메뉴 건너뛰기




Volumn 7, Issue 6, 1997, Pages 357-365

Cell growth inhibition by the Mad/Max complex through recruitment of histone deacetylase activity

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; MAMMALIA;

EID: 0031172243     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(06)00183-7     Document Type: Article
Times cited : (96)

References (72)
  • 1
    • 0025607921 scopus 로고
    • New light on Myc and Myb, Part I. Myc
    • Lüscher B, Eisenman RN: New light on Myc and Myb, Part I. Myc. Genes Dev 1990, 4:2025-2035.
    • (1990) Genes Dev , vol.4 , pp. 2025-2035
    • Lüscher, B.1    Eisenman, R.N.2
  • 3
    • 0029686266 scopus 로고    scopus 로고
    • Proteins of the Myc network: Essential regulators of cell growth and differentiation
    • Henriksson M, Lüscher B: Proteins of the Myc network: essential regulators of cell growth and differentiation. Adv Cancer Res 1996, 68:109-182.
    • (1996) Adv Cancer Res , vol.68 , pp. 109-182
    • Henriksson, M.1    Lüscher, B.2
  • 4
    • 0025763419 scopus 로고
    • Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc
    • Blackwood EM, Eisenman RN: Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 1991, 251:1211-1217.
    • (1991) Science , vol.251 , pp. 1211-1217
    • Blackwood, E.M.1    Eisenman, R.N.2
  • 6
    • 0025829169 scopus 로고
    • Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation- sensitive DNA binding and Ras cotransformation
    • Prendergast GC, Lawe D, Ziff EB: Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation- sensitive DNA binding and Ras cotransformation. Cell 1991, 65:395-407.
    • (1991) Cell , vol.65 , pp. 395-407
    • Prendergast, G.C.1    Lawe, D.2    Ziff, E.B.3
  • 7
    • 0027533679 scopus 로고
    • Oncogenic activity of the c-Myc protein requires dimerization with Max
    • Amati B, Brooks MW, Levy N, Littlewood TD, Evan GI, Land H: Oncogenic activity of the c-Myc protein requires dimerization with Max. Cell 1993, 72:233-245.
    • (1993) Cell , vol.72 , pp. 233-245
    • Amati, B.1    Brooks, M.W.2    Levy, N.3    Littlewood, T.D.4    Evan, G.I.5    Land, H.6
  • 8
    • 0027364326 scopus 로고
    • The c-Myc protein induces cell cycle progression and apoptosis through dimerization with Max
    • Amati B, Littlewood TD, Evan GI, Land H: The c-Myc protein induces cell cycle progression and apoptosis through dimerization with Max. EMBO J 1993, 12:5083-5087.
    • (1993) EMBO J , vol.12 , pp. 5083-5087
    • Amati, B.1    Littlewood, T.D.2    Evan, G.I.3    Land, H.4
  • 9
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer DE, Kretzner L, Eisenman RN: Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 1993, 72:211-222.
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 10
    • 0027511606 scopus 로고
    • Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
    • Zervos AS, Gyuris J, Brent R: Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 1993, 72:223-232.
    • (1993) Cell , vol.72 , pp. 223-232
    • Zervos, A.S.1    Gyuris, J.2    Brent, R.3
  • 11
    • 0028889811 scopus 로고
    • Mad3 and Mad4: Novel Max-interacting transcriptional repressors that suppress c-Myc-dependent transformation and are expressed during neural and epidermal differentiation
    • Hurlin PJ, Quéva C, Koskinen PJ, Steingrimsson E, Ayer DE, Copeland NG, et al.: Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-Myc-dependent transformation and are expressed during neural and epidermal differentiation. EMBO J 1995, 14:5646-5659.
    • (1995) EMBO J , vol.14 , pp. 5646-5659
    • Hurlin, P.J.1    Quéva, C.2    Koskinen, P.J.3    Steingrimsson, E.4    Ayer, D.E.5    Copeland, N.G.6
  • 12
    • 0028318949 scopus 로고
    • Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1
    • Lahoz EG, Xu L, Schreiber-Agus N, DePinho RA:Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1. Proc Natl Acad Sci USA 1994, 91:5503-5507.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5503-5507
    • Lahoz, E.G.1    Xu, L.2    Schreiber-Agus, N.3    DePinho, R.A.4
  • 13
    • 0029077733 scopus 로고
    • Effects of the Myc oncogene antagonist, Mad, on proliferation, cell cycling and the malignant phenotype of human brain tumor cells
    • Chen J, Willingham T, Margraf LR, Schreiber-Agus N, DePinho RA, Nisen PD: Effects of the Myc oncogene antagonist, Mad, on proliferation, cell cycling and the malignant phenotype of human brain tumor cells. Nat Med 1995, 1:638-643.
