메뉴 건너뛰기




Volumn 370, Issue 3, 2003, Pages 737-749

Histone deacetylases (HDACs): Characterization of the classical HDAC family

Author keywords

Characterization; Co repressor; Gene expression; Histone deacetylase; Inhibitor; Tissue distribution

Indexed keywords

CHEMICAL REACTIONS; CHROMATES; ENZYMES; GENES; ORGANIC SOLVENTS; TISSUE;

EID: 0037444803     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021321     Document Type: Review
Times cited : (2634)

References (125)
  • 1
    • 0035063182 scopus 로고    scopus 로고
    • Transcriptional control at regulatory checkpoints by histone deacetylases: Molecular connections between cancer and chromatin
    • Wade, P. A. (2001) Transcriptional control at regulatory checkpoints by histone deacetylases: molecular connections between cancer and chromatin. Hum. Mol. Genet. 10, 693-698
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 693-698
    • Wade, P.A.1
  • 2
    • 0033821409 scopus 로고    scopus 로고
    • Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12
    • Ito, K., Barnes, P. J. and Adcock, I. M. (2000) Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12 Mol. Cell. Biol, 20, 6891-6903
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6891-6903
    • Ito, K.1    Barnes, P.J.2    Adcock, I.M.3
  • 3
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D. and Allis, C. D. (2000) The language of covalent histone modifications. Nature (London) 403, 41-45
    • (2000) Nature (London) , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 4
    • 0036122494 scopus 로고    scopus 로고
    • Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity
    • Bjerling, P., Silverstein, R. A., Thon, G., Caudy, A., Grewal, S. and Ekwall, K. (2002) Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity. Mol. Cell. Biol. 22, 2170-2181
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2170-2181
    • Bjerling, P.1    Silverstein, R.A.2    Thon, G.3    Caudy, A.4    Grewal, S.5    Ekwall, K.6
  • 5
    • 0034814993 scopus 로고    scopus 로고
    • Histone acetylation beyond promoters: Long-range acetylation patterns in the chromatin world
    • Forsberg, E. C. and Bresnick, E. H. (2001) Histone acetylation beyond promoters: long-range acetylation patterns in the chromatin world. Bioessays 23, 820-830
    • (2001) Bioessays , vol.23 , pp. 820-830
    • Forsberg, E.C.1    Bresnick, E.H.2
  • 6
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress, W. D. and Seto, E. (2000) Histone deacetylases, transcriptional control, and cancer. J. Cell. Physiol. 184, 1-16
    • (2000) J. Cell. Physiol. , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 9
    • 0037082488 scopus 로고    scopus 로고
    • Frequent mutations in the ligand-binding domain of PML-RARalpha after multiple relapses of acute promyelocytic leukemia: Analysis for functional relationship to response to all-trans retinoic acid and histone deacetylase inhibitors in vitro and in vivo
    • Zhou, D. C., Kim, S. H., Ding, W., Schultz, C., Warrell, R. P. J. and Gallagher, R. E. (2002) Frequent mutations in the ligand-binding domain of PML-RARalpha after multiple relapses of acute promyelocytic leukemia: analysis for functional relationship to response to all-trans retinoic acid and histone deacetylase inhibitors in vitro and in vivo. Blood 99, 1356-1363
    • (2002) Blood , vol.99 , pp. 1356-1363
    • Zhou, D.C.1    Kim, S.H.2    Ding, W.3    Schultz, C.4    Warrell, R.P.J.5    Gallagher, R.E.6
  • 10
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster, P. N., Troso-Sandoval, T., Rosen, N., Rifkind, R., Marks, P. A. and Richon, V. M. (2001) The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res. 61, 8492-8497
    • (2001) Cancer Res. , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 11
    • 0035962644 scopus 로고    scopus 로고
    • Histone deacetylases: A common molecular target for differentiation treatment of acute myeloid leukemias?
