메뉴 건너뛰기




Volumn 184, Issue 1, 2000, Pages 1-16

Histone deacetylases, transcriptional control, and cancer

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRIC ACID; CELL NUCLEUS RECEPTOR; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HORMONE RECEPTOR; HYBRID PROTEIN;

EID: 0034045040     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(200007)184:1<1::AID-JCP1>3.0.CO;2-7     Document Type: Review
Times cited : (591)

References (222)
  • 1
    • 0028942949 scopus 로고
    • The retinoblastoma susceptibility gene product represses transcription when directly bound to the promoter
    • Adnane J, Shao Z, Robbins PD. 1995. The retinoblastoma susceptibility gene product represses transcription when directly bound to the promoter. J Biol Chem 270:8837-8843.
    • (1995) J Biol Chem , vol.270 , pp. 8837-8843
    • Adnane, J.1    Shao, Z.2    Robbins, P.D.3
  • 3
    • 0001756213 scopus 로고    scopus 로고
    • Second family of histone deacetylases
    • Aravind L, Koonin EV. 1998. Second family of histone deacetylases. Science 280:1167.
    • (1998) Science , vol.280 , pp. 1167
    • Aravind, L.1    Koonin, E.V.2
  • 4
    • 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, Hodin RA. 1998. p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc Natl Acad Sci USA 95:6791-6796.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6791-6796
    • Archer, S.Y.1    Meng, S.2    Shei, A.3    Hodin, R.A.4
  • 5
    • 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. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80:767-776.
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 7
    • 0033555953 scopus 로고    scopus 로고
    • Role of DNA 5-methylcytosine transferase in cell transformation by fos
    • Bakin AV, Curran T. 1999. Role of DNA 5-methylcytosine transferase in cell transformation by fos. Science 283:387-390.
    • (1999) Science , vol.283 , pp. 387-390
    • Bakin, A.V.1    Curran, T.2
  • 8
    • 0026557594 scopus 로고
    • A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor
    • Baniahmad A, Kohne AC, Renkawitz R. 1992. A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J 11:1015-1023.
    • (1992) EMBO J , vol.11 , pp. 1015-1023
    • Baniahmad, A.1    Kohne, A.C.2    Renkawitz, R.3
  • 9
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister AJ, Kouzarides T. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 10
    • 0027617675 scopus 로고
    • Butyrate rapidly induces growth inhibition and differentiation in HT-29 cells
    • Barnard JA, Warwick G. 1993. Butyrate rapidly induces growth inhibition and differentiation in HT-29 cells. Cell Growth Differ 4:495-501.
    • (1993) Cell Growth Differ , vol.4 , pp. 495-501
    • Barnard, J.A.1    Warwick, G.2
  • 11
    • 0030802123 scopus 로고    scopus 로고
    • Identification of mouse histone deacetylase 1 as a growth factor-inducible gene
    • Bartl S, Taplick J, Lagger G, Khier H, Kuchler K, Seiser C. 1997. Identification of mouse histone deacetylase 1 as a growth factor-inducible gene. Mol Cell Biol 17:5033-5043.
    • (1997) Mol Cell Biol , vol.17 , pp. 5033-5043
    • Bartl, S.1    Taplick, J.2    Lagger, G.3    Khier, H.4    Kuchler, K.5    Seiser, C.6
  • 12
    • 0027985749 scopus 로고
    • E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo
    • Beijersbergen RL, Kerkhoven RM, Zhu L, Carlee L, Voorhoeve PM, Bernards R. 1994. E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo. Genes Dev 8:2680-2690.
    • (1994) Genes Dev , vol.8 , pp. 2680-2690
    • Beijersbergen, R.L.1    Kerkhoven, R.M.2    Zhu, L.3    Carlee, L.4    Voorhoeve, P.M.5    Bernards, R.6
  • 14
    • 0033580326 scopus 로고    scopus 로고
    • A mammalian protein with specific demethylase activity for mCpG DNA
    • Bhattacharya SK, Ramchandani S, Cervoni N, Szyf M. 1999. A mammalian protein with specific demethylase activity for mCpG DNA. Nature 397:579-583.
    • (1999) Nature , vol.397 , pp. 579-583
    • Bhattacharya, S.K.1    Ramchandani, S.2    Cervoni, N.3    Szyf, M.4
  • 15
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes J, Byfield P, Nakatani Y, Ogryzko V. 1998. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396:594-598.
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 17
    • 0032768188 scopus 로고    scopus 로고
    • The cell cycle-regulating transcription factors E2F-RB
    • Brehm A, Miska E, Reid J, Bannister A, Kouzarides T. 1999a. The cell cycle-regulating transcription factors E2F-RB. Br J Cancer 80(Suppl 1):38-41.
    • (1999) Br J Cancer , vol.80 , Issue.SUPPL. 1 , pp. 38-41
    • Brehm, A.1    Miska, E.2    Reid, J.3    Bannister, A.4    Kouzarides, T.5
  • 19
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell JE, Zhou J, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 20
    • 0031031755 scopus 로고    scopus 로고
    • Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
    • Candau R, Zhou JX, Allis CD, Berger SL. 1997. Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. EMBO J 16:555-565.
    • (1997) EMBO J , vol.16 , pp. 555-565
    • Candau, R.1    Zhou, J.X.2    Allis, C.D.3    Berger, S.L.4
  • 21
    • 0029991514 scopus 로고    scopus 로고
    • HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex
    • Carmen AA, Rundlett SE, Grunstein M. 1996. HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J Biol Chem 271:15837-15844.
    • (1996) J Biol Chem , vol.271 , pp. 15837-15844
    • Carmen, A.A.1    Rundlett, S.E.2    Grunstein, M.3
  • 22
    • 0028419153 scopus 로고
    • The retinoid signaling pathway: Molecular and genetic analyses
    • Chambon P. 1994. The retinoid signaling pathway: molecular and genetic analyses. Semin Cell Biol 5:115-125.
    • (1994) Semin Cell Biol , vol.5 , pp. 115-125
    • Chambon, P.1
  • 23
    • 0033200392 scopus 로고    scopus 로고
    • A functional interaction between the histone deacetylase Rpd3 and the corepressor groucho in Drosophila development
    • Chen G, Fernandez J, Mische S, Courey AJ. 1999. A functional interaction between the histone deacetylase Rpd3 and the corepressor groucho in Drosophila development. Genes Dev 13:2218-2230.
    • (1999) Genes Dev , vol.13 , pp. 2218-2230
    • Chen, G.1    Fernandez, J.2    Mische, S.3    Courey, A.J.4
  • 24
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 29
    • 0000198187 scopus 로고    scopus 로고
    • Inhibition of N-methylnitrosourea-induced tumors by the cytodifferentiating agent, suberanilohydroxamic acid
    • abstract 736
    • Cohen L, Richon V, Rifkind R, Marks P, Desai D, Amin S. 1998. Inhibition of N-methylnitrosourea-induced tumors by the cytodifferentiating agent, suberanilohydroxamic acid [abstract 736]. Proc Am Assoc Cancer Res 39:108.
    • (1998) Proc Am Assoc Cancer Res , vol.39 , pp. 108
    • Cohen, L.1    Richon, V.2    Rifkind, R.3    Marks, P.4    Desai, D.5    Amin, S.6
  • 31
    • 0033564261 scopus 로고    scopus 로고
    • Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation
    • Criqui-Filipe P, Ducret C, Maira SM, Wasylyk B. 1999. Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation. EMBO J 18:3392-3403.
