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Volumn 10, Issue 2, 1999, Pages 179-188

Histone deacetylases: Complex transducers of nuclear signals

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; FUNGAL PROTEIN; HISTONE; HISTONE DEACETYLASE; INSECT PROTEIN; NONHISTONE PROTEIN; TRANSCRIPTION FACTOR; VEGETABLE PROTEIN;

EID: 0033111685     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1999.0299     Document Type: Article
Times cited : (95)

References (81)
  • 1
    • 0030961614 scopus 로고    scopus 로고
    • Histone acetyltransferases in control
    • Wade P, Wolffe A (1997) Histone acetyltransferases in control. Curr Biol 7:R82-84
    • (1997) Curr Biol , vol.7
    • Wade, P.1    Wolffe, A.2
  • 2
    • 0032055037 scopus 로고    scopus 로고
    • Covalent modifications of histones: Expression from chromatin templates
    • Davie JR (1998) Covalent modifications of histones: expression from chromatin templates. Curr Opin Genet Dev 8:173-178
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 173-178
    • Davie, J.R.1
  • 3
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin M, Kadonaga J (1997) What's up and down with histone deacetylation and transcription? Cell 89:325-328
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.1    Kadonaga, J.2
  • 5
    • 1842411320 scopus 로고    scopus 로고
    • X-ray structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Maeder A, Richmond R, Sargent D, Richmond T (1997) X-ray structure of the nucleosome core particle at 2.8 Å resolution. Nature 389
    • (1997) Nature , vol.389
    • Luger, K.1    Maeder, A.2    Richmond, R.3    Sargent, D.4    Richmond, T.5
  • 7
    • 0032055025 scopus 로고    scopus 로고
    • The histone tails of the nucleosome
    • Luger K, Richmond T (1998) The histone tails of the nucleosome. Curr Opin Genet Dev 8:140-146
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 140-146
    • Luger, K.1    Richmond, T.2
  • 8
    • 0030922941 scopus 로고    scopus 로고
    • Hybrid trypsinized nucleosomal arrays: Identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction
    • Tse C, Hansen J (1997) Hybrid trypsinized nucleosomal arrays: identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction. Biochemistry 36:11381-11388
    • (1997) Biochemistry , vol.36 , pp. 11381-11388
    • Tse, C.1    Hansen, J.2
  • 9
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • Garcia-Ramirez M, Rocchini C, Ausio J (1995) Modulation of chromatin folding by histone acetylation. J Biol Chem 270:17923-17928
    • (1995) J Biol Chem , vol.270 , pp. 17923-17928
    • Garcia-Ramirez, M.1    Rocchini, C.2    Ausio, J.3
  • 10
    • 0032055036 scopus 로고    scopus 로고
    • Transcription of chromatin: These are complex times
    • Armstrong JA, Emerson BM (1998) Transcription of chromatin: these are complex times. Curr Opin Genet Dev 8:165-172
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 165-172
    • Armstrong, J.A.1    Emerson, B.M.2
  • 11
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL (1996) A mammalian histone deacetylase related to 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
  • 12
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisae
    • Vidal M, Gaber R (1991) RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisae. Mol Cell Biol 11:6317-6327
    • (1991) Mol Cell Biol , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.2
  • 13
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang W-M, Inouye C, Zeng Y, Bearss D, Seto E (1996) Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc Nad Acad Sci USA 93:12845-12850
    • (1996) Proc Nad Acad Sci USA , vol.93 , pp. 12845-12850
    • Yang, W.-M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 14
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterisation of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang W-M, Yao Y-L, Sun J-M, Davie J, Seto E (1997) Isolation and characterisation 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.4    Seto, E.5
  • 15
