메뉴 건너뛰기




Volumn 35, Issue 4, 2005, Pages 363-378

Differential effects of histone deacetylase inhibitors in tumor and normal cells - What is the toxicological relevance?

Author keywords

Apoptosis; Differentiation; Hepatoma Cells; Histone Deacetylase Inhibitor; Pharmacotoxicology; Preclinical Drug Development; Primary Hepatocytes; Proliferation; Trichostatin A

Indexed keywords

3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; 4 PHENYLBUTYRIC ACID; 6 (1,3 DIOXO 1H,3H BENZO[DE]ISOQUINOLIN 2 YL) N HYDROXYHEXANAMIDE; ANTINEOPLASTIC AGENT; APICIDIN; AZELAIC BISHYDROXAMIC ACID; BENZAMIDE; BUTYRIC ACID; CCAAT ENHANCER BINDING PROTEIN; CYCLIC HYDROXAMIC ACID CONTAINING PEPTIDE; CYCLIN D; CYCLIN DEPENDENT KINASE 7; CYCLIN E; CYTOSTATIC AGENT; DEOXYCYTIDINE; DEPSIPEPTIDE; FR 901228; HC TOXIN; HEPATOCYTE NUCLEAR FACTOR 3; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; HYDROXAMIC ACID DERIVATIVE; INDOLE AMIDE HYDROXAMIC ACID; INTERLEUKIN 6; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; OXAMFLATIN; PHENYLALANINE DERIVATIVE; PROTEIN BAX; PROTEIN BCL 2; PROTEIN P21; PYROXAMIDE; SUCCINAMIDE HYDROXAMIC ACID; SULFONAMIDE HYDROXAMIC ACID; TETRAPEPTIDE; TRAPOXIN; TRICHOSTATIN A; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 18844407076     PISSN: 10408444     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408440590935639     Document Type: Review
Times cited : (54)

References (213)
  • 1
    • 0032917188 scopus 로고    scopus 로고
    • Differentiation-related changes in the cell cycle traverse
    • Studzinski, G.P., and Harrison, L.E. (1999). Differentiation-related changes in the cell cycle traverse. Int. Rev. Cytol. 189:1-58.
    • (1999) Int. Rev. Cytol. , vol.189 , pp. 1-58
    • Studzinski, G.P.1    Harrison, L.E.2
  • 2
    • 0042933857 scopus 로고    scopus 로고
    • The cell cycle, chromatin and cancer: Mechanism-based therapeutics come of age
    • McLaughlin, F., Finn, P., and La Thangue, N.B. (2003). The cell cycle, chromatin and cancer: Mechanism-based therapeutics come of age. Drug Discov. Today 8:793-802.
    • (2003) Drug Discov. Today , vol.8 , pp. 793-802
    • McLaughlin, F.1    Finn, P.2    La Thangue, N.B.3
  • 3
    • 0344393019 scopus 로고    scopus 로고
    • Perspectives on cancer therapy: Cell cycle blockers and perturbators
    • Dobashi, Y., Takehana, T., and Ooi, A. (2003). Perspectives on cancer therapy: Cell cycle blockers and perturbators. Curr. Med. Chem. 10:2549-2558.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 2549-2558
    • Dobashi, Y.1    Takehana, T.2    Ooi, A.3
  • 4
    • 0038245253 scopus 로고    scopus 로고
    • Small molecules as inhibitors of cyclin-dependent kinases
    • Huwe, A., Mazitschek, R., and Giannis, A. (2003). Small molecules as inhibitors of cyclin-dependent kinases. Angew. Chem. Int. Ed. 42:2122-2138.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 2122-2138
    • Huwe, A.1    Mazitschek, R.2    Giannis, A.3
  • 6
    • 0038052805 scopus 로고    scopus 로고
    • The cell cycle: A review of regulation, deregulation and therapeutic targets in cancer
    • Vermeulen, K., Van Bockstaele, D.R., and Berneman, Z.N. (2003). The cell cycle: A review of regulation, deregulation and therapeutic targets in cancer. Cell Prolif. 36:131-149.
    • (2003) Cell Prolif. , vol.36 , pp. 131-149
    • Vermeulen, K.1    Van Bockstaele, D.R.2    Berneman, Z.N.3
  • 7
    • 0033154454 scopus 로고    scopus 로고
    • Discovery of new anti-cancer agents
    • Lobbezoo, M.W., Krul, M.R., and Pinedo, H.M. (1999). Discovery of new anti-cancer agents. Forum (Geneva) 9(Suppl. 3):47-53.
    • (1999) Forum (Geneva) , vol.9 , Issue.3 SUPPL. , pp. 47-53
    • Lobbezoo, M.W.1    Krul, M.R.2    Pinedo, H.M.3
  • 8
    • 0036817873 scopus 로고    scopus 로고
    • Targeting intracellular signal transduction. A new paradigm for a brave new world of molecularly targeted therapeutics
    • Beeram, M., and Patnaik, A. (2002). Targeting intracellular signal transduction. A new paradigm for a brave new world of molecularly targeted therapeutics. Hematol. Oncol. Clin. North Am. 16:1089-1100.