    • (1999) EMBO J , vol.18 , pp. 3392-3403
    • Criqui-Filipe, P.1    Ducret, C.2    Maira, S.M.3    Wasylyk, B.4
  • 32
    • 0030977310 scopus 로고    scopus 로고
    • A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins
    • Cross SH, Meehan RR, Nan X, Bird A. 1997. A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins. Nat Genet 16:256-259.
    • (1997) Nat Genet , vol.16 , pp. 256-259
    • Cross, S.H.1    Meehan, R.R.2    Nan, X.3    Bird, A.4
  • 33
    • 0032530460 scopus 로고    scopus 로고
    • Transformation of hematopoietic cells by the Ski oncoprotein involves repression of retinoic acid receptor signaling
    • Dahl R, Kieslinger M, Beug H, Hayman MJ. 1998. Transformation of hematopoietic cells by the Ski oncoprotein involves repression of retinoic acid receptor signaling. Proc Natl Acad Sci USA 95:11187-11192.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11187-11192
    • Dahl, R.1    Kieslinger, M.2    Beug, H.3    Hayman, M.J.4
  • 34
    • 0032905924 scopus 로고    scopus 로고
    • c-Myc target genes involved in cell growth, apoptosis, and metabolism
    • Dang CV. 1999. c-Myc target genes involved in cell growth, apoptosis, and metabolism. Mol Cell Biol 19:1-11.
    • (1999) Mol Cell Biol , vol.19 , pp. 1-11
    • Dang, C.V.1
  • 37
    • 0000189644 scopus 로고    scopus 로고
    • Chemopreventative efficacy of suberanilohydroxamic acid (SAHA), a cytodifferentiating agent, against tobacco-specific nitrosamine 4-(methylinitros-amino)-1-(3-pyridyl)-1-butanone (NNK)-induced lung tumorigenesis in female A/J mice
    • abstract 362
    • Desai D, El-Bayoumy K, Amin S. 1999. Chemopreventative efficacy of suberanilohydroxamic acid (SAHA), a cytodifferentiating agent, against tobacco-specific nitrosamine 4-(methylinitros-amino)-1-(3-pyridyl)-1-butanone (NNK)-induced lung tumorigenesis in female A/J mice [abstract 362]. Proc Am Assoc Cancer Res 40:2396.
    • (1999) Proc Am Assoc Cancer Res , vol.40 , pp. 2396
    • Desai, D.1    El-Bayoumy, K.2    Amin, S.3
  • 38
    • 0032531688 scopus 로고    scopus 로고
    • The LAZ3(BCL-6) oncoprotein recruits a SMRT/ mSIN3A/histone deacetylase containing complex to mediate transcriptional repression
    • Dhordain P, Lin RJ, Quief S, Lantoine D, Kerckaert JP, Evans RM, Albagli O. 1998. The LAZ3(BCL-6) oncoprotein recruits a SMRT/ mSIN3A/histone deacetylase containing complex to mediate transcriptional repression. Nucleic Acids Res 26:4645-4651.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4645-4651
    • Dhordain, P.1    Lin, R.J.2    Quief, S.3    Lantoine, D.4    Kerckaert, J.P.5    Evans, R.M.6    Albagli, O.7
  • 39
    • 0033537977 scopus 로고    scopus 로고
    • Two E2F sites control growth-regulated and cell cycle-regulated transcription of the Htf9-a/RanBP1 gene through functionally distinct mechanisms
    • Di Fiore B, Guarguaglini G, Palena A, Kerkhoven RM, Bernards R, Lavia P. 1999. Two E2F sites control growth-regulated and cell cycle-regulated transcription of the Htf9-a/RanBP1 gene through functionally distinct mechanisms. J Biol Chem 274:10339-10348.
    • (1999) J Biol Chem , vol.274 , pp. 10339-10348
    • Di Fiore, B.1    Guarguaglini, G.2    Palena, A.3    Kerkhoven, R.M.4    Bernards, R.5    Lavia, P.6
  • 40
    • 0027970713 scopus 로고
    • DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts
    • Di Leonardo A, Linke SP, Clarkin K, Wahl GM. 1994. DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts. Genes Dev 8:2540-2551.
    • (1994) Genes Dev , vol.8 , pp. 2540-2551
    • Di Leonardo, A.1    Linke, S.P.2    Clarkin, K.3    Wahl, G.M.4
  • 43
    • 0027936686 scopus 로고
    • Differential regulation of E2F transactivation by cyclin/cdk2 complexes
    • Dynlacht BD, Flores O, Lees JA, Harlow E. 1994. Differential regulation of E2F transactivation by cyclin/cdk2 complexes. Genes Dev 8:1772-1786.
    • (1994) Genes Dev , vol.8 , pp. 1772-1786
    • Dynlacht, B.D.1    Flores, O.2    Lees, J.A.3    Harlow, E.4
  • 44
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson N. 1998. The regulation of E2F by pRB-family proteins. Genes Dev 12:2245-2262.
    • (1998) Genes Dev , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 46
    • 0025785484 scopus 로고
    • Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein
    • Ewen ME, Xing YG, Lawrence JB, Livingston DM. 1991. Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein. Cell 66:1155-1164.
    • (1991) Cell , vol.66 , pp. 1155-1164
    • Ewen, M.E.1    Xing, Y.G.2    Lawrence, J.B.3    Livingston, D.M.4
  • 47
    • 0032433144 scopus 로고    scopus 로고
    • Role of histone deacetylases in acute leukemia
    • Fenrick R, Hiebert SW. 1998. Role of histone deacetylases in acute leukemia. J Cell Biochem Suppl 31:194-202.
    • (1998) J Cell Biochem Suppl , vol.31 , pp. 194-202
    • Fenrick, R.1    Hiebert, S.W.2
  • 48
    • 0032168984 scopus 로고    scopus 로고
    • The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase
    • Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D. 1998. The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. Proc Natl Acad Sci USA 95:10493-10498.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10493-10498
    • Ferreira, R.1    Magnaghi-Jaulin, L.2    Robin, P.3    Harel-Bellan, A.4    Trouche, D.5
  • 50
    • 0028986992 scopus 로고
    • Trichostatin A inhibits both ras-induced neurite outgrowth of PC12 cells and morphological transformation of NIH3T3 cells
    • Futamura M, Monden Y, Okabe T, Fujita-Yoshigaki J, Yokoyama S, Nishimura S. 1995. Trichostatin A inhibits both ras-induced neurite outgrowth of PC12 cells and morphological transformation of NIH3T3 cells. Oncogene 10:1119-1123.
    • (1995) Oncogene , vol.10 , pp. 1119-1123
    • Futamura, M.1    Monden, Y.2    Okabe, T.3    Fujita-Yoshigaki, J.4    Yokoyama, S.5    Nishimura, S.6
  • 52
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos T, Thireos G. 1992. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J 11:4145-4152.
    • (1992) EMBO J , vol.11 , pp. 4145-4152
    • Georgakopoulos, T.1    Thireos, G.2
  • 53
    • 0033526809 scopus 로고    scopus 로고
    • MBP-1 physically associates with histone deacetylase for transcriptional repression
    • Ghosh AK, Steele R, Ray RB. 1999. MBP-1 physically associates with histone deacetylase for transcriptional repression. Biochem Biophys Res Commun 260:405-409.
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 405-409
    • Ghosh, A.K.1    Steele, R.2    Ray, R.B.3
  • 55
    • 0023695580 scopus 로고
    • The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements
    • Glass CK, Holloway JM, Devary OV, Rosenfeld MG. 1988. The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements. Cell 54:313-323.
