033556427 scopus 로고    scopus 로고
    • Extensive intra- and interindividual heterogeneity of p15INK4B methylation in acute myeloid leukemia
    • Aggerholm A, Guldberg P, Hokland M, et al: Extensive intra- and interindividual heterogeneity of p15INK4B methylation in acute myeloid leukemia. Cancer Res 59:436-441, 1999
    • (1999) Cancer Res , vol.59 , pp. 436-441
    • Aggerholm, A.1    Guldberg, P.2    Hokland, M.3
  • 52
    • 0033215453 scopus 로고    scopus 로고
    • p15(INK4B) CpG island methylation in primary acute leukemia is heterogeneous and suggests density as a critical factor for transcriptional silencing
    • Cameron EE, Baylin SB, Herman JG: p15(INK4B) CpG island methylation in primary acute leukemia is heterogeneous and suggests density as a critical factor for transcriptional silencing. Blood 94:2445-2451, 1999
    • (1999) Blood , vol.94 , pp. 2445-2451
    • Cameron, E.E.1    Baylin, S.B.2    Herman, J.G.3
  • 53
    • 0742282005 scopus 로고    scopus 로고
    • Hypermethylation of the Ink4b locus in murine myeloid leukemia and increased susceptibility to leukemia in p15(Ink4b)-deficient mice
    • Wolff L, Garin MT, Koller R, et al: Hypermethylation of the Ink4b locus in murine myeloid leukemia and increased susceptibility to leukemia in p15(Ink4b)-deficient mice. Oncogene 22: 9265-9274, 2003
    • (2003) Oncogene , vol.22 , pp. 9265-9274
    • Wolff, L.1    Garin, M.T.2    Koller, R.3
  • 54
    • 0035200467 scopus 로고    scopus 로고
    • Myelodysplastic syndrome: Review of the cytogenetic and molecular data
    • Mhawech P, Saleem A: Myelodysplastic syndrome: Review of the cytogenetic and molecular data. Crit Rev Oncol Hematol 40:229-238, 2001
    • (2001) Crit Rev Oncol Hematol , vol.40 , pp. 229-238
    • Mhawech, P.1    Saleem, A.2
  • 55
    • 0032523011 scopus 로고    scopus 로고
    • Methylation of the p15 (INK4b) gene in myelodysplastic syndromes is frequent and acquired during disease progression
    • Quesnel B, Guillerm G, Vereecque R, et al: Methylation of the p15 (INK4b) gene in myelodysplastic syndromes is frequent and acquired during disease progression. Blood 91:2985-2990, 1998
    • (1998) Blood , vol.91 , pp. 2985-2990
    • Quesnel, B.1    Guillerm, G.2    Vereecque, R.3
  • 56
    • 0028846864 scopus 로고
    • Deletion of cyclin-dependent kinase 4 inhibitor genes P15 and P16 in non-Hodgkin's lymphoma
    • Koduru PR, Zariwala M, Soni M, et al: Deletion of cyclin-dependent kinase 4 inhibitor genes P15 and P16 in non-Hodgkin's lymphoma. Blood 86:2900-2905, 1995
    • (1995) Blood , vol.86 , pp. 2900-2905
    • Koduru, P.R.1    Zariwala, M.2    Soni, M.3
  • 57
    • 0035353188 scopus 로고    scopus 로고
    • Methylation profiling in acute myeloid leukemia
    • Toyota M, Kopecky KJ, Toyota MO, et al: Methylation profiling in acute myeloid leukemia. Blood 97:2823-2829, 2001
    • (2001) Blood , vol.97 , pp. 2823-2829
    • Toyota, M.1    Kopecky, K.J.2    Toyota, M.O.3
  • 58
    • 0030612423 scopus 로고    scopus 로고
    • Hypermethylation of the p15INK4B gene in myelodysplastic syndromes
    • Uchida T, Kinoshita T, Nagai H, et al: Hypermethylation of the p15INK4B gene in myelodysplastic syndromes. Blood 90:1403-1409, 1997
    • (1997) Blood , vol.90 , pp. 1403-1409
    • Uchida, T.1    Kinoshita, T.2    Nagai, H.3
  • 59
    • 0031860559 scopus 로고    scopus 로고
    • Review of alterations of the cyclin-dependent kinase inhibitor INK4 family genes p15, p16, p18 and p19 in human leukemia-lymphoma cells
    • Drexler HG: Review of alterations of the cyclin-dependent kinase inhibitor INK4 family genes p15, p16, p18 and p19 in human leukemia-lymphoma cells. Leukemia 12:845-859, 1998
    • (1998) Leukemia , vol.12 , pp. 845-859
    • Drexler, H.G.1
  • 60
    • 0034741637 scopus 로고    scopus 로고
    • Different p16INK4a and p14ARF expression patterns in acute myeloid leukaemia and normal blood leukocytes
    • Tschan MP, Vonlanthen S, Cajot JF, et al: Different p16INK4a and p14ARF expression patterns in acute myeloid leukaemia and normal blood leukocytes. Leuk Lymphoma 42:1077-1087, 2001
    • (2001) Leuk Lymphoma , vol.42 , pp. 1077-1087
    • Tschan, M.P.1    Vonlanthen, S.2    Cajot, J.F.3
  • 61
    • 0036902962 scopus 로고    scopus 로고
    • DNA methylation and demethylating drugs in myelodysplastic syndromes and secondary leukemias
    • Leone G, Teofili L, Voso MT, et al: DNA methylation and demethylating drugs in myelodysplastic syndromes and secondary leukemias. Haematologica 87:1324-1341, 2002
    • (2002) Haematologica , vol.87 , pp. 1324-1341
    • Leone, G.1    Teofili, L.2    Voso, M.T.3
  • 62
    • 0037625237 scopus 로고    scopus 로고
    • Aberrant DNA methylation of p57KIP2 identifies a cell-cycle regulatory pathway with prognostic impact in adult acute lymphocytic leukemia
    • Shen L, Toyota M, Kondo Y, et al: Aberrant DNA methylation of p57KIP2 identifies a cell-cycle regulatory pathway with prognostic impact in adult acute lymphocytic leukemia. Blood 101: 4131-4136, 2003
    • (2003) Blood , vol.101 , pp. 4131-4136
    • Shen, L.1    Toyota, M.2    Kondo, Y.3
  • 63
    • 0038189509 scopus 로고    scopus 로고
    • Hypermethylation of GpG islands in the promoter region of p15INK4b in acute promyelocytic leukemia represses p15INK4b expression and correlates with poor prognosis
    • Teofili L, Martini M, Luongo M, et al: Hypermethylation of GpG islands in the promoter region of p15INK4b in acute promyelocytic leukemia represses p15INK4b expression and correlates with poor prognosis. Leukemia 17:919-924, 2003
    • (2003) Leukemia , vol.17 , pp. 919-924
    • Teofili, L.1    Martini, M.2    Luongo, M.3
  • 64
    • 0035992430 scopus 로고    scopus 로고
    • DNA methylation of multiple promoter-associated CpG islands in adult acute lymphocytic leukemia
    • Garcia-Manero G, Daniel J, Smith TL, et al: DNA methylation of multiple promoter-associated CpG islands in adult acute lymphocytic leukemia. Clin Cancer Res 8:2217-2224, 2002
    • (2002) Clin Cancer Res , vol.8 , pp. 2217-2224
    • Garcia-Manero, G.1    Daniel, J.2    Smith, T.L.3
  • 65
    • 3242657117 scopus 로고    scopus 로고
    • The clinical application of targeting cancer through histone acetylation and hypomethylation
    • Gilbert J, Gore SD, Herman JG, et al: The clinical application of targeting cancer through histone acetylation and hypomethylation. Clin Cancer Res 10:4589-4596, 2004
    • (2004) Clin Cancer Res , vol.10 , pp. 4589-4596
    • Gilbert, J.1    Gore, S.D.2    Herman, J.G.3
  • 66
    • 0036861629 scopus 로고    scopus 로고
    • DNA methyltransferase inhibitors-state of the art
    • Goffin J, Eisenhauer E: DNA methyltransferase inhibitors-state of the art. Ann Oncol 13:1699-1716, 2002
    • (2002) Ann Oncol , vol.13 , pp. 1699-1716
    • Goffin, J.1    Eisenhauer, E.2
  • 67
    • 16544395591 scopus 로고    scopus 로고
    • DNA methylation and cancer
    • Das PM, Singal R: DNA methylation and cancer. J Clin Oncol 22:4632-4642, 2004
    • (2004) J Clin Oncol , vol.22 , pp. 4632-4642
    • Das, P.M.1    Singal, R.2
  • 68
    • 0742269866 scopus 로고    scopus 로고
    • Decitabine
    • Issa JP: Decitabine. Curr Opin Oncol 15: 446-451, 2003
    • (2003) Curr Opin Oncol , vol.15 , pp. 446-451
    • Issa, J.P.1
  • 69
    • 0020541275 scopus 로고
    • Incorporation of 5-Aza-2′-deoxycytidine- 5′-triphosphate into DNA. Interactions with mammalian DNA polymerase alpha and DNA methylase
    • Bouchard J, Momparler RL: Incorporation of 5-Aza-2′-deoxycytidine- 5′-triphosphate into DNA. Interactions with mammalian DNA polymerase alpha and DNA methylase. Mol Pharmacol 24:109-114, 1983
    • (1983) Mol Pharmacol , vol.24 , pp. 109-114
    • Bouchard, J.1    Momparler, R.L.2
  • 70
    • 0020582853 scopus 로고
    • On the mechanism of inhibition of DNA-cytosine methyltransferases by cytosine analogs
    • Santi DV, Garrett CE, Barr PJ: On the mechanism of inhibition of DNA-cytosine methyltransferases by cytosine analogs. Cell 33:9-10, 1983
    • (1983) Cell , vol.33 , pp. 9-10
    • Santi, D.V.1    Garrett, C.E.2    Barr, P.J.3
  • 71
    • 0021180679 scopus 로고
    • Cell cycle effects and cellular pharmacology of 5-aza-2′-deoxycytidine
    • Momparler RL, Samson J, Momparler LF, et al: Cell cycle effects and cellular pharmacology of 5-aza-2′-deoxycytidine. Cancer Chemother Pharmacol 13:191-194, 1984
    • (1984) Cancer Chemother Pharmacol , vol.13 , pp. 191-194
    • Momparler, R.L.1    Samson, J.2    Momparler, L.F.3
  • 72
    • 0000418476 scopus 로고
    • Covalent bond formation between a DNA-cytosine methyltransferase and DNA containing 5-azacytosine
    • Santi DV, Norment A, Garrett CE: Covalent bond formation between a DNA-cytosine methyltransferase and DNA containing 5-azacytosine. Proc Natl Acad Sci U S A 81:6993-6997, 1984
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 6993-6997
    • Santi, D.V.1    Norment, A.2    Garrett, C.E.3
  • 73
    • 0022404250 scopus 로고
    • Induction of differentiation and inhibition of DNA methylation in HL-60 myeloid leukemic cells by 5-AZA-2′-deoxycytidine
    • Momparler RL, Bouchard J, Samson J: Induction of differentiation and inhibition of DNA methylation in HL-60 myeloid leukemic cells by 5-AZA-2′-deoxycytidine. Leuk Res 9:1361-1366, 1985
    • (1985) Leuk Res , vol.9 , pp. 1361-1366
    • Momparler, R.L.1    Bouchard, J.2    Samson, J.3
  • 74
    • 0021160287 scopus 로고
    • 5-Aza-2′-deoxycytidine induces terminal differentiation of leukemic blasts from patients with acute myeloid leukemias
    • Pinto A, Attadia V, Fusco A, et al: 5-Aza-2′-deoxycytidine induces terminal differentiation of leukemic blasts from patients with acute myeloid leukemias. Blood 64:922-929, 1984
    • (1984) Blood , vol.64 , pp. 922-929
    • Pinto, A.1    Attadia, V.2    Fusco, A.3
  • 75
    • 0031964055 scopus 로고    scopus 로고
    • Inhibition of DNA methylation by 5-aza-2′-deoxycytidine suppresses the growth of human tumor cell lines
    • Bender CM, Pao MM, Jones PA: Inhibition of DNA methylation by 5-aza-2′-deoxycytidine suppresses the growth of human tumor cell lines. Cancer Res 58:95-101, 1998
    • (1998) Cancer Res , vol.58 , pp. 95-101
    • Bender, C.M.1    Pao, M.M.2    Jones, P.A.3
  • 76
    • 0034105545 scopus 로고    scopus 로고
    • DNA methylation inhibitors in the treatment of leukemias, myelodysplastic syndromes and hemoglobinopathies: Clinical results and possible mechanisms of action
    • Lubbert M: DNA methylation inhibitors in the treatment of leukemias, myelodysplastic syndromes and hemoglobinopathies: Clinical results and possible mechanisms of action. Curr Top Microbiol Immunol 249:135-164, 2000
    • (2000) Curr Top Microbiol Immunol , vol.249 , pp. 135-164
    • Lubbert, M.1
  • 77
    • 10744233452 scopus 로고    scopus 로고
    • Phase 1 study of low-dose prolonged exposure schedules of the hypomethylating agent 5-aza-2′- deoxycytidine (decitabine) in hematopoietic malignancies
    • Issa JP, Garcia-Manero G, Giles FJ, et al: Phase 1 study of low-dose prolonged exposure schedules of the hypomethylating agent 5-aza-2′- deoxycytidine (decitabine) in hematopoietic malignancies. Blood 103:1635-1640, 2004
    • (2004) Blood , vol.103 , pp. 1635-1640
    • Issa, J.P.1    Garcia-Manero, G.2    Giles, F.J.3
  • 78
    • 0037108309 scopus 로고    scopus 로고
    • Demethylation of a hypermethylated P15/INK4B gene in patients with myelodysplastic syndrome by 5-Aza-2′-deoxycytidine (decitabine) treatment
    • Daskalakis M, Nguyen TT, Nguyen C, et al: Demethylation of a hypermethylated P15/INK4B gene in patients with myelodysplastic syndrome by 5-Aza-2′-deoxycytidine (decitabine) treatment. Blood 100:2957-2964, 2002
    • (2002) Blood , vol.100 , pp. 2957-2964
    • Daskalakis, M.1    Nguyen, T.T.2    Nguyen, C.3
  • 79
    • 0028151343 scopus 로고
    • Toxicity of 5-aza-2′-deoxycytidine to mammalian cells is mediated primarily by covalent trapping of DNA methyltransferase rather than DNA demethylation