    • (2002) Hematol. Oncol. Clin. North Am. , vol.16 , pp. 1089-1100
    • Beeram, M.1    Patnaik, A.2
  • 9
    • 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
  • 10
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman, J.L., and Kingston, R.E. (1998). Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67:545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 11
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides, T. (1999). Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9:40-48.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 13
    • 0033868452 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases: A new strategy to target epigenetic modifications for anticancer treatment
    • Weidle, U.H., and Grossmann, A. (2000). Inhibition of histone deacetylases: A new strategy to target epigenetic modifications for anticancer treatment. Anticancer Res. 20:1471-1485.
    • (2000) Anticancer Res. , vol.20 , pp. 1471-1485
    • Weidle, U.H.1    Grossmann, A.2
  • 14
    • 0038408486 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion
    • Liu, L.-T., Chang, H.-C., Chiang, L.-C., and Hung, W.-C. (2003). Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion. Cancer Res. 63:3069-3072.
    • (2003) Cancer Res. , vol.63 , pp. 3069-3072
    • Liu, L.-T.1    Chang, H.-C.2    Chiang, L.-C.3    Hung, W.-C.4
  • 16
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity
    • Lee, Y.M., Kim, S.-H., Kim, H.-S., Son, M.J., Nakajima, H., Kwon, H.J., and Kim, K.-W. (2003). Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity. Biochem. Biophys. Res. Commun. 300:241-246.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 241-246
    • Lee, Y.M.1    Kim, S.-H.2    Kim, H.-S.3    Son, M.J.4    Nakajima, H.5    Kwon, H.J.6    Kim, K.-W.7
  • 17
    • 0034899511 scopus 로고    scopus 로고
    • Trichostatin A, an inhibitor of histone deacetylase, inhibits hypoxia-induced angiogenesis
    • Williams, R.J. (2001). Trichostatin A, an inhibitor of histone deacetylase, inhibits hypoxia-induced angiogenesis. Expert Opin. Invest. Drugs 10:1571-1573.
    • (2001) Expert Opin. Invest. Drugs , vol.10 , pp. 1571-1573
    • Williams, R.J.1
  • 18
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • Rössig, L., Li, H., Fisslthaler, B., Urbich, C., Fleming, I., Förstermann, U., Zeiher, A.M., and Dimmeler, S. (2002). Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. Circ. Res. 91:837-844.
    • (2002) Circ. Res. , vol.91 , pp. 837-844
    • Rössig, L.1    Li, H.2    Fisslthaler, B.3    Urbich, C.4    Fleming, I.5    Förstermann, U.6    Zeiher, A.M.7    Dimmeler, S.8
  • 20
    • 0042261694 scopus 로고    scopus 로고
    • Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors
    • Sasakawa, Y., Naoe, Y., Takahisa, N., Inoue, T., Sasakawa, T., Matsuo, M., Manda, T., and Mutoh, S. (2003). Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors. Biochem. Pharmacol. 66:897-906.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 897-906
    • Sasakawa, Y.1    Naoe, Y.2    Takahisa, N.3    Inoue, T.4    Sasakawa, T.5    Matsuo, M.6    Manda, T.7    Mutoh, S.8
  • 21
    • 0036947771 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors such as sodium butyrate and trichostatin A inhibit vascular endothelial growth factor (VEGF) secretion from human glioblastoma cells
    • Sawa, H., Murakami, H., Ohshima, Y., Murakami, M., Yamazaki, I., Tamura, Y., Mima, T., Satone, A., Ide, W., Hashimoto, I., and Karnada, H. (2002). Histone deacetylase inhibitors such as sodium butyrate and trichostatin A inhibit vascular endothelial growth factor (VEGF) secretion from human glioblastoma cells. Brain Tumor Pathol. 19:77-81.
    • (2002) Brain Tumor Pathol. , vol.19 , pp. 77-81
    • Sawa, H.1    Murakami, H.2    Ohshima, Y.3    Murakami, M.4    Yamazaki, I.5    Tamura, Y.6    Mima, T.7    Satone, A.8    Ide, W.9    Hashimoto, I.10    Karnada, H.11
  • 23
    • 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., Park, Y.I., 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    Park, Y.I.4    Moon, A.5
  • 24
    • 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
  • 25
    • 0033367018 scopus 로고    scopus 로고
    • Chemoprevention of carcinogen-induced mammary tumorigenesis by the hybrid polar cytodifferentiation agent, suberoylanilohydroxamic acid (SAHA)
    • Cohen, L.A., Amin, S., Marks, P.A., Rifkind, R.A., Desai, D., and Richon, V.M. (1999). Chemoprevention of carcinogen-induced mammary tumorigenesis by the hybrid polar cytodifferentiation agent, suberoylanilohydroxamic acid (SAHA). Anticancer Res. 19:4999-5005.