    • Minucci, S., Nervi, C., Lo, C. F. and Pelicci, P. G. (2001) Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias? Oncogene 20, 3110-3115
    • (2001) Oncogene , vol.20 , pp. 3110-3115
    • Minucci, S.1    Nervi, C.2    Lo, C.F.3    Pelicci, P.G.4
  • 13
    • 0034030355 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor but not arsenic trioxide differentiates acute promyelocytic leukaemia cells with t(11;17) in combination with all-trans retinoic acid
    • Kitamura, K., Hoshi, S., Koike, M., Kiyoi, H., Saito, H. and Naoe, T. (2000) Histone deacetylase inhibitor but not arsenic trioxide differentiates acute promyelocytic leukaemia cells with t(11;17) in combination with all-trans retinoic acid. Br. J. Haematol. 108, 696-702
    • (2000) Br. J. Haematol. , vol.108 , pp. 696-702
    • Kitamura, K.1    Hoshi, S.2    Koike, M.3    Kiyoi, H.4    Saito, H.5    Naoe, T.6
  • 14
    • 0032516221 scopus 로고    scopus 로고
    • Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein
    • David, G., Alland, L., Hong, S. H., Wong, C. W., DePinho, R. A. and Dejean, A. (1998) Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein. Oncogene 16, 2549-2556
    • (1998) Oncogene , vol.16 , pp. 2549-2556
    • David, G.1    Alland, L.2    Hong, S.H.3    Wong, C.W.4    DePinho, R.A.5    Dejean, A.6
  • 15
    • 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
  • 16
    • 0034176798 scopus 로고    scopus 로고
    • DNA hypermethylation in tumorigenesis: Epigenetics joins genetics
    • Baylin, S. B. and Herman, J. G. (2000) DNA hypermethylation in tumorigenesis: epigenetics joins genetics. Trends Genet. 16, 168-174
    • (2000) Trends Genet. , vol.16 , pp. 168-174
    • Baylin, S.B.1    Herman, J.G.2
  • 17
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron, E. E., Bachman, K. E., Myohanen, S., Herman, J. G. and Baylin, S. B. (1999) Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat. Genet. 21, 103-107
    • (1999) Nat. Genet. , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 18
    • 0035477320 scopus 로고    scopus 로고
    • Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyltransferase and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells
    • Yang, X., Phillips, D. L., Ferguson, A. T., Nelson, W. G., Herman, J. G. and Davidson, N. E. (2001) Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyltransferase and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells. Cancer Res. 61, 7025-7029
    • (2001) Cancer Res. , vol.61 , pp. 7025-7029
    • Yang, X.1    Phillips, D.L.2    Ferguson, A.T.3    Nelson, W.G.4    Herman, J.G.5    Davidson, N.E.6
  • 19
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone, R. W. (2002) Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat. Rev. Drug Discovery 1, 287-299
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 20
    • 0035321333 scopus 로고    scopus 로고
    • Role of DNA methylation and histone acetylation in steroid receptor expression in breast cancer
    • Yah, L., Yang, X. and Davidson, N. E. (2001) Role of DNA methylation and histone acetylation in steroid receptor expression in breast cancer. J. Mammary Gland Biol. Neoplasia 6, 183-192
    • (2001) J. Mammary Gland Biol. Neoplasia , vol.6 , pp. 183-192
    • Yah, L.1    Yang, X.2    Davidson, N.E.3
  • 21
    • 0035866353 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors
    • Zhu, W. G., Lakshmanan, R. R., Beal, M. D. and Otterson, G. A. (2001) DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res. 61, 1327-1333
    • (2001) Cancer Res. , vol.61 , pp. 1327-1333
    • Zhu, W.G.1    Lakshmanan, R.R.2    Beal, M.D.3    Otterson, G.A.4
  • 23
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan, L. J., Shia, W. J., Chen, M. H., Yang, W. M., Seto, E., Lin, Y. S. and Wu, C. W. (2000) Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 275, 20436-20443
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1    Shia, W.J.2    Chen, M.H.3    Yang, W.M.4    Seto, E.5    Lin, Y.S.6    Wu, C.W.7
  • 25
    • 0031939919 scopus 로고    scopus 로고
    • Cytotoxic effects of sodium phenylbutyrate on human neuroblastoma cell lines
    • Pelidis, M. A., Carducci, M. A. and Simons, J. W. (1998) Cytotoxic effects of sodium phenylbutyrate on human neuroblastoma cell lines. Int. J. Oncol. 12, 889-893
    • (1998) Int. J. Oncol. , vol.12 , pp. 889-893
    • Pelidis, M.A.1    Carducci, M.A.2    Simons, J.W.3
  • 30