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate Mad:Max transcriptional repression
    • Laherty C, Yang W-M, Sun J-M, Davie JR, Seto E, Eisenman RN (1997) Histone deacetylases associated with the mSin3 corepressor mediate Mad:Max transcriptional repression. Cell 89:349-356
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.1    Yang, W.-M.2    Sun, J.-M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 16
    • 0031214668 scopus 로고    scopus 로고
    • Transcriptional control: Calling in histone deacetylase
    • Kiermaier A, Eilers M (1997) Transcriptional control: calling in histone deacetylase. Curr Biol 7:505-507
    • (1997) Curr Biol , vol.7 , pp. 505-507
    • Kiermaier, A.1    Eilers, M.2
  • 17
    • 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
  • 18
    • 17744413444 scopus 로고    scopus 로고
    • A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
    • Heinzel T, Lavinsky R, Mullen T-M, Södersrström M, Laherty C et al (1997) A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387:43-48
    • (1997) Nature , vol.387 , pp. 43-48
    • Heinzel, T.1    Lavinsky, R.2    Mullen, T.-M.3    Södersrström, M.4    Laherty, C.5
  • 20
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A and histone deacetylase
    • Nagy L, Kao H, Chakravarti D, Lin R, Hassig C, Ayer D, Schreiber S, Evans R (1997) Nuclear receptor repression mediated by a complex containing SMRT, mSin3A and histone deacetylase. Cell 89:373-380
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.2    Chakravarti, D.3    Lin, R.4    Hassig, C.5    Ayer, D.6    Schreiber, S.7    Evans, R.8
  • 21
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan X, Hg H-H, 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    Hg, H.-H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 22
    • 0025779831 scopus 로고
    • Histone acetylation and control of gene expression
    • Turner BM (1991) Histone acetylation and control of gene expression. J Cell Sci 99:13-20
    • (1991) J Cell Sci , vol.99 , pp. 13-20
    • Turner, B.M.1
  • 23
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M (1997) Histone acetylation in chromatin structure and transcription. Nature 389:349-352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 26
    • 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
  • 28
    • 0032560117 scopus 로고    scopus 로고
    • Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3
    • Rundlett SE, Carmen AA, Suka NR, Turner B, Grunstein M (1998) Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3. Nature 392:831-835
    • (1998) Nature , vol.392 , pp. 831-835
    • Rundlett, S.E.1    Carmen, A.A.2    Suka, N.R.3    Turner, B.4    Grunstein, M.5
  • 29
    • 0033593347 scopus 로고    scopus 로고
    • Identification of a new family of higher eukaryotic histone deacetylases: Co-ordinate expression of differentiation-dependent chromatin modifiers
    • Verdel A, Khochbin S (1999) Identification of a new family of higher eukaryotic histone deacetylases: co-ordinate 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
  • 31
    • 0032500851 scopus 로고    scopus 로고
    • Molecular cloning of Drosaphila melanogaster cDNAs that encode a novel histone deacetylase dHDAC3
    • Johnson CA, Barlow AL, Turner BM (1998) Molecular cloning of Drosaphila 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
  • 32
    • 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
  • 33
    • 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
  • 35
    • 0032520953 scopus 로고    scopus 로고
    • Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo
    • Kadosh D, Struhl K (1998) Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo. Genes Dev 12:797-805
    • (1998) Genes Dev , vol.12 , pp. 797-805
    • Kadosh, D.1    Struhl, K.2
  • 36
    • 0031434997 scopus 로고    scopus 로고
    • The origin and utility of histone deacetylases
    • Khochbin S, Wolffe AP (1997) The origin and utility of histone deacetylases. FEBS Lett 419:157-160
    • (1997) FEBS Lett , vol.419 , pp. 157-160
    • Khochbin, S.1    Wolffe, A.P.2