    • (1999) Anticancer Res. , vol.19 , pp. 4999-5005
    • Cohen, L.A.1    Amin, S.2    Marks, P.A.3    Rifkind, R.A.4    Desai, D.5    Richon, V.M.6
  • 26
    • 0036323115 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA), a histone deacetylase inhibitor, suppresses the growth of carcinogen-induced mammary tumors
    • Cohen, L.A., Marks, P.A., Rifkind, R. A., Amin, S., Desai, D., Pittman, B., and Richon, V. M. (2002). Suberoylanilide hydroxamic acid (SAHA), a histone deacetylase inhibitor, suppresses the growth of carcinogen-induced mammary tumors. Anticancer Res. 22:1497-1504.
    • (2002) Anticancer Res. , vol.22 , pp. 1497-1504
    • Cohen, L.A.1    Marks, P.A.2    Rifkind, R.A.3    Amin, S.4    Desai, D.5    Pittman, B.6    Richon, V.M.7
  • 27
    • 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, H., 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, H.5    Rifkind, R.A.6    Marks, P.A.7    Richon, V.M.8    La Quaglia, M.P.9
  • 28
  • 33
    • 0033672431 scopus 로고    scopus 로고
    • Modifying histones to tame cancer: Clinical development of sodium phenylbutyrate and other histone deacetylase inhibitors
    • Gore, S.D., and Garducci, M.A. (2000). Modifying histones to tame cancer: Clinical development of sodium phenylbutyrate and other histone deacetylase inhibitors. Expert Opin. Invest. Drugs 9:2923-2934.
    • (2000) Expert Opin. Invest. Drugs , vol.9 , pp. 2923-2934
    • Gore, S.D.1    Garducci, M.A.2
  • 34
    • 0035965343 scopus 로고    scopus 로고
    • Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
    • Phiel, C.J., Zhang, F., Huang, E.Y., Guenther, M.G., Lazar, M.A., and Klein, P.S. (2001). Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 276:36734-36741.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36734-36741
    • Phiel, C.J.1    Zhang, F.2    Huang, E.Y.3    Guenther, M.G.4    Lazar, M.A.5    Klein, P.S.6
  • 36
    • 0036890347 scopus 로고    scopus 로고
    • Gap junctions as targets for cancer chemoprevention and chemotherapy
    • Trosko, J.E., and Ruch, R.J. (2002). Gap junctions as targets for cancer chemoprevention and chemotherapy. Curr. Drug Targets 3:465-482.
    • (2002) Curr. Drug Targets , vol.3 , pp. 465-482
    • Trosko, J.E.1    Ruch, R.J.2
  • 37
    • 0035232487 scopus 로고    scopus 로고
    • Cooperation of liver cells in health and disease
    • Kmiec, Z. (2001). Cooperation of liver cells in health and disease. Adv. Anat. Embryol. Cell Biol. 161(3-13):1-151.
    • (2001) Adv. Anat. Embryol. Cell Biol. , vol.161 , Issue.3-13 , pp. 1-151
    • Kmiec, Z.1
  • 39
    • 0033011049 scopus 로고    scopus 로고
    • Analysis of cytochrome P450 and phase II conjugating enzyme expression in adult male rat hepatocytes
    • Davila, F., and Morris, D.L. (1999). Analysis of cytochrome P450 and phase II conjugating enzyme expression in adult male rat hepatocytes. In Vitro Cell. Dev. Biol. Anim. 35:120-130.
    • (1999) In Vitro Cell. Dev. Biol. Anim. , vol.35 , pp. 120-130
    • Davila, F.1    Morris, D.L.2
  • 40
    • 0141806810 scopus 로고    scopus 로고
    • Cell cultures as in vitro tools for biotransformation studies
    • ed. S.G. Pandalai, Kerala, India: Transworld Research Network
    • Papeleu, P., Elaut, G., Rogiers, V., and Vanhaecke, T. (2002). Cell cultures as in vitro tools for biotransformation studies. In Recent Research Developments in Drug Metabolism and Disposition, Vol. 1, ed. S.G. Pandalai, pp. 199-234. Kerala, India: Transworld Research Network.
    • (2002) Recent Research Developments in Drug Metabolism and Disposition , vol.1 , pp. 199-234
    • Papeleu, P.1    Elaut, G.2    Rogiers, V.3    Vanhaecke, T.4
  • 42
    • 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 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 43
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury, E.M. (1992). Reversible histone modifications and the chromosome cell cycle. BioEssays 14:9-16.
    • (1992) BioEssays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 44
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V., Faulkner, R.M., and Mirsky, A.E. (1964). Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA 51:786-794.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.1    Faulkner, R.M.2    Mirsky, A.E.3
  • 45
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl, P. (1994). Histone acetylation: Facts and questions. Chromosoma 103:441-449.
    • (1994) Chromosoma , vol.103 , pp. 441-449
    • Loidl, P.1
  • 46
    • 0002083859 scopus 로고    scopus 로고
    • Sinful repression
    • Wolfe, A.P. (1997). Sinful repression. Nature 387:16-17.
    • (1997) Nature , vol.387 , pp. 16-17
    • Wolfe, A.P.1
  • 47
    • 0027916769 scopus 로고
    • Histone deacetylase - A key enzyme for the binding of regulatory proteins to chromatin
    • Lopez-Rodas, G., Brosch, G., Georgieva, E.I., Sendra, R., Franco, L., and Loidl, P. (1993). Histone deacetylase - A key enzyme for the binding of regulatory proteins to chromatin. FEBS Lett. 317:175-180.
