메뉴 건너뛰기




Volumn 94, Issue 2, 1999, Pages 417-428

Chromatin remodeling and leukemia: New therapeutic paradigms

Author keywords

[No Author keywords available]

Indexed keywords

2 CARBOXYCINNAMIC ACID BISHYDROXAMIDE; ARSENIC TRIOXIDE; ARYLBUTYRIC ACID DERIVATIVE; AZACITIDINE; BUTYRIC ACID; BUTYRIC ACID DERIVATIVE; DNA; DNA TOPOISOMERASE INHIBITOR; ENZYME INHIBITOR; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HYBRID PROTEIN; RETINOIC ACID; RETINOIC ACID RECEPTOR; RETINOID X RECEPTOR; TRAPOXIN; TRIBUTYRIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 0033566302     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v94.2.417.414k49_417_428     Document Type: Review
Times cited : (171)

References (150)
  • 2
    • 0030931494 scopus 로고    scopus 로고
    • Chromatin structure. The nucleosome core all wrapped up
    • Rhodes D: Chromatin structure. The nucleosome core all wrapped up. Nature 389:233, 1997
    • (1997) Nature , vol.389 , pp. 233
    • Rhodes, D.1
  • 3
    • 0015964401 scopus 로고
    • Spheroid chromatin units (v bodies)
    • Olins AL, Olins DE: Spheroid chromatin units (v bodies). Science 183:330, 1974
    • (1974) Science , vol.183 , pp. 330
    • Olins, A.L.1    Olins, D.E.2
  • 4
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch JT, Klug A: Solenoidal model for superstructure in chromatin. Proc Natl Acad Sci USA 73:1897, 1976
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1897
    • Finch, J.T.1    Klug, A.2
  • 7
    • 0028850059 scopus 로고
    • Overcoming a nucleosomal barrier to transcription
    • Studitsky VM, Clark DJ, Felsenfeld G: Overcoming a nucleosomal barrier to transcription. Cell 83:19, 1995
    • (1995) Cell , vol.83 , pp. 19
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 8
    • 0032493667 scopus 로고    scopus 로고
    • Evidence that partial unwrapping of DNA from nucleosomes facilitates the binding of heat shock factor following DNA replication in yeast
    • Geraghty DS, Sucic HB, Chen J, Pederson DS: Evidence that partial unwrapping of DNA from nucleosomes facilitates the binding of heat shock factor following DNA replication in yeast. J Biol Chem 273:20463, 1998
    • (1998) J Biol Chem , vol.273 , pp. 20463
    • Geraghty, D.S.1    Sucic, H.B.2    Chen, J.3    Pederson, D.S.4
  • 9
    • 0031009397 scopus 로고    scopus 로고
    • Chromatin remodeling and transcription
    • Tsukiyama T, Wu C: Chromatin remodeling and transcription. Curr Opin Genet Dev 7:182, 1997
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 182
    • Tsukiyama, T.1    Wu, C.2
  • 10
    • 0029785841 scopus 로고    scopus 로고
    • Moderate increase in histone acetylation activates the mouse mammary tumor virus promoter and remodels its nucleosome structure
    • Bartsch J, Truss M, Bode J, Beato M: Moderate increase in histone acetylation activates the mouse mammary tumor virus promoter and remodels its nucleosome structure. Proc Natl Acad Sci USA 93:10741, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10741
    • Bartsch, J.1    Truss, M.2    Bode, J.3    Beato, M.4
  • 11
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M: Histone acetylation in chromatin structure and transcription. Nature 389:349, 1997
    • (1997) Nature , vol.389 , pp. 349
    • Grunstein, M.1
  • 12
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes TR, Thorne AW, Crane-Robinson C: A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J 7:1395, 1988
    • (1988) EMBO J , vol.7 , pp. 1395
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 13
    • 0031876314 scopus 로고    scopus 로고
    • Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III
    • Tse C, Sera T, Wolffe AP, Hansen JC: Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III. Mol Cell Biol 18:4629, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 4629
    • Tse, C.1    Sera, T.2    Wolffe, A.P.3    Hansen, J.C.4
  • 14
    • 0029985730 scopus 로고    scopus 로고
    • Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro
    • Vettese-Dadey M, Grant PA, Hebbes TR, Crane-Robinson C, Allis CD, Workman JL: Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J 15:2508, 1996
    • (1996) EMBO J , vol.15 , pp. 2508
    • Vettese-Dadey, M.1    Grant, P.A.2    Hebbes, T.R.3    Crane-Robinson, C.4    Allis, C.D.5    Workman, J.L.6
  • 15
    • 7344238492 scopus 로고    scopus 로고
    • Histone acetylation is required to maintain the unfolded nucleosome structure associated with transcribing DNA
    • Walia H, Chen HY, Sun JM, Holth LT, Davie JR: Histone acetylation is required to maintain the unfolded nucleosome structure associated with transcribing DNA. J Biol Chem 273:14516, 1998
    • (1998) J Biol Chem , vol.273 , pp. 14516
    • Walia, H.1    Chen, H.Y.2    Sun, J.M.3    Holth, L.T.4    Davie, J.R.5
  • 16
    • 0030998534 scopus 로고    scopus 로고