  • 37
    • 0030658036 scopus 로고    scopus 로고
    • Xenopus HDm, a maternally expressed histone deacetrylase, belongs to an ancient family of acetyl-metabolising enzymes
    • Ladomery M, Lyons S, Sommerville J (1997) Xenopus HDm, a maternally expressed histone deacetrylase, belongs to an ancient family of acetyl-metabolising enzymes. Gene 198:275-280
    • (1997) Gene , vol.198 , pp. 275-280
    • Ladomery, M.1    Lyons, S.2    Sommerville, J.3
  • 38
    • 0027497020 scopus 로고
    • Identification of genes involved in utilisation of acetate and acetoin in Bacillus subtilis
    • Grundy FJ, Waters DA, Takova TY, Henkin TM (1993) Identification of genes involved in utilisation of acetate and acetoin in Bacillus subtilis. Mol Microbiol 10:259-271
    • (1993) Mol Microbiol , vol.10 , pp. 259-271
    • Grundy, F.J.1    Waters, D.A.2    Takova, T.Y.3    Henkin, T.M.4
  • 39
    • 0029822783 scopus 로고    scopus 로고
    • Acetylpolyamine amidohydrolase from Mycoplana ramosa: Gene cloning and characterisation of the metal-substituted enzyme
    • Sakurada K, Ohta T, Fujishiro K, Hasegawa M, Aisaka K (1996) Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterisation of the metal-substituted enzyme. J Bacteriol 178:5781-5786
    • (1996) J Bacteriol , vol.178 , pp. 5781-5786
    • Sakurada, K.1    Ohta, T.2    Fujishiro, K.3    Hasegawa, M.4    Aisaka, K.5
  • 40
    • 0024266388 scopus 로고
    • Crystallisation and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata
    • Fujishiro K, Ando M, Uwajima T (1988) Crystallisation and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata. Biochem Biophys Res Comm 157: 1169-1174
    • (1988) Biochem Biophys Res Comm , vol.157 , pp. 1169-1174
    • Fujishiro, K.1    Ando, M.2    Uwajima, T.3
  • 41
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee BL, Auld DS (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29:5647-5659
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 42
    • 0000032126 scopus 로고    scopus 로고
    • Depudecin induces morphological reversion of transformed fibroblasts via the inhibition of histone deacetylase
    • Kwon HJ, Owa T, Hassig CA, Shimada J, Schreiber SL (1998) Depudecin induces morphological reversion of transformed fibroblasts via the inhibition of histone deacetylase. Proc Natl Acad Sci USA 95:3356-3361
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3356-3361
    • Kwon, H.J.1    Owa, T.2    Hassig, C.A.3    Shimada, J.4    Schreiber, S.L.5
  • 43
    • 0017886958 scopus 로고
    • Sodium butyrate inhibits histone deacetylation in cultured cells
    • Candido EPM, Reeves R, Davie JR (1978) Sodium butyrate inhibits histone deacetylation in cultured cells. Cell 14: 105-113
    • (1978) Cell , vol.14 , pp. 105-113
    • Candido, E.P.M.1    Reeves, R.2    Davie, J.R.3
  • 44
    • 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
  • 45
    • 0030796349 scopus 로고    scopus 로고
    • Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): Dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway
    • Medina V, Edmonds B, Young GP, James R, Appleton S, Zalewski PD (1997) Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res 57:3697-3707
    • (1997) Cancer Res , vol.57 , pp. 3697-3707
    • Medina, V.1    Edmonds, B.2    Young, G.P.3    James, R.4    Appleton, S.5    Zalewski, P.D.6
  • 46
    • 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 (1995) Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. BioEssays 17:423-430
    • (1995) BioEssays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 47
    • 0025673805 scopus 로고
    • Isolation and structural elucidation of new cyclotetrapeptides, trapoxins A and B, having detransformation activities as antitumour agents
    • Itazaki H, Nagashima K, Sugita K, Yoshida H, Kawamura Y et al (1990) Isolation and structural elucidation of new cyclotetrapeptides, trapoxins A and B, having detransformation activities as antitumour agents. J Antibiot 43:1524-1532
    • (1990) J Antibiot , vol.43 , pp. 1524-1532