    • 0034739319 scopus 로고    scopus 로고
    • Apicidin, an inhibitor of histone deacetylase, prevents H-ras-induced invasive phenotype
    • Kim, M. S., Son, M. W., Kim, W. B., In, P. Y. and Moon, A. (2000) Apicidin, an inhibitor of histone deacetylase, prevents H-ras-induced invasive phenotype. Cancer Lett. 157, 23-30
    • (2000) Cancer Lett. , vol.157 , pp. 23-30
    • Kim, M.S.1    Son, M.W.2    Kim, W.B.3    In, P.Y.4    Moon, A.5
  • 33
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima, M., Yoshida, M., Sugita, K., Horinouchi, S. and Beppu, T. (1993) Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase. J. Biol. Chem. 268, 22429-22435
    • (1993) J. Biol. Chem. , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 34
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint, C., Emiliani, S. and Verdin, E. (1996) The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expression 5, 245-253
    • (1996) Gene Expression , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 35
    • 0034662614 scopus 로고    scopus 로고
    • Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: Comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer
    • Mariadason, J. M., Corner, G. A. and Augenlicht, L. H. (2000) Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer. Cancer Res. 60, 4561-4572
    • (2000) Cancer Res. , vol.60 , pp. 4561-4572
    • Mariadason, J.M.1    Corner, G.A.2    Augenlicht, L.H.3
  • 36
    • 0036161439 scopus 로고    scopus 로고
    • Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR
    • Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W. and Verdin, E. (2002) Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 9, 45-57
    • (2002) Mol. Cell. , vol.9 , pp. 45-57
    • Fischle, W.1    Dequiedt, F.2    Hendzel, M.J.3    Guenther, M.G.4    Lazar, M.A.5    Voelter, W.6    Verdin, E.7
  • 37
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • Gao, L., Cueto, M. A., Asselbergs, F. and Atadia, P. (2002) Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J. Biol. Chem. 277, 25748-25755
    • (2002) J. Biol. Chem. , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadia, P.4
  • 38
  • 39
    • 0037205476 scopus 로고    scopus 로고
    • Phosphatase inhibition leads to histone deacetylase 1/2 phosphorylation and disruption of co-repressor interactions
    • Galasinski, S. C., Resing, K. A., Goodrich, J. A. and Ahn, N. G. (2002) Phosphatase inhibition leads to histone deacetylase 1/2 phosphorylation and disruption of co-repressor interactions. J. Biol. Chem. 277, 19618-19626
    • (2002) J. Biol. Chem. , vol.277 , pp. 19618-19626
    • Galasinski, S.C.1    Resing, K.A.2    Goodrich, J.A.3    Ahn, N.G.4
  • 43
    • 0034885934 scopus 로고    scopus 로고
    • Class II histone deacetylases: Structure, function, and regulation
    • Bertos, N. R., Wang, A. H. and Yang, X. J. (2001) Class II histone deacetylases: structure, function, and regulation. Biochem. Cell Biol. 79, 243-252
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 243-252
    • Bertos, N.R.1    Wang, A.H.2    Yang, X.J.3
  • 45
    • 0037016696 scopus 로고    scopus 로고
    • Isolation and characterization of mammalian HDAC10, a novel histone deacetylase
    • Kao, H. Y., Lee, C. H., Komarov, A., Han, C. C. and Evans, R. M. (2002) Isolation and characterization of mammalian HDAC10, a novel histone deacetylase. J. Biol. Chem. 277, 187-193
    • (2002) J. Biol. Chem. , vol.277 , pp. 187-193
    • Kao, H.Y.1    Lee, C.H.2    Komarov, A.3    Han, C.C.4    Evans, R.M.5
  • 47
    • 0035861594 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
    • Pflum, M. K., Tong, J. K., Lane, W. S. and Schreiber, S. L. (2001) Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J. Biol. Chem. 276, 47733-47741
    • (2001) J. Biol. Chem. , vol.276 , pp. 47733-47741
    • Pflum, M.K.1    Tong, J.K.2    Lane, W.S.3    Schreiber, S.L.4
  • 48
  • 52
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M., Kijima, M., Akita, M. and Beppu, T. (1990) Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 265, 17174-17179
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 53
    • 0035662888 scopus 로고    scopus 로고
    • Structure of histone deacetylases: Insights into substrate recognition and catalysis
    • Marmorstein, R. (2001) Structure of histone deacetylases: insights into substrate recognition and catalysis. Structure 9, 1127-1133
    • (2001) Structure , vol.9 , pp. 1127-1133