    • Histone acetylation: Influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression
    • Ura K, Kurumizaka H, Dimitrov S, Almouzni G, Wolffe AP: Histone acetylation: Influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression. EMBO J 16:2096, 1997
    • (1997) EMBO J , vol.16 , pp. 2096
    • Ura, K.1    Kurumizaka, H.2    Dimitrov, S.3    Almouzni, G.4    Wolffe, A.P.5
  • 17
    • 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, Laherty CD, Turner BM, Eisenman RN, Bird A: Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393: 386, 1998
    • (1998) Nature , vol.393 , pp. 386
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 18
    • 17544363212 scopus 로고    scopus 로고
    • High mobility group protein 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA
    • Tremethick DJ, Hyman L: High mobility group protein 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA. J Biol Chem 271: 12009, 1996
    • (1996) J Biol Chem , vol.271 , pp. 12009
    • Tremethick, D.J.1    Hyman, L.2
  • 19
    • 0031565914 scopus 로고    scopus 로고
    • Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin
    • Postnikov YV, Herrera JE, Hock R, Scheer U, Bustin M: Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin. J Mol Biol 274:454, 1997
    • (1997) J Mol Biol , vol.274 , pp. 454
    • Postnikov, Y.V.1    Herrera, J.E.2    Hock, R.3    Scheer, U.4    Bustin, M.5
  • 22
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R: The steroid and thyroid hormone receptor superfamily. Nature 240:889, 1988
    • (1988) Nature , vol.240 , pp. 889
    • Evans, R.1
  • 24
    • 0025812291 scopus 로고
    • Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors
    • Umesono K, Murakami KK, Thompson CC, Evans RM: Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell 65:1255, 1991
    • (1991) Cell , vol.65 , pp. 1255
    • Umesono, K.1    Murakami, K.K.2    Thompson, C.C.3    Evans, R.M.4
  • 25
    • 0030061554 scopus 로고    scopus 로고
    • AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis
    • Okuda T, van Deursen J, Hiebert SW, Grosveld G, Downing JR: AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis. Cell 84:321, 1996
    • (1996) Cell , vol.84 , pp. 321
    • Okuda, T.1    Van Deursen, J.2    Hiebert, S.W.3    Grosveld, G.4    Downing, J.R.5
  • 26
    • 0025797334 scopus 로고
    • Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor
    • Yang N, Schule R, Mangelsdorf DJ, Evans RM: Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor. Proc Natl Acad Sci USA 9:3559, 1991
    • (1991) Proc Natl Acad Sci USA , vol.9 , pp. 3559
    • Yang, N.1    Schule, R.2    Mangelsdorf, D.J.3    Evans, R.M.4
  • 29
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM: A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454, 1995
    • (1995) Nature , vol.377 , pp. 454
    • Chen, J.D.1    Evans, R.M.2
  • 30
    • 0029794881 scopus 로고    scopus 로고
    • SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers
    • Chen JD, Umesono K, Evans RM: SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers. Proc Natl Acad Sci USA 93:7567, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7567
    • Chen, J.D.1    Umesono, K.2    Evans, R.M.3
  • 32
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate Mad transcriptional repression
    • Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN: Histone deacetylases associated with the mSin3 corepressor mediate Mad transcriptional repression. Cell 89:349, 1997
    • (1997) Cell , vol.89 , pp. 349
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 35
    • 0028905563 scopus 로고
    • Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
    • Ayer DE, Lawrence QA, Eisenman RN: Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80:767, 1995
    • (1995) Cell , vol.80 , pp. 767
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 36
    • 0029737603 scopus 로고    scopus 로고
    • Sin3 corepressor function in Myc-induced transcription and transformation
    • Harper SE, Qiu Y, Sharp PA: Sin3 corepressor function in Myc-induced transcription and transformation. Proc Natl Acad Sci USA 93:8536, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8536
    • Harper, S.E.1    Qiu, Y.2    Sharp, P.A.3
  • 37
    • 0032169858 scopus 로고    scopus 로고
    • ETO, fusion partner in t(8-21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex
    • Wang JX, Hoshino T, Redner RL, Kajigaya S, Liu JM: ETO, fusion partner in t(8-21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex. Proc Natl Acad Sci USA 95:10860, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10860
    • Wang, J.X.1    Hoshino, T.2    Redner, R.L.3    Kajigaya, S.4    Liu, J.M.5
  • 38
    • 0031723957 scopus 로고    scopus 로고
    • Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO
    • Gelmetti V, Zhang JS, Fanelli M, Minucci S, Pelicci PG, Lazar MA: Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO. Mol Cell Biol 18:7185, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 7185
    • Gelmetti, V.1    Zhang, J.S.2    Fanelli, M.3    Minucci, S.4    Pelicci, P.G.5    Lazar, M.A.6
  • 40
    • 0029814796 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in the human retinoic acid receptor detected using monoclonal antibodies
    • Driscoll JE, Seachord CL, Lupisella JA, Darveau RP, Reczek PR: Ligand-induced conformational changes in the human retinoic acid receptor detected using monoclonal antibodies. J Biol Chem 271:22969, 1996
    • (1996) J Biol Chem , vol.271 , pp. 22969
    • Driscoll, J.E.1    Seachord, C.L.2    Lupisella, J.A.3    Darveau, R.P.4    Reczek, P.R.5
  • 41
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG: A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733, 1997
    • (1997) Nature , vol.387 , pp. 733
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 42
    • 0030771328 scopus 로고    scopus 로고
    • A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release
    • Lin BC, Hong SH, Krig S, Yoh SM, Privalsky ML: A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release. Mol Cell Biol 7:6131, 1997
    • (1997) Mol Cell Biol , vol.7 , pp. 6131
    • Lin, B.C.1    Hong, S.H.2    Krig, S.3    Yoh, S.M.4    Privalsky, M.L.5
  • 46
    • 0029921517 scopus 로고    scopus 로고
    • Interaction of steroid hormone receptors with transcription factors involves chromatin remodelling
    • Beato M, Candau R, Chavez S, Mows C, Truss M: Interaction of steroid hormone receptors with transcription factors involves chromatin remodelling. J Steroid Biochem Mol Biol 56:47, 1996
    • (1996) J Steroid Biochem Mol Biol , vol.56 , pp. 47
    • Beato, M.1    Candau, R.2    Chavez, S.3    Mows, C.4    Truss, M.5
  • 48
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2
    • Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci USA 94:8479, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8479
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 49
    • 0032080173 scopus 로고    scopus 로고
    • A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia
    • Carapeti M, Aguiar RC, Goldman JM, Cross NC: A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. Blood 91:3127, 1998
    • (1998) Blood , vol.91 , pp. 3127
    • Carapeti, M.1    Aguiar, R.C.2    Goldman, J.M.3    Cross, N.C.4
  • 50
    • 0029854180 scopus 로고    scopus 로고
    • p300 and CBP as transcriptional regulators and targets of oncogenic events
    • Eckner R: p300 and CBP as transcriptional regulators and targets of oncogenic events. Biol Chem 377:685, 1996
    • (1996) Biol Chem , vol.377 , pp. 685
    • Eckner, R.1
  • 52
    • 0032076229 scopus 로고    scopus 로고
    • Conjunction dysfunction-CBP/p300 in human disease
    • Giles RH, Peters D, Breuning MH: Conjunction dysfunction-CBP/p300 in human disease. Trends Genet 14:178, 1998
    • (1998) Trends Genet , vol.14 , pp. 178
    • Giles, R.H.1    Peters, D.2    Breuning, M.H.3
  • 55
    • 0025945632 scopus 로고
    • DNA methylation and gene expression
    • Razin A, Cedar H: DNA methylation and gene expression. Microbiol Rev 55:451, 1991
    • (1991) Microbiol Rev , vol.55 , pp. 451
    • Razin, A.1    Cedar, H.2
  • 56
    • 0031588962 scopus 로고    scopus 로고
    • CpG methylation remodels chromatin structure in vitro
    • Davey C, Pennings S, Allan J: CpG methylation remodels chromatin structure in vitro. J Mol Biol 267:276, 1997
    • (1997) J Mol Biol , vol.267 , pp. 276
    • Davey, C.1    Pennings, S.2    Allan, J.3
  • 57
    • 0342437491 scopus 로고    scopus 로고
    • MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin
    • Nan X, Campoy FJ, Bird A: MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin. Cell 88:471, 1997
    • (1997) Cell , vol.88 , pp. 471
    • Nan, X.1    Campoy, F.J.2    Bird, A.3
  • 58
    • 0022032204 scopus 로고
    • Altering gene expression with 5-azacytidine
    • Jones PA: Altering gene expression with 5-azacytidine. Cell 40:485, 1985
    • (1985) Cell , vol.40 , pp. 485
    • Jones, P.A.1
  • 59
    • 0030842478 scopus 로고    scopus 로고
    • The yeast SW1-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo
    • Burns LG, Peterson CL: The yeast SW1-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo. Mol Cell Biol 17:4811, 1997
    • (1997) Mol Cell Biol , vol.17 , pp. 4811
    • Burns, L.G.1    Peterson, C.L.2
  • 60
    • 0032574802 scopus 로고    scopus 로고
    • Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding
    • Cote J, Peterson CL, Workman JL: Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding. Proc Natl Acad Sci USA 95:4947, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4947
    • Cote, J.1    Peterson, C.L.2    Workman, J.L.3
  • 61
    • 0030782468 scopus 로고    scopus 로고
    • Catalytic activity of the yeast SWI/SNF complex on reconstituted nucleosome arrays