    • Juttermann R, Li E, Jaenisch R: Toxicity of 5-aza-2′-deoxycytidine to mammalian cells is mediated primarily by covalent trapping of DNA methyltransferase rather than DNA demethylation. Proc Natl Acad Sci U S A 91:11797-11801, 1994
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 11797-11801
    • Juttermann, R.1    Li, E.2    Jaenisch, R.3
  • 80
    • 0037420191 scopus 로고    scopus 로고
    • Inhibition of DNA methylation and reactivation of silenced genes by zebularine
    • Cheng JC, Matsen CB, Gonzales FA, et al: Inhibition of DNA methylation and reactivation of silenced genes by zebularine. J Natl Cancer Inst 95:399-409, 2003
    • (2003) J Natl Cancer Inst , vol.95 , pp. 399-409
    • Cheng, J.C.1    Matsen, C.B.2    Gonzales, F.A.3
  • 81
    • 5144228492 scopus 로고    scopus 로고
    • Preferential response of cancer cells to zebularine
    • Cheng JC, Yoo CB, Weisenberger DJ, et al: Preferential response of cancer cells to zebularine. Cancer Cell 6:151-158, 2004
    • (2004) Cancer Cell , vol.6 , pp. 151-158
    • Cheng, J.C.1    Yoo, C.B.2    Weisenberger, D.J.3
  • 82
    • 0038443956 scopus 로고    scopus 로고
    • A phase I pharmacokinetic and pharmacodynamic study of the DNA methyltransferase 1 inhibitor MG98 administered twice weekly
    • Stewart DJ, Donehower RC, Eisenhauer EA, et al: A phase I pharmacokinetic and pharmacodynamic study of the DNA methyltransferase 1 inhibitor MG98 administered twice weekly. Ann Oncol 14:766-774, 2003
    • (2003) Ann Oncol , vol.14 , pp. 766-774
    • Stewart, D.J.1    Donehower, R.C.2    Eisenhauer, E.A.3
  • 83
    • 0015839018 scopus 로고
    • 5-Azacytidine: A new active agent for the treatment of acute leukemia
    • Karon M, Sieger L, Leimbrock S, et al: 5-Azacytidine: A new active agent for the treatment of acute leukemia. Blood 42:359-365, 1973
    • (1973) Blood , vol.42 , pp. 359-365
    • Karon, M.1    Sieger, L.2    Leimbrock, S.3
  • 84
    • 0015844307 scopus 로고
    • Treatment of acute leukemia with 5-azacytidine (NSC-102816)
    • McCredie KB, Bodey GP, Burgess MA, et al: Treatment of acute leukemia with 5-azacytidine (NSC-102816). Cancer Chemother Rep 57:319-323, 1973
    • (1973) Cancer Chemother Rep , vol.57 , pp. 319-323
    • McCredie, K.B.1    Bodey, G.P.2    Burgess, M.A.3
  • 85
    • 0017136745 scopus 로고
    • A comparative clinical trial of 5-azacytidine and guanazole in previously treated adults with acute nonlymphocytic leukemia
    • Levi JA, Wiernik PH: A comparative clinical trial of 5-azacytidine and guanazole in previously treated adults with acute nonlymphocytic leukemia. Cancer 38:36-41, 1976
    • (1976) Cancer , vol.38 , pp. 36-41
    • Levi, J.A.1    Wiernik, P.H.2
  • 86
    • 0018251578 scopus 로고
    • 5-azacytidine in acute leukemia
    • Saiki JH, McCredie KB, Vietti TJ, et al: 5-azacytidine in acute leukemia. Cancer 42:2111-2114, 1978
    • (1978) Cancer , vol.42 , pp. 2111-2114
    • Saiki, J.H.1    McCredie, K.B.2    Vietti, T.J.3
  • 87
    • 0019471960 scopus 로고
    • Effect of schedule on activity and toxicity of 5-azacytidine in acute leukemia: A Southwest Oncology Group Study
    • Saiki JH, Bodey GP, Hewlett JS, et al: Effect of schedule on activity and toxicity of 5-azacytidine in acute leukemia: a Southwest Oncology Group Study. Cancer 47:1739-1742, 1981
    • (1981) Cancer , vol.47 , pp. 1739-1742
    • Saiki, J.H.1    Bodey, G.P.2    Hewlett, J.S.3
  • 88
    • 0025831445 scopus 로고
    • Evaluation of continuous infusion low-dose 5-azacytidine in the treatment of myelodysplastic syndromes
    • Chitambar CR, Libnoch JA, Matthaeus WG, et al: Evaluation of continuous infusion low-dose 5-azacytidine in the treatment of myelodysplastic syndromes. Am J Hematol 37:100-104, 1991
    • (1991) Am J Hematol , vol.37 , pp. 100-104
    • Chitambar, C.R.1    Libnoch, J.A.2    Matthaeus, W.G.3
  • 89
    • 0027154222 scopus 로고
    • Effects of treatment with 5-azacytidine on the in vivo and in vitro hematopoiesis in patients with myelodysplastic syndromes
    • suppl 1
    • Silverman LR, Holland JF, Weinberg RS, et al: Effects of treatment with 5-azacytidine on the in vivo and in vitro hematopoiesis in patients with myelodysplastic syndromes. Leukemia 7: 21-29, 1993 (suppl 1)
    • (1993) Leukemia , vol.7 , pp. 21-29
    • Silverman, L.R.1    Holland, J.F.2    Weinberg, R.S.3
  • 90
  • 91
    • 0036342388 scopus 로고    scopus 로고
    • Treatment of myelodysplastic syndromes with 5-azacytidine
    • Gryn J, Zeigler ZR, Shadduck RK, et al: Treatment of myelodysplastic syndromes with 5-azacytidine. Leuk Res 26:893-897, 2002
    • (2002) Leuk Res , vol.26 , pp. 893-897
    • Gryn, J.1    Zeigler, Z.R.2    Shadduck, R.K.3
  • 92
    • 0037093195 scopus 로고    scopus 로고
    • Randomized controlled trial of azacitidine in patients with the myelodysplastic syndrome: A study of the cancer and leukemia group B
    • Silverman LR, Demakos EP, Peterson BL, et al: Randomized controlled trial of azacitidine in patients with the myelodysplastic syndrome: A study of the cancer and leukemia group B. J Clin Oncol 20:2429-2440, 2002
    • (2002) J Clin Oncol , vol.20 , pp. 2429-2440
    • Silverman, L.R.1    Demakos, E.P.2    Peterson, B.L.3
  • 93
    • 0022303520 scopus 로고
    • Clinical trial on 5-aza-2′- deoxycytidine in patients with acute leukemia
    • Momparler RL, Rivard GE, Gyger M: Clinical trial on 5-aza-2′- deoxycytidine in patients with acute leukemia. Pharmacol Ther 30:277-286, 1985
    • (1985) Pharmacol Ther , vol.30 , pp. 277-286
    • Momparler, R.L.1    Rivard, G.E.2    Gyger, M.3
  • 94
    • 0027309013 scopus 로고
    • Pilot study of 5-aza-2′-deoxycytidine (Decitabine) in the treatment of poor prognosis acute myelogenous leukemia patients: Preliminary results
    • suppl 1
    • Petti MC, Mandelli F, Zagonel V, et al: Pilot study of 5-aza-2′-deoxycytidine (Decitabine) in the treatment of poor prognosis acute myelogenous leukemia patients: Preliminary results. Leukemia 7:36-41, 1993 (suppl 1)
    • (1993) Leukemia , vol.7 , pp. 36-41
    • Petti, M.C.1    Mandelli, F.2    Zagonel, V.3
  • 95
    • 0030985020 scopus 로고    scopus 로고
    • Decitabine studies in chronic and acute myelogenous leukemia
    • suppl 1
    • Kantarjian HM, O'Brien SM, Estey E, et al: Decitabine studies in chronic and acute myelogenous leukemia. Leukemia 11:S35-S36, 1997 (suppl 1)
    • (1997) Leukemia , vol.11
    • Kantarjian, H.M.1    O'Brien, S.M.2    Estey, E.3
  • 96
    • 16944363756 scopus 로고    scopus 로고
    • Results of decitabine therapy in the accelerated and blastic phases of chronic myelogenous leukemia
    • Kantarjian HM, O'Brien SM, Keating M, et al: Results of decitabine therapy in the accelerated and blastic phases of chronic myelogenous leukemia. Leukemia 11:1617-1620, 1997
    • (1997) Leukemia , vol.11 , pp. 1617-1620
    • Kantarjian, H.M.1    O'Brien, S.M.2    Keating, M.3
  • 97
    • 0033572876 scopus 로고    scopus 로고
    • Chronic myelogenous leukemia in nonlymphoid blastic phase: Analysis of the results of first salvage therapy with three different treatment approaches for 162 patients
    • Sacchi S, Kantarjian HM, O'Brien S, et al: Chronic myelogenous leukemia in nonlymphoid blastic phase: Analysis of the results of first salvage therapy with three different treatment approaches for 162 patients. Cancer 86:2632-2641, 1999
    • (1999) Cancer , vol.86 , pp. 2632-2641
    • Sacchi, S.1    Kantarjian, H.M.2    O'Brien, S.3
  • 98
    • 32644459379 scopus 로고    scopus 로고
    • Hypomethylation dynamics following decitabine therapy in chronic myelogenous leukemia
    • Issa JP, Gharibyan V, Jelinek J, et al: Hypomethylation dynamics following decitabine therapy in chronic myelogenous leukemia. Blood 104:2956, 2004
    • (2004) Blood , vol.104 , pp. 2956
    • Issa, J.P.1    Gharibyan, V.2    Jelinek, J.3
  • 99
    • 17444452612 scopus 로고    scopus 로고
    • Low-dose 5-aza-2′- deoxycytidine, a DNA hypomethylating agent, for the treatment of high-risk myelodysplastic syndrome: A multicenter phase II study in elderly patients
    • Wijermans P, Lubbert M, Verhoef G, et al: Low-dose 5-aza-2′- deoxycytidine, a DNA hypomethylating agent, for the treatment of high-risk myelodysplastic syndrome: A multicenter phase II study in elderly patients. J Clin Oncol 18:956-962, 2000
    • (2000) J Clin Oncol , vol.18 , pp. 956-962
    • Wijermans, P.1    Lubbert, M.2    Verhoef, G.3
  • 100
    • 25844436759 scopus 로고    scopus 로고
    • Decitabine low-dose schedule (100 mg/m2/ course) in myelodysplastic syndrome (MDS). Comparison of 3 different dose schedules
    • Kantarjian HM, Ravandi F, O'Brien S, et al: Decitabine low-dose schedule (100 mg/m2/ course) in myelodysplastic syndrome (MDS). Comparison of 3 different dose schedules. Blood 104:1437, 2004
    • (2004) Blood , vol.104 , pp. 1437
    • Kantarjian, H.M.1    Ravandi, F.2    O'Brien, S.3
  • 101
    • 20344393720 scopus 로고    scopus 로고
    • First Report of the Phase III North American Trial of Decitabine in Advanced Myelodysplastic Syndrome (MDS)
    • Saba H, Rosenfeld C, Issa JP, et al: First Report of the Phase III North American Trial of Decitabine in Advanced Myelodysplastic Syndrome (MDS). Blood 104:67, 2004
    • (2004) Blood , vol.104 , pp. 67
    • Saba, H.1    Rosenfeld, C.2    Issa, J.P.3
  • 102
    • 0017253916 scopus 로고
    • The disposition and pharmacokinetics in humans of 5-azacytidine administered intravenously as a bolus or by continuous infusion
    • Israili ZH, Vogler WR, Mingioli ES, et al: The disposition and pharmacokinetics in humans of 5-azacytidine administered intravenously as a bolus or by continuous infusion. Cancer Res 36:1453-1461, 1976
    • (1976) Cancer Res , vol.36 , pp. 1453-1461
    • Israili, Z.H.1    Vogler, W.R.2    Mingioli, E.S.3
  • 103
    • 0000213517 scopus 로고
    • Absorption, distribution, and excretion of 5-azacytidine (NSC-1028116) in man
    • Troetel WM, Weiss AJ, Stambaugh JE: Absorption, distribution, and excretion of 5-azacytidine (NSC-1028116) in man. Cancer Chemother Rep 56:405-411, 1972
    • (1972) Cancer Chemother Rep , vol.56 , pp. 405-411
    • Troetel, W.M.1    Weiss, A.J.2    Stambaugh, J.E.3
  • 104
    • 0017083209 scopus 로고
    • 5-Azacytidine (NSC 102816): A new drug for the treatment of myeloblastic leukemia
    • Vogler WR, Miller DS, Keller JW: 5-Azacytidine (NSC 102816): A new drug for the treatment of myeloblastic leukemia. Blood 48:331-337, 1976
    • (1976) Blood , vol.48 , pp. 331-337
    • Vogler, W.R.1    Miller, D.S.2    Keller, J.W.3
  • 105
    • 0037092962 scopus 로고    scopus 로고
    • Impact of azacytidine on the quality of life of patients with myelodysplastic syndrome treated in a randomized phase III trial: A Cancer and Leukemia Group B study
    • Kornblith AB, Herndon JE, Silverman LR, et al: Impact of azacytidine on the quality of life of patients with myelodysplastic syndrome treated in a randomized phase III trial: A Cancer and Leukemia Group B study. J Clin Oncol 20:2441-2452, 2002
    • (2002) J Clin Oncol , vol.20 , pp. 2441-2452
    • Kornblith, A.B.1    Herndon, J.E.2    Silverman, L.R.3
  • 106
    • 0035988868 scopus 로고    scopus 로고
    • Review of the clinical experience with 5-azacytidine and 5-aza-2′-deoxycytidine in solid tumors
    • Aparicio A, Weber JS: Review of the clinical experience with 5-azacytidine and 5-aza-2′-deoxycytidine in solid tumors. Curr Opin Investig Drugs 3:627-633, 2002
    • (2002) Curr Opin Investig Drugs , vol.3 , pp. 627-633
    • Aparicio, A.1    Weber, J.S.2
  • 107
    • 0030985018 scopus 로고    scopus 로고
    • Continuous infusion of low-dose 5-Aza-2′-deoxycytidine in elderly patients with high-risk myelodysplastic syndrome
    • Wijermans P, Krulder JW, Huijgens PC, et al: Continuous infusion of low-dose 5-Aza-2′-deoxycytidine in elderly patients with high-risk myelodysplastic syndrome. Leukemia 11:1-5, 1997
    • (1997) Leukemia , vol.11 , pp. 1-5
    • Wijermans, P.1    Krulder, J.W.2    Huijgens, P.C.3
  • 108
    • 0022283817 scopus 로고
    • Molecular, cellular and animal pharmacology of 5-aza-2′-deoxycytidine