    • (1995) Nat Med , vol.1 , pp. 638-643
    • Chen, J.1    Willingham, T.2    Margraf, L.R.3    Schreiber-Agus, N.4    DePinho, R.A.5    Nisen, P.D.6
  • 14
    • 0029129054 scopus 로고
    • Differential effects by Mad and Max on transformation by cellular and viral oncoproteins
    • Cerni C, Bousset K, Seelos C, Burkhardt H, Henriksson M, Lüscher B: Differential effects by Mad and Max on transformation by cellular and viral oncoproteins. Oncogene 1995, 11:587-596.
    • (1995) Oncogene , vol.11 , pp. 587-596
    • Cerni, C.1    Bousset, K.2    Seelos, C.3    Burkhardt, H.4    Henriksson, M.5    Lüscher, B.6
  • 15
    • 0028938120 scopus 로고
    • Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro
    • Västrik I, Kaipainen A, Penttilä T-L, Lymboussakis A, Alitalo R, Parvinen M, et al.: Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro. J Cell Biol 1995, 128:1197-1208.
    • (1995) J Cell Biol , vol.128 , pp. 1197-1208
    • Västrik, I.1    Kaipainen, A.2    Penttilä, T.-L.3    Lymboussakis, A.4    Alitalo, R.5    Parvinen, M.6
  • 17
    • 0028905563 scopus 로고
    • Mad:Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of the yeast repressor Sin3
    • Ayer DE, Lawrence QA, Eisenman RN: Mad:Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of the yeast repressor Sin3. Cell 1995, 80:767-776.
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 18
    • 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, et al.: An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 1995, 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
  • 19
    • 0027479075 scopus 로고
    • Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein
    • Wang H, Stillman DJ: Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein. Mol Cell Biol 1993, 13:1805-1814.
    • (1993) Mol Cell Biol , vol.13 , pp. 1805-1814
    • Wang, H.1    Stillman, D.J.2
  • 21
    • 0029737603 scopus 로고    scopus 로고
    • Sin3 corepressor function in Myc-induced transcription and transformation
    • Harper SE, Qiu Y, Sharp PA: Sin3 corepressor function in Myc-induced transcription and transformation. Proc Natl Acad Sci USA 1996, 93:8636-8540.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8636-18540
    • Harper, S.E.1    Qiu, Y.2    Sharp, P.A.3
  • 22
    • 0029982704 scopus 로고    scopus 로고
    • SIN3-dependent transcriptional repression by interaction with the Mad1 DNA-binding protein
    • Kasten MM, Ayer DE, Stillman DJ: SIN3-dependent transcriptional repression by interaction with the Mad1 DNA-binding protein. Mol Cell Biol 1996, 16:4215-4221.
    • (1996) Mol Cell Biol , vol.16 , pp. 4215-4221
    • Kasten, M.M.1    Ayer, D.E.2    Stillman, D.J.3
  • 23
    • 9244234957 scopus 로고    scopus 로고
    • Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression domain of the Myc antagonist Mxi1
    • Rao G, Alland L, Guida P, Schreiber-Agus N, Chen K, Chin L, et al.: Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression domain of the Myc antagonist Mxi1. Oncogene 1996, 12:1165-1172.
    • (1996) Oncogene , vol.12 , pp. 1165-1172
    • Rao, G.1    Alland, L.2    Guida, P.3    Schreiber-Agus, N.4    Chen, K.5    Chin, L.6
  • 24
    • 0030581149 scopus 로고    scopus 로고
    • Chromatin unfolds
    • Felsenfeld G: Chromatin unfolds. Cell 1996, 86:13-19.