    • (1988) Cell , vol.54 , pp. 313-323
    • Glass, C.K.1    Holloway, J.M.2    Devary, O.V.3    Rosenfeld, M.G.4
  • 58
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger CM, Hassig CA, Schreiber SL. 1999. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc Natl Acad Sci USA 96:4868-4873.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 59
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. 1997. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 60
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu W, Shi XL, Roeder RG. 1997. Synergistic activation of transcription by CBP and p53. Nature 387:819-823.
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 61
    • 0032522962 scopus 로고    scopus 로고
    • Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia
    • Guidez F, Ivins S, Zhu J, Soderstrom M, Waxman S, Zelent A. 1998. Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia. Blood 91: 2634-2642.
    • (1998) Blood , vol.91 , pp. 2634-2642
    • Guidez, F.1    Ivins, S.2    Zhu, J.3    Soderstrom, M.4    Waxman, S.5    Zelent, A.6
  • 63
    • 0030031542 scopus 로고    scopus 로고
    • E2F-1 blocks terminal differentiation and causes proliferation in transgenic megakaryocytes
    • Guy CT, Zhou W, Kaufman S, Robinson MO. 1996. E2F-1 blocks terminal differentiation and causes proliferation in transgenic megakaryocytes. Mol Cell Biol 16:685-693.
    • (1996) Mol Cell Biol , vol.16 , pp. 685-693
    • Guy, C.T.1    Zhou, W.2    Kaufman, S.3    Robinson, M.O.4
  • 64
    • 0029921317 scopus 로고    scopus 로고
    • Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer
    • Hall M, Peters G. 1996. Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer. Adv Cancer Res 68:67-108.
    • (1996) Adv Cancer Res , vol.68 , pp. 67-108
    • Hall, M.1    Peters, G.2
  • 65
    • 0031265050 scopus 로고    scopus 로고
    • A SAGA of histone acetylation and gene expression
    • Hampsey M. 1997. A SAGA of histone acetylation and gene expression. Trends Genet 13:427-429.
    • (1997) Trends Genet , vol.13 , pp. 427-429
    • Hampsey, M.1
  • 66
    • 0027142956 scopus 로고
    • Isolation of the Rb-related p130 through its interaction with CDK2 and cyclins
    • Hannon GJ, Demetrick D, Beach D. 1993. Isolation of the Rb-related p130 through its interaction with CDK2 and cyclins. Genes Dev 7:2378-2391.
    • (1993) Genes Dev , vol.7 , pp. 2378-2391
    • Hannon, G.J.1    Demetrick, D.2    Beach, D.3
  • 67
    • 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. 1997. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89:341-347.
    • (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
  • 68
    • 0031941912 scopus 로고    scopus 로고
    • Distinct interactions of PML-RARalpha and PLZF-RARalpha with co-repressors determine differential responses to RA in APL
    • He LZ, Guidez F, Tribioli C, Peruzzi D, Ruthardt M, Zelent A, Pandolfi PP. 1998. Distinct interactions of PML-RARalpha and PLZF-RARalpha with co-repressors determine differential responses to RA in APL. Nat Genet 18:126-135.
    • (1998) Nat Genet , vol.18 , pp. 126-135
    • He, L.Z.1    Guidez, F.2    Tribioli, C.3    Peruzzi, D.4    Ruthardt, M.5    Zelent, A.6    Pandolfi, P.P.7
  • 70
    • 0027426917 scopus 로고
    • Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative, trans-activation
    • Helin K, Wu C-L, Lees JA, Dynlacht BD, Ngwu C, Harlow E. 1993. Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative, trans-activation. Genes Dev 7:1850-1861.
    • (1993) Genes Dev , vol.7 , pp. 1850-1861
    • Helin, K.1    Wu, C.-L.2    Lees, J.A.3    Dynlacht, B.D.4    Ngwu, C.5    Harlow, E.6
  • 72
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding proteins
    • Hendrich B, Bird A. 1998. Identification and characterization of a family of mammalian methyl-CpG binding proteins. Mol Cell Biol 18:6538-6547.
    • (1998) Mol Cell Biol , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.2
  • 73
    • 0026537277 scopus 로고
    • The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F
    • Hiebert SW, Chellappan SP, Horowitz JM, Nevins JR. 1992. The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F. Genes Dev 6:177-185.
    • (1992) Genes Dev , vol.6 , pp. 177-185
    • Hiebert, S.W.1    Chellappan, S.P.2    Horowitz, J.M.3    Nevins, J.R.4
  • 76
    • 0033524444 scopus 로고    scopus 로고
    • CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex
    • Hsieh JJ, Zhou S, Chen L, Young DB, Hayward SD. 1999. CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. Proc Natl Acad Sci USA 96:23-28.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 23-28
    • Hsieh, J.J.1    Zhou, S.2    Chen, L.3    Young, D.B.4    Hayward, S.D.5
  • 77
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang EY, Zhang J, Miska EA, Guenther MG, Kouzarides T, Lazar MA. 2000. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev 14:45-54.
    • (2000) Genes Dev , vol.14 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 78
    • 0025735647 scopus 로고
    • A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product
    • Huang S, Lee WH, Lee EY. 1991. A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product. Nature 350:160-162.
    • (1991) Nature , vol.350 , pp. 160-162
    • Huang, S.1    Lee, W.H.2    Lee, E.Y.3
  • 79
    • 0033306577 scopus 로고    scopus 로고
    • Transcriptional repression by REST: Recruitment of Sin3A and histone deacetylase to neuronal genes
    • Huang Y, Myers SJ, Dingledine R. 1999. Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes. Nat Neurosci 2:867-872.
    • (1999) Nat Neurosci , vol.2 , pp. 867-872
    • Huang, Y.1    Myers, S.J.2    Dingledine, R.3
  • 80
    • 15444353328 scopus 로고    scopus 로고
    • pRB and p107/ p130 are required for the regulated expression of different sets of E2F responsive genes
    • Hurford RK Jr, Cobrinik D, Lee MH, Dyson N. 1997. pRB and p107/ p130 are required for the regulated expression of different sets of E2F responsive genes. Genes Dev 11:1447-1463.
    • (1997) Genes Dev , vol.11 , pp. 1447-1463
    • Hurford R.K., Jr.1    Cobrinik, D.2    Lee, M.H.3    Dyson, N.4
  • 81
    • 0032933352 scopus 로고    scopus 로고
    • E2F and histone deacetylase mediate transforming growth factor beta repression of cdc25A during keratinocyte cell cycle arrest
    • Iavarone A, Massague J. 1999. E2F and histone deacetylase mediate transforming growth factor beta repression of cdc25A during keratinocyte cell cycle arrest. Mol Cell Biol 19:916-922.
    • (1999) Mol Cell Biol , vol.19 , pp. 916-922
    • Iavarone, A.1    Massague, J.2
  • 82
    • 0028335152 scopus 로고
    • Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23
    • Inouye CJ, Seto E. 1994. Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23. J Biol Chem 269:6506-6510.
    • (1994) J Biol Chem , vol.269 , pp. 6506-6510
    • Inouye, C.J.1    Seto, E.2
  • 83
    • 0029800326 scopus 로고    scopus 로고
    • Inhibition of cell proliferation by an RNA ligand that selectively blocks E2F function
    • Ishizaki J, Nevins JR, Sullenger BA. 1996. Inhibition of cell proliferation by an RNA ligand that selectively blocks E2F function. Nat Med 2:1386-1389.
