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Volumn 91, Issue 15, 1999, Pages 1288-1294

Chromatin remodeling and transcriptional regulation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE;

EID: 0033523203     PISSN: 00278874     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnci/91.15.1288     Document Type: Review
Times cited : (118)

References (67)
  • 1
    • 0028239906 scopus 로고
    • Role of chromatin structure in the regulation of transcription by RNA polymerase II
    • Paranjape SM, Kamakaka RT, Kadonaga JT. Role of chromatin structure in the regulation of transcription by RNA polymerase II. Annu Rev Biochem 1994;63:265-97.
    • (1994) Annu Rev Biochem , vol.63 , pp. 265-297
    • Paranjape, S.M.1    Kamakaka, R.T.2    Kadonaga, J.T.3
  • 2
    • 0032055037 scopus 로고    scopus 로고
    • Covalent modifications of histones: Expression from chromatin templates
    • Davie JR. Covalent modifications of histones: expression from chromatin templates. Curr Opin Genet Dev 1998;8:173-8.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 173-178
    • Davie, J.R.1
  • 3
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey V, Faulkner RM, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci U S A 1966;51:786-4.
    • (1966) Proc Natl Acad Sci U S A , vol.51 , pp. 786-794
    • Allfrey, V.1    Faulkner, R.M.2    Mirsky, A.E.3
  • 4
    • 0013900616 scopus 로고
    • RNA synthesis and histone acetylation during the course of gene activation in lymphocytes
    • Pogo BG, Allfrey VG, Mirsky AE. RNA synthesis and histone acetylation during the course of gene activation in lymphocytes. Proc Natl Acad Sci U S A 1966;55:805-12.
    • (1966) Proc Natl Acad Sci U S A , vol.55 , pp. 805-812
    • Pogo, B.G.1    Allfrey, V.G.2    Mirsky, A.E.3
  • 5
    • 0017815160 scopus 로고
    • DNA associated with hyperacetylated histone is preferentially digested by DNase I
    • Sealy L, Chalkley R. DNA associated with hyperacetylated histone is preferentially digested by DNase I. Nucleic Acids Res 1978;5:1863-76.
    • (1978) Nucleic Acids Res , vol.5 , pp. 1863-1876
    • Sealy, L.1    Chalkley, R.2
  • 7
    • 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 1988; 7:1395-402.
    • (1988) EMBO J , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 8
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev 1998;12:599-606.
    • (1998) Genes Dev , vol.12 , pp. 599-606
    • Struhl, K.1
  • 9
  • 10
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee DY, Hayes JJ, Pruss D, Wolffe AP. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 1993;72: 73-84.
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 11
    • 0028883875 scopus 로고
    • The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/ TFIIA association with nucleosomal DNA
    • Godde JS, Nakatani Y, Wolffe AP. The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/ TFIIA association with nucleosomal DNA. Nucleic Acids Res 1995;23: 4557-64.
    • (1995) Nucleic Acids Res , vol.23 , pp. 4557-4564
    • Godde, J.S.1    Nakatani, Y.2    Wolffe, A.P.3
  • 12
    • 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 1996; 15:2508-18.
    • (1996) EMBO J , vol.15 , pp. 2508-2518
    • Vettese-Dadey, M.1    Grant, P.A.2    Hebbes, T.R.3    Crane-Robinson, C.4    Allis, C.D.5    Workman, J.L.6
  • 13
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin LK, Mann RK, Kayne PS, Grunstein M. Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell 1991; 65:1023-31.
    • (1991) Cell , vol.65 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 14
    • 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 1995;17:423-30.
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 15
    • 0030625679 scopus 로고    scopus 로고
    • The multifunctional role of the coactivator CBP in transcriptional regulation
    • Goldman PS, Tran VK, Goodman RH. The multifunctional role of the coactivator CBP in transcriptional regulation. Recent Prog Horm Res 1997; 52:105-19.
