메뉴 건너뛰기




Volumn 17, Issue 6, 2007, Pages 708-719

Butyrate mediates decrease of histone acetylation centered on transcription start sites and down-regulation of associated genes

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRIC ACID; HISTONE DEACETYLASE INHIBITOR; RNA POLYMERASE II; TRICHOSTATIN A;

EID: 34250326306     PISSN: 10889051     EISSN: 15495469     Source Type: Journal    
DOI: 10.1101/gr.5540007     Document Type: Article
Times cited : (135)

References (65)
  • 2
    • 0032490917 scopus 로고    scopus 로고
    • Perinuclear localization of chromatin facilitates transcriptional silencing
    • Andrulis, E.D., Neiman, A.M., Zappulla, D.C., and Sternglanz, R. 1998. Perinuclear localization of chromatin facilitates transcriptional silencing. Nature 394: 592-595.
    • (1998) Nature , vol.394 , pp. 592-595
    • Andrulis, E.D.1    Neiman, A.M.2    Zappulla, D.C.3    Sternglanz, R.4
  • 5
    • 31344466008 scopus 로고    scopus 로고
    • DNA methylation and gene silencing in cancer
    • Baylin, S.B. 2005. DNA methylation and gene silencing in cancer. Nat. Clin. Pract. Oncol. (Suppl. 1) 2: S4-11.
    • (2005) Nat. Clin. Pract. Oncol , vol.2 , Issue.SUPPL. 1
    • Baylin, S.B.1
  • 7
    • 30644463203 scopus 로고    scopus 로고
    • Microarray analysis of butyrate regulated genes in colonic epithelial cells
    • Daly, K. and Shirazi-Beechey, S.P. 2006. Microarray analysis of butyrate regulated genes in colonic epithelial cells. DNA Cell Biol. 25: 49-62.
    • (2006) DNA Cell Biol , vol.25 , pp. 49-62
    • Daly, K.1    Shirazi-Beechey, S.P.2
  • 8
    • 31544436888 scopus 로고    scopus 로고
    • Dietary HDAC inhibitors: Time to rethink weak ligands in cancer chemoprevention?
    • Dashwood, R.H., Myzak, M.C., and Ho, E. 2006. Dietary HDAC inhibitors: Time to rethink weak ligands in cancer chemoprevention? Carcinogenesis 27: 344-349.
    • (2006) Carcinogenesis , vol.27 , pp. 344-349
    • Dashwood, R.H.1    Myzak, M.C.2    Ho, E.3
  • 9
    • 0038676409 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity by butyrate
    • Davie, J.R. 2003. Inhibition of histone deacetylase activity by butyrate. J. Nutr. 133: 2485S-2493S.
    • (2003) J. Nutr , vol.133
    • Davie, J.R.1
  • 10
    • 1542344342 scopus 로고    scopus 로고
    • SRC proximal and core promoter elements dictate TAF1 dependence and transcriptional repression by histone deacetylase inhibitors
    • Dehm, S.M., Hilton, T.L., Wang, E.H., and Bonham, K. 2004. SRC proximal and core promoter elements dictate TAF1 dependence and transcriptional repression by histone deacetylase inhibitors. Mol. Cell. Biol. 24: 2296-2307.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2296-2307
    • Dehm, S.M.1    Hilton, T.L.2    Wang, E.H.3    Bonham, K.4
  • 11
    • 24944585561 scopus 로고    scopus 로고
    • Gene expression profiling in response to the histone deacetylase inhibitor BL1521 in neuroblastoma
    • de Ruijter, A.J., Meinsma, R.J., Bosma, P., Kemp, S., Caron, H.N., and van Kuilenburg, A.B. 2005. Gene expression profiling in response to the histone deacetylase inhibitor BL1521 in neuroblastoma. Exp. Cell Res. 309: 451-467.
    • (2005) Exp. Cell Res , vol.309 , pp. 451-467
    • de Ruijter, A.J.1    Meinsma, R.J.2    Bosma, P.3    Kemp, S.4    Caron, H.N.5    van Kuilenburg, A.B.6
  • 12
    • 12344298627 scopus 로고    scopus 로고
    • The paradox of functional heterochromatin
    • Dimitri, P., Corradini, N., Rossi, F., and Verni, F. 2005. The paradox of functional heterochromatin. Bioessays 27: 29-41.