    • (1996) Cell , vol.86 , pp. 13-19
    • Felsenfeld, G.1
  • 25
    • 0029917840 scopus 로고    scopus 로고
    • Repression and activation by multiprotein complexes that alter chromatin structure
    • Kingston RE, Bunker CA, Imbalzano AN: Repression and activation by multiprotein complexes that alter chromatin structure. Genes Dev 1996, 10:905-920.
    • (1996) Genes Dev , vol.10 , pp. 905-920
    • Kingston, R.E.1    Bunker, C.A.2    Imbalzano, A.N.3
  • 26
    • 0030134433 scopus 로고    scopus 로고
    • Chromatin: Pushing nucleosomes around
    • Krude T, Elgin SCR: Chromatin: pushing nucleosomes around. Curr Biol 1996, 6:511-515.
    • (1996) Curr Biol , vol.6 , pp. 511-515
    • Krude, T.1    Elgin, S.C.R.2
  • 27
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation
    • Brownell JE, Allis CD: Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr Opin Genet Dev 1996, 6:176-184.
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 176-184
    • Brownell, J.E.1    Allis, C.D.2
  • 28
    • 0030271391 scopus 로고    scopus 로고
    • Histone acetylation and chromatin assembly: A single escort, multiple dances?
    • Roth SY, Allis CD: Histone acetylation and chromatin assembly: a single escort, multiple dances? Cell 1996, 87:5-8.
    • (1996) Cell , vol.87 , pp. 5-8
    • Roth, S.Y.1    Allis, C.D.2
  • 29
    • 0029869172 scopus 로고    scopus 로고
    • Histone deacetylase: A regulator of transcription
    • Wolffe AP: Histone deacetylase: a regulator of transcription. Science 1996, 272:371-372.
    • (1996) Science , vol.272 , pp. 371-372
    • Wolffe, A.P.1
  • 30
    • 0030092108 scopus 로고    scopus 로고
    • Hanging on to histones
    • Wolffe AP, Pruss D: Hanging on to histones. Curr Biol 1996, 6:234-237.
    • (1996) Curr Biol , vol.6 , pp. 234-237
    • Wolffe, A.P.1    Pruss, D.2
  • 31
    • 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
  • 32
    • 0028127762 scopus 로고
    • Role of the histone amino termini in facilitating binding of a transcription factor, Gal4-AH, to nucleosome cores
    • Vettese-Dadey M, Walter P, Chen H, Juan L-J, Workman JL: Role of the histone amino termini in facilitating binding of a transcription factor, Gal4-AH, to nucleosome cores. Mol Cell Biol 1994, 14:970-981.
    • (1994) Mol Cell Biol , vol.14 , pp. 970-981
    • Vettese-Dadey, M.1    Walter, P.2    Chen, H.3    Juan, L.-J.4    Workman, J.L.5
  • 33
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner BM, Birley AJ, Lavender J: Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 1992, 69:375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 34
    • 0027183088 scopus 로고
    • The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression
    • Jeppesen P, Turner BM: The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression. Cell 1993, 74:281-289.
    • (1993) Cell , vol.74 , pp. 281-289
    • Jeppesen, P.1    Turner, B.M.2
  • 35
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • O'Neill LP, Turner BM: Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J 1995, 14:3946-3957.
    • (1995) EMBO J , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Turner, B.M.2
  • 36
  • 37
    • 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, 87:953-959.
    • (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
  • 38
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang X-J, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 1996, 282:319-324.
    • (1996) Nature , vol.282 , pp. 319-324
    • Yang, X.-J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 39
    • 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, et al.: Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 1996, 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
  • 40
    • 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, 384:641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 42
    • 0031036154 scopus 로고    scopus 로고
    • Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation
    • Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, et al.: Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation. Mol Cell Biol 1997, 17:519-527.
    • (1997) Mol Cell Biol , vol.17 , pp. 519-527
    • Wang, L.1    Mizzen, C.2    Ying, C.3    Candau, R.4    Barlev, N.5    Brownell, J.6
  • 46
    • 0029886810 scopus 로고    scopus 로고
    • Interaction of the co-activator CBP with Myb-proteins: Effect on Myb-specific transactivation and on the cooperativity with NF-M
    • Oelgeschläger M, Janknecht R, Krieg J, Schreek S, Lüscher B: Interaction of the co-activator CBP with Myb-proteins: effect on Myb-specific transactivation and on the cooperativity with NF-M. EMBO J 1996, 15:2771-2780.