    • (1997) Recent Prog Horm Res , vol.52 , pp. 105-119
    • Goldman, P.S.1    Tran, V.K.2    Goodman, R.H.3
  • 16
    • 0028985162 scopus 로고
    • Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP
    • Lundblad JR, Kwok RP, Laurance ME, Harter ML, Goodman RH. Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature 1995;374:85-8.
    • (1995) Nature , vol.374 , pp. 85-88
    • Lundblad, J.R.1    Kwok, R.P.2    Laurance, M.E.3    Harter, M.L.4    Goodman, R.H.5
  • 17
    • 0028296414 scopus 로고
    • Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor
    • Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, et al. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev 1994;15:869-84.
    • (1994) Genes Dev , vol.15 , pp. 869-884
    • Eckner, R.1    Ewen, M.E.2    Newsome, D.3    Gerdes, M.4    DeCaprio, J.A.5    Lawrence, J.B.6
  • 18
    • 0029665857 scopus 로고    scopus 로고
    • A p300/ CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y. A p300/ CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 1996;382:319-24.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 19
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, et al. Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol Cell Biol 1996;16: 593-602.
    • (1996) Mol Cell Biol , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.A.2    Wang, L.3    Barlev, N.4    Ying, C.Y.5    Rosen, C.A.6
  • 20
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 1996;384:641-3.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 21
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 1996;87:953-9.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 22
    • 0030902507 scopus 로고    scopus 로고
    • Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors
    • Nakajima T, Uchida C, Anderson SF, Parvin JD, Montminy M. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors. Genes Dev 1997;11: 738-47.
    • (1997) Genes Dev , vol.11 , pp. 738-747
    • Nakajima, T.1    Uchida, C.2    Anderson, S.F.3    Parvin, J.D.4    Montminy, M.5
  • 23
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, et al. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 1997;90: 569-80.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6
  • 25
    • 0031835267 scopus 로고    scopus 로고
    • Co-activators and co-repressors in the integration of transcriptional responses
    • Torchia J, Glass C, Rosenfeld MG. Co-activators and co-repressors in the integration of transcriptional responses. Curr Opin Cell Biol 1998;10: 373-83.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 373-383
    • Torchia, J.1    Glass, C.2    Rosenfeld, M.G.3
  • 27
    • 0032523882 scopus 로고    scopus 로고
    • Regulation of gene expression by TBP-associated proteins
    • Lee TI, Young RA. Regulation of gene expression by TBP-associated proteins. Genes Dev 1998;12:1398-408.
    • (1998) Genes Dev , vol.12 , pp. 1398-1408
    • Lee, T.I.1    Young, R.A.2
  • 28
    • 0032504104 scopus 로고    scopus 로고
    • A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation
    • Grant PA, Schieltz D, Pray-Grant MG, Steger DJ, Reese JC, Yates JR 3rd, et al. A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation. Cell 1998;94:45-53.
    • (1998) Cell , vol.94 , pp. 45-53
    • Grant, P.A.1    Schieltz, D.2    Pray-Grant, M.G.3    Steger, D.J.4    Reese, J.C.5    Yates J.R. III6
  • 31
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997;90:595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 32
    • 0032030906 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo
    • Kuo MH, Zhou J, Jambeck P, Churchill ME, Allis CD. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. Genes Dev 1998;12:627-39.
    • (1998) Genes Dev , vol.12 , pp. 627-639
    • Kuo, M.H.1    Zhou, J.2    Jambeck, P.3    Churchill, M.E.4    Allis, C.D.5
  • 33
    • 0032031606 scopus 로고    scopus 로고
    • Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
    • Wang L, Liu L, Berger SL. Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes Dev 1998;12:640-53.
    • (1998) Genes Dev , vol.12 , pp. 640-653
    • Wang, L.1    Liu, L.2    Berger, S.L.3
  • 34
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 1996;272: 408-11.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 35
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 1997;89:341-7.
