메뉴 건너뛰기




Volumn 12, Issue 5, 1998, Pages 599-606

Histone acetylation and transcriptional regulatory mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE;

EID: 0032030770     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.5.599     Document Type: Review
Times cited : (1595)

References (58)
  • 1
    • 0030959244 scopus 로고    scopus 로고
    • Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression
    • Alland, L., R. Muhle, H. Hou, J. Potes, L. Chin, N. Schreiber-Agus, and R.A. DePinho. 1997. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 387: 49-55.
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L.1    Muhle, R.2    Hou, H.3    Potes, J.4    Chin, L.5    Schreiber-Agus, N.6    DePinho, R.A.7
  • 2
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V., R.M. Faulkner, and A.E. Mirsky. 1964. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. 51: 786-794.
    • (1964) Proc. Natl. Acad. Sci. , vol.51 , pp. 786-794
    • Allfrey, V.1    Faulkner, R.M.2    Mirsky, A.E.3
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A.J. and T. Kouzarides. 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
  • 4
    • 0026645025 scopus 로고
    • Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains
    • Berger, S.L., B. Pina, N. Silverman, G.A. Marcus, J. Agapite, J.L. Regier, S.J. Triezenberg, and L. Guarente. 1992. Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains Cell 70: 251-265.
    • (1992) Cell , vol.70 , pp. 251-265
    • Berger, S.L.1    Pina, B.2    Silverman, N.3    Marcus, G.A.4    Agapite, J.5    Regier, J.L.6    Triezenberg, S.J.7    Guarente, L.8
  • 5
    • 0029953722 scopus 로고    scopus 로고
    • Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern
    • Braunstein, M., R.E. Sobel, C.D. Allis, B.M. Turner, and J.R. Broach. 1996. Efficient transcriptional silencing in Saccharomyces cerevisiae 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
  • 6
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J.E., J. Zhou, T. Ranalli, R. Kobayashi, D.G. Edmondson, S.Y. Roth, and C.D. Allis. 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
  • 7
    • 0030030611 scopus 로고    scopus 로고
    • Identification of functionally conserved human homologues of the yeast adaptors ADA2 and GCN5
    • Candau, R., P. Moore, L. Wang, N. Barlev, C. Ying, C. Rosen, and S. Berger. 1996. Identification of functionally conserved human homologues of the yeast adaptors ADA2 and GCN5. Mol. Cell. Biol. 16: 593-602.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.2    Wang, L.3    Barlev, N.4    Ying, C.5    Rosen, C.6    Berger, S.7
  • 8
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen, H., R.J. Lin, R.L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M.L. Privalsky, Y. Nakatani, and R.M. Evans. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90: 569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 9
    • 0026741634 scopus 로고
    • The TATA-binding protein is required for transcription by all three nuclear RNA polymerases in yeast cells
    • Cormack, B.P. and K. Struhl. 1992. The TATA-binding protein is required for transcription by all three nuclear RNA polymerases in yeast cells. Cell 69: 685-696.
    • (1992) Cell , vol.69 , pp. 685-696
    • Cormack, B.P.1    Struhl, K.2
  • 10
    • 0029805633 scopus 로고    scopus 로고
    • The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
    • DeRubertis, F., D. Kadosh, S. Henchoz, D. Pauli, G. Reuter, K. Struhl, and P. Spierer. 1996. The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast Nature 384: 389-391.
    • (1996) Nature , vol.384 , pp. 389-391
    • DeRubertis, F.1    Kadosh, D.2    Henchoz, S.3    Pauli, D.4    Reuter, G.5    Struhl, K.6    Spierer, P.7
  • 11
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin, L.K., R.K. Mann, P.S. Kayne, and M. Grunstein. 1991. Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell 65: 1023-1031.
    • (1991) Cell , vol.65 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 12
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor TUP1 interacts directly with histones H3 and H4
    • Edmondson, D.G., M.M. Smith, and S.Y. Roth. 1996. Repression domain of the yeast global repressor 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
  • 13
    • 0026764896 scopus 로고
    • SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae
    • Eisenmann, D.M., K.M. Arndt, S.L. Ricupero, J.W. Rooney, and F. Winston. 1992. SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae. Genes & Dev. 6: 1319-1331.
    • (1992) Genes & Dev. , vol.6 , pp. 1319-1331
    • Eisenmann, D.M.1    Arndt, K.M.2    Ricupero, S.L.3    Rooney, J.W.4    Winston, F.5
  • 14
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos, T. and G. Thireos. 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
  • 16
    • 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
  • 17
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W. and R.G. Roeder. 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
  • 18
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig, C.A., T.C. Fleischer, A.N. Billin, S.L. Schreiber, and D.E. Ayer. 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
  • 19
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T.R., A.W. Thorne, and C. Crane-Robinson. 1988. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7: 1395-1402.
    • (1988) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 21
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA
    • Hong, L., G.P. Schroth, H.R. Matthews, P. Yau, and E.M. Bradbury. 1993. Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA. J. Biol. Chem. 268: 305-314.