    • (1996) Nat Med , vol.2 , pp. 1386-1389
    • Ishizaki, J.1    Nevins, J.R.2    Sullenger, B.A.3
  • 84
    • 0030570961 scopus 로고    scopus 로고
    • Transcription: A growing coactivator network
    • Janknecht R, Hunter T. 1996. Transcription: a growing coactivator network [news; comment]. Nature 383:22-23.
    • (1996) Nature , vol.383 , pp. 22-23
    • Janknecht, R.1    Hunter, T.2
  • 85
    • 0032500851 scopus 로고    scopus 로고
    • Molecular cloning of Drosophila melanogaster cDNAs that encode a novel histone deacetylase dHDAC3
    • Johnson CA, Barlow AL, Turner BM. 1998. Molecular cloning of Drosophila melanogaster cDNAs that encode a novel histone deacetylase dHDAC3. Gene 221:127-134.
    • (1998) Gene , vol.221 , pp. 127-134
    • Johnson, C.A.1    Barlow, A.L.2    Turner, B.M.3
  • 87
    • 0028364529 scopus 로고
    • Autoregulatory control of E2F1 expression in response to positive and negative regulators of cell cycle progression
    • Johnson DG, Ohtani K, Nevins JR. 1994b. Autoregulatory control of E2F1 expression in response to positive and negative regulators of cell cycle progression. Genes Dev 8:1514-1525.
    • (1994) Genes Dev , vol.8 , pp. 1514-1525
    • Johnson, D.G.1    Ohtani, K.2    Nevins, J.R.3
  • 88
    • 0000223931 scopus 로고    scopus 로고
    • Role of E2F in cell cycle control and cancer
    • Johnson DG, Schneider-Broussard R. 1998. Role of E2F in cell cycle control and cancer. Front Biosci 3:447-448.
    • (1998) Front Biosci , vol.3 , pp. 447-448
    • Johnson, D.G.1    Schneider-Broussard, R.2
  • 89
    • 0032960181 scopus 로고    scopus 로고
    • Cancer epigenetics comes of age
    • Jones PA, Laird PW. 1999. Cancer epigenetics comes of age. Nat Genet 21:163-167.
    • (1999) Nat Genet , vol.21 , pp. 163-167
    • Jones, P.A.1    Laird, P.W.2
  • 92
    • 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. 1997. Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters. Cell 89:365-371.
    • (1997) Cell , vol.89 , pp. 365-371
    • Kadosh, D.1    Struhl, K.2
  • 93
    • 0026021882 scopus 로고
    • Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product
    • Kaelin WG Jr, Pallas DC, DeCaprio JA, Kaye FJ, Livingston DM. 1991. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product. Cell 64:521-532.
    • (1991) Cell , vol.64 , pp. 521-532
    • Kaelin W.G., Jr.1    Pallas, D.C.2    DeCaprio, J.A.3    Kaye, F.J.4    Livingston, D.M.5
  • 94
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao HY, Downes M, Ordentlich P, Evans RM. 2000. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev 14:55-66.
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 96
    • 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. 1993. Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase. J Biol Chem 268:22429-22435.
    • (1993) J Biol Chem , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 97
    • 0033615547 scopus 로고    scopus 로고
    • Sensing of ionizing radiation-induced DNA damage by ATM through interaction with histone deacetylase
    • Kim GD, Choi YH, Dimtchev A, Jeong SJ, Dritschilo A, Jung M. 1999a. Sensing of ionizing radiation-induced DNA damage by ATM through interaction with histone deacetylase. J Biol Chem 274: 31127-31130.
    • (1999) J Biol Chem , vol.274 , pp. 31127-31130
    • Kim, G.D.1    Choi, Y.H.2    Dimtchev, A.3    Jeong, S.J.4    Dritschilo, A.5    Jung, M.6
  • 99
    • 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. 1998. Interaction and functional cooperation of the leukemia-associated factors AML1 and p300 in myeloid cell differentiation. EMBO J 17:2994-3004.
    • (1998) EMBO J , vol.17 , pp. 2994-3004
    • Kitabayashi, I.1    Yokoyama, A.2    Shimizu, K.3    Ohki, M.4
  • 100
    • 0033152491 scopus 로고    scopus 로고
    • Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes
    • Koipally J, Renold A, Kim J, Georgopoulos K. 1999. Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes. EMBO J 18:3090-3100.
    • (1999) EMBO J , vol.18 , pp. 3090-3100
    • Koipally, J.1    Renold, A.2    Kim, J.3    Georgopoulos, K.4
  • 102
    • 0030658036 scopus 로고    scopus 로고
    • Xenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes
    • Ladomery M, Lyons S, Sommerville J. 1997. Xenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes. Gene 198:275-280.
    • (1997) Gene , vol.198 , pp. 275-280
    • Ladomery, M.1    Lyons, S.2    Sommerville, J.3
  • 103
    • 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. 1997. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89:349-356.
    • (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
  • 105
    • 0032849352 scopus 로고    scopus 로고
    • RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins
    • Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG Jr, Seto E, Branton PE. 1999. RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins. Mol Cell Biol 19:6632-6641.
    • (1999) Mol Cell Biol , vol.19 , pp. 6632-6641
    • Lai, A.1    Lee, J.M.2    Yang, W.M.3    DeCaprio, J.A.4    Kaelin W.G., Jr.5    Seto, E.6    Branton, P.E.7
  • 106
    • 0027316813 scopus 로고
    • An E2F-binding site mediates cell-cycle regulated repression of mouse B-myb transcription
    • Lam EW, Watson RJ. 1993. An E2F-binding site mediates cell-cycle regulated repression of mouse B-myb transcription. EMBO J 12: 2705-2713.
    • (1993) EMBO J , vol.12 , pp. 2705-2713
    • Lam, E.W.1    Watson, R.J.2
  • 107
    • 0029094856 scopus 로고
    • Cell-cycle regulation of human B-myb transcription
    • Lam EW, Bennett JD, Watson RJ. 1995. Cell-cycle regulation of human B-myb transcription. Gene 160:277-281.
    • (1995) Gene , vol.160 , pp. 277-281
    • Lam, E.W.1    Bennett, J.D.2    Watson, R.J.3
  • 109
    • 0029004774 scopus 로고
    • Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300
    • Lee JS, Galvin KM, See RH, Eckner R, Livingston D, Moran E, Shi Y. 1995. Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300. Genes Dev 9:1188-1198.
    • (1995) Genes Dev , vol.9 , pp. 1188-1198
    • Lee, J.S.1    Galvin, K.M.2    See, R.H.3    Eckner, R.4    Livingston, D.5    Moran, E.6    Shi, Y.7
  • 111
    • 0031214702 scopus 로고    scopus 로고
    • Transcriptional regulation during myelopoiesis
    • Lenny N, Westendorf JJ, Hiebert SW. 1997. Transcriptional regulation during myelopoiesis. Mol Biol Rep 24:157-168.
    • (1997) Mol Biol Rep , vol.24 , pp. 157-168
    • Lenny, N.1    Westendorf, J.J.2    Hiebert, S.W.3
  • 112
    • 0026747761 scopus 로고
    • Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA
    • Lewis JD, Meehan RR, Henzel WJ, Maurer-Fogy I, Jeppesen P, Klein F, Bird A. 1992. Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA. Cell 69:905-914.
    • (1992) Cell , vol.69 , pp. 905-914
    • Lewis, J.D.1    Meehan, R.R.2    Henzel, W.J.3    Maurer-Fogy, I.4    Jeppesen, P.5    Klein, F.6    Bird, A.7
  • 113
    • 0022635969 scopus 로고
    • Unique sequence, ski, in Sloan-Kettering avian retroviruses with properties of a new cell-derived oncogene
    • Li Y, Turck CM, Teumer JK, Stavnezer E. 1986. Unique sequence, ski, in Sloan-Kettering avian retroviruses with properties of a new cell-derived oncogene. J Virol 57:1065-1072.