    • (2005) Bioessays , vol.27 , pp. 29-41
    • Dimitri, P.1    Corradini, N.2    Rossi, F.3    Verni, F.4
  • 13
    • 0026020263 scopus 로고
    • Identification of a novel nuclear protein synthesized in growth-arrested human hepatoblastoma HepG2 cells
    • Donadel, G., Garzelli, C., Frank, R., and Gabrielli, F. 1991. Identification of a novel nuclear protein synthesized in growth-arrested human hepatoblastoma HepG2 cells. Eur. J. Biochem. 195: 723-729.
    • (1991) Eur. J. Biochem , vol.195 , pp. 723-729
    • Donadel, G.1    Garzelli, C.2    Frank, R.3    Gabrielli, F.4
  • 14
    • 20444397430 scopus 로고    scopus 로고
    • Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
    • Dou, Y., Milne, T.A., Tackett, A.J., Smith, E.R., Fukuda, A., Wysocka, J., Allis, C.D., Chait, B.T., Hess, J.L., and Roeder, R.G. 2005. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121: 873-885.
    • (2005) Cell , vol.121 , pp. 873-885
    • Dou, Y.1    Milne, T.A.2    Tackett, A.J.3    Smith, E.R.4    Fukuda, A.5    Wysocka, J.6    Allis, C.D.7    Chait, B.T.8    Hess, J.L.9    Roeder, R.G.10
  • 15
    • 14044276343 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors down-regulate bcl-2 expression and induce apoptosis in t(14;18) lymphomas
    • Duan, H., Heckman, C.A., and Boxer, L.M. 2005. Histone deacetylase inhibitors down-regulate bcl-2 expression and induce apoptosis in t(14;18) lymphomas. Mol. Cell. Biol. 25: 1608-1619.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 1608-1619
    • Duan, H.1    Heckman, C.A.2    Boxer, L.M.3
  • 16
    • 0033959619 scopus 로고    scopus 로고
    • Requirement for TAF(II)250 acetyltransferase activity in cell cycle progression
    • Dunphy, E.L., Johnson, T., Auerbach, S.S., and Wang, E.H. 2000. Requirement for TAF(II)250 acetyltransferase activity in cell cycle progression. Mol. Cell. Biol. 20: 1134-1139.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 1134-1139
    • Dunphy, E.L.1    Johnson, T.2    Auerbach, S.S.3    Wang, E.H.4
  • 17
    • 2942605897 scopus 로고    scopus 로고
    • Sodium butyrate induces apoptosis in human hepatoma cells by a mitochondria/caspase pathway, associated with degradation of β-catenin, pRb and Bcl-XL
    • Emanuele, S., D'Anneo, A., Bellavia, G., Vassallo, B., Lauricella, M., De Blasio, A., Vento, R., and Tesoriere, G. 2004. Sodium butyrate induces apoptosis in human hepatoma cells by a mitochondria/caspase pathway, associated with degradation of β-catenin, pRb and Bcl-XL. Eur. J. Cancer 40: 1441-1452.
    • (2004) Eur. J. Cancer , vol.40 , pp. 1441-1452
    • Emanuele, S.1    D'Anneo, A.2    Bellavia, G.3    Vassallo, B.4    Lauricella, M.5    De Blasio, A.6    Vento, R.7    Tesoriere, G.8
  • 18
    • 7444260846 scopus 로고    scopus 로고
    • The ENCODE (ENCyclopedia Of DNA Elements) Project
    • The ENCODE Project Consortium
    • The ENCODE Project Consortium. 2004. The ENCODE (ENCyclopedia Of DNA Elements) Project. Science 306: 636-640.
    • (2004) Science , vol.306 , pp. 636-640
  • 21
    • 14944357254 scopus 로고    scopus 로고
    • Modulation of translation factor's gene expression by histone deacetylase inhibitors in breast cancer cells
    • Goncalves, J., Malta-Vacas, J., Louis, M., Brault, L., Bagrel, D., Monteiro, C., and Brito, M. 2005. Modulation of translation factor's gene expression by histone deacetylase inhibitors in breast cancer cells. Clin. Chem. Lab. Med. 43: 151-156.