    • Marmorstein, R.1
  • 54
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao, H. Y., Downes, M., Ordentlich, P. and Evans, R. M. (2000) Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev. 14, 55-66
    • (2000) Genes Dev. , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 55
    • 0037087573 scopus 로고    scopus 로고
    • Specific targeting and constitutive association of histone deacetylase complexes during transcriptional repression
    • Li, J., Lin, Q., Wang, W., Wade, P. and Wong, J. (2002) Specific targeting and constitutive association of histone deacetylase complexes during transcriptional repression. Genes Dev. 16, 687-692
    • (2002) Genes Dev. , vol.16 , pp. 687-692
    • Li, J.1    Lin, Q.2    Wang, W.3    Wade, P.4    Wong, J.5
  • 56
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
    • Zhang, Y., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Bird, A. and Reinberg, D. (1999) Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. Genes Dev. 13, 1924-1935
    • (1999) Genes Dev. , vol.13 , pp. 1924-1935
    • Zhang, Y.1    Ng, H.H.2    Erdjument-Bromage, H.3    Tempst, P.4    Bird, A.5    Reinberg, D.6
  • 59
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • Ashburner, B. P., Westerheide, S. D. and Baldwin, A. S. J. (2001) The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol. Cell. Biol. 21, 7065-7077
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin, A.S.J.3
  • 60
    • 0035917322 scopus 로고    scopus 로고
    • Homo-oligomerisation and nuclear localisation of mouse histone deacetylase 1
    • Taplick, J., Kurtev, V., Kroboth, K., Posch, M., Lechner, T. and Seiser, C. (2001) Homo-oligomerisation and nuclear localisation of mouse histone deacetylase 1. J. Mol. Biol. 308, 27-38
    • (2001) J. Mol. Biol. , vol.308 , pp. 27-38
    • Taplick, J.1    Kurtev, V.2    Kroboth, K.3    Posch, M.4    Lechner, T.5    Seiser, C.6
  • 61
    • 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
  • 62
    • 0033152491 scopus 로고    scopus 로고
    • Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes
    • Koipally, J., Renold, A., Kim, J. and Georgopoulos, K. (1999) Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes. EMBO J. 18, 3090-3100
    • (1999) EMBO J. , vol.18 , pp. 3090-3100
    • Koipally, J.1    Renold, A.2    Kim, J.3    Georgopoulos, K.4
  • 63
    • 0035968274 scopus 로고    scopus 로고
    • SMRTE inhibits MEF2C transcriptional activation by targeting HDAC4 and 5 to nuclear domains
    • Wu, X., Li, H., Park, E. J. and Chen, J. D. (2001) SMRTE inhibits MEF2C transcriptional activation by targeting HDAC4 and 5 to nuclear domains. J. Biol. Chem. 276, 24177-24185
    • (2001) J. Biol. Chem. , vol.276 , pp. 24177-24185
    • Wu, X.1    Li, H.2    Park, E.J.3    Chen, J.D.4
  • 64
    • 0035837658 scopus 로고    scopus 로고
    • Paradoxical effects of trichostatin A: Inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and downregulation of cyclin A and B1 mRNA
    • Nair A. R., Boersma, L. J., Schlitz, L., Chaudry, A. and Muschel, R. J. (2001) Paradoxical effects of trichostatin A: inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and downregulation of cyclin A and B1 mRNA. Cancer Lett. 166, 55-64
    • (2001) Cancer Lett. , vol.166 , pp. 55-64
    • Nair, A.R.1    Boersma, L.J.2    Schlitz, L.3    Chaudry, A.4    Muschel, R.J.5
  • 65
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
    • Guenther, M. G., Barak, O. and Lazar, M. A. (2001) The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol. Cell. Biol. 21, 6091-6101
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6091-6101
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 67
    • 0033950652 scopus 로고    scopus 로고
    • Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
    • Zhou, X., Richon, V. M., Rifkind, R. A. and Marks, P. A. (2000) Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5. Proc. Natl. Acad. Sci. U.S.A. 97, 1056-1061
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1056-1061
    • Zhou, X.1    Richon, V.M.2    Rifkind, R.A.3    Marks, P.A.4
  • 68
    • 0035420715 scopus 로고    scopus 로고
    • The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein
    • Nicolas, E., Alt-Si-Ali, S. and Trouche, D. (2001) The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein. Nucleic Acids Res. 29, 3131-3136
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3131-3136