    • (1986) J Virol , vol.57 , pp. 1065-1072
    • Li, Y.1    Turck, C.M.2    Teumer, J.K.3    Stavnezer, E.4
  • 114
    • 0027135209 scopus 로고
    • The adenovirus E1A-associated 130-kD protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E
    • Li Y, Graham C, Lacy S, Duncan AM, Whyte P. 1993. The adenovirus E1A-associated 130-kD protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E. Genes Dev 7:2366-2377.
    • (1993) Genes Dev , vol.7 , pp. 2366-2377
    • Li, Y.1    Graham, C.2    Lacy, S.3    Duncan, A.M.4    Whyte, P.5
  • 115
    • 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. 1998. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391:811-814.
    • (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
  • 116
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. 1997. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 117
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo RX, Postigo AA, Dean DC. 1998. Rb interacts with histone deacetylase to repress transcription. Cell 92:463-473.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 118
    • 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. 1997. Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science 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
  • 123
    • 0027948984 scopus 로고
    • Functional similarity and physical association between GCN5 and ADA2: Putative transcriptional adaptors
    • Marcus GA, Silverman N, Berger SL, Horiuchi J, Guarente L. 1994. Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors. EMBO J 13:4807-4815.
    • (1994) EMBO J , vol.13 , pp. 4807-4815
    • Marcus, G.A.1    Silverman, N.2    Berger, S.L.3    Horiuchi, J.4    Guarente, L.5
  • 124
    • 12044258811 scopus 로고
    • Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain
    • Mayol X, Grana X, Baldi A, Sang N, Hu Q, Giordano A. 1993. Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain. Oncogene 8:2561-2566.
    • (1993) Oncogene , vol.8 , pp. 2561-2566
    • Mayol, X.1    Grana, X.2    Baldi, A.3    Sang, N.4    Hu, Q.5    Giordano, A.6
  • 126
    • 0030741385 scopus 로고    scopus 로고
    • Apoptotic death in adenocarcinoma cell lines induced by butyrate and other histone deacetylase inhibitors
    • McBain JA, Eastman A, Nobel CS, Mueller GC. 1997. Apoptotic death in adenocarcinoma cell lines induced by butyrate and other histone deacetylase inhibitors. Biochem Pharmacol 53:1357-1368.
    • (1997) Biochem Pharmacol , vol.53 , pp. 1357-1368
    • McBain, J.A.1    Eastman, A.2    Nobel, C.S.3    Mueller, G.C.4
  • 127
    • 0025952138 scopus 로고
    • Different fibers have different regional effects on luminal contents of rat colon
    • McIntyre A, Young GP, Taranto T, Gibson PR, Ward PB. 1991. Different fibers have different regional effects on luminal contents of rat colon. Gastroenterology 101:1274-1281.
    • (1991) Gastroenterology , vol.101 , pp. 1274-1281
    • McIntyre, A.1    Young, G.P.2    Taranto, T.3    Gibson, P.R.4    Ward, P.B.5
  • 128
    • 0027463032 scopus 로고
    • Butyrate production from dietary fibre and protection against large bowel cancer in a rat model
    • McIntyre A, Gibson PR, Young GP. 1993. Butyrate production from dietary fibre and protection against large bowel cancer in a rat model. Gut 34:386-391.
    • (1993) Gut , vol.34 , pp. 386-391
    • McIntyre, A.1    Gibson, P.R.2    Young, G.P.3
  • 129
    • 0032493894 scopus 로고    scopus 로고
    • The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins
    • McMahon SB, Van Buskirk HA, Dugan KA, Copeland TD, Cole MD. 1998. The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins. Cell 94:363-374.
    • (1998) Cell , vol.94 , pp. 363-374
    • McMahon, S.B.1    Van Buskirk, H.A.2    Dugan, K.A.3    Copeland, T.D.4    Cole, M.D.5
  • 130
    • 0033970431 scopus 로고    scopus 로고
    • The essential cofactor TRRAP recruits the histone acetyltransferase hGCNS to c-Myc
    • McMahon SB, Wood MA, Cole MD. 2000. The essential cofactor TRRAP recruits the histone acetyltransferase hGCNS to c-Myc. Mol Cell Biol 20:556-562.
    • (2000) Mol Cell Biol , vol.20 , pp. 556-562
    • McMahon, S.B.1    Wood, M.A.2    Cole, M.D.3
  • 131
    • 0024342686 scopus 로고
    • Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs
    • Meehan RR, Lewis JD, McKay S, Kleiner EL, Bird AP. 1989. Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs. Cell 58:499-507.
    • (1989) Cell , vol.58 , pp. 499-507
    • Meehan, R.R.1    Lewis, J.D.2    McKay, S.3    Kleiner, E.L.4    Bird, A.P.5
  • 132
  • 133
    • 0033215387 scopus 로고    scopus 로고
    • Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a
    • Murphy M, Ahn J, Walker KK, Hoffman WH, Evans RM, Levine AJ, George DL. 1999. Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a. Genes Dev 13:2490-2501.
    • (1999) Genes Dev , vol.13 , pp. 2490-2501
    • Murphy, M.1    Ahn, J.2    Walker, K.K.3    Hoffman, W.H.4    Evans, R.M.5    Levine, A.J.6    George, D.L.7
  • 134
    • 0342437491 scopus 로고    scopus 로고
    • MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin
    • Nan X, Campoy FJ, Bird A. 1997. MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin. Cell 88:471-481.
    • (1997) Cell , vol.88 , pp. 471-481
    • Nan, X.1    Campoy, F.J.2    Bird, A.3
  • 135
    • 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. 1998. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393:386-389.
    • (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    Bird, A.7
  • 136
    • 0028008441 scopus 로고
    • Cell cycle targets of the DNA tumor viruses
    • Nevins JR. 1994. Cell cycle targets of the DNA tumor viruses. Curr Opin Genet Dev 4:130-134.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 130-134
    • Nevins, J.R.1
  • 137
    • 0031815596 scopus 로고    scopus 로고
    • Toward an understanding of the functional complexity of the E2F and retinoblastoma families
    • Nevins JR. 1998. Toward an understanding of the functional complexity of the E2F and retinoblastoma families. Cell Growth Differ 9:585-593.
    • (1998) Cell Growth Differ , vol.9 , pp. 585-593
    • Nevins, J.R.1
  • 139
    • 0033557497 scopus 로고    scopus 로고
    • Ski is a component of the histone deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptor
    • Nomura T, Khan MM, Kaul SC, Dong HD, Wadhwa R, Colmenares C, Kohno I, Ishii S. 1999. Ski is a component of the histone deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptor. Genes Dev 13:412-423.
    • (1999) Genes Dev , vol.13 , pp. 412-423
    • Nomura, T.1    Khan, M.M.2    Kaul, S.C.3    Dong, H.D.4    Wadhwa, R.5    Colmenares, C.6    Kohno, I.7    Ishii, S.8
  • 140
    • 0029019659 scopus 로고
    • AML1 and the 8;21 and 3;21 translocations in acute and chronic myeloid leukemia
    • Nucifora G, Rowley JD. 1995. AML1 and the 8;21 and 3;21 translocations in acute and chronic myeloid leukemia. Blood 86:1-14.