    • (1997) Cell , vol.89 , pp. 341-347
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 36
    • 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 1997;89:349-56.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 37
    • 0030959244 scopus 로고    scopus 로고
    • Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression
    • Alland L, Muhle R, Hou H Jr, Potes J, Chin L, Schreiber-Agus N, et al. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 1997;387:49-55.
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L.1    Muhle, R.2    Hou H., Jr.3    Potes, J.4    Chin, L.5    Schreiber-Agus, N.6
  • 38
    • 0343924289 scopus 로고    scopus 로고
    • Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
    • Kadosh D, Struhl K. Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters. Cell 1997;89:365-71.
    • (1997) Cell , vol.89 , pp. 365-371
    • Kadosh, D.1    Struhl, K.2
  • 39
    • 17744413444 scopus 로고    scopus 로고
    • A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
    • Heinzel T, Lavinsky RM, Mullen TM, Soderstrom M, Laherty CD, Torchia J, et al. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 1997;387:43-8.
    • (1997) Nature , vol.387 , pp. 43-48
    • Heinzel, T.1    Lavinsky, R.M.2    Mullen, T.M.3    Soderstrom, M.4    Laherty, C.D.5    Torchia, J.6
  • 42
    • 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 1998;92:463-73.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 44
    • 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, et al. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 1998;393:386-9.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6
  • 45
    • 0025943945 scopus 로고
    • Transcriptional repression by YY1, a human GLI-Kruppel-related protein, and relief of repression by adenovirus E1A protein
    • Shi Y, Seto E, Chang LS, Shenk T. Transcriptional repression by YY1, a human GLI-Kruppel-related protein, and relief of repression by adenovirus E1A protein. Cell 1991;67:377-88.
    • (1991) Cell , vol.67 , pp. 377-388
    • Shi, Y.1    Seto, E.2    Chang, L.S.3    Shenk, T.4
  • 46
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang WM, Yao YL, Sun JM, Davie JR, Seto E. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J Biol Chem 1997;272: 28001-7.
    • (1997) J Biol Chem , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 47
    • 0029997146 scopus 로고    scopus 로고
    • The CBP co-activator stimulates E2F1/ DPI activity
    • Trouche D, Cook A, Kouzarides T. The CBP co-activator stimulates E2F1/ DPI activity. Nucleic Acids Res 1996;24:4139-45.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4139-4145
    • Trouche, D.1    Cook, A.2    Kouzarides, T.3
  • 48
    • 0033083003 scopus 로고    scopus 로고
    • Mechanism of transcriptional repression of E2F by the retinoblastoma tumor suppressor protein
    • Ross JF, Liu X, Dynlacht BD. Mechanism of transcriptional repression of E2F by the retinoblastoma tumor suppressor protein. Mol Cell 1999;3: 195-205.
    • (1999) Mol Cell , vol.3 , pp. 195-205
    • Ross, J.F.1    Liu, X.2    Dynlacht, B.D.3
  • 49
    • 0030771898 scopus 로고    scopus 로고
    • Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
    • Lusser A, Brosch G, Loidl A, Haas H, Loidl P. Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science 1997;277:88-91.
    • (1997) Science , vol.277 , pp. 88-91
    • Lusser, A.1    Brosch, G.2    Loidl, A.3    Haas, H.4    Loidl, P.5
  • 51
    • 0032520953 scopus 로고    scopus 로고
    • Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo
    • Kadosh D, Struhl K. Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo. Genes Dev 1998;12:797-805.
    • (1998) Genes Dev , vol.12 , pp. 797-805
    • Kadosh, D.1    Struhl, K.2
  • 52
    • 0032560117 scopus 로고    scopus 로고
    • Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3
    • Rundlett SE. Carmen AA, Suka N, Turner BM, Grunstein M. Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3. Nature 1998;392:831-5.