    • (1993) J. Biol. Chem. , vol.268 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 22
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof, A., X.J. Yang, V.V. Ogryzko, Y. Nakatani, A.P. Wolffe, and H. Ge. 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, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 23
    • 0030570961 scopus 로고    scopus 로고
    • A growing coactivator network
    • Janknecht, R. and T. Hunter. 1996. A growing coactivator network. Nature 383: 22-23.
    • (1996) Nature , vol.383 , pp. 22-23
    • Janknecht, R.1    Hunter, T.2
  • 24
    • 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. and K. Struhl. 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
  • 25
    • 0032520953 scopus 로고    scopus 로고
    • Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo
    • in press
    • _. 1998. Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo. Genes & Dev. 12: (in press).
    • (1998) Genes & Dev. , vol.12
  • 27
    • 0032030906 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo
    • this issue
    • Kuo, M.-H., J. Zhou, P. Jambeck, M.E.A. Churchill, and C.D. Allis. 1998. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. Genes & Dev. 12: (this issue).
    • (1998) Genes & Dev. , vol.12
    • Kuo, M.-H.1    Zhou, J.2    Jambeck, P.3    Churchill, M.E.A.4    Allis, C.D.5
  • 28
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate Mad: Max transcriptional repression
    • Laherty, C., W.-M. Yang, J.-M. Sun, J.R. Davie, E. Seto, and R.N. Eisenman. 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
  • 29
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee, D.Y., J.J. Hayes, D. Pruss, and A.P. Wolffe. 1993. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 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
  • 30
    • 0030771898 scopus 로고    scopus 로고
    • Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
    • Lusser, A., G. Brosch, A. Loidl, H. Haas, and P. Loidl. 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
  • 32
    • 0029811986 scopus 로고    scopus 로고
    • TBP-associated factors are not generally required for transcriptional activation in yeast
    • Moqtaderi, Z., Y. Bai, D. Poon, P.A. Weil, and K. Struhl. 1996. TBP-associated factors are not generally required for transcriptional activation in yeast. Nature 382: 188-191.
    • (1996) Nature , vol.382 , pp. 188-191
    • Moqtaderi, Z.1    Bai, Y.2    Poon, D.3    Weil, P.A.4    Struhl, K.5
  • 33
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSinSA, and histone deacetylase
    • Nagy, L., H.-Y. Kao, D. Chakravarti, R.J. Lin, C.A. Hassig, D.E. Ayer, S.L. Schreiber, and R.M. Evans. 1997. Nuclear receptor repression mediated by a complex containing SMRT, mSinSA, and histone deacetylase. Cell 89: 373-380.
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.-Y.2    Chakravarti, D.3    Lin, R.J.4    Hassig, C.A.5    Ayer, D.E.6    Schreiber, S.L.7    Evans, R.M.8
  • 34
    • 0030902507 scopus 로고    scopus 로고
    • Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcnptional induction via signal-dependent factors
    • Nakajima, T., C. Uchida, S. Anderson, J. Parvin, and M. Montminy. 1997. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcnptional induction via signal-dependent factors. Genes &. Dev. 11: 738-747.
    • (1997) Genes &. Dev. , vol.11 , pp. 738-747
    • Nakajima, T.1    Uchida, C.2    Anderson, S.3    Parvin, J.4    Montminy, M.5
  • 35
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton, V.G., B.S. Imai, P. Yau, and E.M. Bradbury. 1989. Histone acetylation reduces nucleosome core particle linking number change. Cell 57: 449-457.
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 36
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., R.L. Schiltz, V. Russanova, B.H. Howard, and Y. Nakatani. 1996. 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
  • 37
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin, M.J. and J.T. Kadonaga. 1997. What's up and down with histone deacetylation and transcription? Cell 89: 325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 38
    • 0013900616 scopus 로고
    • RNA synthesis and histone acetylation during the course of gene activation in lymphocytes
    • Pogo, B.G.T., V.G. Allfrey, and A.E. Mirsky. 1966. RNA synthesis and histone acetylation during the course of gene activation in lymphocytes. Proc. Natl. Acad. Sci. 55: 805-812.
    • (1966) Proc. Natl. Acad. Sci. , vol.55 , pp. 805-812
    • Pogo, B.G.T.1    Allfrey, V.G.2    Mirsky, A.E.3
  • 39
    • 0030881740 scopus 로고    scopus 로고
    • Role for Ada/Gcn5 products in antagonizing chromatin-mediated transcriptional repression
    • Pollard, K.J. and C.L. Peterson. 1997. Role For Ada/Gcn5 products in antagonizing chromatin-mediated transcriptional repression. Mol. Cell. Biol. 17: 6212-6222.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6212-6222
    • Pollard, K.J.1    Peterson, C.L.2
  • 40
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne, M. and A. Gann. 1997. Transcriptional activation by recruitment. Nature 386: 569-577.
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 42
    • 0017815160 scopus 로고
    • DNA associated with hyperacetylated histone is preferentially digested by DNase I
    • Sealy, L. and R. Chalkley. 1978. DNA associated with hyperacetylated histone is preferentially digested by DNase I. Nucleic Acids Res. 5: 1863-1876.