    • Momparler RL: Molecular, cellular and animal pharmacology of 5-aza-2′-deoxycytidine. Pharmacol Ther 30:287-299, 1985
    • (1985) Pharmacol Ther , vol.30 , pp. 287-299
    • Momparler, R.L.1
  • 109
    • 0022364737 scopus 로고
    • Mode of action and effects of 5-azacytidine and of its derivatives in eukaryotic cells
    • Vesely J: Mode of action and effects of 5-azacytidine and of its derivatives in eukaryotic cells. Pharmacol Ther 28:227-235, 1985
    • (1985) Pharmacol Ther , vol.28 , pp. 227-235
    • Vesely, J.1
  • 110
    • 0030722392 scopus 로고    scopus 로고
    • Altered methylation of the human MDR1 promoter is associated with acquired multidrug resistance
    • Kantharidis P, EI Osta A, deSilva M, et al: Altered methylation of the human MDR1 promoter is associated with acquired multidrug resistance. Clin Cancer Res 3:2025-2032, 1997
    • (1997) Clin Cancer Res , vol.3 , pp. 2025-2032
    • Kantharidis, P.1    EI Osta, A.2    deSilva, M.3
  • 111
    • 0035542974 scopus 로고    scopus 로고
    • Methyl CpG-binding proteins and transcriptional repression
    • Wade PA: Methyl CpG-binding proteins and transcriptional repression. Bioessays 23: 1131-1137, 2001
    • (2001) Bioessays , vol.23 , pp. 1131-1137
    • Wade, P.A.1
  • 112
    • 0035815697 scopus 로고    scopus 로고
    • Regulation of an endogenous locus using a panel of designed zinc finger proteins targeted to accessible chromatin regions. Activation of vascular endothelial growth factor A
    • Liu PQ, Rebar EJ, Zhang L, et al: Regulation of an endogenous locus using a panel of designed zinc finger proteins targeted to accessible chromatin regions. Activation of vascular endothelial growth factor A. J Biol Chem 276: 11323-11334, 2001
    • (2001) J Biol Chem , vol.276 , pp. 11323-11334
    • Liu, P.Q.1    Rebar, E.J.2    Zhang, L.3
  • 113
    • 85015069067 scopus 로고    scopus 로고
    • Controlling the double helix
    • Felsenfeld G, Groudine M: Controlling the double helix. Nature 421:448-453, 2003
    • (2003) Nature , vol.421 , pp. 448-453
    • Felsenfeld, G.1    Groudine, M.2
  • 114
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: From genomic organization to genomic regulation
    • Khorasanizadeh S: The nucleosome: From genomic organization to genomic regulation. Cell 116:259-272, 2004
    • (2004) Cell , vol.116 , pp. 259-272
    • Khorasanizadeh, S.1
  • 115
    • 0038057380 scopus 로고    scopus 로고
    • Memorable transcription
    • Turner BM: Memorable transcription. Nat Cell Biol 5:390-393, 2003
    • (2003) Nat Cell Biol , vol.5 , pp. 390-393
    • Turner, B.M.1
  • 116
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD: Translating the histone code. Science 293:1074-1080, 2001
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 117
    • 0037074010 scopus 로고    scopus 로고
    • Signaling network model of chromatin
    • Schreiber SL, Bernstein BE: Signaling network model of chromatin. Cell 111:771-778, 2002
    • (2002) Cell , vol.111 , pp. 771-778
    • Schreiber, S.L.1    Bernstein, B.E.2
  • 118
    • 2642570305 scopus 로고    scopus 로고
    • The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
    • Schübeler D, MacAlpine DM, Scalzo D, et al: The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev 18: 1263-1271, 2004
    • (2004) Genes Dev , vol.18 , pp. 1263-1271
    • Schübeler, D.1    MacAlpine, D.M.2    Scalzo, D.3
  • 119
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylase, transcription control and cancer
    • Cress WD, Seto E: Histone deacetylase, transcription control and cancer. J Cell Physiol 184:1-16, 2000
    • (2000) J Cell Physiol , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 120
    • 0035755974 scopus 로고    scopus 로고
    • Histone deacetylases and cancer: Causes and therapies
    • Marks P, Rifkind RA, Richon VM, et al: Histone deacetylases and cancer: Causes and therapies. Nat Rev Cancer 1:194-202, 2001
    • (2001) Nat Rev Cancer , vol.1 , pp. 194-202
    • Marks, P.1    Rifkind, R.A.2    Richon, V.M.3
  • 121
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone RW, Licht JD: Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target? Cancer Cell 4:13-18, 2003
    • (2003) Cancer Cell , vol.4 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 122
    • 10444282190 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors for the treatment of cancer
    • Lindemann RK, Gabrielli B, Johnstone RW: Histone-deacetylase inhibitors for the treatment of cancer. Cell Cycle 3:779-788, 2004
    • (2004) Cell Cycle , vol.3 , pp. 779-788
    • Lindemann, R.K.1    Gabrielli, B.2    Johnstone, R.W.3
  • 123
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective amall-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty SJ, Koeller KM, Wong JC, et al: Domain-selective amall-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc Natl Acad Sci U S A 100: 4389-4394, 2003
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3
  • 124
    • 0037067691 scopus 로고    scopus 로고
    • Acetylation of beta-catenin by CREB-binding protein (CBP)
    • Wolf D, Rodova M, Miska EA, et al: Acetylation of beta-catenin by CREB-binding protein (CBP). J Biol Chem 277:25562-25567, 2002
    • (2002) J Biol Chem , vol.277 , pp. 25562-25567
    • Wolf, D.1    Rodova, M.2    Miska, E.A.3
  • 125
    • 0034177669 scopus 로고    scopus 로고
    • Acetylation of importin-alpha nuclear import factors by CBP/p300
    • Bannister AJ, Miska EA, Gorlich D, et al: Acetylation of importin-alpha nuclear import factors by CBP/p300. Curr Biol 10:467-470, 2000
    • (2000) Curr Biol , vol.10 , pp. 467-470
    • Bannister, A.J.1    Miska, E.A.2    Gorlich, D.3
  • 126
    • 0037185024 scopus 로고    scopus 로고
    • DNA damage-induced translocation of the Werner helicase is regulated by acetylation
    • Blander G, Zalle N, Daniely Y, et al: DNA damage-induced translocation of the Werner helicase is regulated by acetylation. J Biol Chem 277:50934-50940, 2002
    • (2002) J Biol Chem , vol.277 , pp. 50934-50940
    • Blander, G.1    Zalle, N.2    Daniely, Y.3
  • 127
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis
    • Cohen HY, Lavu S, Bitterman KJ, et al: Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis. Mol Cell 13:627-638, 2004
    • (2004) Mol Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1    Lavu, S.2    Bitterman, K.J.3
  • 128
    • 1642490813 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 down-regulates Her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone B
    • Fuino L, Bali P, Wittmann S, et al: Histone deacetylase inhibitor LAQ824 down-regulates Her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone B. Mol Cancer Ther 2:971-984, 2003
    • (2003) Mol Cancer Ther , vol.2 , pp. 971-984
    • Fuino, L.1    Bali, P.2    Wittmann, S.3
  • 129
    • 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 417:455-458, 2002
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 130
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • Yang XJ: The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Nucleic Acids Res 32:959-976, 2004
    • (2004) Nucleic Acids Res , vol.32 , pp. 959-976
    • Yang, X.J.1
  • 131
    • 0034141972 scopus 로고    scopus 로고
    • CREB-binding protein and p300: Molecular integrators of hematopoietic transcription
    • Blobel GA: CREB-binding protein and p300: Molecular integrators of hematopoietic transcription. Blood 95:745-755, 2000
    • (2000) Blood , vol.95 , pp. 745-755
    • Blobel, G.A.1
  • 132
    • 0034104047 scopus 로고    scopus 로고
    • Mutations truncating the EP300 acetylase in human cancers
    • Gayther SA, Batley SJ, Linger L, et al: Mutations truncating the EP300 acetylase in human cancers. Nat Genet 24:300-303, 2000
    • (2000) Nat Genet , vol.24 , pp. 300-303
    • Gayther, S.A.1    Batley, S.J.2    Linger, L.3
  • 133
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein
    • Borrow J, Stanton VP Jr, Andresen JM, et al: The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet 14:33-41, 1996
    • (1996) Nat Genet , vol.14 , pp. 33-41
    • Borrow, J.1    Stanton Jr, V.P.2    Andresen, J.M.3
  • 134
    • 12644314103 scopus 로고    scopus 로고
    • MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3)
    • Sobulo OM, Borrow J, Tomek R, et al: MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3). Proc Natl Acad Sci U S A 94:8732-8737, 1997
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8732-8737
    • Sobulo, O.M.1    Borrow, J.2    Tomek, R.3
  • 135
    • 0035865032 scopus 로고    scopus 로고
    • Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)
    • Panagopoulos I, Fioretos T, Isaksson M, et al: Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet 10:395-404, 2001
    • (2001) Hum Mol Genet , vol.10 , pp. 395-404
    • Panagopoulos, I.1    Fioretos, T.2    Isaksson, M.3
  • 136
    • 3843124232 scopus 로고    scopus 로고
    • Dimerization a versatile switch for oncogenesis
    • So CW, Cleary MJ: Dimerization a versatile switch for oncogenesis. Blood 104:919-922, 2004
    • (2004) Blood , vol.104 , pp. 919-922
    • So, C.W.1    Cleary, M.J.2
  • 137
    • 0037071408 scopus 로고    scopus 로고
    • Transcription factor fusions in acute leukemia: Variations on a theme
    • Scandura JM, Boccuni P, Cammenga J, et al: Transcription factor fusions in acute leukemia: Variations on a theme. Oncogene 21:3422-3444, 2002
    • (2002) Oncogene , vol.21 , pp. 3422-3444
    • Scandura, J.M.1    Boccuni, P.2    Cammenga, J.3
  • 138
    • 2942575919 scopus 로고    scopus 로고
    • Role of RUNX family members in transcriptional repression and gene silencing
    • Durst KL, Hiebert SW: Role of RUNX family members in transcriptional repression and gene silencing. Oncogene 23:4220-4224, 2004
    • (2004) Oncogene , vol.23 , pp. 4220-4224
    • Durst, K.L.1    Hiebert, S.W.2
  • 139
    • 10344247666 scopus 로고    scopus 로고
    • The BCL6 proto-oncogene suppresses p53 expression in germinal-centre B cells
    • Phan RT, Dalla-Favera R: The BCL6 proto-oncogene suppresses p53 expression in germinal-centre B cells. Nature 432:635-639, 2004
    • (2004) Nature , vol.432 , pp. 635-639
    • Phan, R.T.1    Dalla-Favera, R.2
  • 140
    • 5344280456 scopus 로고    scopus 로고
    • MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation
    • Fujita N, Jaye DL, Geigerman C, et al: MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation. Cell 119:75-86, 2004
    • (2004) Cell , vol.119 , pp. 75-86
    • Fujita, N.1    Jaye, D.L.2    Geigerman, C.3
  • 141
    • 11144277489 scopus 로고    scopus 로고
    • Specific peptide interference reveals BCL6 transcriptional and oncogenic mechanisms in B-cell lymphoma cells
    • Polo JM, Dell'Osa T, Ranuncolo SM, et al: Specific peptide interference reveals BCL6 transcriptional and oncogenic mechanisms in B-cell lymphoma cells. Nat Med 10:1329-1334, 2004
    • (2004) Nat Med , vol.10 , pp. 1329-1334
    • Polo, J.M.1    Dell'Osa, T.2    Ranuncolo, S.M.3
  • 142
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks PA, Richon VA, Rifkind RA: Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells. J Natl Cancer Inst 92:1210-1216, 2000
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.A.2    Rifkind, R.A.3
  • 143
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye RA: Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260:273-279, 1999
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 144
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, et al: The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11:437-444, 2003
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3
  • 145
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, et al: Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107:137-148, 2001
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3
  • 146
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint C, Emiliani S, Verdin E: The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr 5:245-253, 1996
    • (1996) Gene Expr , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 147
    • 0034297220 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment
    • Huang L, Pardee AB: Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment. Mol Med 6:849-866, 2000
    • (2000) Mol Med , vol.6 , pp. 849-866
    • Huang, L.1    Pardee, A.B.2
  • 148
    • 0042905956 scopus 로고    scopus 로고
    • Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: Defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines
    • Glaser KB, Staver MJ, Waring JF, et al: Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: Defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines. Mol Cancer Ther 2:151-163, 2003
    • (2003) Mol Cancer Ther , vol.2 , pp. 151-163
    • Glaser, K.B.1    Staver, M.J.2    Waring, J.F.3
  • 149
    • 9144220841 scopus 로고    scopus 로고
    • Transcriptional signature of histone deacetylase inhibition in multiple myeloma: Biological and clinical implications
    • Mitsiades CS, Mitsiades NS, McMullan CJ, et al: Transcriptional signature of histone deacetylase inhibition in multiple myeloma: Biological and clinical implications. Proc Natl Acad Sci U S A 101:540-545, 2004
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 540-545
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 150
    • 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 U S A 97:10014-10019, 2000
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3
  • 151
    • 0033604457 scopus 로고    scopus 로고
    • Induction of apoptosis in U937 human leukemia cells by Suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53
    • Vrana JA, Decker RH, Johnson CR, et al: Induction of apoptosis in U937 human leukemia cells by Suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53. Oncogene 18:7016-7025, 1999
    • (1999) Oncogene , vol.18 , pp. 7016-7025
    • Vrana, J.A.1    Decker, R.H.2    Johnson, C.R.3
  • 152
    • 0038620379 scopus 로고    scopus 로고
    • Co-treatment with the histone deacetylase inhibitor Suberoylanilide hydroxamic acid (SAHA) enhances Gleevec-induced apoptosis of Bcr-Abl positive human acute leukemia cells
    • Nimmanapalli R, Fuino L, Stobaugh C, et al: Co-treatment with the histone deacetylase inhibitor Suberoylanilide hydroxamic acid (SAHA) enhances Gleevec-induced apoptosis of Bcr-Abl positive human acute leukemia cells. Blood 101: 3236-3239, 2003
    • (2003) Blood , vol.101 , pp. 3236-3239
    • Nimmanapalli, R.1    Fuino, L.2    Stobaugh, C.3
  • 153
    • 0036731055 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors all induce p21 but differentially cause tubulin acetylation, mitotic arrest, and cytotoxicity
    • Blagosklonny MV, Robey R, Sackett DL, et al: Histone deacetylase inhibitors all induce p21 but differentially cause tubulin acetylation, mitotic arrest, and cytotoxicity. Mol Cancer Ther 1:937-941, 2002
    • (2002) Mol Cancer Ther , vol.1 , pp. 937-941
    • Blagosklonny, M.V.1    Robey, R.2    Sackett, D.L.3
  • 154
    • 0842277812 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1
    • Gui CY, Ngo L, Xu WS, et al: Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1. Proc Natl Acad Sci U S A 101:1241-1246, 2004
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1241-1246
    • Gui, C.Y.1    Ngo, L.2    Xu, W.S.3
  • 155
    • 0033822112 scopus 로고    scopus 로고
    • P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228
    • Sandor V, Senderowicz A, Mertins S, et al: P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228. Br J Cancer 83:817-825, 2000
    • (2000) Br J Cancer , vol.83 , pp. 817-825
    • Sandor, V.1    Senderowicz, A.2    Mertins, S.3
  • 156
    • 0033520944 scopus 로고    scopus 로고
    • Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects
    • Sambucetti LC, Fischer DD, Zabludoff S, et al: Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects. J Biol Chem 274: 34940-34947, 1999
    • (1999) J Biol Chem , vol.274 , pp. 34940-34947
    • Sambucetti, L.C.1    Fischer, D.D.2    Zabludoff, S.3
  • 157
    • 0034721941 scopus 로고    scopus 로고
    • Inhibition of mitogenesis in Balb/c-3T3 cells by trichostatin A. multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes
    • Wharton W, Savell J, Cress WD, et al: Inhibition of mitogenesis in Balb/c-3T3 cells by trichostatin A. multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes. J Biol Chem 275:33981-33987, 2000
    • (2000) J Biol Chem , vol.275 , pp. 33981-33987
    • Wharton, W.1    Savell, J.2    Cress, W.D.3
  • 158
    • 0036884829 scopus 로고    scopus 로고
    • The retinoblastoma tumour suppressor in development and cancer
    • Classon M, Harlow E: The retinoblastoma tumour suppressor in development and cancer. Nat Rev Cancer 2:910-917, 2002
    • (2002) Nat Rev Cancer , vol.2 , pp. 910-917
    • Classon, M.1    Harlow, E.2
  • 159
    • 18644367141 scopus 로고    scopus 로고
    • Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) alpha and beta messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells
    • Chen Z, Clark S, Birkeland M, et al: Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) alpha and beta messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells. Cancer Lett 188:127-140, 2002
    • (2002) Cancer Lett , vol.188 , pp. 127-140
    • Chen, Z.1    Clark, S.2    Birkeland, M.3
  • 160
    • 0035878721 scopus 로고    scopus 로고
    • Telomerase activation by histone deacetylase inhibitor in normal cells
    • Takakura M, Kyo S, Sowa Y, et al: Telomerase activation by histone deacetylase inhibitor in normal cells. Nucleic Acids Res 29: 3006-3011, 2001
    • (2001) Nucleic Acids Res , vol.29 , pp. 3006-3011
    • Takakura, M.1    Kyo, S.2    Sowa, Y.3
  • 161
    • 0034880682 scopus 로고    scopus 로고
    • Impact of the putative differentiating agent sodium phenylbutyrate on myelodysplastic syndromes and acute myeloid leukemia
    • Gore SD, Weng LJ, Zhai S, et al: Impact of the putative differentiating agent sodium phenylbutyrate on myelodysplastic syndromes and acute myeloid leukemia. Clin Cancer Res 7: 2330-2339, 2001
    • (2001) Clin Cancer Res , vol.7 , pp. 2330-2339
    • Gore, S.D.1    Weng, L.J.2    Zhai, S.3
  • 162
    • 1542588471 scopus 로고    scopus 로고
    • Second generation hybrid polar compounds are potent inducers of transformed cell differentiation
    • Richon VM, Webb Y, Merger R, et al: Second generation hybrid polar compounds are potent inducers of transformed cell differentiation. Proc Natl Acad Sci U S A 93:5705-5708, 1996
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5705-5708
    • Richon, V.M.1    Webb, Y.2    Merger, R.3
  • 163
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster PN, Troso-Sandoval T, Rosen N, et al: The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res 61:8492-8497, 2001
    • (2001) Cancer Res , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3
  • 164
    • 0032868044 scopus 로고    scopus 로고
    • Augmentation of phenylbutyrate-induced differentiation of myeloid leukemia cells using all-trans retinoic acid
    • Yu KH, Weng LJ, Fu S, et al: Augmentation of phenylbutyrate-induced differentiation of myeloid leukemia cells using all-trans retinoic acid. Leukemia 13:1258-1265, 1999
    • (1999) Leukemia , vol.13 , pp. 1258-1265
    • Yu, K.H.1    Weng, L.J.2    Fu, S.3
  • 165
    • 0032499756 scopus 로고    scopus 로고
    • p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells
    • Archer SY, Meng S, Shei A, et al: p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc Natl Acad Sci U S A 95:6791-6796, 1998
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6791-6796
    • Archer, S.Y.1    Meng, S.2    Shei, A.3
  • 166
    • 0035189761 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia
    • He LZ, Tolentino T, Grayson P, et al: Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia. J Clin Invest 108:1321-1330, 2001
    • (2001) J Clin Invest , vol.108 , pp. 1321-1330
    • He, L.Z.1    Tolentino, T.2    Grayson, P.3
  • 167
    • 0035132140 scopus 로고    scopus 로고
    • Histone deacetylase-targed treatment restores retinoic acid signaling and differentiation in acute myeloid leukemia
    • Ferrara FF, Fazi F, Bianchini A, et al: Histone deacetylase-targed 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
  • 168
    • 84871473478 scopus 로고    scopus 로고
    • Promotes gene expression by disrupting the DNA binding of the AML1/ETO and HDAC1 represser complex
    • Liu S, Klisovic MI, Shen T, et al: Promotes gene expression by disrupting the DNA binding of the AML1/ETO and HDAC1 represser complex. Blood 104:4386, 2004
    • (2004) Blood , vol.104 , pp. 4386
    • Liu, S.1    Klisovic, M.I.2    Shen, T.3
  • 169
    • 18244383806 scopus 로고    scopus 로고
    • Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
    • Gottlicher M, Minucci S, Zhu P, et al: Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells. EMBO J 20:6969-6978, 2001
    • (2001) EMBO J , vol.20 , pp. 6969-6978
    • Gottlicher, M.1    Minucci, S.2    Zhu, P.3
  • 170
    • 0033602765 scopus 로고    scopus 로고
    • Epigenetic regulation of gelsolin expression in human breast cancer cells
    • Mielnicki LM, Ying AM, Head KL, et al: Epigenetic regulation of gelsolin expression in human breast cancer cells. Exp Cell Res 249: 161-176, 1999
    • (1999) Exp Cell Res , vol.249 , pp. 161-176
    • Mielnicki, L.M.1    Ying, A.M.2    Head, K.L.3
  • 171
    • 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 AA, Ausserlechner MJ, 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 98:10833-10838, 2001
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3
  • 172
    • 11144358387 scopus 로고    scopus 로고
    • Co-treatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/TRAIL-induced death inducing signaling complex and apoptosis of human acute leukemia cells
    • Quo F, Sigua C, Tao J, et al: Co-treatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/TRAIL-induced death inducing signaling complex and apoptosis of human acute leukemia cells. Cancer Res 64:2580-2589, 2004
    • (2004) Cancer Res , vol.64 , pp. 2580-2589
    • Quo, F.1    Sigua, C.2    Tao, J.3
  • 173
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells
    • Rosato RR, Almenara JA, Dai Y, et al: Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol Cancer Ther 2:1273-1284, 2003
    • (2003) Mol Cancer Ther , vol.2 , pp. 1273-1284
    • Rosato, R.R.1    Almenara, J.A.2    Dai, Y.3
  • 174
    • 0042090495 scopus 로고    scopus 로고
    • Novel mechanisms of apoptosis induced by histone deacetylase inhibitors
    • Peart MJ, Tainton KM, Ruefli AA, et al: Novel mechanisms of apoptosis induced by histone deacetylase inhibitors. Cancer Res 63: 4460-4471, 2003
    • (2003) Cancer Res , vol.63 , pp. 4460-4471
    • Peart, M.J.1    Tainton, K.M.2    Ruefli, A.A.3
  • 176
    • 0037589018 scopus 로고    scopus 로고
    • Molecular sequelae of histone deacetylase inhibition in human malignant B cells
    • Mitsiades N, Mitsiades CS, Richardson PG, et al: Molecular sequelae of histone deacetylase inhibition in human malignant B cells. Blood 101:4055-4062, 2003
    • (2003) Blood , vol.101 , pp. 4055-4062
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 177
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • Henderson C, Mizzau M, Paroni G, et al: Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J Biol Chem 278: 12579-12589, 2003
    • (2003) J Biol Chem , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3
  • 178
    • 0034802325 scopus 로고    scopus 로고
    • Up-regulation of p21(WAF1/CIP1) by histone deacetylase inhibitors reduces their cytotoxicity
    • Burgess AJ, Pavey S, Warrener R, et al: Up-regulation of p21(WAF1/CIP1) by histone deacetylase inhibitors reduces their cytotoxicity. Mol Pharmacol 60:828-837, 2001
    • (2001) Mol Pharmacol , vol.60 , pp. 828-837
    • Burgess, A.J.1    Pavey, S.2    Warrener, R.3
  • 179
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma
    • Click RD, Swendeman SL, Coffey DC, et al: Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma. Cancer Res 59:4392-4399, 1999
    • (1999) Cancer Res , vol.59 , pp. 4392-4399
    • Click, R.D.1    Swendeman, S.L.2    Coffey, D.C.3