    • Nicolas, E.1    Alt-Si-Ali, S.2    Trouche, D.3
  • 70
    • 0035480033 scopus 로고    scopus 로고
    • Control of muscle development by dueling HATs and HDACs
    • McKinsey, T. A., Zhang, C. L. and Olson, E. N. (2001) Control of muscle development by dueling HATs and HDACs. Curr. Opin. Genet. Dev. 11, 497-504
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 497-504
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 72
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • McKinsey, T. A., Zhang, C. L., Lu, J. and Olson, E. N. (2000) Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature (London) 408, 106-111
    • (2000) Nature (London) , vol.408 , pp. 106-111
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 74
    • 0035384863 scopus 로고    scopus 로고
    • 14-3-3tau associates with and activates the MEF2D transcription factor during musde cell differentiation
    • Choi, S. J., Park, S. Y. and Han, T. H. (2001) 14-3-3tau associates with and activates the MEF2D transcription factor during musde cell differentiation. Nucleic Acids Res. 29, 2836-2842
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2836-2842
    • Choi, S.J.1    Park, S.Y.2    Han, T.H.3
  • 75
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola, A. R. and Yao, T. P. (2002) Molecular cloning and characterization of a novel histone deacetylase HDAC10. J. Biol. Chem. 277, 3350-3356
    • (2002) J. Biol. Chem. , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 76
    • 0036493156 scopus 로고    scopus 로고
    • Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain
    • Tong, J. J., Liu, J., Bertos, N. R. and Yang, X. J. (2002) Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain. Nucleic Acids Res. 30, 1114-1123
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1114-1123
    • Tong, J.J.1    Liu, J.2    Bertos, N.R.3    Yang, X.J.4
  • 78
  • 79
    • 0032577868 scopus 로고    scopus 로고
    • Differential expression of human histone deacetylase mRNAs in response to immune cell apoptosis induction by trichostatin A and butyrate
    • Dangond, F. and Gullans, S. R. (1998) Differential expression of human histone deacetylase mRNAs in response to immune cell apoptosis induction by trichostatin A and butyrate. Biochem. Biophys. Res. Commun. 247, 833-837
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 833-837
    • Dangond, F.1    Gullans, S.R.2
  • 80
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray, S. G. and Ekstrom, T. J. (2001) The human histone deacetylase family. Exp. Cell Res. 262, 75-83
    • (2001) Exp. Cell Res. , vol.262 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 81
    • 0036599352 scopus 로고    scopus 로고
    • Regulation of lifespan by histone deacetylase
    • Chang, K. T. and Min, K. T. (2002) Regulation of lifespan by histone deacetylase. Ageing Res. Rev. 1, 313-326
    • (2002) Ageing Res. Rev. , vol.1 , pp. 313-326
    • Chang, K.T.1    Min, K.T.2
  • 82
    • 0037123767 scopus 로고    scopus 로고
    • Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases
    • Robyr, D.; Suka, Y., Xenarios, I., Kurdistani, S. K., Wang, A., Suka, N. and Grunstein, M. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109, 437-446
    • (2002) Cell , vol.109 , pp. 437-446
    • Robyr, D.1    Suka, Y.2    Xenarios, I.3    Kurdistani, S.K.4    Wang, A.5    Suka, N.6    Grunstein, M.7
  • 83
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai, R., Komatsu, Y., Nishino, N., Khochbin, S., Yoshida, M. and Horinouchi, S. (2001) Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc. Natl. Acad. Sci. U.S.A. 98, 87-92
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 84
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • Kim, Y. B., Lee, K. H., Sugita, K., Yoshida, M. and Horinouchi, S. (1999) Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene 18, 2461-2470
    • (1999) Oncogene , vol.18 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 88
    • 0034885248 scopus 로고    scopus 로고
    • A phase I dose escalation and bioavailability study of oral sodium phenylbutyrate in patients with refractory solid tumor malignancies
    • Gilbert, J., Baker, S. D., Bowling, M. K., Grochow, L., Figg, W. D., Zabelina, Y., Donehower, R. C. and Carducci, M. A. (2001) A phase I dose escalation and bioavailability study of oral sodium phenylbutyrate in patients with refractory solid tumor malignancies. Clin. Cancer Res. 7, 2292-2300