    • Itazaki, H.1    Nagashima, K.2    Sugita, K.3    Yoshida, H.4    Kawamura, Y.5
  • 48
    • 0029411482 scopus 로고
    • Inhibition of maize histone deacetylase by HC toxin, the host-selective toxin of Cochliobolus carbonum
    • Brosch G, Ransom R, Lechner T, Walton JD, Loidl P (1995) Inhibition of maize histone deacetylase by HC toxin, the host-selective toxin of Cochliobolus carbonum. Plant Cell 7:1941-1950
    • (1995) Plant Cell , vol.7 , pp. 1941-1950
    • Brosch, G.1    Ransom, R.2    Lechner, T.3    Walton, J.D.4    Loidl, P.5
  • 49
    • 0025083327 scopus 로고
    • Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in friend leukemia cells
    • Yoshida M, Hoshikawa Y, Koseki K, Mori K, Beppu T (1990) Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells. J Antibiot 43:1101-1106
    • (1990) J Antibiot , vol.43 , pp. 1101-1106
    • Yoshida, M.1    Hoshikawa, Y.2    Koseki, K.3    Mori, K.4    Beppu, T.5
  • 51
    • 0028022785 scopus 로고
    • Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines
    • Hoshikawa Y, Kwon HJ, Yoshida M, Horinouchi S, Beppu T (1994) Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp Cell Res 214:189-197
    • (1994) Exp Cell Res , vol.214 , pp. 189-197
    • Hoshikawa, Y.1    Kwon, H.J.2    Yoshida, M.3    Horinouchi, S.4    Beppu, T.5
  • 53
    • 0024817526 scopus 로고
    • Carboxypeptidase A: Mechanism of zinc inhibition
    • Larsen KS, Auld DS (1989) Carboxypeptidase A: mechanism of zinc inhibition. Biochemistry 28:9620-9625
    • (1989) Biochemistry , vol.28 , pp. 9620-9625
    • Larsen, K.S.1    Auld, D.S.2
  • 55
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner BM (1993) Decoding the nucleosome. Cell 75:5-8
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 56
    • 0031963718 scopus 로고    scopus 로고
    • Histone acetylation as an epigenetic determinant of long-term transcriptional competence
    • Turner BM (1998) Histone acetylation as an epigenetic determinant of long-term transcriptional competence. Cell Mol Life Sci 54:21-31
    • (1998) Cell Mol Life Sci , vol.54 , pp. 21-31
    • Turner, B.M.1
  • 57
    • 0031026487 scopus 로고    scopus 로고
    • Histones in transit: Cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells
    • Chang L, Loranger SS, Mizzen C, Ernst SG, Allis CD, Annunziato AT (1997) Histones in transit: cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells. Biochemistry 36:469-480
    • (1997) Biochemistry , vol.36 , pp. 469-480
    • Chang, L.1    Loranger, S.S.2    Mizzen, C.3    Ernst, S.G.4    Allis, C.D.5    Annunziato, A.T.6
  • 59
    • 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 H-P, Lane WS, Reinberg D (1998) 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
  • 60
    • 0024396097 scopus 로고
    • Histone H4 acetylation in human cells; frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies
    • Turner BM, O'Neill LP, Allan IM (1989) Histone H4 acetylation in human cells; frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies. FEBS Lett 253:141-145
    • (1989) FEBS Lett , vol.253 , pp. 141-145
    • Turner, B.M.1    O'Neill, L.P.2    Allan, I.M.3
  • 61
    • 0032519341 scopus 로고    scopus 로고
    • Distinctive patterns of histone H4 acetylation are associated with defined sequence elements within both heterochromatic and euchromatic regions of the human genome
    • Johnson CA, O'Neill LP, Mitchell A, Turner BM (1998) Distinctive patterns of histone H4 acetylation are associated with defined sequence elements within both heterochromatic and euchromatic regions of the human genome. Nucleic Acids Res 26:994-1001
    • (1998) Nucleic Acids Res , vol.26 , pp. 994-1001
    • Johnson, C.A.1    O'Neill, L.P.2    Mitchell, A.3    Turner, B.M.4
  • 62
    • 0029953722 scopus 로고    scopus 로고
    • Efficient transcriptional silencing in Saccharomyces cerevisae requires a heterochromatin histone acetylation pattern
    • Braunstein M, Sobel RE, Allis CD, Turner BM, Broach JR (1996) Efficient transcriptional silencing in Saccharomyces cerevisae requires a heterochromatin histone acetylation pattern. Mol Cell Biol 16:4349-4356