  • 180
    • 0038494686 scopus 로고    scopus 로고
    • Depsipeptide (FR901228) induces histone acetylation and inhibition of histone deacetylase in chronic lymphocytic leukemia cells concurrent with activation of caspase 8-mediated apoptosis and down-regulation of c-FLIP protein
    • Aron JL, Parthun MR, Marcucci G, et al: Depsipeptide (FR901228) induces histone acetylation and inhibition of histone deacetylase in chronic lymphocytic leukemia cells concurrent with activation of caspase 8-mediated apoptosis and down-regulation of c-FLIP protein. Blood 102:652-658, 2003
    • (2003) Blood , vol.102 , pp. 652-658
    • Aron, J.L.1    Parthun, M.R.2    Marcucci, G.3
  • 181
    • 13444274622 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway
    • Insinga A, Monestiroli S, Ronzoni S, et al: Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway. Nat Med 11:71-76, 2005
    • (2005) Nat Med , vol.11 , pp. 71-76
    • Insinga, A.1    Monestiroli, S.2    Ronzoni, S.3
  • 182
    • 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 11:77-84, 2005
    • (2005) Nat Med , vol.11 , pp. 77-84
    • Nebbioso, A.1    Clarke, N.2    Voltz, E.3
  • 183
    • 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 LM, Zhou X, Xu WS, 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 99:11700-11705, 2002
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3
  • 184
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao Y, Gao Z, Marks PA, et al: Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci U S A 101:18030-18035, 2004
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3
  • 185
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells of depsipeptide FR901228
    • Yu X, Guo ZS, Marcu MG, et al: Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells of depsipeptide FR901228. J Natl Cancer Inst 94:504-513, 2002
    • (2002) J Natl Cancer Inst , vol.94 , pp. 504-513
    • Yu, X.1    Guo, Z.S.2    Marcu, M.G.3
  • 186
    • 0043016178 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or-refractory chronic myelogenous leukemia-blast crisis cells
    • Nimmanapalli R, Fuino L, Bali P, et al: Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or-refractory chronic myelogenous leukemia-blast crisis cells. Cancer Res 63:5126-5135, 2003
    • (2003) Cancer Res , vol.63 , pp. 5126-5135
    • Nimmanapalli, R.1    Fuino, L.2    Bali, P.3
  • 187
    • 0141925960 scopus 로고    scopus 로고
    • FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases
    • Yao Q, Nishiuchi R, Li Q, et al: FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases. Clin Cancer Res 9:4483-4493, 2003
    • (2003) Clin Cancer Res , vol.9 , pp. 4483-4493
    • Yao, Q.1    Nishiuchi, R.2    Li, Q.3
  • 188
    • 20844444898 scopus 로고    scopus 로고
    • Combination of histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3
    • George P, Bali P, Annavarapu S, et al: Combination of histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood 105:1768-1776, 2005
    • (2005) Blood , vol.105 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3
  • 189
    • 4143053577 scopus 로고    scopus 로고
    • Superior activity of the combination of histone deacetylase inhibitor LAQ824 and the FLT-3 kinase inhibitor PKC412 against human acute myelogenous leukemia cells with mutant FLT-3
    • Bali P, George P, Cohen P, et al: Superior activity of the combination of histone deacetylase inhibitor LAQ824 and the FLT-3 kinase inhibitor PKC412 against human acute myelogenous leukemia cells with mutant FLT-3. Clin Cancer Res 10:4991-4997, 2004
    • (2004) Clin Cancer Res , vol.10 , pp. 4991-4997
    • Bali, P.1    George, P.2    Cohen, P.3
  • 190
    • 0035048449 scopus 로고    scopus 로고
    • Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes
    • Kim MS, Kwon HJ, Lee YM, et al: Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. Nat Med 7:437-443, 2001
    • (2001) Nat Med , vol.7 , pp. 437-443
    • Kim, M.S.1    Kwon, H.J.2    Lee, Y.M.3
  • 191
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1 alpha activity
    • Mie Lee Y, Kim SH, Kim HS, et al: Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1 alpha activity. Biochem Biophys Res Commun 300:241-246, 2003
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 241-246
    • Mie Lee, Y.1    Kim, S.H.2    Kim, H.S.3
  • 192
    • 85047699941 scopus 로고    scopus 로고
    • Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling
    • Deroanne CF, Bonjean K, Servotte S, et al: Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. Oncogene 21:427-436, 2002
    • (2002) Oncogene , vol.21 , pp. 427-436
    • Deroanne, C.F.1    Bonjean, K.2    Servotte, S.3
  • 193
    • 4644364508 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584
    • Qian DZ, Wang X, Kachhap SK, et al: The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584. Cancer Res 64: 6626-6634, 2004
    • (2004) Cancer Res , vol.64 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3
  • 194
    • 0035406174 scopus 로고    scopus 로고
    • Evidence of a functional role for the cyclin-dependent kinase-inhibitor p21WAF1/CIP1/ MDA6 in promoting differentiation and preventing mitochondrial dysfunction and apoptosis induced by sodium butyrate in human myelomonocytic leukemia cells (U937)
    • Rosato RR, Wang Z, Gopalkrishnan RV, et al: Evidence of a functional role for the cyclin-dependent kinase-inhibitor p21WAF1/CIP1/ MDA6 in promoting differentiation and preventing mitochondrial dysfunction and apoptosis induced by sodium butyrate in human myelomonocytic leukemia cells (U937). Int J Oncol 19: 181-191, 2001
    • (2001) Int J Oncol , vol.19 , pp. 181-191
    • Rosato, R.R.1    Wang, Z.2    Gopalkrishnan, R.V.3
  • 195
    • 0032842703 scopus 로고    scopus 로고
    • Phenylbutyrate-induced G1 arrest and apoptosis in myeloid leukemia cells: Structure-function analysis
    • DiGiuseppe JA, Weng LJ, Yu KH, et al: Phenylbutyrate-induced G1 arrest and apoptosis in myeloid leukemia cells: Structure-function analysis. Leukemia 13:1243-1253, 1999
    • (1999) Leukemia , vol.13 , pp. 1243-1253
    • DiGiuseppe, J.A.1    Weng, L.J.2    Yu, K.H.3
  • 196
    • 4444309863 scopus 로고    scopus 로고
    • Treatment of myelodysplastic syndromes with valproic acid alone or in combination with alltrans retinoic acid
    • Kuendgen A, Strupp C, Aivado M, et al: Treatment of myelodysplastic syndromes with valproic acid alone or in combination with alltrans retinoic acid. Blood 104:1266-1269, 2004
    • (2004) Blood , vol.104 , pp. 1266-1269
    • Kuendgen, A.1    Strupp, C.2    Aivado, M.3
  • 197
    • 28644440470 scopus 로고    scopus 로고
    • Valproic acid plus retinoic acid induce myeloid differentiation in chemotherapy-resistant acute myeloid leukemia patients
    • Nervi C, Lo Coco F, Minucci S, et al: Valproic acid plus retinoic acid induce myeloid differentiation in chemotherapy-resistant acute myeloid leukemia patients. Blood 104:1805, 2004
    • (2004) Blood , vol.104 , pp. 1805
    • Nervi, C.1    Lo Coco, F.2    Minucci, S.3
  • 198
    • 12444321545 scopus 로고    scopus 로고
    • Phase I clinical trial of histone deacetylase inhibitor: Suberoylanilide hydroxamic acid administered intravenously
    • Kelly WK, Richon VM, O'Connor O, et al: Phase I clinical trial of histone deacetylase inhibitor: Suberoylanilide hydroxamic acid administered intravenously. Clin Cancer Res 9:3578-3588, 2003
    • (2003) Clin Cancer Res , vol.9 , pp. 3578-3588
    • Kelly, W.K.1    Richon, V.M.2    O'Connor, O.3
  • 199
    • 33645336095 scopus 로고    scopus 로고
    • Phase I clnical trial of oral administration of the histone deacetylase (HDAC) inhibitor suberoylanilide hydroxamic acid (SAHA) in patients with relapsed/refractory multiple myeloma (MM)
    • Richardson P, Schlossman RB, Mitsiades CS, et al: Phase I clnical trial of oral administration of the histone deacetylase (HDAC) inhibitor suberoylanilide hydroxamic acid (SAHA) in patients with relapsed/refractory multiple myeloma (MM). Blood 104:1503, 2004
    • (2004) Blood , vol.104 , pp. 1503
    • Richardson, P.1    Schlossman, R.B.2    Mitsiades, C.S.3
  • 200
    • 3042728781 scopus 로고    scopus 로고
    • Phase II trial of oral suberoylanilide hydroxamic acid (SAHA) for cutaneous T-cell lymphorna (CTCL) and peripheral T-cell lymphoma (PTCL)
    • Duvic M, Talpur R, Chiao N, et al: Phase II trial of oral suberoylanilide hydroxamic acid (SAHA) for cutaneous T-cell lymphorna (CTCL) and peripheral T-cell lymphoma (PTCL). Blood 102:625, 2003
    • (2003) Blood , vol.102 , pp. 625
    • Duvic, M.1    Talpur, R.2    Chiao, N.3
  • 201
    • 1642415712 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect
    • Reddy P, Maeda Y, Hotary K, et al: Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect. Proc Natl Acad Sci U S A 101:3921-3926, 2004
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3921-3926
    • Reddy, P.1    Maeda, Y.2    Hotary, K.3
  • 202
    • 0141953928 scopus 로고    scopus 로고
    • The Discovery of NVP-LAQ824: From concept to clinic
    • Remiszewski SW: The Discovery of NVP-LAQ824: From concept to clinic. Curr Med Chem 10:2393-2402, 2003
    • (2003) Curr Med Chem , vol.10 , pp. 2393-2402
    • Remiszewski, S.W.1
  • 203
    • 9144225360 scopus 로고    scopus 로고
    • Selective growth inhibition of tumor cells by a novel histone deacetylase inhibitor, NVP-LAQ824
    • Atadja P, Gao L, Kwon P, et al: Selective growth inhibition of tumor cells by a novel histone deacetylase inhibitor, NVP-LAQ824. Cancer Res 64:689-695, 2004
    • (2004) Cancer Res , vol.64 , pp. 689-695
    • Atadja, P.1    Gao, L.2    Kwon, P.3
  • 204
    • 11144334135 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor NVP-LAQ824 has significant activity against myeloid leukemia cells in vitro and in vivo
    • Weisberg E, Catley L, Kujawa J, et al: Histone deacetylase inhibitor NVP-LAQ824 has significant activity against myeloid leukemia cells in vitro and in vivo. Leukemia 18:1951-1963, 2004
    • (2004) Leukemia , vol.18 , pp. 1951-1963
    • Weisberg, E.1    Catley, L.2    Kujawa, J.3
  • 205
    • 25144519688 scopus 로고    scopus 로고
    • A phase I, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase inhibitor LAQ824 in patients with hematologic malignancies
    • abstr 3024; suppl, 201s
    • Ottmann OG, Deangelo DJ, Stone RM, et al: A phase I, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase inhibitor LAQ824 in patients with hematologic malignancies. J Clin Oncol 22:201s, 2004 (abstr 3024; suppl)
    • (2004) J Clin Oncol , vol.22
    • Ottmann, O.G.1    Deangelo, D.J.2    Stone, R.M.3
  • 206
    • 31744431821 scopus 로고    scopus 로고
    • A phase I/II study of intravenous LBH589, a novel histone deacetylase (HDAC) inhibitor, in patients (pts) with advanced hematologic malignancies
    • Giles F, Fischer T, Cortes J, et al: A phase I/II study of intravenous LBH589, a novel histone deacetylase (HDAC) inhibitor, in patients (pts) with advanced hematologic malignancies. Blood 104:1802, 2004
    • (2004) Blood , vol.104 , pp. 1802
    • Giles, F.1    Fischer, T.2    Cortes, J.3
  • 207
    • 0033614993 scopus 로고    scopus 로고
    • Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives
    • Suzuki T, Ando T, Tsuchiya K, et al: Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives. J Med Chem 42:3001-3003, 1999
    • (1999) J Med Chem , vol.42 , pp. 3001-3003
    • Suzuki, T.1    Ando, T.2    Tsuchiya, K.3
  • 208
    • 0033551152 scopus 로고    scopus 로고
    • A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
    • Saito A, Yamashita T, Mariko Y, et al: A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors. Proc Natl Acad Sci U S A 96:4592-4597, 1999
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 4592-4597
    • Saito, A.1    Yamashita, T.2    Mariko, Y.3
  • 209
    • 0035113602 scopus 로고    scopus 로고
    • MS-275, a histone deacetylase inhibitor, selectively induces transforming growth factor beta type II receptor expression in human breast cancer cells