    • Logic C, Peterson CL: Catalytic activity of the yeast SWI/SNF complex on reconstituted nucleosome arrays. EMBO J 16:6772, 1997
    • (1997) EMBO J , vol.16 , pp. 6772
    • Logic, C.1    Peterson, C.L.2
  • 62
    • 0032504102 scopus 로고    scopus 로고
    • Human SWI/SNF interconverts a nucleosome between its base state and a stable remodeled state
    • Schnitzler G, Sif S, Kingston RE: Human SWI/SNF interconverts a nucleosome between its base state and a stable remodeled state. Cell 94:17, 1998
    • (1998) Cell , vol.94 , pp. 17
    • Schnitzler, G.1    Sif, S.2    Kingston, R.E.3
  • 63
    • 0031947549 scopus 로고    scopus 로고
    • SWI-SNF complex participation in transcriptional activation at a step subsequent to activator binding
    • Ryan MP, Jones R, Morse RH: SWI-SNF complex participation in transcriptional activation at a step subsequent to activator binding. Mol Cell Biol 18:1774, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 1774
    • Ryan, M.P.1    Jones, R.2    Morse, R.H.3
  • 64
    • 0031306557 scopus 로고    scopus 로고
    • Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin
    • Mizuguchi G, Tsukiyama T, Wisniewski J, Wu C: Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin. Mol Cell 1:141, 1997
    • (1997) Mol Cell , vol.1 , pp. 141
    • Mizuguchi, G.1    Tsukiyama, T.2    Wisniewski, J.3    Wu, C.4
  • 66
    • 0032504059 scopus 로고    scopus 로고
    • Activated RSC-nucleosome complex and persistently altered form of the nucleosome
    • Lorch Y, Cairns BR, Zhang M, Kornberg RD: Activated RSC-nucleosome complex and persistently altered form of the nucleosome. Cell 94:29, 1998
    • (1998) Cell , vol.94 , pp. 29
    • Lorch, Y.1    Cairns, B.R.2    Zhang, M.3    Kornberg, R.D.4
  • 67
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • Ito T, Bulger M, Pazin MJ, Kobayashi R, Kadonaga JT: ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90:145, 1997
    • (1997) Cell , vol.90 , pp. 145
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 68
    • 0030835671 scopus 로고    scopus 로고
    • Molecular analysis of the SNF2/SWI2 protein family member Mot1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA
    • Auble DT, Wang DY, Post KW, Hahn S: Molecular analysis of the SNF2/SWI2 protein family member Mot1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA. Mol Cell Biol 17:4842, 1997
    • (1997) Mol Cell Biol , vol.17 , pp. 4842
    • Auble, D.T.1    Wang, D.Y.2    Post, K.W.3    Hahn, S.4
  • 75
    • 0027297095 scopus 로고
    • A dominant negative retinoic acid receptor blocks neutrophil differentiation at the promyelocyte stage
    • Tsai S, Collins SJ: A dominant negative retinoic acid receptor blocks neutrophil differentiation at the promyelocyte stage. Proc Natl Acad Sci USA 90:7153, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7153
    • Tsai, S.1    Collins, S.J.2
  • 76
    • 0027078742 scopus 로고
    • A mutated retinoic acid receptor-alpha exhibiting dominant-negative activity alters the lineage evelopment of a multipotent hematopoietic cell line
    • Tsai S, Bartelmez S, Heyman R, Damm K, Evans R, Collins S: A mutated retinoic acid receptor-alpha exhibiting dominant-negative activity alters the lineage evelopment of a multipotent hematopoietic cell line. Genes Dev 6:2258, 1992
    • (1992) Genes Dev , vol.6 , pp. 2258
    • Tsai, S.1    Bartelmez, S.2    Heyman, R.3    Damm, K.4    Evans, R.5    Collins, S.6
  • 77
    • 0025089467 scopus 로고
    • Molecular analysis of acute promyelocytic leukemia breakpoint cluster region on chromosome 17
    • Borrow J, Goddard AD, Sheer D, Solomon E: Molecular analysis of acute promyelocytic leukemia breakpoint cluster region on chromosome 17. Science 249:1577, 1990
    • (1990) Science , vol.249 , pp. 1577
    • Borrow, J.1    Goddard, A.D.2    Sheer, D.3    Solomon, E.4
  • 78
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • Kakizuka A, Miller WJ, Umesono K, Warrell RJ, Frankel SR, Murty VV, Dmitrovsky E, Evans RM: Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 66:663, 1991
    • (1991) Cell , vol.66 , pp. 663
    • Kakizuka, A.1    Miller, W.J.2    Umesono, K.3    Warrell, R.J.4    Frankel, S.R.5    Murty, V.V.6    Dmitrovsky, E.7    Evans, R.M.8
  • 79
    • 0025043959 scopus 로고
    • The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor alpha gene to a novel transcribed locus
    • de The H, Chomienne C, Lanotte M, Degos L, Dejean A: The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor alpha gene to a novel transcribed locus. Nature 347:558, 1990
    • (1990) Nature , vol.347 , pp. 558
    • De The, H.1    Chomienne, C.2    Lanotte, M.3    Degos, L.4    Dejean, A.5
  • 80
    • 0027411688 scopus 로고
    • Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia
    • Chen Z, Brand NJ, Chen A, Chen SJ, Tong JH, Wang ZY, Waxman S, Zelent A: Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia. EMBO J 12:1161, 1993
    • (1993) EMBO J , vol.12 , pp. 1161
    • Chen, Z.1    Brand, N.J.2    Chen, A.3    Chen, S.J.4    Tong, J.H.5    Wang, Z.Y.6    Waxman, S.7    Zelent, A.8
  • 81
    • 0030022316 scopus 로고    scopus 로고
    • The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion
    • Redner RL, Rush EA, Faas S, Rudert WA, Corey SJ: The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion. Blood 87:882, 1996
    • (1996) Blood , vol.87 , pp. 882
    • Redner, R.L.1    Rush, E.A.2    Faas, S.3    Rudert, W.A.4    Corey, S.J.5
  • 82
    • 0029924195 scopus 로고    scopus 로고
    • A new variant translocation in acute promyelocytic leukaemia: Molecular characterization and clinical correlation
    • Wells RA, Hummel JL, De Koven A, Zipursky A, Kirby M, Dube I, Kamel-Reid S: A new variant translocation in acute promyelocytic leukaemia: Molecular characterization and clinical correlation. Leukemia 10:735, 1996
    • (1996) Leukemia , vol.10 , pp. 735
    • Wells, R.A.1    Hummel, J.L.2    De Koven, A.3    Zipursky, A.4    Kirby, M.5    Dube, I.6    Kamel-Reid, S.7
  • 84
    • 0030063530 scopus 로고    scopus 로고
    • Reduced and altered DNA-binding and transcriptional properties of the PLZF-retinoic acid receptor-α chimera generated in t(11;17)-associated acute promyelocytic leukemia
    • Licht JD, Shaknovitch R, English MA, Melnick A, Li J-Y, Reddy JC, Dong S, Chen S-J, Zelent A, Waxman S: Reduced and altered DNA-binding and transcriptional properties of the PLZF-retinoic acid receptor-α chimera generated in t(11;17)-associated acute promyelocytic leukemia. Oncogene 12:323, 1996
    • (1996) Oncogene , vol.12 , pp. 323
    • Licht, J.D.1    Shaknovitch, R.2    English, M.A.3    Melnick, A.4    Li, J.-Y.5    Reddy, J.C.6    Dong, S.7    Chen, S.-J.8    Zelent, A.9    Waxman, S.10
  • 85
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The H, Lavau C, Marchio A, Chomienne C, Degos L, Dejean A: The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66:675, 1991
    • (1991) Cell , vol.66 , pp. 675
    • De The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 87
    • 0032522962 scopus 로고    scopus 로고
    • Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML-and PLZF-RAR-alpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia
    • Guidez F, Ivins S, Zhu J, Soderstrom M, Waxman S, Zelent A: Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML-and PLZF-RAR-alpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia. Blood 91:2634, 1998
    • (1998) Blood , vol.91 , pp. 2634
    • Guidez, F.1    Ivins, S.2    Zhu, J.3    Soderstrom, M.4    Waxman, S.5    Zelent, A.6
  • 88
    • 0031941912 scopus 로고    scopus 로고
    • Distinct interactions of PML-RAR-alpha and PLZF-RAR-alpha with co-repressors determine differential responses to RA in APL
    • He LZ, Guidez F, Tribioli C, Peruzzi D, Ruthardt M, Zelent A, Pandolfi PP: Distinct interactions of PML-RAR-alpha and PLZF-RAR-alpha with co-repressors determine differential responses to RA in APL. Nat Genet 18:126, 1998
    • (1998) Nat Genet , vol.18 , pp. 126
    • He, L.Z.1    Guidez, F.2    Tribioli, C.3    Peruzzi, D.4    Ruthardt, M.5    Zelent, A.6    Pandolfi, P.P.7
  • 89
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin RJ, Nagy L, Inoue S, Shao WL, Miller WH, Evans RM: Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391:811, 1998
    • (1998) Nature , vol.391 , pp. 811
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.L.4    Miller, W.H.5    Evans, R.M.6
  • 90
    • 0030739980 scopus 로고    scopus 로고
    • Differentiation of t(5;17) variant acute promyelocytic leukemic blasts by all-trans retinoic acid
    • Redner RL, Corey SJ, Rush EA: Differentiation of t(5;17) variant acute promyelocytic leukemic blasts by all-trans retinoic acid. Leukemia 11:1014, 1997
    • (1997) Leukemia , vol.11 , pp. 1014
    • Redner, R.L.1    Corey, S.J.2    Rush, E.A.3
  • 92
    • 0030828003 scopus 로고    scopus 로고
    • Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein
    • Li X, Lopez-Guisa JM, Ninan N, Weiner EJ, Rauscher F3, Marmorstein R: Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein. J Biol Chem 272:27324, 1997
    • (1997) J Biol Chem , vol.272 , pp. 27324
    • Li, X.1    Lopez-Guisa, J.M.2    Ninan, N.3    Weiner, E.J.4    Rauscher F. III5    Marmorstein, R.6
  • 93
    • 0030847164 scopus 로고    scopus 로고
    • SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia
    • Hong SH, David G, Wong CW, Dejean A, Privalsky ML: SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia. Proc Natl Acad Sci USA 94:9028, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9028
    • Hong, S.H.1    David, G.2    Wong, C.W.3    Dejean, A.4    Privalsky, M.L.5
  • 94
    • 0032516221 scopus 로고    scopus 로고
    • Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein
    • David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A: Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein. Oncogene 16:2549, 1998
    • (1998) Oncogene , vol.16 , pp. 2549
    • David, G.1    Alland, L.2    Hong, S.H.3    Wong, C.W.4    DePinho, R.A.5    Dejean, A.6
  • 100
    • 0027383818 scopus 로고
    • Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: The runt homology domain is required for DNA binding and protein-protein interactions
    • Meyers S, Downing JR, Hiebert SW: Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: The runt homology domain is required for DNA binding and protein-protein interactions. Mol Cell Biol 13:6336, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 6336
    • Meyers, S.1    Downing, J.R.2    Hiebert, S.W.3
  • 101
    • 0032101379 scopus 로고    scopus 로고
    • Interaction and functional cooperation of the leukemia-associated factors AML1 and p300 in myeloid cell differentiation
    • Kitabayashi I, Yokoyama A, Shimizu K, Ohki M: Interaction and functional cooperation of the leukemia-associated factors AML1 and p300 in myeloid cell differentiation. EMBO J 17:2994, 1998
    • (1998) EMBO J , vol.17 , pp. 2994
    • Kitabayashi, I.1    Yokoyama, A.2    Shimizu, K.3    Ohki, M.4
  • 102
    • 0029616633 scopus 로고
    • The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B
    • Frank R, Zhang J, Uchida H, Meyers S, Hiebert SW, Nimer SD: The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B. Oncogene 11:2667, 1995
    • (1995) Oncogene , vol.11 , pp. 2667
    • Frank, R.1    Zhang, J.2    Uchida, H.3    Meyers, S.4    Hiebert, S.W.5    Nimer, S.D.6
  • 104
    • 0028786125 scopus 로고
    • Functional domains of the t(8;21) fusion protein, AML-1/ETO
    • Lenny N, Meyers S, Hiebert SW: Functional domains of the t(8;21) fusion protein, AML-1/ETO. Oncogene 11:1761, 1995
    • (1995) Oncogene , vol.11 , pp. 1761
    • Lenny, N.1    Meyers, S.2    Hiebert, S.W.3
  • 106
    • 0030787009 scopus 로고    scopus 로고
    • Transformation properties of the ETO gene, fusion partner in t(8;21) leukemias
    • Wang J, Wang M, Liu JM: Transformation properties of the ETO gene, fusion partner in t(8;21) leukemias. Cancer Res 57:2951, 1997
    • (1997) Cancer Res , vol.57 , pp. 2951
    • Wang, J.1    Wang, M.2    Liu, J.M.3
  • 107
    • 0029704584 scopus 로고    scopus 로고
    • MLL fusion genes in the 11q23 acute leukemias
    • Downing JR, Look AT: MLL fusion genes in the 11q23 acute leukemias. Cancer Treat Res 84:73, 1996
    • (1996) Cancer Treat Res , vol.84 , pp. 73
    • Downing, J.R.1    Look, A.T.2
  • 108
    • 0031958621 scopus 로고    scopus 로고
    • ALL1 gene alterations in acute leukemia: Biological and clinical aspects
    • Cimino G, Rapanotti MC, Sprovieri T, Elia L: ALL1 gene alterations in acute leukemia: Biological and clinical aspects. Haematologica 83:350, 1998
    • (1998) Haematologica , vol.83 , pp. 350
    • Cimino, G.1    Rapanotti, M.C.2    Sprovieri, T.3    Elia, L.4
  • 112
    • 0026936328 scopus 로고
    • A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias
    • Djabali M, Selleri L, Parry P, Bower M, Young BD, Evans GA: A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat Genet 2:113, 1992
    • (1992) Nat Genet , vol.2 , pp. 113
    • Djabali, M.1    Selleri, L.2    Parry, P.3    Bower, M.4    Young, B.D.5    Evans, G.A.6
  • 115
    • 0026454451 scopus 로고
    • Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias
    • Tkachuk DC, Kohler S, Cleary ML: Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell 71:691, 1992
    • (1992) Cell , vol.71 , pp. 691
    • Tkachuk, D.C.1    Kohler, S.2    Cleary, M.L.3
  • 116
    • 0026075637 scopus 로고
    • Molecular characterization of the trithorax gene, a positive regulator of homeotic gene expression in Drosophila
    • Breen TR, Harte PJ: Molecular characterization of the trithorax gene, a positive regulator of homeotic gene expression in Drosophila. Mech Dev 35:113, 1991
    • (1991) Mech Dev , vol.35 , pp. 113
    • Breen, T.R.1    Harte, P.J.2
  • 117
    • 0027536183 scopus 로고
    • Trithorax regulates multiple homeotic genes in the bithorax and Antennapedia complexes and exerts different tissue-specific, parasegment-specific and promoter-specific effects on each
    • Breen TR, Harte PJ: Trithorax regulates multiple homeotic genes in the bithorax and Antennapedia complexes and exerts different tissue-specific, parasegment-specific and promoter-specific effects on each. Development 117:119, 1993
    • (1993) Development , vol.117 , pp. 119
    • Breen, T.R.1    Harte, P.J.2
  • 118
    • 0025247728 scopus 로고
    • The trithorax gene, a trans-acting regulator of the bithorax complex in Drosophila, encodes a protein with zinc-binding domains