    • (2001) Clin. Cancer Res. , vol.7 , pp. 2292-2300
    • Gilbert, J.1    Baker, S.D.2    Bowling, M.K.3    Grochow, L.4    Figg, W.D.5    Zabelina, Y.6    Donehower, R.C.7    Carducci, M.A.8
  • 89
    • 0036554808 scopus 로고    scopus 로고
    • Impact of prolonged infusions of the putative differentiating agent sodium phenylbutyrate on myelodysplastic syndromes and acute myeloid leukemia
    • Gore, S. D., Weng, L. J., Zhai, S., Figg, W. D., Donehower, R. C., Dover, G. J., Grever, M, Griffin, C. A., Grochow, L. B., Rowinsky, E. K. et al. (2002) Impact of prolonged infusions of the putative differentiating agent sodium phenylbutyrate on myelodysplastic syndromes and acute myeloid leukemia. Clin. Cancer Res. 8, 963-970
    • (2002) Clin. Cancer Res. , vol.8 , pp. 963-970
    • Gore, S.D.1    Weng, L.J.2    Zhai, S.3    Figg, W.D.4    Donehower, R.C.5    Dover, G.J.6    Grever, M.7    Griffin, C.A.8    Grochow, L.B.9    Rowinsky, E.K.10
  • 90
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell, Jr, R. P., He, L. Z., Richon, V., Calleja, E. and Pandolfi, P. P. (1998) Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J. Natl. Cancer Inst. 90, 1621-1625
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 1621-1625
    • Warrell R.P., Jr.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 91
  • 92
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report
    • Piekarz, R. L., Robey, R., Sandor, V., Bakke, S., Wilson, W. H., Dahmoush, L., Kingma, D. M., Turner, M. L., Altemus, R. and Bates, S. E. (2001) Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report. Blood 98, 2865-2868
    • (2001) Blood , vol.98 , pp. 2865-2868
    • Piekarz, R.L.1    Robey, R.2    Sandor, V.3    Bakke, S.4    Wilson, W.H.5    Dahmoush, L.6    Kingma, D.M.7    Turner, M.L.8    Altemus, R.9    Bates, S.E.10
  • 93
    • 0036304760 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A new class of potential therapeutic agents for cancer treatment: Commentary
    • Richon, V. M. and O'Brien, J. P. (2002) Histone deacetylase inhibitors: a new class of potential therapeutic agents for cancer treatment: commentary. Clin. Cancer Res. 8, 662-664
    • (2002) Clin. Cancer Res. , vol.8 , pp. 662-664
    • Richon, V.M.1    O'Brien, J.P.2
  • 95
    • 0036787922 scopus 로고    scopus 로고
    • Association of class II histone deacetylases with heterochromatin protein 1: Potential role for histone methylation in control of muscle differentiation
    • Zhang, C. L., McKinsey, T. A. and Olson, E. N. (2002) Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation. Mol. Cell. Biol. 22, 7302-7312
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7302-7312
    • Zhang, C.L.1    McKinsey, T.A.2    Olson, E.N.3
  • 96
    • 0034124166 scopus 로고    scopus 로고
    • A novel histone deacetylase inhibitor identified by high-throughput transcriptional screening of a compound library
    • Su, G. H., Sohn, T. A., Ryu, B. and Kern, S. E. (2000) A novel histone deacetylase inhibitor identified by high-throughput transcriptional screening of a compound library. Cancer Res. 60, 3137-3142
    • (2000) Cancer Res. , vol.60 , pp. 3137-3142
    • Su, G.H.1    Sohn, T.A.2    Ryu, B.3    Kern, S.E.4
  • 97
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228
    • Yu, X., Guo, Z. S., Marcu, M. G., Neckers, L., Nguyen, D. M., Chen, G. A and Schrump, D. S. (2002) Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J. Natl. Cancer Inst. 94, 504-513
    • (2002) J. Natl. Cancer Inst. , vol.94 , pp. 504-513
    • Yu, X.1    Guo, Z.S.2    Marcu, M.G.3    Neckers, L.4    Nguyen, D.M.5    Chen, G.A.6    Schrump, D.S.7
  • 99
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma
    • Glick, R. D., Swendeman, S. L., Coffey, D. C., Rifkind, R. A., Marks, P. A. Richon, V. M. and La Quaglia, M. P. (1999) Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma. Cancer Res. 59, 4392-4399
    • (1999) Cancer Res. , vol.59 , pp. 4392-4399
    • Glick, R.D.1    Swendeman, S.L.2    Coffey, D.C.3    Rifkind, R.A.4    Marks, P.A.5    Richon, V.M.6    La Quaglia, M.P.7
  • 100
    • 0034326799 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/Cip1 and gelsolin
    • Han, J. W., Ahn, S. H., Park, S. H., Wang, S. Y., Bae, G. U., Seo, D. W., Kwon, H. K., Hong, S., Lee, H. Y., Lee, Y. W. and Lee, H. W. (2000) Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/Cip1 and gelsolin. Cancer Res. 60, 6068-6074