    • (1993) FEBS Lett. , vol.317 , pp. 175-180
    • Lopez-Rodas, G.1    Brosch, G.2    Georgieva, E.I.3    Sendra, R.4    Franco, L.5    Loidl, P.6
  • 49
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R.G. (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
  • 50
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes, J., Byfield, P., Nakatami, Y., and Ogryzko, V. (1998). Regulation of activity of the transcription factor GATA-1 by acetylation. Nature (Lond.) 396:594-598.
    • (1998) Nature (Lond.) , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatami, Y.3    Ogryzko, V.4
  • 51
    • 0031861729 scopus 로고    scopus 로고
    • Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y
    • Jin, S., and Scotto, K.W. (1998). Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y. Mol. Cell Biol. 18:4377-4384.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4377-4384
    • Jin, S.1    Scotto, K.W.2
  • 52
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof, A., Yang, Y.J., Ogryzko, V.V., Nakatani, Y., Wolffe, A.P., and Ge, H. (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, Y.J.2    Ogryzko, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 53
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • Munshi, N., Merika, M., Yie, J., Senger, K., Chen, G., and Thanos, D. (1998). Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. Mol. Cell 2:457-467.
    • (1998) Mol. Cell , vol.2 , pp. 457-467
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 56
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A., and Schreiber, S.L. (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
  • 57
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization 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.R., and Seto, E. (1997). Isolation and characterization 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.R.4    Seto, E.5
  • 60
  • 62
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray, S.G., and Ekström, 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    Ekström, T.J.2
  • 63
    • 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 Atadja, 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    Atadja, P.4
  • 64
    • 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
  • 65
    • 0343416249 scopus 로고    scopus 로고
    • Histone deacetylases: Silencers for hire
    • Ng, H.H., and Bird, A. (2000). Histone deacetylases: Silencers for hire. Trends Biochem. Sci. 25:121-126.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 121-126
    • Ng, H.H.1    Bird, A.2
  • 67
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3
    • Li, J., Wang, J., Nawaz, Z., Liu, J.M., Qin, J., and Wong, J. (2000). Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. EMBO J. 19:4342-4350.
    • (2000) EMBO J. , vol.19 , pp. 4342-4350
    • Li, J.1    Wang, J.2    Nawaz, Z.3    Liu, J.M.4    Qin, J.5    Wong, J.6
  • 72
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska, E.A., Karlsson, C., Langley, E., Nielsen, S.J., Pines, J., and Kouzarides, T. (1999). HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 18:5099-5107.
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1    Karlsson, C.2    Langley, E.3    Nielsen, S.J.4    Pines, J.5    Kouzarides, T.6
  • 73
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hdalp
    • Grozinger, C.M., Hassig, C.A., and Schreiber, S.L. (1999). Three proteins define a class of human histone deacetylases related to yeast Hdalp. Proc. Natl. Acad. Sci. USA 96:4868-4873.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 74
    • 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
  • 76
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye, R.A. (1999). Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260:273-279.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 78
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R.A. (2000). Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273:793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 79
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of 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 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
  • 81
    • 0035024737 scopus 로고    scopus 로고
    • Histone deacetylase: A target for antiproliferative and antiprotozoal agents
    • Meinke, P.T., and Liberator, P. (2001). Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr. Med. Chem. 8:211-235.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 211-235
    • Meinke, P.T.1    Liberator, P.2
  • 82
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute myelocytic leukemia
    • Warrell, R.P., He, L.Z., Richon, V.M., Calleja, E., and Pandolfi, P.P. (1998) Therapeutic targeting of transcription in acute myelocytic leukemia. JNCI 90:1621-1625.
    • (1998) JNCI , vol.90 , pp. 1621-1625
    • Warrell, R.P.1    He, L.Z.2    Richon, V.M.3    Calleja, E.4    Pandolfi, P.P.5
  • 87
    • 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. USA 98:87-92.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 88
    • 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
  • 90
    • 0033520944 scopus 로고    scopus 로고
    • Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects
    • Sambucetti, L.C., Fischer, D.D., Zabludoff, S., Kwon, P.O., Chamberlin, H., Trogani, N., Xu, H., and Cohen, D. (1999). Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects. J. Biol. Chem. 274:34940-34947.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34940-34947
    • Sambucetti, L.C.1    Fischer, D.D.2    Zabludoff, S.3    Kwon, P.O.4    Chamberlin, H.5    Trogani, N.6    Xu, H.7    Cohen, D.8
  • 91
    • 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
  • 92
    • 0036775301 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo
    • Sasakawa, Y., Naoe, Y., Inoue, T., Sasakawa, T., Matsuo, M., Manda, T., and Mutoh, S. (2002). Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo. Biochem. Pharmacol. 64:1079-1090.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1079-1090
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6    Mutoh, S.7
  • 93
    • 0035113602 scopus 로고    scopus 로고
    • MS-275, a histone deacetylase inhibitor, selectively induced transforming growth factor β type II receptor expression in human breast cancer cells
    • Lee, B.I., Park, S.H., Kim, J.W., Sausville, E.A., Kim, H.T., Nakanishi, O., Trepel, J.B., and Kim, S.J. (2001). MS-275, a histone deacetylase inhibitor, selectively induced transforming growth factor β type II receptor expression in human breast cancer cells. Cancer Res. 91:931-934.