    • Lee BI, Park SH, Kim JW, et al: MS-275, a histone deacetylase inhibitor, selectively induces transforming growth factor beta type II receptor expression in human breast cancer cells. Cancer Res 61:931-934, 2001
    • (2001) Cancer Res , vol.61 , pp. 931-934
    • Lee, B.I.1    Park, S.H.2    Kim, J.W.3
  • 210
    • 0036828101 scopus 로고    scopus 로고
    • MS-27-275, an inhibitor of histone deacetylase, has marked in vitro and in vivo antitumor activity against pediatric solid tumors
    • Jaboin J, Wild J, Hamidi H, et al: MS-27-275, an inhibitor of histone deacetylase, has marked in vitro and in vivo antitumor activity against pediatric solid tumors. Cancer Res 62: 6108-6115, 2002
    • (2002) Cancer Res , vol.62 , pp. 6108-6115
    • Jaboin, J.1    Wild, J.2    Hamidi, H.3
  • 211
    • 3142689788 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells
    • Lucas DM, Davis ME, Parthun MR, et al: The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells. Leukemia 18:1207-1214, 2004
    • (2004) Leukemia , vol.18 , pp. 1207-1214
    • Lucas, D.M.1    Davis, M.E.2    Parthun, M.R.3
  • 212
    • 20044390016 scopus 로고    scopus 로고
    • Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors
    • Ungerstedt JS, Sowa Y, Xu WS, et al: Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proc Natl Acad Sci U S A 102:673-678, 2005
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 673-678
    • Ungerstedt, J.S.1    Sowa, Y.2    Xu, W.S.3
  • 213
    • 3042827659 scopus 로고    scopus 로고
    • A phase I trial of an oral histone deacetylase inhibitor, MS-275, in advanced solid tumor and lymphoma patients
    • abstr 802
    • Ryan QC, Headlee D, Sparreboom A, et al: A phase I trial of an oral histone deacetylase inhibitor, MS-275, in advanced solid tumor and lymphoma patients. Proc Am Soc Clin Oncol 21:200, 2003 (abstr 802)
    • (2003) Proc Am Soc Clin Oncol , vol.21 , pp. 200
    • Ryan, Q.C.1    Headlee, D.2    Sparreboom, A.3
  • 214
    • 0035098155 scopus 로고    scopus 로고
    • Chronic oral administration of CI-994: A phase 1 study
    • Prakash S, Foster BJ, Meyer M, et al: Chronic oral administration of CI-994: A phase 1 study. Invest New Drugs 19:1-11, 2001
    • (2001) Invest New Drugs , vol.19 , pp. 1-11
    • Prakash, S.1    Foster, B.J.2    Meyer, M.3
  • 215
    • 0036775301 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo
    • Sasakawa Y, Naoe Y, Inoue T, et al: Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo. Biochem Pharmacol 64:1079-1090, 2002
    • (2002) Biochem Pharmacol , vol.64 , pp. 1079-1090
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3
  • 216
    • 0034326799 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/ Cip1 and gelsolin
    • Han JW, Ahn SH, Park SH, et al: Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/ Cip1 and gelsolin. Cancer Res 60:6068-6074, 2000
    • (2000) Cancer Res , vol.60 , pp. 6068-6074
    • Han, J.W.1    Ahn, S.H.2    Park, S.H.3
  • 217
    • 0033566643 scopus 로고    scopus 로고
    • Depsipeptide (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: Depsipeptide (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
  • 218
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases
    • Furumai R, Matsuyama A, Kobashi N, et al: FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res 62:4916-4821, 2002
    • (2002) Cancer Res , vol.62 , pp. 4916-4821
    • Furumai, R.1    Matsuyama, A.2    Kobashi, N.3
  • 219
    • 84871466145 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor Depsipeptide (FK228) induces apoptosis through histone acetylation and upregulation of annexin A1 in AML-ETO expressing kasumi-1 cells
    • Tabe Y, Contractor R, Radke S, et al: Histone deacetylase inhibitor Depsipeptide (FK228) induces apoptosis through histone acetylation and upregulation of annexin A1 in AML-ETO expressing kasumi-1 cells. Blood 104:4343, 2004
    • (2004) Blood , vol.104 , pp. 4343
    • Tabe, Y.1    Contractor, R.2    Radke, S.3
  • 220
    • 0037137896 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis
    • Kwon HJ, Kim MJ, Nakajima H, et al: Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis. Int J Cancer 97:290-296, 2002
    • (2002) Int J Cancer , vol.97 , pp. 290-296
    • Kwon, H.J.1    Kim, M.J.2    Nakajima, H.3
  • 221
    • 3042785975 scopus 로고    scopus 로고
    • A review of depsipeptide and other histone deacetylase inhibitors in clinical trials
    • Piekarz R, Bates S: A review of depsipeptide and other histone deacetylase inhibitors in clinical trials. Curr Pharm Des 10:2289-2298, 2004
    • (2004) Curr Pharm Des , vol.10 , pp. 2289-2298
    • Piekarz, R.1    Bates, S.2
  • 222
    • 29744453804 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor Depsipeptide has differential activity in specific cytogenetic subsets of acute myeloid leukemia (AML)
    • Odenike OM, Alkan S, Sher D: The histone deacetylase inhibitor Depsipeptide has differential activity in specific cytogenetic subsets of acute myeloid leukemia (AML). Blood 104:264, 2004
    • (2004) Blood , vol.104 , pp. 264
    • Odenike, O.M.1    Alkan, S.2    Sher, D.3
  • 223
    • 33846891184 scopus 로고    scopus 로고
    • Analysis of the effect of the novel histone deacetylase inhibitor, Depsipeptide (FK288/FR901228) on mantle cell lymphoma
    • Paner GP, Alkan S: Analysis of the effect of the novel histone deacetylase inhibitor, Depsipeptide (FK288/FR901228) on mantle cell lymphoma. Blood 104:2499, 2004
    • (2004) Blood , vol.104 , pp. 2499
    • Paner, G.P.1    Alkan, S.2
  • 224
    • 33846863446 scopus 로고    scopus 로고
    • Mantle cell lymphoma: SAHA blocks Akt/mTOR pathway and reduces cyclin D1 protein levels by affecting translation
    • Kawamata N, Koeffler HP: Mantle cell lymphoma: SAHA blocks Akt/mTOR pathway and reduces cyclin D1 protein levels by affecting translation. Blood 104:3293, 2004
    • (2004) Blood , vol.104 , pp. 3293
    • Kawamata, N.1    Koeffler, H.P.2
  • 225
    • 0032989027 scopus 로고    scopus 로고
    • Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • Qiu L, Kelso MJ, Hansen C, et al: Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate. Br J Cancer 80:1252-1258, 1999
    • (1999) Br J Cancer , vol.80 , pp. 1252-1258
    • Qiu, L.1    Kelso, M.J.2    Hansen, C.3
  • 226
    • 0035933731 scopus 로고    scopus 로고
    • Histone hyperacetylation induced by histone deacetylase inhibitors is not sufficient to cause growth inhibition in human dermal fibroblasts
    • Brinkmann H, Dahler AL, Popa C, et al: Histone hyperacetylation induced by histone deacetylase inhibitors is not sufficient to cause growth inhibition in human dermal fibroblasts. J Biol Chem 276:22491-22499, 2001
    • (2001) J Biol Chem , vol.276 , pp. 22491-22499
    • Brinkmann, H.1    Dahler, A.L.2    Popa, C.3
  • 227
    • 0642345200 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberic bishydroxamate: A potential sensitizer of melanoma to TNF-related apoptosis-inducing ligand (TRAIL) induced apoptosis
    • Zhang XD, Gillespie SK, Borrow JM, et al: The histone deacetylase inhibitor suberic bishydroxamate: A potential sensitizer of melanoma to TNF-related apoptosis-inducing ligand (TRAIL) induced apoptosis. Biochem Pharmacol 66: 1537-1545, 2003
    • (2003) Biochem Pharmacol , vol.66 , pp. 1537-1545
    • Zhang, X.D.1    Gillespie, S.K.2    Borrow, J.M.3
  • 228
    • 0842346437 scopus 로고    scopus 로고
    • Principles of tumor suppression
    • Sherr CJ: Principles of tumor suppression. Cell 116:235-246, 2004
    • (2004) Cell , vol.116 , pp. 235-246
    • Sherr, C.J.1
  • 230
    • 4344666663 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells
    • Nakata S, Yoshida T, Horinaka M, et al: Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells. Oncogene 23:6261-6271, 2004
    • (2004) Oncogene , vol.23 , pp. 6261-6271
    • Nakata, S.1    Yoshida, T.2    Horinaka, M.3
  • 231
    • 0037115392 scopus 로고    scopus 로고
    • Dependence of histone modifications and gene expression on DNA hypermethylation in cancer
    • Fahrner JA, Eguchi S, Herman JG, et al: Dependence of histone modifications and gene expression on DNA hypermethylation in cancer. Cancer Res 62:7213-7218, 2002
    • (2002) Cancer Res , vol.62 , pp. 7213-7218
    • Fahrner, J.A.1    Eguchi, S.2    Herman, J.G.3
  • 232
    • 0037924433 scopus 로고    scopus 로고
    • Histone modifications and silencing prior to DNA methylation of a tumor suppressor gene
    • Bachman KE, Park BH, Rhee I, et al: Histone modifications and silencing prior to DNA methylation of a tumor suppressor gene. Cancer Cell 3:89-95, 2003
    • (2003) Cancer Cell , vol.3 , pp. 89-95
    • Bachman, K.E.1    Park, B.H.2    Rhee, I.3
  • 233
    • 2542545717 scopus 로고    scopus 로고
    • Transcriptional gene silencing promotes DNA hypermethylation through a sequential change in chromatin modifications in cancer cells
    • Stirzaker C, Song JZ, Davidson B, et al: Transcriptional gene silencing promotes DNA hypermethylation through a sequential change in chromatin modifications in cancer cells. Cancer Res 64:3871-3877, 2004
    • (2004) Cancer Res , vol.64 , pp. 3871-3877
    • Stirzaker, C.1    Song, J.Z.2    Davidson, B.3
  • 234
    • 0037112369 scopus 로고    scopus 로고
    • Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2′-deoxycytidine
    • Nguyen CT, Weisenberger DJ, Velicescu M, et al: Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2′-deoxycytidine. Cancer Res 62:6456-6461, 2002
    • (2002) Cancer Res , vol.62 , pp. 6456-6461
    • Nguyen, C.T.1    Weisenberger, D.J.2    Velicescu, M.3
  • 235
    • 0035866353 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors
    • Zhu WG, Lakshmanan RR, Beal MD, et al: DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res 61:1327-1333, 2001
    • (2001) Cancer Res , vol.61 , pp. 1327-1333
    • Zhu, W.G.1    Lakshmanan, R.R.2    Beal, M.D.3
  • 236
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron EE, Bachman KE, Myohanen S, et al: Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet 21:103-107, 1999
    • (1999) Nat Genet , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3
  • 237
    • 0242442588 scopus 로고    scopus 로고
    • Inhibition of DNA methylation and histone deacetylation prevents murine lung cancer
    • Belinsky SA, Klinge DM, Stidley CA, et al: Inhibition of DNA methylation and histone deacetylation prevents murine lung cancer. Cancer Res 63:7089-7093, 2003
    • (2003) Cancer Res , vol.63 , pp. 7089-7093
    • Belinsky, S.A.1    Klinge, D.M.2    Stidley, C.A.3
  • 238
    • 0037276902 scopus 로고    scopus 로고
    • The interaction of histone deacetylase inhibitors and DNA methyltransferase inhibitors in the treatment of human cancer cells
    • Zhu WG, Otterson GA: The interaction of histone deacetylase inhibitors and DNA methyltransferase inhibitors in the treatment of human cancer cells. Curr Med Chem Anti-Canc Agents 3:187-199, 2003
    • (2003) Curr Med Chem Anti-Canc Agents , vol.3 , pp. 187-199
    • Zhu, W.G.1    Otterson, G.A.2
  • 239
    • 3242722145 scopus 로고    scopus 로고
    • State of the translational science: Summary of Baltimore workshop on gene re-expression as a therapeutic target in cancer January 2003
    • Zelent A, Waxman S, Carducci M, et al: State of the translational science: Summary of Baltimore workshop on gene re-expression as a therapeutic target in cancer January 2003. Clin Cancer Res 10:4622-4629, 2004
    • (2004) Clin Cancer Res , vol.10 , pp. 4622-4629
    • Zelent, A.1    Waxman, S.2    Carducci, M.3
  • 240
    • 21844444900 scopus 로고    scopus 로고
    • Changes in promoter methylation and gene expression in patients with MDS and MDS-AML treated with 5-Azacitidine and sodium phenylbutyrate
    • Gore SD, Baylin SB, Dauses T, et al: Changes in promoter methylation and gene expression in patients with MDS and MDS-AML treated with 5-Azacitidine and sodium phenylbutyrate. Blood 104:469, 2004
    • (2004) Blood , vol.104 , pp. 469
    • Gore, S.D.1    Baylin, S.B.2    Dauses, T.3
  • 241
    • 20344393986 scopus 로고    scopus 로고