    • (1978) Nucleic Acids Res. , vol.5 , pp. 1863-1876
    • Sealy, L.1    Chalkley, R.2
  • 43
    • 0031455415 scopus 로고    scopus 로고
    • Histone acetyltransferases regulate HIV-1 enhancer activity in vitro
    • Sheridan, P.L., T.P. Mayall, E. Verdin, and K.A. Jones. 1997. Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes & Dev. 11: 3327-3340.
    • (1997) Genes & Dev. , vol.11 , pp. 3327-3340
    • Sheridan, P.L.1    Mayall, T.P.2    Verdin, E.3    Jones, K.A.4
  • 44
    • 0028104786 scopus 로고
    • Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription
    • Silverman, N., J. Agapite, and L. Guarente. 1994. Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription. Proc. Natl. Acad. Sci. 91: 11665-11668.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 11665-11668
    • Silverman, N.1    Agapite, J.2    Guarente, L.3
  • 46
    • 0030054054 scopus 로고    scopus 로고
    • Chromatin structure and RNA polymerase II connection: Implications for transcription
    • Struhl, K. 1996. Chromatin structure and RNA polymerase II connection: Implications for transcription. Cell 84: 179-182.
    • (1996) Cell , vol.84 , pp. 179-182
    • Struhl, K.1
  • 47
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., C.A. Hassig, and S.L. Schreiber. 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
  • 48
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner, B.M., A.J. Birley, and J. Lavender. 1992. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69: 375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 49
    • 0030465738 scopus 로고    scopus 로고
    • Evidence that the transcriptional regulators, SIN3 and RPD3, and a novel gene (SDS3) with similar functions, are involved in transcriptional silencing in S. cerevisiae
    • Vannier, D., D. Balderes, and D. Shore. 1996. Evidence that the transcriptional regulators, SIN3 and RPD3, and a novel gene (SDS3) with similar functions, are involved in transcriptional silencing in S. cerevisiae. Genetics 144: 1343-1353.
    • (1996) Genetics , vol.144 , pp. 1343-1353
    • Vannier, D.1    Balderes, D.2    Shore, D.3
  • 50
    • 0029985730 scopus 로고    scopus 로고
    • Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNa in vitro
    • Vettese-Dadey, M., P.A. Grant, T.R. Hebbes, C. Crane-Robinson, C.D. Allis, and J.L. Workman. 1996. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J. 15: 2508-2518.
    • (1996) EMBO J. , vol.15 , pp. 2508-2518
    • Vettese-Dadey, M.1    Grant, P.A.2    Hebbes, T.R.3    Crane-Robinson, C.4    Allis, C.D.5    Workman, J.L.6
  • 51
    • 0017867123 scopus 로고
    • Btyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences
    • Vidali, G., L.C. Boffa, E.M. Bradbury, and V.G. Allfrey. 1978. Btyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences. Proc. Natl. Acad. Sci. 75: 2239-2243.
    • (1978) Proc. Natl. Acad. Sci. , vol.75 , pp. 2239-2243
    • Vidali, G.1    Boffa, L.C.2    Bradbury, E.M.3    Allfrey, V.G.4
  • 52
    • 0030940298 scopus 로고    scopus 로고
    • Histone acetylation: Chromatin in action
    • Wade, P.A., D. Pruss, and A.P. Wolffe. 1997. Histone acetylation: Chromatin in action. Trends Biochem Sci. 22: 128-132.
    • (1997) Trends Biochem Sci. , vol.22 , pp. 128-132
    • Wade, P.A.1    Pruss, D.2    Wolffe, A.P.3
  • 54
    • 0032031606 scopus 로고    scopus 로고
    • Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
    • in press
    • Wang, L., L. Liu, and S.L. Berger. 1998. Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes & Dev. 12: (in press).
    • (1998) Genes & Dev. , vol.12
    • Wang, L.1    Liu, L.2    Berger, S.L.3
  • 55
    • 0030033699 scopus 로고    scopus 로고
    • RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling
    • Wilson, C.J., D.M. Chao, A.N. Imbalzano, G.R. Schnitzler, R.E. Kingston, and R.A. Young. 1996. RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling. Cell 84: 235-244.
    • (1996) Cell , vol.84 , pp. 235-244
    • Wilson, C.J.1    Chao, D.M.2    Imbalzano, A.N.3    Schnitzler, G.R.4    Kingston, R.E.5    Young, R.A.6
  • 56
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with the mammalian homolog of the yeast global regulator RPD3
    • Yang, W.-M., C. Inouye, Y. Zeng, D. Bearss, and E. Seto. 1996a. Transcriptional repression by YY1 is mediated by interaction with the mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. 93: 12845-12850.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 12845-12850
    • Yang, W.-M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 57
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X.-J., V.V. Ogryzko, J. Nishikawa, B.H. Howard, and Y. Nakatani. 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
  • 58
    • 0029294663 scopus 로고
    • Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
    • Yoshida, M., S. Horinouchi, and T. Beppu. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.