    • (2001) Cancer Res. , vol.91 , pp. 931-934
    • Lee, B.I.1    Park, S.H.2    Kim, J.W.3    Sausville, E.A.4    Kim, H.T.5    Nakanishi, O.6    Trepel, J.B.7    Kim, S.J.8
  • 94
    • 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
  • 95
    • 0029946960 scopus 로고    scopus 로고
    • Oxamflatin: A novel compound which reverses malignant phenotype to normal one via induction of junD
    • Sonoda, H., Nishida, K., Yoshioka, T., Ohtani, M., and Sugita, K. (1996). Oxamflatin: A novel compound which reverses malignant phenotype to normal one via induction of junD. Oncogene 13:143-149.
    • (1996) Oncogene , vol.13 , pp. 143-149
    • Sonoda, H.1    Nishida, K.2    Yoshioka, T.3    Ohtani, M.4    Sugita, K.5
  • 96
    • 18844441264 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of hi stone deacetylase and inducers of terminal cell differentiation
    • Jung, M., Brosch, G., Kolle, D., Scherf, H.,Gerhauser, C., and Loidl, P. (1999). Amide analogues of trichostatin A as inhibitors of hi stone deacetylase and inducers of terminal cell differentiation. J. Med. Chem. 8:1505-1511.
    • (1999) J. Med. Chem. , vol.8 , pp. 1505-1511
    • Jung, M.1    Brosch, G.2    Kolle, D.3    Scherf, H.4    Gerhauser, C.5    Loidl, P.6
  • 99
  • 103
    • 0029998412 scopus 로고    scopus 로고
    • (2E)-5-[3-[Phenylsulfonylamino]phenyl]-pent-2-en-4-ynohydroxamic acid and its derivatives as novel and potent inhibitors of ras transformation
    • Ohtani, M., Matsuura, T., Shirase, K., and Sugita, K. (1996). (2E)-5-[3-[Phenylsulfonyl)amino]phenyl]-pent-2-en-4-ynohydroxamic acid and its derivatives as novel and potent inhibitors of ras transformation. J. Med. Chem. 39:2871-2873.
    • (1996) J. Med. Chem. , vol.39 , pp. 2871-2873
    • Ohtani, M.1    Matsuura, T.2    Shirase, K.3    Sugita, K.4
  • 104
    • 0037130244 scopus 로고    scopus 로고
    • Structure-activity relationships on phenylalanine-containing inhibitors of histone deacetylase: In vitro enzyme inhibition, induction of differentiation, and inhibition of proliferation in Friend leukemic cells
    • Wittich, S., Scherf, H., Xie, C., Brosch, G., Loidl, P., Gerhäuser, C., and Jung, M. (2002). Structure-activity relationships on phenylalanine-containing inhibitors of histone deacetylase: In vitro enzyme inhibition, induction of differentiation, and inhibition of proliferation in Friend leukemic cells. J. Med. Chem. 45:3296-3309.
    • (2002) J. Med. Chem. , vol.45 , pp. 3296-3309
    • Wittich, S.1    Scherf, H.2    Xie, C.3    Brosch, G.4    Loidl, P.5    Gerhäuser, C.6    Jung, M.7
  • 105
    • 0035927427 scopus 로고    scopus 로고
    • 3-(4-Aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors
    • Massa, S., Mai, A., Sbardella, G., Esposito, M., Ragno, R., Loidl, P., and Brosch, G. (2001). 3-(4-Aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors. J. Med. Chem. 44:2069-2072.
    • (2001) J. Med. Chem. , vol.44 , pp. 2069-2072
    • Massa, S.1    Mai, A.2    Sbardella, G.3    Esposito, M.4    Ragno, R.5    Loidl, P.6    Brosch, G.7
  • 107
    • 0037335407 scopus 로고    scopus 로고
    • Hydroxamide derivatives of short-chain fatty acids are potent inducers of human fetal globin gene expression
    • Skarpidi, E., Cao, H., Heltweg, V., White, B.F., Marhenke, R.L., Jung, M., and Stammatoyannopoulos, G. (2003). Hydroxamide derivatives of short-chain fatty acids are potent inducers of human fetal globin gene expression. Exp. Haematol. 31:197-203.
    • (2003) Exp. Haematol. , vol.31 , pp. 197-203
    • Skarpidi, E.1    Cao, H.2    Heltweg, V.3    White, B.F.4    Marhenke, R.L.5    Jung, M.6    Stammatoyannopoulos, G.7
  • 108
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2 and down-regulates thioredoxin
    • Butler, L.M., Zhou, X., Xu, W.S., Sher, H.I., Rifkind, R.A., Marks, P.A., and Richon, V.M. (2002). The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2 and down-regulates thioredoxin. Proc. Natl. Acad. Sci. USA 99:11700-11705.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3    Sher, H.I.4    Rifkind, R.A.5    Marks, P.A.6    Richon, V.M.7
  • 111
    • 0034086168 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells
    • Qiu, L., Burgess, A., Fairlie, D.P., Leonard, H., Parsons, P.G., and Gabrielli, B.G. (2000). Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells. Mol Biol. Cell 11:2069-2083.