    • (2005) Clin. Chem. Lab. Med , vol.43 , pp. 151-156
    • Goncalves, J.1    Malta-Vacas, J.2    Louis, M.3    Brault, L.4    Bagrel, D.5    Monteiro, C.6    Brito, M.7
  • 22
    • 0035834786 scopus 로고    scopus 로고
    • Han, J.W., Ahn, S.H., Kim, Y.K., Bae, G.U., Yoon, J.W., Hong, S., Lee, H.Y., Lee, Y.W., and Lee, H.W. 2001. Activation of p21(WAF1/Cip1) transcription through Sp1 sites by histone deacetylase inhibitor apicidin: Involvement of protein kinase C. J. Biol. Chem. 276: 42084-42090.
    • Han, J.W., Ahn, S.H., Kim, Y.K., Bae, G.U., Yoon, J.W., Hong, S., Lee, H.Y., Lee, Y.W., and Lee, H.W. 2001. Activation of p21(WAF1/Cip1) transcription through Sp1 sites by histone deacetylase inhibitor apicidin: Involvement of protein kinase C. J. Biol. Chem. 276: 42084-42090.
  • 23
    • 29144463657 scopus 로고    scopus 로고
    • Dynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: Analysis at c-fos and c-jun
    • Hazzalin, C.A. and Mahadevan, L.C. 2005. Dynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: Analysis at c-fos and c-jun. PLoS Biol. 3: e393.
    • (2005) PLoS Biol , vol.3
    • Hazzalin, C.A.1    Mahadevan, L.C.2
  • 24
    • 0027170789 scopus 로고
    • Sodium butyrate causes an increase in the block to transcriptional elongation in the c-myc gene in SW837 rectal carcinoma cells
    • Heruth, D.P., Zirnstein, G.W., Bradley, J.F., and Rothberg, P.G. 1993. Sodium butyrate causes an increase in the block to transcriptional elongation in the c-myc gene in SW837 rectal carcinoma cells. J. Biol. Chem. 268: 20466-20472.
    • (1993) J. Biol. Chem , vol.268 , pp. 20466-20472
    • Heruth, D.P.1    Zirnstein, G.W.2    Bradley, J.F.3    Rothberg, P.G.4
  • 25
    • 3142562320 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors regulate p21WAF1 gene expression at the post-transcriptional level in HepG2 cells
    • Hirsch, C.L. and Bonham, K. 2004. Histone deacetylase inhibitors regulate p21WAF1 gene expression at the post-transcriptional level in HepG2 cells. FEBS Lett. 570: 37-40.
    • (2004) FEBS Lett , vol.570 , pp. 37-40
    • Hirsch, C.L.1    Bonham, K.2
  • 26
    • 33645219500 scopus 로고    scopus 로고
    • Primary and compensatory roles for RB family members at cell cycle gene promoters that are deacetylated and downregulated in doxorubicin-induced senescence of breast cancer cells
    • Jackson, J.G. and Pereira-Smith, O.M. 2006. Primary and compensatory roles for RB family members at cell cycle gene promoters that are deacetylated and downregulated in doxorubicin-induced senescence of breast cancer cells. Mol. Cell. Biol. 26: 2501-2510.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2501-2510
    • Jackson, J.G.1    Pereira-Smith, O.M.2
  • 27
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones, P.A. and Baylin, S.B. 2002. The fundamental role of epigenetic events in cancer. Nat. Rev. Genet. 3: 415-428.
    • (2002) Nat. Rev. Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 28
    • 27144451394 scopus 로고    scopus 로고
    • Sodium butyrate sensitizes human glioma cells to TRAIL-mediated apoptosis through inhibition of Cdc2 and the subsequent downregulation of survivin and XIAP
    • Kim, E.H., Kim, H.S., Kim, S.U., Noh, E.J., Lee, J.S., and Choi, K.S. 2005a. Sodium butyrate sensitizes human glioma cells to TRAIL-mediated apoptosis through inhibition of Cdc2 and the subsequent downregulation of survivin and XIAP. Oncogene 24: 6877-6889.
    • (2005) Oncogene , vol.24 , pp. 6877-6889
    • Kim, E.H.1    Kim, H.S.2    Kim, S.U.3    Noh, E.J.4    Lee, J.S.5    Choi, K.S.6
  • 30
    • 0037068754 scopus 로고    scopus 로고
    • The ubiquitous and tissue specific promoters of the human SRC gene are repressed by inhibitors of histone deacetylases
    • Kostyniuk, C.L., Dehm, S.M., Batten, D., and Bonham, K. 2002. The ubiquitous and tissue specific promoters of the human SRC gene are repressed by inhibitors of histone deacetylases. Oncogene 21: 6340-6347.