    • (1996) Mol Cell Biol , vol.16 , pp. 4349-4356
    • Braunstein, M.1    Sobel, R.E.2    Allis, C.D.3    Turner, B.M.4    Broach, J.R.5
  • 63
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosaphila polytene nuclei
    • Turner BM, Birley AJ, Lavender J (1992) Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosaphila polytene nuclei. Cell 69:375-384
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 64
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global represser Tup1 interacts directly with histones H3 and H4
    • Edmondson DG, Smith MM, Roth SY (1996) Repression domain of the yeast global represser Tup1 interacts directly with histones H3 and H4. Genes Dev 10:1247-1259
    • (1996) Genes Dev , vol.10 , pp. 1247-1259
    • Edmondson, D.G.1    Smith, M.M.2    Roth, S.Y.3
  • 65
    • 0019877270 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins
    • Sterner R, Vidali G, Allfrey VG (1981) Studies of acetylation and deacetylation in High Mobility Group proteins. J Biol Chem 256:8892-8895
    • (1981) J Biol Chem , vol.256 , pp. 8892-8895
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 66
    • 0024212838 scopus 로고
    • Acetylated alpha-tubulin in microtubules during mouse fertilisation and early development
    • Schatten G, Simerly C, Asal DJ, Szoke E, Cooke P, Schatten H (1988) Acetylated alpha-tubulin in microtubules during mouse fertilisation and early development. Dev Biol 130: 74-86
    • (1988) Dev Biol , vol.130 , pp. 74-86
    • Schatten, G.1    Simerly, C.2    Asal, D.J.3    Szoke, E.4    Cooke, P.5    Schatten, H.6
  • 67
    • 0025811929 scopus 로고
    • Detection of acetylated alpha-tubulin by specific antibodies
    • (Vallee RB, ed), Academic Press, 1991
    • LeDizet M, Piperno G (1991) Detection of acetylated alpha-tubulin by specific antibodies, in Methods in Enzymology (Vallee RB, ed) pp 264-274. Academic Press, 1991
    • (1991) Methods in Enzymology , pp. 264-274
    • LeDizet, M.1    Piperno, G.2
  • 68
    • 0030250994 scopus 로고    scopus 로고
    • 2+) enhancement of alpha-tubulin acetylation in cultured 3T3 cells
    • 2+) enhancement of alpha-tubulin acetylation in cultured 3T3 cells. Toxicol App Pharmacol 140:461-470
    • (1996) Toxicol App Pharmacol , vol.140 , pp. 461-470
    • Li, W.1    Zhao, Y.2    Chou, I.N.3
  • 69
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof A, Yang XJ, Ogryzko W, Nakatani Y, Wolffe AP (1997) Acetylation of general transcription factors by histone acetyltransferases. Curr Biol 7:689-692
    • (1997) Curr Biol , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.J.2    Ogryzko, W.3    Nakatani, Y.4    Wolffe, A.P.5
  • 70
    • 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
  • 73
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80:225-236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 74
    • 0026625939 scopus 로고
    • Immunophilin-sensitive phosphatase action in cell signalling pathways
    • Schreiber SL (1992) Immunophilin-sensitive phosphatase action in cell signalling pathways. Cell 70:365-368
    • (1992) Cell , vol.70 , pp. 365-368
    • Schreiber, S.L.1
  • 75
    • 0026733493 scopus 로고
    • Specificity of Zea mays histone deacetylase is regulated by phosphorylation
    • Brosch G, Georgieva EI, López-Rodas G, Lindner H, Loidl P (1992) Specificity of Zea mays histone deacetylase is regulated by phosphorylation. J Biol Chem 267:20561-20564
    • (1992) J Biol Chem , vol.267 , pp. 20561-20564
    • Brosch, G.1    Georgieva, E.I.2    López-Rodas, G.3    Lindner, H.4    Loidl, P.5
  • 76
    • 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
  • 79
    • 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
  • 80
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg RA (1995) The retinoblastoma protein and cell cycle control. Cell 81:323-330
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1


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