    • (2000) Mol Biol. Cell , vol.11 , pp. 2069-2083
    • Qiu, L.1    Burgess, A.2    Fairlie, D.P.3    Leonard, H.4    Parsons, P.G.5    Gabrielli, B.G.6
  • 112
    • 0036086135 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and anticancer therapy
    • Kouraklis, G., and Theocharis, S. (2002). Histone deacetylase inhibitors and anticancer therapy. Curr. Med. Chem. 2:477-4484.
    • (2002) Curr. Med. Chem. , vol.2 , pp. 477-4484
    • Kouraklis, G.1    Theocharis, S.2
  • 113
    • 0038544192 scopus 로고    scopus 로고
    • Histone deacetylase in carcinogenesis and its inhibitors as anti-cancer agents
    • Kim, D.H., Kim, M., and Kwon, H.J. (2003). Histone deacetylase in carcinogenesis and its inhibitors as anti-cancer agents. J. Biochem. Mol. Biol. 36:110-119.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 110-119
    • Kim, D.H.1    Kim, M.2    Kwon, H.J.3
  • 114
    • 0042830316 scopus 로고    scopus 로고
    • Trichostatin A induces differential cell cycle arrests but does not induce apoptosis in primary cultures of mitogen-stimulated rat hepatocytes
    • Papeleu, P., Loyer, P., Vanhaecke, T., Elaut, G., Geerts, A., Guguen-Guillouzo, C., and Rogiers, V. (2003). Trichostatin A induces differential cell cycle arrests but does not induce apoptosis in primary cultures of mitogen-stimulated rat hepatocytes. J. Hepatol. 39:374-382.
    • (2003) J. Hepatol. , vol.39 , pp. 374-382
    • Papeleu, P.1    Loyer, P.2    Vanhaecke, T.3    Elaut, G.4    Geerts, A.5    Guguen-Guillouzo, C.6    Rogiers, V.7
  • 115
    • 0036171675 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor Trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells
    • Herold, C., Ganslmayer, M., Ocker, M., Hermann, M., Geerts, A., Hahn, E.G., and Schuppan, D. (2002). The histone deacetylase inhibitor Trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells. J. Hepatol. 36:233-240.
    • (2002) J. Hepatol. , vol.36 , pp. 233-240
    • Herold, C.1    Ganslmayer, M.2    Ocker, M.3    Hermann, M.4    Geerts, A.5    Hahn, E.G.6    Schuppan, D.7
  • 116
    • 0037455825 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor trichostatin A induces cell cycle arrest/apoptosis and hepatocyte differentiation in human hepatoma cells
    • Yamashita, Y., Shimada, M., Harimoto, N., Rikimaru, T., Shirabe, K., Tanaka, S., and Sugimachi, K. (2003). Histone deacetylase inhibitor trichostatin A induces cell cycle arrest/apoptosis and hepatocyte differentiation in human hepatoma cells. Int. J. Cancer 103:572-576.
    • (2003) Int. J. Cancer , vol.103 , pp. 572-576
    • Yamashita, Y.1    Shimada, M.2    Harimoto, N.3    Rikimaru, T.4    Shirabe, K.5    Tanaka, S.6    Sugimachi, K.7
  • 117
    • 0032540122 scopus 로고    scopus 로고
    • Effects of cell density and trichostatin A on the expression of HDAC1 and p57Kip2 in Hep3B cells
    • Gray, S.G., and Ekström, T.J. (1998). Effects of cell density and trichostatin A on the expression of HDAC1 and p57Kip2 in Hep3B cells. Biochem. Biophys. Res. Commun. 245:423-427.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 423-427
    • Gray, S.G.1    Ekström, T.J.2
  • 118
    • 0028145285 scopus 로고
    • Expression and activation of cdks (1 and 2) and cyclins in the cell cycle progression during liver regeneration
    • Loyer, P., Glaise, D., Cariou, S., Baffet, G., Meijer, L., and Guguen-Guillouzo, C. (1994). Expression and activation of cdks (1 and 2) and cyclins in the cell cycle progression during liver regeneration. J. Biol. Chem. 269:2491-2500.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2491-2500
    • Loyer, P.1    Glaise, D.2    Cariou, S.3    Baffet, G.4    Meijer, L.5    Guguen-Guillouzo, C.6
  • 120
    • 0032499756 scopus 로고    scopus 로고
    • P21 (WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells
    • Archer, S.Y., Meng, S., Shei, A., and Hodin, R.A. (1998). p21 (WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc. Natl. Acad. Sci. USA 95:6791-6796.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6791-6796
    • Archer, S.Y.1    Meng, S.2    Shei, A.3    Hodin, R.A.4
  • 121
    • 0033822112 scopus 로고    scopus 로고
    • p21-dependent G1 arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228
    • Sandor, V., Senderowicz, A., Mertins, S., Sackett, D., Sausville, E., Blagosklonny, M.V., and Bates, S.E. (2000). p21-dependent G1 arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228. Br. J. Cancer 83:817-825.