    • Mazo AM, Huang DH, Mozer BA, Dawid IB: The trithorax gene, a trans-acting regulator of the bithorax complex in Drosophila, encodes a protein with zinc-binding domains. Proc Natl Acad Sci USA 87:2112, 1990
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2112
    • Mazo, A.M.1    Huang, D.H.2    Mozer, B.A.3    Dawid, I.B.4
  • 119
    • 0032169352 scopus 로고    scopus 로고
    • Binding of trithorax and polycomb proteins to the bithorax complex - Dynamic changes during early drosophila embryogenesis
    • Orlando V, Jane EP, Chinwalla V, Harte PJ, Paro R: Binding of trithorax and polycomb proteins to the bithorax complex - Dynamic changes during early drosophila embryogenesis. EMBO J 17:5141, 1998
    • (1998) EMBO J , vol.17 , pp. 5141
    • Orlando, V.1    Jane, E.P.2    Chinwalla, V.3    Harte, P.J.4    Paro, R.5
  • 120
    • 0032168459 scopus 로고    scopus 로고
    • MLL, a mammalian trithorax-group gene, functions as a transcriptional maintenance factor in morphogenesis
    • Yu BD, Hanson RD, Hess JL, Horning SE, Korsmeyer SJ: MLL, a mammalian trithorax-group gene, functions as a transcriptional maintenance factor in morphogenesis. Proc Natl Acad Sci USA 95:10632, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10632
    • Yu, B.D.1    Hanson, R.D.2    Hess, J.L.3    Horning, S.E.4    Korsmeyer, S.J.5
  • 122
    • 0028091804 scopus 로고
    • 11q23 translocations split the "AT-hook" cruciform DNA-binding region and the transcriptional repression domain from the activation domain of the mixed-lineage leukemia (MLL) gene
    • Zeleznik-Le NJ, Harden AM, Rowley JD: 11q23 translocations split the "AT-hook" cruciform DNA-binding region and the transcriptional repression domain from the activation domain of the mixed-lineage leukemia (MLL) gene. Proc Natl Acad Sci USA 91:10610, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10610
    • Zeleznik-Le, N.J.1    Harden, A.M.2    Rowley, J.D.3
  • 124
    • 0029665594 scopus 로고    scopus 로고
    • TFG/TAF30/ANC1, a component of the yeast SWI/SNF complex that is similar to the leukemogenic proteins ENL and AF-9
    • Cairns BR, Henry NL, Kornberg RD: TFG/TAF30/ANC1, a component of the yeast SWI/SNF complex that is similar to the leukemogenic proteins ENL and AF-9. Mol Cell Biol 16:3308, 1996
    • (1996) Mol Cell Biol , vol.16 , pp. 3308
    • Cairns, B.R.1    Henry, N.L.2    Kornberg, R.D.3
  • 127
    • 0030967030 scopus 로고    scopus 로고
    • The t(11;16)(q23;p13) translocation in myelodysplastic syndrome fuses the MLL gene to the CBP gene
    • Taki T, Sako M, Tsuchida M, Hayashi Y: The t(11;16)(q23;p13) translocation in myelodysplastic syndrome fuses the MLL gene to the CBP gene. Blood 89:3945, 1997
    • (1997) Blood , vol.89 , pp. 3945
    • Taki, T.1    Sako, M.2    Tsuchida, M.3    Hayashi, Y.4
  • 128
    • 0031439397 scopus 로고    scopus 로고
    • Adenoviral E1A-associated protein p300 is involved in acute myeloid leukemia with t(11;22)(q23;q13)
    • Ida K, Kitabayashi I, Taki T, Taniwaki M, Noro K, Yamamoto M, Ohki M, Hayashi Y: Adenoviral E1A-associated protein p300 is involved in acute myeloid leukemia with t(11;22)(q23;q13). Blood 90:4699,1997
    • (1997) Blood , vol.90 , pp. 4699
    • Ida, K.1    Kitabayashi, I.2    Taki, T.3    Taniwaki, M.4    Noro, K.5    Yamamoto, M.6    Ohki, M.7    Hayashi, Y.8
  • 130
    • 0017886958 scopus 로고
    • Sodium butyrate inhibits histone deacetylation in cultured cells
    • Candido EP, Reeves R, Davie JR: Sodium butyrate inhibits histone deacetylation in cultured cells. Cell 14:105, 1978
    • (1978) Cell , vol.14 , pp. 105
    • Candido, E.P.1    Reeves, R.2    Davie, J.R.3
  • 131
    • 0017898940 scopus 로고
    • Suppression of histone deacetylation in vivo and in vitro by sodium butyrate
    • Boffa LC, Vidali G, Mann RS, Allfrey VG: Suppression of histone deacetylation in vivo and in vitro by sodium butyrate. J Biol Chem 253:3364, 1978
    • (1978) J Biol Chem , vol.253 , pp. 3364
    • Boffa, L.C.1    Vidali, G.2    Mann, R.S.3    Allfrey, V.G.4
  • 132
    • 0017867123 scopus 로고
    • Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences
    • Vidali G, Boffa LC, Bradbury EM, Allfrey VG: Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences. Proc Natl Acad Sci USA 75:2239, 1978
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 2239
    • Vidali, G.1    Boffa, L.C.2    Bradbury, E.M.3    Allfrey, V.G.4
  • 133
    • 0026542876 scopus 로고
    • Anaerobic degradation of trans-cinnamate and omega-phenylalkane carboxylic acids by the photosynthetic bacterium rhodopseudomonas palustris: Evidence for a beta-oxidation mechanism
    • Elder DJ, Morgan P, Kelly DJ: Anaerobic degradation of trans-cinnamate and omega-phenylalkane carboxylic acids by the photosynthetic bacterium Rhodopseudomonas palustris: Evidence for a beta-oxidation mechanism. Arch Microbiol 157:148, 1992