    • (1996) EMBO J , vol.15 , pp. 2771-2780
    • Oelgeschläger, M.1    Janknecht, R.2    Krieg, J.3    Schreek, S.4    Lüscher, B.5
  • 47
    • 0030207894 scopus 로고    scopus 로고
    • Transcriptional control: Versatile molecular glue
    • Janknecht R, Hunter T: Transcriptional control: versatile molecular glue. Curr Biol 1996, 6:951-954.
    • (1996) Curr Biol , vol.6 , pp. 951-954
    • Janknecht, R.1    Hunter, T.2
  • 48
    • 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, 272:408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 49
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidai M, Gaber RF: RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol Cell Biol 1991, 11:6317-6327.
    • (1991) Mol Cell Biol , vol.11 , pp. 6317-6327
    • Vidai, M.1    Gaber, R.F.2
  • 50
    • 0026046959 scopus 로고
    • RPD1 (Sin3/UME4) is required for maximal activation and repression of diverse yeast genes
    • Vidai M, Strich R, Esposito RE, Gaber RF: RPD1 (Sin3/UME4) is required for maximal activation and repression of diverse yeast genes. Mol Cell Biol 1991, 11:6306-6316.
    • (1991) Mol Cell Biol , vol.11 , pp. 6306-6316
    • Vidai, M.1    Strich, R.2    Esposito, R.E.3    Gaber, R.F.4
  • 51
    • 0025096058 scopus 로고
    • The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs
    • Wang H, Clark I, Nicholson PR, Herskowitz I, Stillman DJ: The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs. Mol Cell Biol 1990, 10:5927-5936.
    • (1990) Mol Cell Biol , vol.10 , pp. 5927-5936
    • Wang, H.1    Clark, I.2    Nicholson, P.R.3    Herskowitz, I.4    Stillman, D.J.5
  • 52
    • 0031027008 scopus 로고    scopus 로고
    • Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites
    • Hurlin PJ, Quéva C, Eisenman RN: Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites Genes Dev 1997, 11:44-58.
    • (1997) Genes Dev , vol.11 , pp. 44-58
    • Hurlin, P.J.1    Quéva, C.2    Eisenman, R.N.3
  • 53
    • 0027431276 scopus 로고
    • A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation
    • Ayer DE, Eisenman RN: A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. Genes Dev 1993, 7:2110-2119.
    • (1993) Genes Dev , vol.7 , pp. 2110-2119
    • Ayer, D.E.1    Eisenman, R.N.2
  • 54
    • 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, 17:423-430.
    • (1995) BioEssays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 55
    • 0022431493 scopus 로고
    • Minichromosome assembly of non-integrated plasmid DNA transfected into mammalian cells
    • Reeves R, Gorman CM, Howard B: Minichromosome assembly of non-integrated plasmid DNA transfected into mammalian cells. Nucleic Acids Res 1985, 13:3599-3615.
    • (1985) Nucleic Acids Res , vol.13 , pp. 3599-3615
    • Reeves, R.1    Gorman, C.M.2    Howard, B.3
  • 56
    • 0028217604 scopus 로고
    • Micrococcal nuclease digestion of nuclei reveals extended nucleosome ladders having anomalous DNA lengths for chromatin assembled on non-replicated plasmids in transfected cells
    • Jeong S, Stein A: Micrococcal nuclease digestion of nuclei reveals extended nucleosome ladders having anomalous DNA lengths for chromatin assembled on non-replicated plasmids in transfected cells. Nucleic Acids Res 1994, 22:370-375.
    • (1994) Nucleic Acids Res , vol.22 , pp. 370-375
    • Jeong, S.1    Stein, A.2
  • 57
    • 0023689244 scopus 로고
    • Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by trichostatin A
    • Yoshida M, Beppu T: Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by trichostatin A. Exp Cell Res 1988, 177:122-131.
    • (1988) Exp Cell Res , vol.177 , pp. 122-131
    • Yoshida, M.1    Beppu, T.2
  • 58
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • Hecht A, Laroche T, Strahl-Baslinger S, Gasser SM, Grunstein M: Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell 1995, 80:583-592.