    • (2000) Br. J. Cancer , vol.83 , pp. 817-825
    • Sandor, V.1    Senderowicz, A.2    Mertins, S.3    Sackett, D.4    Sausville, E.5    Blagosklonny, M.V.6    Bates, S.E.7
  • 123
    • 0034706893 scopus 로고    scopus 로고
    • Activation of the p21 promoter independent of p53 by the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) through the Sp1 sites
    • Huang, L., Sowa, Y., Sakai, T., and Pardee, A.B. (2000). Activation of the p21 promoter independent of p53 by the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) through the Sp1 sites. Oncogene 19:5712-5719.
    • (2000) Oncogene , vol.19 , pp. 5712-5719
    • Huang, L.1    Sowa, Y.2    Sakai, T.3    Pardee, A.B.4
  • 124
    • 0042905956 scopus 로고    scopus 로고
    • Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: Defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines
    • Glaser, K.B., Staver, M.J., Waring, J.F., Stender, J., Ulrich, R.G., and Davidsen, S.K. (2003). Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: Defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines. Mol. Cancer Ther. 2:151-163.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 151-163
    • Glaser, K.B.1    Staver, M.J.2    Waring, J.F.3    Stender, J.4    Ulrich, R.G.5    Davidsen, S.K.6
  • 125
    • 0034721941 scopus 로고    scopus 로고
    • Inhibition of mitogenesis in Balb/c-3T3 cells by Trichostatin A. Multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes
    • Wharton, W., Savell, J., Cress, W.D., Seto, E., and Pledger, W.J. (2000). Inhibition of mitogenesis in Balb/c-3T3 cells by Trichostatin A. Multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes. J. Biol. Chem. 275:33981-33987.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33981-33987
    • Wharton, W.1    Savell, J.2    Cress, W.D.3    Seto, E.4    Pledger, W.J.5
  • 126
    • 0037315344 scopus 로고    scopus 로고
    • Selective E2F-dependent gene transcription is controlled by histone deacetylase activity during neuronal apoptosis
    • Boutillier, A.-L., Trinh, E., and Loeffler, J.-P. (2003). Selective E2F-dependent gene transcription is controlled by histone deacetylase activity during neuronal apoptosis. J. Neurochem. 84:814-828.
    • (2003) J. Neurochem. , vol.84 , pp. 814-828
    • Boutillier, A.-L.1    Trinh, E.2    Loeffler, J.-P.3
  • 127
    • 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 Exp. 5:245-253.
    • (1996) Gene Exp. , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 128
    • 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
    • Mariadson, J., Corner, G., and Augenlicht, L. (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
    • Mariadson, J.1    Corner, G.2    Augenlicht, L.3
  • 129
    • 0036205092 scopus 로고    scopus 로고
    • Expression profile analysis of trichostatin A in human gastric cancer cells
    • Lee, H., Lee, S., Baek, M., Kim, H.-Y., and Jeoung, D.-I. (2002). Expression profile analysis of trichostatin A in human gastric cancer cells. Biotech. Lett. 24:377-381.
    • (2002) Biotech. Lett. , vol.24 , pp. 377-381
    • Lee, H.1    Lee, S.2    Baek, M.3    Kim, H.-Y.4    Jeoung, D.-I.5
  • 130
    • 3242732116 scopus 로고    scopus 로고
    • Effect of the histone deacetylase inhibitor Trichostatin A on spontaneous apoptosis in various adult rat hepatocyte cultures
    • Vanhaecke, T., Henkens, T., Kass, G., and Rogiers, V. (2004). Effect of the histone deacetylase inhibitor Trichostatin A on spontaneous apoptosis in various adult rat hepatocyte cultures. Biochem. Pharmacol. 68:753-760.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 753-760
    • Vanhaecke, T.1    Henkens, T.2    Kass, G.3    Rogiers, V.4
  • 131
    • 0035873906 scopus 로고    scopus 로고
    • Effects of epidermal growth factor on CYP inducibility by xenobiotics, DNA replication, and caspase activations in collagen I gel sandwich cultures of rat hepatocytes
    • De Smet, K., Loyer, P., Gilot, D., Vercruysse, A., Guguen-Guillouzo, C., and Rogiers, V. (2001). Effects of epidermal growth factor on CYP inducibility by xenobiotics, DNA replication, and caspase activations in collagen I gel sandwich cultures of rat hepatocytes. Biochem. Pharmacol. 61:1293-1303.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 1293-1303
    • De Smet, K.1    Loyer, P.2    Gilot, D.3    Vercruysse, A.4    Guguen-Guillouzo, C.5    Rogiers, V.6
  • 133
    • 0036200587 scopus 로고    scopus 로고
    • Liver-enriched transcription factors in liver function and development. Part 1: The hepatocyte nuclear factor network and liver-specific gene expression
    • Schrem, H., Klempnauer, J., and Borlak, J. (2002) Liver-enriched transcription factors in liver function and development. Part 1: The hepatocyte nuclear factor network and liver-specific gene expression. Pharmacol. Rev. 54:129-158.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 129-158
    • Schrem, H.1    Klempnauer, J.2    Borlak, J.3
  • 134
    • 0038241793 scopus 로고    scopus 로고
    • HNF4: A central regulator of hepatocyte differentiation and function
    • Watt, A.J., Garrison, W.D., and Duncan, S.A. (2003). HNF4: A central regulator of hepatocyte differentiation and function. Hepatology 37:1249-1253.