    • (2002) Oncogene , vol.21 , pp. 6340-6347
    • Kostyniuk, C.L.1    Dehm, S.M.2    Batten, D.3    Bonham, K.4
  • 31
    • 9144274420 scopus 로고    scopus 로고
    • Evidence for distinct mechanisms facilitating transcript elongation through chromatin in vivo
    • Kristjuhan, A. and Svejstrup, J.Q. 2004. Evidence for distinct mechanisms facilitating transcript elongation through chromatin in vivo. EMBO J. 23: 4243-4252.
    • (2004) EMBO J , vol.23 , pp. 4243-4252
    • Kristjuhan, A.1    Svejstrup, J.Q.2
  • 33
    • 3543023310 scopus 로고    scopus 로고
    • Evidence for nucleosome depletion at active regulatory regions genome-wide
    • Lee, C.K., Shibata, Y., Rao, B., Strahl, B.D., and Lieb, J.D. 2004. Evidence for nucleosome depletion at active regulatory regions genome-wide. Nat. Genet. 36: 900-905.
    • (2004) Nat. Genet , vol.36 , pp. 900-905
    • Lee, C.K.1    Shibata, Y.2    Rao, B.3    Strahl, B.D.4    Lieb, J.D.5
  • 34
    • 29244490064 scopus 로고    scopus 로고
    • Control of transcription through intragenic patterns of nucleosome composition
    • Lieb, J.D. and Clarke, N.D. 2005. Control of transcription through intragenic patterns of nucleosome composition. Cell 123: 1187-1190.
    • (2005) Cell , vol.123 , pp. 1187-1190
    • Lieb, J.D.1    Clarke, N.D.2
  • 35
    • 10444282190 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors for the treatment of cancer
    • Lindemann, R.K., Gabrielli, B., and Johnstone, R.W. 2004. Histone-deacetylase inhibitors for the treatment of cancer. Cell Cycle 3: 779-788.
    • (2004) Cell Cycle , vol.3 , pp. 779-788
    • Lindemann, R.K.1    Gabrielli, B.2    Johnstone, R.W.3
  • 36
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison, C., Bailly, D., Peters, A.H., Quivy, J.P., Roche, D., Taddei, A., Lachner, M., Jenuwein, T., and Almouzni, G. 2002. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat. Genet. 30: 329-334.
    • (2002) Nat. Genet , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3    Quivy, J.P.4    Roche, D.5    Taddei, A.6    Lachner, M.7    Jenuwein, T.8    Almouzni, G.9
  • 39
    • 0034646349 scopus 로고    scopus 로고
    • Different functional domains of TAFII250 modulate expression of distinct subsets of mammalian genes
    • O'Brien, T. and Tjian, R. 2000. Different functional domains of TAFII250 modulate expression of distinct subsets of mammalian genes. Proc. Natl. Acad. Sci. 97: 2456-2461.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 2456-2461
    • O'Brien, T.1    Tjian, R.2
  • 41
    • 0037195811 scopus 로고    scopus 로고
    • Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1
    • Piluso, D., Bilan, P., and Capone, J.P. 2002. Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1. J. Biol. Chem. 277: 46799-46808.
    • (2002) J. Biol. Chem , vol.277 , pp. 46799-46808
    • Piluso, D.1    Bilan, P.2    Capone, J.P.3
  • 44
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • Pray-Grant, M.G., Daniel, J.A., Schieltz, D., Yates 3rd, J.R., and Grant, P.A. 2005. Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 433: 434-438.