    • (1992) Arch Microbiol , vol.157 , pp. 148
    • Elder, D.J.1    Morgan, P.2    Kelly, D.J.3
  • 135
    • 0023689244 scopus 로고
    • Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by trichostatin A
    • Yoshida M, Beppu T: Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by trichostatin A. Exp Cell Res 177:122, 1988
    • (1988) Exp Cell Res , vol.177 , pp. 122
    • Yoshida, M.1    Beppu, T.2
  • 136
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, Beppu T: Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 265:17174, 1990
    • (1990) J Biol Chem , vol.265 , pp. 17174
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 138
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima M, Yoshida M, Sugita K, Horinouchi S, Beppu T: Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase. J Biol Chem 268:22429, 1993
    • (1993) J Biol Chem , vol.268 , pp. 22429
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 139
    • 0029294663 scopus 로고
    • Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
    • Yoshida M, Horinouchi S, Beppu T: Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 17:423, 1995
    • (1995) Bioessays , vol.17 , pp. 423
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 142
    • 0029460568 scopus 로고
    • Butyrate and phenylacetate as differentiating agents: Practical problems and opportunities
    • Newmark HL, Young CW: Butyrate and phenylacetate as differentiating agents: practical problems and opportunities. J Cell Biochem 22:247, 1995 (suppl 1)
    • (1995) J Cell Biochem , vol.22 , Issue.SUPPL. 1 , pp. 247
    • Newmark, H.L.1    Young, C.W.2
  • 143
    • 0023195737 scopus 로고
    • Effects of trichostatins on differentiation of marine erythroleukemia cells
    • Yoshida M, Nomura S, Beppu T: Effects of trichostatins on differentiation of marine erythroleukemia cells. Cancer Res 47:3688, 1987
    • (1987) Cancer Res , vol.47 , pp. 3688
    • Yoshida, M.1    Nomura, S.2    Beppu, T.3
  • 144
    • 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 Exp 5:245, 1996
    • (1996) Gene Exp , vol.5 , pp. 245
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 146
    • 0032529284 scopus 로고    scopus 로고
    • Leukemic cellular retinoic acid resistance and missense mutations in the PML-RARα fusion gene after relapse of acute promyelocytic leukemia from treatment with all-trans retinoic acid and intensive chemotherapy
    • Ding W, Li YP, Nobile LM, Grills G, Carrera I, Paietta E, Tallman M, Wiernik PH, Gallagher RE: Leukemic cellular retinoic acid resistance and missense mutations in the PML-RARα fusion gene after relapse of acute promyelocytic leukemia from treatment with all-trans retinoic acid and intensive chemotherapy. Blood 92:1172, 1998
    • (1998) Blood , vol.92 , pp. 1172
    • Ding, W.1    Li, Y.P.2    Nobile, L.M.3    Grills, G.4    Carrera, I.5    Paietta, E.6    Tallman, M.7    Wiernik, P.H.8    Gallagher, R.E.9
  • 147
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell RP, He LZ, Richon V, Calleja E, Pandolfi PP: Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J Nat Cancer Inst 90:1621, 1998
    • (1998) J Nat Cancer Inst , vol.90 , pp. 1621
    • Warrell, R.P.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 148
    • 0033564130 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase relieve ETO-mediated repression and induce differentiation of AML1-ETO leukemia cells
    • in press
    • Wang JX, Saunthararajah Y, Redner RL, Liv JM: Inhibitors of histone deacetylase relieve ETO-mediated repression and induce differentiation of AML1-ETO leukemia cells. Cancer Res (in press)
    • Cancer Res
    • Wang, J.X.1    Saunthararajah, Y.2    Redner, R.L.3    Liv, J.M.4
  • 149
    • 0020693603 scopus 로고
    • Effect of polar organic compounds on leukemic cells. Butyrate-induced partial remission of acute myelogenous leukemia in a child
    • Novogrodsky A, Dvir A, Ravid A, Shkolnik T, Stenzel KH, Rubin AL, Zaizov R: Effect of polar organic compounds on leukemic cells. Butyrate-induced partial remission of acute myelogenous leukemia in a child. Cancer 51:9, 1983
    • (1983) Cancer , vol.51 , pp. 9
    • Novogrodsky, A.1    Dvir, A.2    Ravid, A.3    Shkolnik, T.4    Stenzel, K.H.5    Rubin, A.L.6    Zaizov, R.7
  • 150
    • 26544450266 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylase upregulates B7 molecules in acute myelogenous leukemia
    • abstr
    • Mizuno S, Tokunaga Y, Maeda M, Inaba S, Miyamoto T, Akashi K, Godno H, Niho Y: Inhibitor of histone deacetylase upregulates B7 molecules in acute myelogenous leukemia. Blood 92:616a, 1998 (abstr, suppl 1)
    • (1998) Blood , vol.92 , Issue.SUPPL. 1
    • Mizuno, S.1    Tokunaga, Y.2    Maeda, M.3    Inaba, S.4    Miyamoto, T.5    Akashi, K.6    Godno, H.7    Niho, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.