    • (1995) Blood , vol.86 , pp. 1-14
    • Nucifora, G.1    Rowley, J.D.2
  • 141
    • 0029778901 scopus 로고    scopus 로고
    • Human fibroblast commitment to a senescence-like state in response to histone deacetylase inhibitors is cell cycle dependent
    • Ogryzko VV, Hirai TH, Russanova VR, Barbie DA, Howard BH. 1996a. Human fibroblast commitment to a senescence-like state in response to histone deacetylase inhibitors is cell cycle dependent. Mol Cell Biol 16:5210-5218.
    • (1996) Mol Cell Biol , vol.16 , pp. 5210-5218
    • Ogryzko, V.V.1    Hirai, T.H.2    Russanova, V.R.3    Barbie, D.A.4    Howard, B.H.5
  • 142
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. 1996b. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953-959.
    • (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
  • 143
    • 0030271392 scopus 로고    scopus 로고
    • The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin replication and histone metabolism
    • Parthun MR, Widom J, Gottschling DE. 1996. The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism. Cell 87:85-94.
    • (1996) Cell , vol.87 , pp. 85-94
    • Parthun, M.R.1    Widom, J.2    Gottschling, D.E.3
  • 144
  • 145
    • 0032510342 scopus 로고    scopus 로고
    • Deregulated expression of E2F1 induces hyperplasia and cooperates with ras in skin tumor development
    • Pierce AM, Fisher SM, Conti CJ, Johnson DG. 1998a. Deregulated expression of E2F1 induces hyperplasia and cooperates with ras in skin tumor development. Oncogene 16:1267-1276.
    • (1998) Oncogene , vol.16 , pp. 1267-1276
    • Pierce, A.M.1    Fisher, S.M.2    Conti, C.J.3    Johnson, D.G.4
  • 147
    • 0028856782 scopus 로고
    • Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast
    • Qian YW, Lee EY. 1995. Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast. J Biol Chem 270:25507-25513.
    • (1995) J Biol Chem , vol.270 , pp. 25507-25513
    • Qian, Y.W.1    Lee, E.Y.2
  • 148
  • 149
    • 0026648086 scopus 로고
    • Identification of a growth suppression domain within the retinoblastoma gene product
    • Qin XQ, Chittenden T, Livingston DM, Kaelin WG Jr. 1992. Identification of a growth suppression domain within the retinoblastoma gene product. Genes Dev 6:953-964.
    • (1992) Genes Dev , vol.6 , pp. 953-964
    • Qin, X.Q.1    Chittenden, T.2    Livingston, D.M.3    Kaelin W.G., Jr.4
  • 152
    • 0017767153 scopus 로고
    • n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
    • Riggs MG, Whittaker RG, Neumann JR, Ingram VM. 1977. n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 268:462-464.
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 153
    • 0033083003 scopus 로고    scopus 로고
    • Mechanism of transcriptional repression of E2F by the retinoblastoma tumor suppressor protein
    • Ross JF, Liu X, Dynlacht BD. 1999. Mechanism of transcriptional repression of E2F by the retinoblastoma tumor suppressor protein. Mol Cell 3:195-205.
    • (1999) Mol Cell , vol.3 , pp. 195-205
    • Ross, J.F.1    Liu, X.2    Dynlacht, B.D.3
  • 154
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett SE, Carmen AA, Kobayashi R, Bavykin S, Turner BM, Grunstein M. 1996. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci USA 93:14503-14508.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1    Carmen, A.A.2    Kobayashi, R.3    Bavykin, S.4    Turner, B.M.5    Grunstein, M.6
  • 161
    • 0028940364 scopus 로고
    • An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3
    • Schreiber-Agus N, Chin L, Chen K, Torres R, Rao G, Guida P, Skoultchi AI, DePinho RA. 1995. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80:777-786.
    • (1995) Cell , vol.80 , pp. 777-786
    • Schreiber-Agus, N.1    Chin, L.2    Chen, K.3    Torres, R.4    Rao, G.5    Guida, P.6    Skoultchi, A.I.7    DePinho, R.A.8
  • 162
    • 0017864644 scopus 로고
    • The effect of sodium butyrate on histone modification
    • Sealy L, Chalkley R. 1978. The effect of sodium butyrate on histone modification. Cell 14:115-121.
    • (1978) Cell , vol.14 , pp. 115-121
    • Sealy, L.1    Chalkley, R.2
  • 163
    • 0030747725 scopus 로고    scopus 로고
    • Identification of positively and negatively acting elements regulating expression of the E2F2 gene in response to cell growth signals
    • Sears R, Ohtani K, Nevins JR. 1997. Identification of positively and negatively acting elements regulating expression of the E2F2 gene in response to cell growth signals. Mol Cell Biol 17:5227-5235.
    • (1997) Mol Cell Biol , vol.17 , pp. 5227-5235
    • Sears, R.1    Ohtani, K.2    Nevins, J.R.3
  • 164
    • 0030678627 scopus 로고    scopus 로고
    • Role of the retinoblastoma protein in the pathogenesis of human cancer
    • Sellers WR, Kaelin WG Jr. 1997. Role of the retinoblastoma protein in the pathogenesis of human cancer. J Clin Oncol 15:3301-3312.
    • (1997) J Clin Oncol , vol.15 , pp. 3301-3312
    • Sellers, W.R.1    Kaelin W.G., Jr.2
  • 165
    • 0029612231 scopus 로고
    • A potent transrepression domain in the retinoblastoma protein induces a cell cycle arrest when bound to E2F sites
    • Sellers WR, Rodgers JW, Kaelin WG Jr. 1995. A potent transrepression domain in the retinoblastoma protein induces a cell cycle arrest when bound to E2F sites. Proc Natl Acad Sci USA 92:11544-11548.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11544-11548
    • Sellers, W.R.1    Rodgers, J.W.2    Kaelin W.G., Jr.3
  • 166
    • 0032053770 scopus 로고    scopus 로고
    • A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegans
    • Shi Y, Mello C. 1998. A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegans. Genes Dev 12:943-955.
    • (1998) Genes Dev , vol.12 , pp. 943-955
    • Shi, Y.1    Mello, C.2
  • 167
    • 0031149162 scopus 로고    scopus 로고
    • DNA methylation: A molecular lock
    • Siegfried Z, Cedar H. 1997. DNA methylation: a molecular lock. Curr Biol 7:R305-R307.
    • (1997) Curr Biol , vol.7
    • Siegfried, Z.1    Cedar, H.2
  • 169
    • 0028360766 scopus 로고
    • Overexpression of E2F-1 in rat embryo fibroblasts leads to neoplastic transformation
    • Singh P, Wong SH, Hong W. 1994. Overexpression of E2F-1 in rat embryo fibroblasts leads to neoplastic transformation. EMBO J 13:3329-3338.
    • (1994) EMBO J , vol.13 , pp. 3329-3338
    • Singh, P.1    Wong, S.H.2    Hong, W.3
  • 172
    • 0033199611 scopus 로고    scopus 로고
    • Sp3, but not Sp1, mediates the transcriptional activation of the p21/WAF1/Cip1 gene promoter by histone deacetylase inhibitor
    • Sowa Y, Orita T, Minamikawa-Hiranabe S, Mizuno T, Nomura H, Sakai T. 1999. Sp3, but not Sp1, mediates the transcriptional activation of the p21/WAF1/Cip1 gene promoter by histone deacetylase inhibitor. Cancer Res 59:4266-4270.