    • (1998) Nature , vol.392 , pp. 831-835
    • Rundlett, S.E.1    Carmen, A.A.2    Suka, N.3    Turner, B.M.4    Grunstein, M.5
  • 53
    • 0032055036 scopus 로고    scopus 로고
    • Transcription of chromatin: These are complex times
    • Armstrong JA, Emerson BM. Transcription of chromatin: these are complex times. Curr Opin Genet Dev 1998;8:165-72.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 165-172
    • Armstrong, J.A.1    Emerson, B.M.2
  • 54
    • 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 1998;94: 17-27.
    • (1998) Cell , vol.94 , pp. 17-27
    • Schnitzler, G.1    Sif, S.2    Kingston, R.E.3
  • 55
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D. The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 1998;95: 279-89.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 57
    • 0028060515 scopus 로고
    • The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest
    • Dunaief JL, Strober BE, Guha S, Khavari PA, Alin K, Luban J, et al. The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 1994;79:119-30.
    • (1994) Cell , vol.79 , pp. 119-130
    • Dunaief, J.L.1    Strober, B.E.2    Guha, S.3    Khavari, P.A.4    Alin, K.5    Luban, J.6
  • 58
    • 0030960672 scopus 로고    scopus 로고
    • Transcription activation by recruitment
    • Ptashne M, Gann A. Transcription activation by recruitment. Nature 1997; 386:569-77.
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 59
    • 0025222518 scopus 로고
    • Histone function in transcription
    • Grunstein M. Histone function in transcription. Annu Rev Cell Biol 1990; 6:643-78.
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 643-678
    • Grunstein, M.1
  • 60
    • 0029978521 scopus 로고    scopus 로고
    • Active repression mechanisms of eukaryotic transcription repressors
    • Hanna-Rose W, Hansen U. Active repression mechanisms of eukaryotic transcription repressors. Trends Genet 1996;12:229-34.
    • (1996) Trends Genet , vol.12 , pp. 229-234
    • Hanna-Rose, W.1    Hansen, U.2
  • 61
    • 0027256440 scopus 로고
    • Transcriptional repression by the Drosophila evenskipped protein: Definition of a minimal repression domain
    • Han K, Manley JL. Transcriptional repression by the Drosophila evenskipped protein: definition of a minimal repression domain. Genes Dev 1993;7:491-503.
    • (1993) Genes Dev , vol.7 , pp. 491-503
    • Han, K.1    Manley, J.L.2
  • 62
    • 0029043782 scopus 로고
    • Mechanism of active transcriptional repression by the retinoblastoma protein
    • Weintraub SJ, Chow KN, Luo RX, Zhang SH, He S, Dean DC. Mechanism of active transcriptional repression by the retinoblastoma protein. Nature 1995;375:812-5.
    • (1995) Nature , vol.375 , pp. 812-815
    • Weintraub, S.J.1    Chow, K.N.2    Luo, R.X.3    Zhang, S.H.4    He, S.5    Dean, D.C.6
  • 63
    • 0029022770 scopus 로고
    • Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
    • Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, et al. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 1995;376:348-51.
    • (1995) Nature , vol.376 , pp. 348-351
    • Petrij, F.1    Giles, R.H.2    Dauwerse, H.G.3    Saris, J.J.4    Hennekam, R.C.5    Masuno, M.6
  • 64
    • 17144458786 scopus 로고    scopus 로고
    • Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia
    • Grignani F, De Matteis S, Nervi C, Tomassoni L, Gelmetti V, Cioce M, et al. Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. Nature 1998;391:815-8.
    • (1998) Nature , vol.391 , pp. 815-818
    • Grignani, F.1    De Matteis, S.2    Nervi, C.3    Tomassoni, L.4    Gelmetti, V.5    Cioce, M.6
  • 65
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin RJ, Nagy L, Inoue S, Shao W, Miller WH Jr, Evans RM. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 1998;391:811-4.
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller W.H., Jr.5    Evans, R.M.6
  • 66
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell RP Jr, 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 Natl Cancer Inst 1998;90:1621-5.
    • (1998) J Natl Cancer Inst , vol.90 , pp. 1621-1625
    • Warrell R.P., Jr.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5


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