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates 3rd, J.R.4    Grant, P.A.5
  • 45
    • 27944435825 scopus 로고    scopus 로고
    • Binding sites for metabolic disease related transcription factors inferred at base pair resolution by chromatin immunoprecipitation and genomic microarrays
    • Rada-Iglesias, A., Wallerman, O., Koch, C., Ameur, A., Enroth, S., Clelland, G., Wester, K., Wilcox, S., Dovey, O.M., Ellis, P.D., et al. 2005. Binding sites for metabolic disease related transcription factors inferred at base pair resolution by chromatin immunoprecipitation and genomic microarrays. Hum. Mol. Genet. 14: 3435-3447.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 3435-3447
    • Rada-Iglesias, A.1    Wallerman, O.2    Koch, C.3    Ameur, A.4    Enroth, S.5    Clelland, G.6    Wester, K.7    Wilcox, S.8    Dovey, O.M.9    Ellis, P.D.10
  • 47
    • 23744495968 scopus 로고    scopus 로고
    • Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor α, in response to deacetylase inhibition by valproic acid and trichostatin A
    • Reid, G., Metivier, R., Lin, C.Y., Denger, S., Ibberson, D., Ivacevic, T., Brand, H., Benes, V., Liu, E.T., and Gannon, F. 2005. Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor α, in response to deacetylase inhibition by valproic acid and trichostatin A. Oncogene 24: 4894-4907.
    • (2005) Oncogene , vol.24 , pp. 4894-4907
    • Reid, G.1    Metivier, R.2    Lin, C.Y.3    Denger, S.4    Ibberson, D.5    Ivacevic, T.6    Brand, H.7    Benes, V.8    Liu, E.T.9    Gannon, F.10
  • 48
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon, V.M., Sandhoff, T.W., Rifkind, R.A., and Marks, P.A. 2000. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc. Natl. Acad. Sci. 97: 10014-10019.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 49
    • 0037214386 scopus 로고    scopus 로고
    • Butyrate induced Caco-2 cell apoptosis is mediated via the mitochondrial pathway
    • Ruemmele, F.M., Schwartz, S., Seidman, E.G., Dionne, S., Levy, E., and Lentze, M.J. 2003. Butyrate induced Caco-2 cell apoptosis is mediated via the mitochondrial pathway. Gut 52: 94-100.
    • (2003) Gut , vol.52 , pp. 94-100
    • Ruemmele, F.M.1    Schwartz, S.2    Seidman, E.G.3    Dionne, S.4    Levy, E.5    Lentze, M.J.6
  • 50
    • 0033588973 scopus 로고    scopus 로고
    • Nuclear organization of mammalian genomes. Polar chromosome territories build up functionally distinct higher order compartments
    • Sadoni, N., Langer, S., Fauth, C., Bernardi, G., Cremer, T., Turner, B.M., and Zink, D. 1999. Nuclear organization of mammalian genomes. Polar chromosome territories build up functionally distinct higher order compartments. J. Cell Biol. 146: 1211-1226.
    • (1999) J. Cell Biol , vol.146 , pp. 1211-1226
    • Sadoni, N.1    Langer, S.2    Fauth, C.3    Bernardi, G.4    Cremer, T.5    Turner, B.M.6    Zink, D.7
  • 52
    • 32944462300 scopus 로고    scopus 로고
    • Rapid alteration of microRNA levels by histone deacetylase inhibition
    • Scott, G.K., Mattie, M.D., Berger, C.E., Benz, S.C., and Benz, C.C. 2006. Rapid alteration of microRNA levels by histone deacetylase inhibition. Cancer Res. 66: 1277-1281.
    • (2006) Cancer Res , vol.66 , pp. 1277-1281
    • Scott, G.K.1    Mattie, M.D.2    Berger, C.E.3    Benz, S.C.4    Benz, C.C.5
  • 53
    • 0043269205 scopus 로고    scopus 로고
    • The RNA polymerase II core promoter
    • Smale, S.T. and Kadonaga, J.T. 2003. The RNA polymerase II core promoter. Annu. Rev. Biochem. 72: 449-479.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 449-479
    • Smale, S.T.1    Kadonaga, J.T.2
  • 54
    • 26444589253 scopus 로고    scopus 로고
    • The nuclear-envelope protein and transcriptional repressor LAP2β interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
    • Somech, R., Shaklai, S., Geller, O., Amariglio, N., Simon, A.J., Rechavi, G., and Gal-Yam, E.N. 2005. The nuclear-envelope protein and transcriptional repressor LAP2β interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J. Cell Sci. 118: 4017-4025.
    • (2005) J. Cell Sci , vol.118 , pp. 4017-4025
    • Somech, R.1    Shaklai, S.2    Geller, O.3    Amariglio, N.4    Simon, A.J.5    Rechavi, G.6    Gal-Yam, E.N.7
  • 55
    • 0033636892 scopus 로고    scopus 로고
    • Acetylation regulates transcription factor activity at multiple levels
    • Soutoglou, E., Katrakili, N., and Talianidis, I. 2000. Acetylation regulates transcription factor activity at multiple levels. Mol. Cell 5: 745-751.