    • (2000) Cancer Res. , vol.60 , pp. 6068-6074
    • Han, J.W.1    Ahn, S.H.2    Park, S.H.3    Wang, S.Y.4    Bae, G.U.5    Seo, D.W.6    Kwon, H.K.7    Hong, S.8    Lee, H.Y.9    Lee, Y.W.10    Lee, H.W.11
  • 101
    • 0034901985 scopus 로고    scopus 로고
    • Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo
    • Vigushin, D. M., Ali, S., Pace, P. E., Mirsaidi, N., Ito, K., Adcock, I. and Coombes, R. C. (2001) Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo. Clin. Cancer Res. 7, 971-976
    • (2001) Clin. Cancer Res. , vol.7 , pp. 971-976
    • Vigushin, D.M.1    Ali, S.2    Pace, P.E.3    Mirsaidi, N.4    Ito, K.5    Adcock, I.6    Coombes, R.C.7
  • 102
    • 0035866388 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity by trichostatin A modulates gene expression during mouse embryogenesis without apparent toxicity
    • Nervi, C., Borello, U., Fazi, F., Buffa, V., Pelicci, P. G. and Cossu, G. (2001) Inhibition of histone deacetylase activity by trichostatin A modulates gene expression during mouse embryogenesis without apparent toxicity. Cancer Res. 61, 1247-1249
    • (2001) Cancer Res. , vol.61 , pp. 1247-1249
    • Nervi, C.1    Borello, U.2    Fazi, F.3    Buffa, V.4    Pelicci, P.G.5    Cossu, G.6
  • 103
    • 0035328528 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, CBHA, inhibits growth of human neuroblastoma xenografts in vivo, alone and synergistically with all-trans retinoic acid
    • Coffey, D. C., Kutko, M. C., Glick, R. D., Butler, L. M., Heller, G., Rifkind, R. A., Marks, P. A., Richon, V. M. and La Quaglia, M. P. (2001) The histone deacetylase inhibitor, CBHA, inhibits growth of human neuroblastoma xenografts in vivo, alone and synergistically with all-trans retinoic acid. Cancer Res. 61, 3591-3594
    • (2001) Cancer Res. , vol.61 , pp. 3591-3594
    • Coffey, D.C.1    Kutko, M.C.2    Glick, R.D.3    Butler, L.M.4    Heller, G.5    Rifkind, R.A.6    Marks, P.A.7    Richon, V.M.8    La Quaglia, M.P.9
  • 104
    • 0034105047 scopus 로고    scopus 로고
    • Butyrate and trichostatin A effects on the proliferation/differentiation of human intestinal epithelial cells: Induction of cyclin D3 and p21 expression
    • Siavoshian, S., Segain, J. P., Kornprobst, M., Bonnet, C., Cherbut, C., Galmiche, J. P. and Blottiere, H. M. (2000) Butyrate and trichostatin A effects on the proliferation/differentiation of human intestinal epithelial cells: induction of cyclin D3 and p21 expression. Gut 46, 507-514
    • (2000) Gut , vol.46 , pp. 507-514
    • Siavoshian, S.1    Segain, J.P.2    Kornprobst, M.3    Bonnet, C.4    Cherbut, C.5    Galmiche, J.P.6    Blottiere, H.M.7
  • 106
    • 0034635983 scopus 로고    scopus 로고
    • Stra13 expression is associated with growth arrest and represses transcription through histone deacetylase (HDAC)-dependent and HDAC-independent mechanisms
    • Sun, H. and Taneja, R. (2000) Stra13 expression is associated with growth arrest and represses transcription through histone deacetylase (HDAC)-dependent and HDAC-independent mechanisms. Proc. Natl. Acad. Sci. U.S.A. 97, 4058-4063
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 4058-4063
    • Sun, H.1    Taneja, R.2
  • 107
    • 0034663182 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress IL-2-mediated gene expression prior to induction of apoptosis
    • Koyama, Y., Adachi, M., Sekiya, M., Takekawa, M. and Imai, K. (2000) Histone deacetylase inhibitors suppress IL-2-mediated gene expression prior to induction of apoptosis. Blood 96, 1490-1495
    • (2000) Blood , vol.96 , pp. 1490-1495
    • Koyama, Y.1    Adachi, M.2    Sekiya, M.3    Takekawa, M.4    Imai, K.5
  • 109
    • 0034770423 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors increase p21(WAF1) and induce apoptosis of human myeloma cell lines independent of decreased IL-6 receptor expression
    • Lavelle, D., Chen, Y. H., Hankewych, M. and DeSimone, J. (2001) Histone deacetylase inhibitors increase p21(WAF1) and induce apoptosis of human myeloma cell lines independent of decreased IL-6 receptor expression. Am. J. Hematol. 68, 170-178
    • (2001) Am. J. Hematol. , vol.68 , pp. 170-178
    • Lavelle, D.1    Chen, Y.H.2    Hankewych, M.3    DeSimone, J.4
  • 111
    • 0000032126 scopus 로고    scopus 로고
    • Depudecin induces morphological reversion of transformed fibroblasts via the inhibition of histone deacetylase