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Baslinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 60
    • 0028267869 scopus 로고
    • DRTF1/E2F: An expanding family of heterodimeric transcription factors implicated in cell-cycle control
    • La Thangue NB: DRTF1/E2F: an expanding family of heterodimeric transcription factors implicated in cell-cycle control. Trends Biochem Sci 1994, 19:108-114.
    • (1994) Trends Biochem Sci , vol.19 , pp. 108-114
    • La Thangue, N.B.1
  • 61
    • 0028918028 scopus 로고
    • Transcriptional regulation during the mammalian cell cycle
    • Müller R: Transcriptional regulation during the mammalian cell cycle. Trends Genet 1995, 11:173-178.
    • (1995) Trends Genet , vol.11 , pp. 173-178
    • Müller, R.1
  • 62
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg RA: The retinoblastoma protein and cell cycle control. Cell 1995, 81:323-330.
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 63
    • 0029043782 scopus 로고
    • Mechanism of active transcriptional repression by the retinoblastoma protein
    • Weintraub SJ, Chow KNB, Luo RX, Zhang SH, He S, Dean DC: Mechanism of active transcriptional repression by the retinoblastoma protein. Nature 1995, 375:812-815.
    • (1995) Nature , vol.375 , pp. 812-815
    • Weintraub, S.J.1    Chow, K.N.B.2    Luo, R.X.3    Zhang, S.H.4    He, S.5    Dean, D.C.6
  • 64
    • 0031054892 scopus 로고    scopus 로고
    • Cell-cycle regulation of gene expression by transcriptional repression
    • Zwicker J, Müller R: Cell-cycle regulation of gene expression by transcriptional repression. Trends Genet 1997, 13:3-6.
    • (1997) Trends Genet , vol.13 , pp. 3-6
    • Zwicker, J.1    Müller, R.2
  • 65
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global transcription repressor RPD3
    • Yang W-M, Inouye C, Zeng Y, Bearss D, Seto E: Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global transcription repressor RPD3. Proc Natl Acad Sci USA 1996, 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
  • 66
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen CA, Okayama H: Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. BioTech 1988, 6:632-638.
    • (1988) BioTech , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 67
    • 0023919063 scopus 로고
    • c-myc and c-myb protein degradation: Effect of metabolic inhibitors and heat shock
    • Lüscher B, Eisenman RN: c-myc and c-myb protein degradation: effect of metabolic inhibitors and heat shock. Mol Cell Biol 1988, 8:2504-2512.
    • (1988) Mol Cell Biol , vol.8 , pp. 2504-2512
    • Lüscher, B.1    Eisenman, R.N.2
  • 68
    • 0028820121 scopus 로고
    • Casein kinase II phosphorylation site mutations in c-Myb affect DNA binding and transcriptional cooperativity with NF-M
    • Oelgeschläger M, Krieg J, Lüscher-Firzlaff JM, Lüscher B: Casein kinase II phosphorylation site mutations in c-Myb affect DNA binding and transcriptional cooperativity with NF-M. Mol Cell Biol 1995, 15:5966-5974.
    • (1995) Mol Cell Biol , vol.15 , pp. 5966-5974
    • Oelgeschläger, M.1    Krieg, J.2    Lüscher-Firzlaff, J.M.3    Lüscher, B.4
  • 69
    • 0027385033 scopus 로고
    • Identification of casein kinase II phosphorylation sites in Max: Effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers
    • Bousset K, Henriksson M, Lüscher-Firzlaff JM, Litchfield DW, Lüscher B: Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers. Oncogene 1993, 8:3211-3220.
    • (1993) Oncogene , vol.8 , pp. 3211-3220
    • Bousset, K.1    Henriksson, M.2    Lüscher-Firzlaff, J.M.3    Litchfield, D.W.4    Lüscher, B.5
  • 71
    • 0025996009 scopus 로고
    • Histone acetylation in Zea mays. I. Activities of histone acetyltransferases and histone deacetylases
    • Lòpez-Rodas G, Georgieva EI, Sendra R, Loidl P: Histone acetylation in Zea mays. I. Activities of histone acetyltransferases and histone deacetylases. J Biol Chem 1991, 266:18745-18750.
    • (1991) J Biol Chem , vol.266 , pp. 18745-18750
    • Lòpez-Rodas, G.1    Georgieva, E.I.2    Sendra, R.3    Loidl, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.