    • (1999) Cancer Res , vol.59 , pp. 4266-4270
    • Sowa, Y.1    Orita, T.2    Minamikawa-Hiranabe, S.3    Mizuno, T.4    Nomura, H.5    Sakai, T.6
  • 173
    • 0032533860 scopus 로고    scopus 로고
    • The COOH-terminal region of pRb2/p130 binds to histone deacetylase 1 (HDAC1), enhancing transcriptional repression of the E2F-dependent cyclin A promoter
    • Stiegler P, De Luca A, Bagella L, Giordano A. 1998. The COOH-terminal region of pRb2/p130 binds to histone deacetylase 1 (HDAC1), enhancing transcriptional repression of the E2F-dependent cyclin A promoter. Cancer Res 58:5049-5052.
    • (1998) Cancer Res , vol.58 , pp. 5049-5052
    • Stiegler, P.1    De Luca, A.2    Bagella, L.3    Giordano, A.4
  • 175
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. 1998. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev 12:599-606.
    • (1998) Genes Dev , vol.12 , pp. 599-606
    • Struhl, K.1
  • 176
    • 0032814843 scopus 로고    scopus 로고
    • A general requirement for the Sin3-rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae
    • Sun ZW, Hampsey M. 1999. A general requirement for the Sin3-rpd3 histone
    • (1999) Genetics , vol.152 , pp. 921-932
    • Sun, Z.W.1    Hampsey, M.2
  • 177
    • 0033588156 scopus 로고    scopus 로고
    • Chicken histone deacetylase-2 controls the amount of the IgM H-chain at the steps of both transcription of its gene and alternative processing of its pre-mRNA in the DT40 cell line
    • Takami Y, Kikuchi H, Nakayama T. 1999. Chicken histone deacetylase-2 controls the amount of the IgM H-chain at the steps of both transcription of its gene and alternative processing of its pre-mRNA in the DT40 cell line. J Biol Chem 274:23977-23990.
    • (1999) J Biol Chem , vol.274 , pp. 23977-23990
    • Takami, Y.1    Kikuchi, H.2    Nakayama, T.3
  • 178
    • 0021796111 scopus 로고
    • The association between Mi-2 antibodies and dermatomyositis
    • Targoff IN, Reichlin M. 1985. The association between Mi-2 antibodies and dermatomyositis. Arthritis Rheum 28:796-803.
    • (1985) Arthritis Rheum , vol.28 , pp. 796-803
    • Targoff, I.N.1    Reichlin, M.2
  • 179
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 180
    • 0031016121 scopus 로고    scopus 로고
    • RB kinases and RB-binding proteins: New points of view
    • Taya Y. 1997. RB kinases and RB-binding proteins: new points of view. Trends Biochem Sci 22:14-17.
    • (1997) Trends Biochem Sci , vol.22 , pp. 14-17
    • Taya, Y.1
  • 181
    • 0032819331 scopus 로고    scopus 로고
    • Unlocking the mechanisms of transcription factor YY1: Are chromatin modifying enzymes the key?
    • Thomas MJ, Seto E. 1999. Unlocking the mechanisms of transcription factor YY1: are chromatin modifying enzymes the key? Gene 236: 197-208.
    • (1999) Gene , vol.236 , pp. 197-208
    • Thomas, M.J.1    Seto, E.2
  • 182
    • 0033582492 scopus 로고    scopus 로고
    • Viral ski inhibits retinoblastoma protein (Rb)-mediated transcriptional repression in a dominant negative fashion
    • Tokitou F, Nomura T, Khan MM, Kaul SC, Wadhwa R, Yasukawa T, Kohno I, Ishii S. 1999. Viral ski inhibits retinoblastoma protein (Rb)-mediated transcriptional repression in a dominant negative fashion. J Biol Chem 274:4485-4488.
    • (1999) J Biol Chem , vol.274 , pp. 4485-4488
    • Tokitou, F.1    Nomura, T.2    Khan, M.M.3    Kaul, S.C.4    Wadhwa, R.5    Yasukawa, T.6    Kohno, I.7    Ishii, S.8
  • 184
    • 0025232254 scopus 로고
    • Dietary fiber, vegetables, and colon cancer: Critical review and meta-analyses of the epidemiologic evidence
    • Trock B, Lanza E, Greenwald P. 1990a. Dietary fiber, vegetables, and colon cancer: critical review and meta-analyses of the epidemiologic evidence. J Natl Cancer Inst 82:650-661.
    • (1990) J Natl Cancer Inst , vol.82 , pp. 650-661
    • Trock, B.1    Lanza, E.2    Greenwald, P.3
  • 185
    • 0025026668 scopus 로고
    • High fiber diet and colon cancer: A critical review
    • Trock BJ, Lanza E, Greenwald P. 1990b. High fiber diet and colon cancer: a critical review. Prog Clin Biol Res 346:145-157.
    • (1990) Prog Clin Biol Res , vol.346 , pp. 145-157
    • Trock, B.J.1    Lanza, E.2    Greenwald, P.3
  • 186
    • 0032751323 scopus 로고    scopus 로고
    • Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation
    • van der Vlag J, Otte AP. 1999. Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. Nat Genet 23:474-478.
    • (1999) Nat Genet , vol.23 , pp. 474-478
    • Van Der Vlag, J.1    Otte, A.P.2
  • 188
    • 0033593347 scopus 로고    scopus 로고
    • Identification of a new family of higher eukaryotic histone deacetylases: Coordinate expression of differentiation-dependent chromatin modifiers
    • Verdel A, Khochbin S. 1999. Identification of a new family of higher eukaryotic histone deacetylases: coordinate expression of differentiation-dependent chromatin modifiers. J Biol Chem 274:2440-2445.
    • (1999) J Biol Chem , vol.274 , pp. 2440-2445
    • Verdel, A.1    Khochbin, S.2
  • 189
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault A, Kaufman PD, Kobayashi R, Stillman B. 1996. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87:95-104.
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 190
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault A, Kaufman PD, Kobayashi R, Stillman B. 1998. Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Curr Biol 8:96-108.
    • (1998) Curr Biol , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 191
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidal M, Gaber RF. 1991. RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol Cell Biol 11:6317-6327.
    • (1991) Mol Cell Biol , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.F.2
  • 192
    • 0029840668 scopus 로고    scopus 로고
    • Genetic characterization of a mammalian protein-protein interaction domain by using a yeast reverse two-hybrid system
    • Vidal M, Braun P, Chen E, Boeke JD, Harlow E. 1996. Genetic characterization of a mammalian protein-protein interaction domain by using a yeast reverse two-hybrid system. Proc Natl Acad Sci USA 93:10321-10326.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10321-10326
    • Vidal, M.1    Braun, P.2    Chen, E.3    Boeke, J.D.4    Harlow, E.5
  • 194
    • 0032474826 scopus 로고    scopus 로고
    • A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase
    • Wade PA, Jones PL, Vermaak D, Wolffe AP. 1998b. A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase. Curr Biol 8:843-846.
    • (1998) Curr Biol , vol.8 , pp. 843-846
    • Wade, P.A.1    Jones, P.L.2    Vermaak, D.3    Wolffe, A.P.4
  • 196
    • 0028784499 scopus 로고
    • Inhibition of in vitro myogenic differentiation by cellular transcription factor E2F1
    • Wang J, Helin C, Jin P, Nadal-Ginard B. 1995. Inhibition of in vitro myogenic differentiation by cellular transcription factor E2F1. Cell Growth Differ 6:1299-1306.