    • Results of a phase I/II study of the combination of 5-aza-2′-deoxycytidine (DAC) and valproic acid (VPA) in patients (pts) with leukemia
    • Garcia-Manero G, Kantarjian H, Sanchez-Gonzalez B, et al: Results of a phase I/II study of the combination of 5-aza-2′-deoxycytidine (DAC) and valproic acid (VPA) in patients (pts) with leukemia. Blood 104:263, 2004
    • (2004) Blood , vol.104 , pp. 263
    • Garcia-Manero, G.1    Kantarjian, H.2    Sanchez-Gonzalez, B.3
  • 242
    • 0033646839 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and retinoic acids inhibit growth of human neuroblastoma in vitro
    • Coffey DC, Kutko MC, Glick RD, et al: Histone deacetylase inhibitors and retinoic acids inhibit growth of human neuroblastoma in vitro. Med Pediatr Oncol 35:577-581, 2000
    • (2000) Med Pediatr Oncol , vol.35 , pp. 577-581
    • Coffey, D.C.1    Kutko, M.C.2    Glick, R.D.3
  • 243
    • 0035328528 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, CBHA, inhibits growth of human neuroblastoma xenografts in vivo, alone and synergistically with all-trans retinoic acid
    • Coffey DC, Kutko MC, Glick RD, et al: The histone deacetylase inhibitor, CBHA, inhibits growth of human neuroblastoma xenografts in vivo, alone and synergistically with all-trans retinoic acid. Cancer Res 61:3591-3594, 2001
    • (2001) Cancer Res , vol.61 , pp. 3591-3594
    • Coffey, D.C.1    Kutko, M.C.2    Glick, R.D.3
  • 244
    • 0036093681 scopus 로고    scopus 로고
    • Flavopiridol, a novel cyclin-dependent kinase inhibitor, in clinical development
    • Zhai S, Senderowicz AM, Sausville EA, et al: Flavopiridol, a novel cyclin-dependent kinase inhibitor, in clinical development. Ann Pharmacother 36:905-911, 2002
    • (2002) Ann Pharmacother , vol.36 , pp. 905-911
    • Zhai, S.1    Senderowicz, A.M.2    Sausville, E.A.3
  • 245
    • 0036050151 scopus 로고    scopus 로고
    • Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA)
    • Almenara J, Rosato R, Grant S: Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA). Leukemia 16:1331-1343, 2002
    • (2002) Leukemia , vol.16 , pp. 1331-1343
    • Almenara, J.1    Rosato, R.2    Grant, S.3
  • 246
    • 0036463521 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor flavopiridol disrupts sodium butyrate-induced p21WAF1/ CIP1 expression and maturation while reciprocally potentiating apoptosis in human leukemia cells
    • Rosato RR, Almenara JA, Cartee L, et al: The cyclin-dependent kinase inhibitor flavopiridol disrupts sodium butyrate-induced p21WAF1/ CIP1 expression and maturation while reciprocally potentiating apoptosis in human leukemia cells. Mol Cancer Ther 1:253-266, 2002
    • (2002) Mol Cancer Ther , vol.1 , pp. 253-266
    • Rosato, R.R.1    Almenara, J.A.2    Cartee, L.3
  • 247
    • 1842481018 scopus 로고    scopus 로고
    • Abrogation of p21 expression by flavopiridol enhances depsipeptide-mediated apoptosis in malignant pleural mesothelioma cells
    • Nguyen DM, Schrump WD, Chen GA, et al: Abrogation of p21 expression by flavopiridol enhances depsipeptide-mediated apoptosis in malignant pleural mesothelioma cells. Clin Cancer Res 10:1813-1825, 2004
    • (2004) Clin Cancer Res , vol.10 , pp. 1813-1825
    • Nguyen, D.M.1    Schrump, W.D.2    Chen, G.A.3
  • 248
    • 4844224868 scopus 로고    scopus 로고
    • Contribution of disruption of the nuclear factor-kappaB pathway to induction of apoptosis in human leukemia cells by histone deacetylase inhibitors and flavopiridol
    • Gao N, Dai Y, Rahmani M, et al: Contribution of disruption of the nuclear factor-kappaB pathway to induction of apoptosis in human leukemia cells by histone deacetylase inhibitors and flavopiridol. Mol Pharmacol 66:956-963, 2004
    • (2004) Mol Pharmacol , vol.66 , pp. 956-963
    • Gao, N.1    Dai, Y.2    Rahmani, M.3
  • 249
    • 20244362748 scopus 로고    scopus 로고
    • Flavopiridol downregulates antiapoptotic proteins and sensitizes human breast cancer cells to epothilone B-induced apoptosis
    • Wittmann S, Bali P, Donapaty S, et al: Flavopiridol downregulates antiapoptotic proteins and sensitizes human breast cancer cells to epothilone B-induced apoptosis. Cancer Res 63:93-99, 2003
    • (2003) Cancer Res , vol.63 , pp. 93-99
    • Wittmann, S.1    Bali, P.2    Donapaty, S.3
  • 250
    • 0036850211 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1
    • Gojo I, Zhang B, Fenton RG: The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1. Clin Cancer Res 8:3527-3538, 2002
    • (2002) Clin Cancer Res , vol.8 , pp. 3527-3538
    • Gojo, I.1    Zhang, B.2    Fenton, R.G.3
  • 251
    • 0037228959 scopus 로고    scopus 로고
    • Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumor cell apoptosis
    • Wall NR, O'Connor DS, Plescia J, et al: Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumor cell apoptosis. Cancer Res 63:230-235, 2003
    • (2003) Cancer Res , vol.63 , pp. 230-235
    • Wall, N.R.1    O'Connor, D.S.2    Plescia, J.3
  • 252
    • 84871468750 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SANA) attenuates Her-2 levels and exerts synergistic cytotoxicity with trastuzumab or docetaxel against breast cancer cells with amplification of Her-2
    • Manuscript submitted
    • Bali P, Pranpat M, Swaby R, et al: Suberoylanilide hydroxamic acid (SANA) attenuates Her-2 levels and exerts synergistic cytotoxicity with trastuzumab or docetaxel against breast cancer cells with amplification of Her-2. Manuscript submitted, 2004
    • (2004)
    • Bali, P.1    Pranpat, M.2    Swaby, R.3
  • 253
    • 0031723393 scopus 로고    scopus 로고
    • Enhanced growth inhibition and differentiation of fluorodeoxyuridine-treated human colon carcinoma cells by phenylbutyrate
    • Huang Y, Waxman S: Enhanced growth inhibition and differentiation of fluorodeoxyuridine-treated human colon carcinoma cells by phenylbutyrate. Clin Cancer Res 4:2503-2509, 1998
    • (1998) Clin Cancer Res , vol.4 , pp. 2503-2509
    • Huang, Y.1    Waxman, S.2
  • 254
    • 0242610850 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA
    • Kim MS, Blake M, Baek JH, et al: Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA. Cancer Res 63:7291-7300, 2003
    • (2003) Cancer Res , vol.63 , pp. 7291-7300
    • Kim, M.S.1    Blake, M.2    Baek, J.H.3
  • 255
    • 0035552571 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor sodium butyrate induces DNA topoisomerase II alpha expression and confers hypersensitivity to etoposide in human leukemic cell lines
    • Kurz EU, Wilson SE, Leader KB, et al: The histone deacetylase inhibitor sodium butyrate induces DNA topoisomerase II alpha expression and confers hypersensitivity to etoposide in human leukemic cell lines. Mol Cancer Ther 1:121-131, 2001
    • (2001) Mol Cancer Ther , vol.1 , pp. 121-131
    • Kurz, E.U.1    Wilson, S.E.2    Leader, K.B.3
  • 256
    • 16544379283 scopus 로고    scopus 로고
    • Sequence-specific potentiation of topoisomerase II inhibitors by the histone deacetylase inhibitor suberoylanilide hydroxamic acid
    • Marchion DC, Bicaku E, Daud AI, et al: Sequence-specific potentiation of topoisomerase II inhibitors by the histone deacetylase inhibitor suberoylanilide hydroxamic acid. J Cell Biochem 92:223-237, 2004
    • (2004) J Cell Biochem , vol.92 , pp. 223-237
    • Marchion, D.C.1    Bicaku, E.2    Daud, A.I.3
  • 257
    • 0033952555 scopus 로고    scopus 로고
    • Induction of apoptosis in malignant B cells by phenylbutyrate or phenylacetate in combination with chemotherapeutic agents
    • Witzig TE, Timm M, Stenson M, et al: Induction of apoptosis in malignant B cells by phenylbutyrate or phenylacetate in combination with chemotherapeutic agents. Clin Cancer Res 6:681-692, 2000
    • (2000) Clin Cancer Res , vol.6 , pp. 681-692
    • Witzig, T.E.1    Timm, M.2    Stenson, M.3
  • 258
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells
    • Rosato RR, Almenara JA, Dai Y, et al: Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol Cancer Ther 2:1273-1284, 2003
    • (2003) Mol Cancer Ther , vol.2 , pp. 1273-1284
    • Rosato, R.R.1    Almenara, J.A.2    Dai, Y.3
  • 259
    • 0345734267 scopus 로고    scopus 로고
    • Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells
    • Rahmani M, Yu C, Dai Y, et al: Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells. Cancer Res 63:8420-8427, 2003
    • (2003) Cancer Res , vol.63 , pp. 8420-8427
    • Rahmani, M.1    Yu, C.2    Dai, Y.3
  • 260
    • 3142676436 scopus 로고    scopus 로고
    • Overriding imatinib resistance with a novel ABL kinase inhibitor
    • Shah NP, Tran C, Lee FY, et al: Overriding imatinib resistance with a novel ABL kinase inhibitor. Science 305:399-401, 2004
    • (2004) Science , vol.305 , pp. 399-401
    • Shah, N.P.1    Tran, C.2    Lee, F.Y.3
  • 261
    • 16844379200 scopus 로고    scopus 로고
    • Hematologic and cytogenetic responses in imatinib-resistant chronic phase chronic myeloid leukemia patients treated with the dual SRC/ ABL kinase inhibitor BMS-354825: Results from a phase I dose escalation study
    • Sawyers CL, Shah NP, Kantarjian HM, et al: Hematologic and cytogenetic responses in imatinib-resistant chronic phase chronic myeloid leukemia patients treated with the dual SRC/ ABL kinase inhibitor BMS-354825: Results from a phase I dose escalation study. Blood 104:1, 2004
    • (2004) Blood , vol.104 , pp. 1
    • Sawyers, C.L.1    Shah, N.P.2    Kantarjian, H.M.3
  • 262
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J: The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5:417-421, 2004
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 263
    • 0242493856 scopus 로고    scopus 로고
    • The proteasorne inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571
    • Yu C, Rahmani M, Conrad D, et al: The proteasorne inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571. Blood 102:3765-3774, 2003
    • (2003) Blood , vol.102 , pp. 3765-3774
    • Yu, C.1    Rahmani, M.2    Conrad, D.3
  • 264
    • 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 XY, 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 10:3839-3852, 2004
    • (2004) Clin Cancer Res , vol.10 , pp. 3839-3852
    • Pei, X.Y.1    Dai, Y.2    Grant, S.3
  • 265
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, Eisenhaber F, O'Carroll D, et al: Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406:593-599, 2000
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3
  • 267
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • Bannister AJ, Zegerman P, Partridge JF, et al: Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410:120-124, 2001
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3
  • 268
    • 17944380227 scopus 로고    scopus 로고
    • Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability
    • Peters AH, O'Carroll D, Scherthan H, et al: Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 107:323-337, 2001
    • (2001) Cell , vol.107 , pp. 323-337
    • Peters, A.H.1    O'Carroll, D.2    Scherthan, H.3
  • 269
    • 0345275880 scopus 로고    scopus 로고
    • Inactivation of a histone methyltransferase by mutations in human cancers
    • Kim KC, Geng L, Huang S: Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res 63:7619-7623, 2003
    • (2003) Cancer Res , vol.63 , pp. 7619-7623
    • Kim, K.C.1    Geng, L.2    Huang, S.3
  • 270
    • 0032723317 scopus 로고    scopus 로고
    • Forced expression of the leukemia-associated gene EVI1 in ES cells: A model for myeloid leukemia with 3q26 rearrangements
    • Sitailo S, Sood R, Barton K, et al: Forced expression of the leukemia-associated gene EVI1 in ES cells: A model for myeloid leukemia with 3q26 rearrangements. Leukemia 13:1639-1645, 1999
    • (1999) Leukemia , vol.13 , pp. 1639-1645
    • Sitailo, S.1    Sood, R.2    Barton, K.3
  • 271
    • 0037305621 scopus 로고    scopus 로고
    • Barjesteh van Waalwijkvan Doorn-Khosrovani S, Erpelinck C, van Putten WL, et al: High EVI1 expression predicts poor survival in acute myeloid leukemia: A study of 319 de novo AML patients. Blood 101:837-845, 2003