    • Kwon, H. J., Owa, T., Hassig, C. A., Shimada, J. and Schreiber, S. L. (1998) Depudecin induces morphological reversion of transformed fibroblasts via the inhibition of histone deacetylase. Proc. Natl. Acad. Sci. U.S.A. 95, 3356-3361
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3356-3361
    • Kwon, H.J.1    Owa, T.2    Hassig, C.A.3    Shimada, J.4    Schreiber, S.L.5
  • 112
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks, P. A., Richon, V. M. and Rifkind, R. A. (2000) Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J. Natl. Cancer Inst. 92, 1210-1216
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 114
    • 0037079677 scopus 로고    scopus 로고
    • Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases
    • Vaute, O., Nicolas, E., Vandel, L. and Trouche, D. (2002) Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases. Nucleic Acids Res. 30, 475-481
    • (2002) Nucleic Acids Res. , vol.30 , pp. 475-481
    • Vaute, O.1    Nicolas, E.2    Vandel, L.3    Trouche, D.4
  • 116
    • 0035854763 scopus 로고    scopus 로고
    • Sodium butyrate induces transcription from the G alpha(I2) gene promoter through multiple Sp1 sites in the promoter and by activating the MEK-ERK signal transduction pathway
    • Yang, J., Kawai, Y., Hanson, R. W. and Arinze, I. J. (2001) Sodium butyrate induces transcription from the G alpha(I2) gene promoter through multiple Sp1 sites in the promoter and by activating the MEK-ERK signal transduction pathway. J. Biol. Chem. 276, 25742-25752
    • (2001) J. Biol. Chem. , vol.276 , pp. 25742-25752
    • Yang, J.1    Kawai, Y.2    Hanson, R.W.3    Arinze, I.J.4
  • 117
    • 0035866341 scopus 로고    scopus 로고
    • Combination of phenylbutyrate and 13-cis retinoic acid inhibits prostate tumor growth and angiogenesis
    • Pili, R., Kruszewski, M. P., Hager, B. W., Lantz, J. and Carducci, M. A. (2001) Combination of phenylbutyrate and 13-cis retinoic acid inhibits prostate tumor growth and angiogenesis. Cancer Res. 61, 1477-1485
    • (2001) Cancer Res. , vol.61 , pp. 1477-1485
    • Pili, R.1    Kruszewski, M.P.2    Hager, B.W.3    Lantz, J.4    Carducci, M.A.5
  • 118
    • 0016334991 scopus 로고
    • Cytostatic activity of chlamydocin, a rapidly inactivated cyclic tetrapeptide
    • Stahelin, H. and Trippmacher, A. (1974) Cytostatic activity of chlamydocin, a rapidly inactivated cyclic tetrapeptide. Eur. J. Cancer 10, 801-808
    • (1974) Eur. J. Cancer , vol.10 , pp. 801-808
    • Stahelin, H.1    Trippmacher, A.2
  • 119
    • 0037085773 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FR901228 enhances adenovirus infection of hematopoietic cells
    • Kitazono, M., Rao, V. K., Robey, R., Aikou, T., Bates, S, Fojo, T. and Goldsmith, M. E. (2002) Histone deacetylase inhibitor FR901228 enhances adenovirus infection of hematopoietic cells. Blood 99, 2248-2251
    • (2002) Blood , vol.99 , pp. 2248-2251
    • Kitazono, M.1    Rao, V.K.2    Robey, R.3    Aikou, T.4    Bates, S.5    Fojo, T.6    Goldsmith, M.E.7
  • 120
    • 0037137896 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis
    • Kwon, H. J., Kim, M. S., Kim, M. J., Nakajima, H. and Kim, K. W. (2002) Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis. Int. J. Cancer 97, 290-296
    • (2002) Int. J. Cancer , vol.97 , pp. 290-296
    • Kwon, H.J.1    Kim, M.S.2    Kim, M.J.3    Nakajima, H.4    Kim, K.W.5
  • 121
    • 0030271680 scopus 로고    scopus 로고
    • Efficacy of dinaline and its methyl and acetyl derivatives against colorectal cancer in vivo and in vitro
    • Seelig, M. H. and Berger, M. R. (1996) Efficacy of dinaline and its methyl and acetyl derivatives against colorectal cancer in vivo and in vitro. Eur. J. Cancer 32A, 1968-1976
    • (1996) Eur. J. Cancer , vol.32 A , pp. 1968-1976
    • Seelig, M.H.1    Berger, M.R.2
  • 123
    • 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. U.S.A. 97, 10014-10019
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 124
    • 0033564458 scopus 로고    scopus 로고
    • Carboxypeptidase A3 (CPA3): A novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells
    • Huang, H., Reed, C. P., Zhang, J. S., Shridhar, V., Wang, L. and Smith, D. I. (1999) Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. Cancer Res. 59, 2981-2988
    • (1999) Cancer Res. , vol.59 , pp. 2981-2988
    • Huang, H.1    Reed, C.P.2    Zhang, J.S.3    Shridhar, V.4    Wang, L.5    Smith, D.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.