    • (2000) Mol. Cell , vol.5 , pp. 745-751
    • Soutoglou, E.1    Katrakili, N.2    Talianidis, I.3
  • 56
    • 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
  • 58
    • 0035147369 scopus 로고    scopus 로고
    • Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases
    • Taddei, A., Maison, C., Roche, D., and Almouzni, G. 2001. Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases. Nat. Cell Biol. 3: 114-120.
    • (2001) Nat. Cell Biol , vol.3 , pp. 114-120
    • Taddei, A.1    Maison, C.2    Roche, D.3    Almouzni, G.4
  • 59
    • 22144434077 scopus 로고    scopus 로고
    • The effects of histone deacetylase inhibitors on heterochromatin: Implications for anticancer therapy?
    • Taddei, A., Roche, D., Bickmore, W.A., and Almouzni, G. 2005. The effects of histone deacetylase inhibitors on heterochromatin: Implications for anticancer therapy? EMBO Rep. 6: 520-524.
    • (2005) EMBO Rep , vol.6 , pp. 520-524
    • Taddei, A.1    Roche, D.2    Bickmore, W.A.3    Almouzni, G.4
  • 60
    • 18144381890 scopus 로고    scopus 로고
    • Cyclooxygenase-2 regulation in colon cancer cells: Modulation of RNA polymerase II elongation by histone deacetylase inhibitors
    • Tong, X., Yin, L., Joshi, S., Rosenberg, D.W., and Giardina, C. 2005. Cyclooxygenase-2 regulation in colon cancer cells: Modulation of RNA polymerase II elongation by histone deacetylase inhibitors. J. Biol. Chem. 280: 15503-15509.
    • (2005) J. Biol. Chem , vol.280 , pp. 15503-15509
    • Tong, X.1    Yin, L.2    Joshi, S.3    Rosenberg, D.W.4    Giardina, C.5
  • 61
    • 4544323749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Understanding a new wave of anticancer agents
    • Villar-Garea, A. and Esteller, M. 2004. Histone deacetylase inhibitors: Understanding a new wave of anticancer agents. Int. J. Cancer 112: 171-178.
    • (2004) Int. J. Cancer , vol.112 , pp. 171-178
    • Villar-Garea, A.1    Esteller, M.2
  • 63
    • 0043180471 scopus 로고    scopus 로고
    • Three-dimensional arrangements of centromeres and telomeres in nuclei of human and murine lymphocytes
    • Weierich, C., Brero, A., Stein, S., von Hase, J., Cremer, C., Cremer, T., and Solovei, I. 2003. Three-dimensional arrangements of centromeres and telomeres in nuclei of human and murine lymphocytes. Chromosome Res. 11: 485-502.
    • (2003) Chromosome Res , vol.11 , pp. 485-502
    • Weierich, C.1    Brero, A.2    Stein, S.3    von Hase, J.4    Cremer, C.5    Cremer, T.6    Solovei, I.7
  • 64
    • 0034905085 scopus 로고    scopus 로고
    • Regulation of transcription factor YY1 by acetylation and deacetylation
    • Yao, Y.L., Yang, W.M., and Seto, E. 2001. Regulation of transcription factor YY1 by acetylation and deacetylation. Mol. Cell. Biol. 21: 5979-5991.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 5979-5991
    • Yao, Y.L.1    Yang, W.M.2    Seto, E.3
  • 65
    • 10644242733 scopus 로고    scopus 로고
    • Histone acetylation regulates both transcription initiation and elongation of hsp22 gene in Drosophila
    • Zhao, Y., Lu, J., Sun, H., Chen, X., Huang, W., Tao, D., and Huang, B. 2005. Histone acetylation regulates both transcription initiation and elongation of hsp22 gene in Drosophila. Biochem. Biophys. Res. Commun. 326: 811-816.
    • (2005) Biochem. Biophys. Res. Commun , vol.326 , pp. 811-816
    • Zhao, Y.1    Lu, J.2    Sun, H.3    Chen, X.4    Huang, W.5    Tao, D.6    Huang, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.