    • (1995) Cell Growth Differ , vol.6 , pp. 1299-1306
    • Wang, J.1    Helin, C.2    Jin, P.3    Nadal-Ginard, B.4
  • 197
    • 0026636908 scopus 로고
    • Retinoblastoma protein switches the E2F site from positive to negative element
    • Weintraub SJ, Prater CA, Dean DC. 1992. Retinoblastoma protein switches the E2F site from positive to negative element. Nature 358:259-261.
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 198
    • 0029043782 scopus 로고
    • Mechanism of active transcriptional repression by the retinoblastoma protein
    • Weintraub SJ, Chow KN, Luo RX, Zhang SH, He S, Dean DC. 1995. Mechanism of active transcriptional repression by the retinoblastoma protein. Nature 375:812-815.
    • (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
  • 199
    • 0022978527 scopus 로고
    • Effects of short chain fatty acids on a new human colon carcinoma cell line (LIM1215)
    • Whitehead RH, Young GP, Bhathal PS. 1986. Effects of short chain fatty acids on a new human colon carcinoma cell line (LIM1215). Gut 27:1457-1463.
    • (1986) Gut , vol.27 , pp. 1457-1463
    • Whitehead, R.H.1    Young, G.P.2    Bhathal, P.S.3
  • 201
    • 0033515620 scopus 로고    scopus 로고
    • A Smad transcriptional corepressor
    • Wotton D, Lo RS, Lee S, Massague J. 1999. A Smad transcriptional corepressor. Cell 97:29-39.
    • (1999) Cell , vol.97 , pp. 29-39
    • Wotton, D.1    Lo, R.S.2    Lee, S.3    Massague, J.4
  • 202
    • 0030008768 scopus 로고    scopus 로고
    • Expression of dominant-negative mutant DP-1 blocks cell cycle progression in G1
    • Wu CL, Classon M, Dyson N, Harlow E. 1996. Expression of dominant-negative mutant DP-1 blocks cell cycle progression in G1. Mol Cell Biol 16:3698-3706.
    • (1996) Mol Cell Biol , vol.16 , pp. 3698-3706
    • Wu, C.L.1    Classon, M.2    Dyson, N.3    Harlow, E.4
  • 203
    • 0031577480 scopus 로고    scopus 로고
    • Sodium butyrate induces NIH3T3 cells to senescence-like state and enhances promoter activity of p21WAF/CIP1 in p53-independent manner
    • Xiao H, Hasegawa T, Miyaishi O, Ohkusu K, Isobe K. 1997. Sodium butyrate induces NIH3T3 cells to senescence-like state and enhances promoter activity of p21WAF/CIP1 in p53-independent manner. Biochem Biophys Res Commun 237:457-460.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 457-460
    • Xiao, H.1    Hasegawa, T.2    Miyaishi, O.3    Ohkusu, K.4    Isobe, K.5
  • 204
    • 0033562343 scopus 로고    scopus 로고
    • Both Sp1 and Sp3 are responsible for p21waf1 promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells
    • Xiao H, Hasegawa T, Isobe K. 1999. Both Sp1 and Sp3 are responsible for p21waf1 promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells. J Cell Biochem 73:291-302.
    • (1999) J Cell Biochem , vol.73 , pp. 291-302
    • Xiao, H.1    Hasegawa, T.2    Isobe, K.3
  • 205
    • 0028945789 scopus 로고
    • Multiple members of the E2F transcription factor family are the products of oncogenes
    • Xu G, Livingston DM, Krek W. 1995. Multiple members of the E2F transcription factor family are the products of oncogenes. Proc Natl Acad Sci USA 92:1357-1361.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1357-1361
    • Xu, G.1    Livingston, D.M.2    Krek, W.3
  • 206
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang WM, Inouye C, Zeng Y, Bearss D, Seto E. 1996a. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc Natl Acad Sci USA 93:12845-12850.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 207
    • 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. 1997. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J Biol Chem 272: 28001-28007.
    • (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
  • 208
    • 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. 1996b. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
    • (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
  • 209
    • 0033609057 scopus 로고    scopus 로고
    • BRCA1 interacts with components of the histone deacetylase complex
    • Yarden RI, Brody LC. 1999. BRCA1 interacts with components of the histone deacetylase complex. Proc Natl Acad Sci USA 96:4983-4988.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4983-4988
    • Yarden, R.I.1    Brody, L.C.2
  • 210
    • 0026509298 scopus 로고
    • A novel tetracyclic peptide, trapoxin, induces phenotypic change from transformed to normal in sis-oncogene-transformed NIH3T3 cells
    • Yoshida H, Sugita K. 1992. A novel tetracyclic peptide, trapoxin, induces phenotypic change from transformed to normal in sis-oncogene-transformed NIH3T3 cells. Jpn J Cancer Res 83:324-328.
    • (1992) Jpn J Cancer Res , vol.83 , pp. 324-328
    • Yoshida, H.1    Sugita, K.2
  • 211
    • 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. 1990. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 265:17174-17179.
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 213
    • 0029837730 scopus 로고    scopus 로고
    • A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains
    • Zamir I, Harding HP, Atkins GB, Horlein A, Glass CK, Rosenfeld MG, Lazar MA. 1996. A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains. Mol Cell Biol 16:5458-5465.
    • (1996) Mol Cell Biol , vol.16 , pp. 5458-5465
    • Zamir, I.1    Harding, H.P.2    Atkins, G.B.3    Horlein, A.4    Glass, C.K.5    Rosenfeld, M.G.6    Lazar, M.A.7
  • 214
    • 0033515424 scopus 로고    scopus 로고
    • Active transcriptional repression by the Rb-E2F complex mediates G1 arrest triggered by p16INK4a, TGFbeta, and contact inhibition
    • Zhang HS, Postigo AA, Dean DC. 1999a. Active transcriptional repression by the Rb-E2F complex mediates G1 arrest triggered by p16INK4a, TGFbeta, and contact inhibition. Cell 97:53-61.
    • (1999) Cell , vol.97 , pp. 53-61
    • Zhang, H.S.1    Postigo, A.A.2    Dean, D.C.3
  • 215
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. 1997. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89:357-364.
    • (1997) Cell , vol.89 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 216
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • Zhang W, Bieker JJ. 1998. Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc Natl Acad Sci USA 95:9855-9860.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.J.2
  • 217
    • 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. 1998a. The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95:279-289.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 218
    • 0032088533 scopus 로고    scopus 로고
    • SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex
    • Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D. 1998b. SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. Mol Cell 1:1021-1031.
    • (1998) Mol Cell , vol.1 , pp. 1021-1031
    • Zhang, Y.1    Sun, Z.W.2    Iratni, R.3    Erdjument-Bromage, H.4    Tempst, P.5    Hampsey, M.6    Reinberg, D.7
  • 219
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
    • Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D. 1999b. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. Genes Dev 13:1924-1935.
    • (1999) Genes Dev , vol.13 , pp. 1924-1935
    • Zhang, Y.1    Ng, H.H.2    Erdjument-Bromage, H.3    Tempst, P.4    Bird, A.5    Reinberg, D.6
  • 221
    • 0029026176 scopus 로고
    • The pRB-related protein p107 contains two growth suppression domains: Independent interactions with E2F and cyclin/cdk complexes
    • Zhu L, Enders G, Lees JA, Beijersbergen RL, Bernards R, Harlow E. 1995. The pRB-related protein p107 contains two growth suppression domains: independent interactions with E2F and cyclin/cdk complexes. EMBO J 14:1904-1913.
    • (1995) EMBO J , vol.14 , pp. 1904-1913
    • Zhu, L.1    Enders, G.2    Lees, J.A.3    Beijersbergen, R.L.4    Bernards, R.5    Harlow, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.