    • Barjesteh van Waalwijkvan Doorn-Khosrovani S, Erpelinck C, van Putten WL, et al: High EVI1 expression predicts poor survival in acute myeloid leukemia: A study of 319 de novo AML patients. Blood 101:837-845, 2003
  • 272
    • 0035839841 scopus 로고    scopus 로고
    • Chromosome translocations in multiple myeloma
    • Bergsagel PL, Kuehl WM: Chromosome translocations in multiple myeloma. Oncogene 20:5611-5622, 2001
    • (2001) Oncogene , vol.20 , pp. 5611-5622
    • Bergsagel, P.L.1    Kuehl, W.M.2
  • 274
    • 18644382388 scopus 로고    scopus 로고
    • The polycomb group protein EZH2 is involved in progression of prostate cancer
    • Varambally S, Dhanasekaran SM, Zhou M, et al: The polycomb group protein EZH2 is involved in progression of prostate cancer. Nature 419:624-629, 2002
    • (2002) Nature , vol.419 , pp. 624-629
    • Varambally, S.1    Dhanasekaran, S.M.2    Zhou, M.3
  • 275
    • 0141816752 scopus 로고    scopus 로고
    • EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
    • Kleer CG, Cao Q, Varambally S, et al: EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells. Proc Natl Acad Sci U S A 100: 11606-11611, 2003
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11606-11611
    • Kleer, C.G.1    Cao, Q.2    Varambally, S.3
  • 276
    • 0142105414 scopus 로고    scopus 로고
    • EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer
    • Bracken AP, Pasini D, Capra M, et al: EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer. EMBO J 22:5323-5335, 2003
    • (2003) EMBO J , vol.22 , pp. 5323-5335
    • Bracken, A.P.1    Pasini, D.2    Capra, M.3
  • 277
    • 2442591839 scopus 로고    scopus 로고
    • Extending the repertoire of the mixed-lineage leukemia gene MLL in leukemogenesis
    • Daser A, Rabbitts TH: Extending the repertoire of the mixed-lineage leukemia gene MLL in leukemogenesis. Genes Dev 18:965-974, 2004
    • (2004) Genes Dev , vol.18 , pp. 965-974
    • Daser, A.1    Rabbitts, T.H.2
  • 278
    • 18744373853 scopus 로고    scopus 로고
    • MLL targets SET domain methyltransferase activity to Hox gene promoters
    • Milne TA, Briggs SD, Brock HW, et al: MLL targets SET domain methyltransferase activity to Hox gene promoters. Mol Cell 10:1107-1117, 2002
    • (2002) Mol Cell , vol.10 , pp. 1107-1117
    • Milne, T.A.1    Briggs, S.D.2    Brock, H.W.3
  • 279
    • 18744410349 scopus 로고    scopus 로고
    • ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation
    • Nakamura T, Mori T, Tada S, et al: ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol Cell 10:1119-1128, 2002
    • (2002) Mol Cell , vol.10 , pp. 1119-1128
    • Nakamura, T.1    Mori, T.2    Tada, S.3
  • 280
    • 0042885909 scopus 로고    scopus 로고
    • Dimerization contributes to oncogenic activation of MLL chimeras in acute leukemias
    • So CW, Lin M, Ayton PM, et al: Dimerization contributes to oncogenic activation of MLL chimeras in acute leukemias. Cancer Cell 4:99-110, 2003
    • (2003) Cancer Cell , vol.4 , pp. 99-110
    • So, C.W.1    Lin, M.2    Ayton, P.M.3
  • 281
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker PB, Horz W: ATP-dependent nucleosome remodeling. Annu Rev Biochem 71: 247-273, 2002
    • (2002) Annu Rev Biochem , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 282
    • 0037043825 scopus 로고    scopus 로고
    • Re-expression of hSNF5/INI1/BAF47 in pediatric tumor cells leads to G1 arrest associated with induction of p16ink4a and activation of RB
    • Betz BL, Strobeck MW, Reisman DN, et al: Re-expression of hSNF5/INI1/BAF47 in pediatric tumor cells leads to G1 arrest associated with induction of p16ink4a and activation of RB. Oncogene 21:5193-5203, 2002
    • (2002) Oncogene , vol.21 , pp. 5193-5203
    • Betz, B.L.1    Strobeck, M.W.2    Reisman, D.N.3
  • 283
    • 0042452295 scopus 로고    scopus 로고
    • Highly penetrant, rapid tumorigenesis through conditional inversion of the tumor suppressor gene Snf5
    • Roberts CW, Leroux MM, Fleming MD, et al: Highly penetrant, rapid tumorigenesis through conditional inversion of the tumor suppressor gene Snf5. Cancer Cell 2:415-425, 2002
    • (2002) Cancer Cell , vol.2 , pp. 415-425
    • Roberts, C.W.1    Leroux, M.M.2    Fleming, M.D.3
  • 284
    • 0033082238 scopus 로고    scopus 로고
    • Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits
    • Phelan ML, Sif S, Narlikar GJ, et al: Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits. Mol Cell 3: 247-253, 1999
    • (1999) Mol Cell , vol.3 , pp. 247-253
    • Phelan, M.L.1    Sif, S.2    Narlikar, G.J.3
  • 285
    • 0037308717 scopus 로고    scopus 로고
    • Loss of BRG1/BRM in human lung cancer cell lines and primary lung cancers: Correlation with poor prognosis
    • Reisman DN, Sciarrotta J, Wang W, et al: Loss of BRG1/BRM in human lung cancer cell lines and primary lung cancers: Correlation with poor prognosis. Cancer Res 63:560-566, 2003
    • (2003) Cancer Res , vol.63 , pp. 560-566
    • Reisman, D.N.1    Sciarrotta, J.2    Wang, W.3
  • 286
    • 2942746179 scopus 로고    scopus 로고
    • Histone variants, nucleosome assembly and epigenetic inheritance
    • Henikoff S, Furuyama T, Ahmad K: Histone variants, nucleosome assembly and epigenetic inheritance. Trends Genet 20:320-326, 2004
    • (2004) Trends Genet , vol.20 , pp. 320-326
    • Henikoff, S.1    Furuyama, T.2    Ahmad, K.3
  • 287
    • 0037062492 scopus 로고    scopus 로고
    • Increased ionizing radiation sensitivity and genomic instability in the absence of histone H2AX
    • Bassing CH, Chua KF, Sekiguchi J, et al: Increased ionizing radiation sensitivity and genomic instability in the absence of histone H2AX. Proc Natl Acad Sci U S A 99:8173-8178, 2002
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 8173-8178
    • Bassing, C.H.1    Chua, K.F.2    Sekiguchi, J.3
  • 288
    • 0042991379 scopus 로고    scopus 로고
    • Histone H2AX: A dosage-dependent suppressor of oncogenic translocations and tumors
    • Bassing CH, Suh H, Ferguson DO, et al: Histone H2AX: A dosage-dependent suppressor of oncogenic translocations and tumors. Cell 114:359-370, 2003
    • (2003) Cell , vol.114 , pp. 359-370
    • Bassing, C.H.1    Suh, H.2    Ferguson, D.O.3
  • 289
    • 0042991383 scopus 로고    scopus 로고
    • H2AX haploinsufficiency modifies genomic stability and tumor susceptibility
    • Celeste A, Difilippantonio S, Difilippantonio MJ, et al: H2AX haploinsufficiency modifies genomic stability and tumor susceptibility. Cell 114:371-383, 2003
    • (2003) Cell , vol.114 , pp. 371-383
    • Celeste, A.1    Difilippantonio, S.2    Difilippantonio, M.J.3
  • 290
    • 3042642001 scopus 로고    scopus 로고
    • RNA interference demonstrates a novel role for H2A.Z in chromosome segregation
    • Rangasamy D, Greaves I, Tremethick DJ: RNA interference demonstrates a novel role for H2A.Z in chromosome segregation. Nat Struct Mol Biol 11:650-655, 2004
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 650-655
    • Rangasamy, D.1    Greaves, I.2    Tremethick, D.J.3
  • 291
    • 0034691161 scopus 로고    scopus 로고
    • Human centromere protein A (CENP-A) can replace histone H3 in nucleosome reconstitution in vitro
    • Yoda K, Ando S, Morishita S, et al: Human centromere protein A (CENP-A) can replace histone H3 in nucleosome reconstitution in vitro. Proc Natl Acad Sci U S A 97:7266-7271, 2000
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7266-7271
    • Yoda, K.1    Ando, S.2    Morishita, S.3
  • 292
    • 0038079839 scopus 로고    scopus 로고
    • Overexpression and mistargeting of centromere protein-A in human primary colorectal cancer
    • Tomonaga T, Matsushita K, Yamaguchi S, et al: Overexpression and mistargeting of centromere protein-A in human primary colorectal cancer. Cancer Res 63:3511-3516, 2003
    • (2003) Cancer Res , vol.63 , pp. 3511-3516
    • Tomonaga, T.1    Matsushita, K.2    Yamaguchi, S.3
  • 293
    • 0036229658 scopus 로고    scopus 로고
    • Avian bic, a gene isolated from a common retroviral site in avian leukosis virus-induced lymphomas that encodes a noncoding RNA, cooperates with c-myc in lymphomagenesis and erythroleukemogenesis
    • Tarn W, Hughes SH, Hayward WS, et al: Avian bic, a gene isolated from a common retroviral site in avian leukosis virus-induced lymphomas that encodes a noncoding RNA, cooperates with c-myc in lymphomagenesis and erythroleukemogenesis. J Virol 76:4275-4286, 2002
    • (2002) J Virol , vol.76 , pp. 4275-4286
    • Tarn, W.1    Hughes, S.H.2    Hayward, W.S.3
  • 294
    • 18744396337 scopus 로고    scopus 로고
    • Frequent deletions and down-regulation of micro- RNA genes miR15 and miR16 at 13q14 in chronic lymphocytic leukemia
    • Calin GA, Dumitru CD, Shimizu M, et al: Frequent deletions and down-regulation of micro- RNA genes miR15 and miR16 at 13q14 in chronic lymphocytic leukemia. Proc Natl Acad Sci U S A 99:15524-15529, 2002
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 15524-15529
    • Calin, G.A.1    Dumitru, C.D.2    Shimizu, M.3
  • 295
    • 12144290519 scopus 로고    scopus 로고
    • Human microRNA genes are frequently located at fragile sites and genomic regions involved in cancers
    • Calin GA, Sevignani C, Dumitru CD, et al: Human microRNA genes are frequently located at fragile sites and genomic regions involved in cancers. Proc Natl Acad Sci U S A 101:2999-3004, 2004
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2999-3004
    • Calin, G.A.1    Sevignani, C.2    Dumitru, C.D.3
  • 296
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir SM, Harborth J, Lendeckel W, et al: Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411:494-498, 2001
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3
  • 297
    • 0942279615 scopus 로고    scopus 로고
    • Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery
    • Pal-Bhadra M, Leibovitch BA, Gandhi SG, et al: Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery. Science 303:669-672, 2004
    • (2004) Science , vol.303 , pp. 669-672
    • Pal-Bhadra, M.1    Leibovitch, B.A.2    Gandhi, S.G.3
  • 298
    • 0036184188 scopus 로고    scopus 로고
    • RNAi related mechanisms affect both transcriptional and posttranscriptional transgene silencing in Drosophila
    • Pal-Bhadra M, Bhadra U, Birchler JA: RNAi related mechanisms affect both transcriptional and posttranscriptional transgene silencing in Drosophila. Mol Cell 9:315-327, 2002
    • (2002) Mol Cell , vol.9 , pp. 315-327
    • Pal-Bhadra, M.1    Bhadra, U.2    Birchler, J.A.3
  • 299
    • 9144247189 scopus 로고    scopus 로고
    • Therapeutic silencing of an endogenous gene by systemic administration of modified siRNAs
    • Soutschek J, Akinc A, Bramlage B, et al: Therapeutic silencing of an endogenous gene by systemic administration of modified siRNAs. Nature 432:173-178, 2004
    • (2004) Nature , vol.432 , pp. 173-178
    • Soutschek, J.1    Akinc, A.2    Bramlage, B.3
  • 300
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo RX, Postigo AA, Dean DC: Rb interacts with histone deacetylase to repress transcription. Cell 92:463-473, 1998
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 301
    • 0034785586 scopus 로고    scopus 로고
    • Linking the Rb and polycomb pathways
    • Dahiya A, Wong S, Gonzalo S, et al: Linking the Rb and polycomb pathways. Mol Cell 8:557-569, 2001
    • (2001) Mol Cell , vol.8 , pp. 557-569
    • Dahiya, A.1    Wong, S.2    Gonzalo, S.3
  • 302
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • Marita M, Nunez S, Heard E, et al: Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Cell 113:703-716, 2003
    • (2003) Cell , vol.113 , pp. 703-716
    • Marita, M.1    Nunez, S.2    Heard, E.3
  • 303
    • 0029020759 scopus 로고
    • The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1A protein
    • Buyse IM, Shao G, Huang S: The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1A protein. Proc Natl Acad Sci U S A 92:4467-4471, 1995
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4467-4471
    • Buyse, I.M.1    Shao, G.2    Huang, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.