    • (2003) Hepatology , vol.37 , pp. 1249-1253
    • Watt, A.J.1    Garrison, W.D.2    Duncan, S.A.3
  • 135
    • 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
  • 136
    • 0034724671 scopus 로고    scopus 로고
    • Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins
    • Soutoglou, E., Papafotiou, G., Katrakili, N., and Talianidis, I. (2000). Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins. J. Biol. Chem. 275:12515-12520.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12515-12520
    • Soutoglou, E.1    Papafotiou, G.2    Katrakili, N.3    Talianidis, I.4
  • 137
    • 0031652740 scopus 로고    scopus 로고
    • Phenotypic characterization of rat hepatoma cell lines and lineage-specific regulation of gene expression by differentiation agents
    • Zvibel, I., Fiorino, A.S., Shlomo, B., and Lola, M.R. (1998). Phenotypic characterization of rat hepatoma cell lines and lineage-specific regulation of gene expression by differentiation agents. Differentiation 63:215-223.
    • (1998) Differentiation , vol.63 , pp. 215-223
    • Zvibel, I.1    Fiorino, A.S.2    Shlomo, B.3    Lola, M.R.4
  • 138
    • 0030957866 scopus 로고    scopus 로고
    • Effect of the histone deacetylase inhibitor Trichostatin A on the responsiveness of rat hepatocytes to dioxin
    • Xu, L., Ruh, T.S., and Ruh, M.R (1997). Effect of the histone deacetylase inhibitor Trichostatin A on the responsiveness of rat hepatocytes to dioxin. Biochem. Pharmacol. 53:951-957.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 951-957
    • Xu, L.1    Ruh, T.S.2    Ruh, M.R.3
  • 139
    • 0034090310 scopus 로고    scopus 로고
    • Mammalian hepatocyte differentiation requires the transcription factor HNF-4α
    • Li, J., Ning, G., and Duncan, S.A. (2000). Mammalian hepatocyte differentiation requires the transcription factor HNF-4α. Genes Dev. 14:464-474.
    • (2000) Genes Dev. , vol.14 , pp. 464-474
    • Li, J.1    Ning, G.2    Duncan, S.A.3
  • 140
    • 0033105622 scopus 로고    scopus 로고
    • Upstream region of rat serum albumin gene promoter contributes to promoter activity: Presence of functional binding site for hepatocyte nuclear factor-3
    • Hsiang, C.H., Marten, N.W., and Straus, D.S. (1999). Upstream region of rat serum albumin gene promoter contributes to promoter activity: Presence of functional binding site for hepatocyte nuclear factor-3. Biochem. J. 338:241-249.
    • (1999) Biochem. J. , vol.338 , pp. 241-249
    • Hsiang, C.H.1    Marten, N.W.2    Straus, D.S.3
  • 141
    • 0025811870 scopus 로고
    • The different tissue transcription patterns of genes for HNF-1, CEBP, HNF-3 and HNF-4, protein factors that govern liver-specific transcription
    • Xanthopoulos, K.G., Prezioso, V.R., Chen, W.S., Sladek, F.M., Cortese, F.M., Cortese, R., and Darnell, J.E., Jr. (1991). The different tissue transcription patterns of genes for HNF-1, C[EBP, HNF-3 and HNF-4, protein factors that govern liver-specific transcription. Proc. Natl. Acad. Sci. USA 88:3807-3811.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3807-3811
    • Xanthopoulos, K.G.1    Prezioso, V.R.2    Chen, W.S.3    Sladek, F.M.4    Cortese, F.M.5    Cortese, R.6    Darnell Jr., J.E.7
  • 144
    • 0037428248 scopus 로고    scopus 로고
    • Differential effects of trichostatin A on gelatinase a expression in 3T3 fibroblasts and HT-1080 fibrosarcoma cells: Implications for use of TSA in cancer therapy
    • Ailenberg, M., and Silverman, M. (2003). Differential effects of trichostatin A on gelatinase A expression in 3T3 fibroblasts and HT-1080 fibrosarcoma cells: Implications for use of TSA in cancer therapy. Biochem. Biophys. Res. Commun. 302:181-185.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 181-185
    • Ailenberg, M.1    Silverman, M.2
  • 145
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid and p53 in the apoptotic response triggered by histone deacetylase inhibitors TSA and SAHA
    • Henderson, C., Mizzau, M., Paroni, G., Maestro, R., Schneider, C., and Brancolini, C. (2003). Role of caspases, Bid and p53 in the apoptotic response triggered by histone deacetylase inhibitors TSA and SAHA. J. Biol. Chem. 278:12579-12589.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 146
    • 0033556077 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as potential anti-skin cancer agents
    • Saunders, N., Dicker, A., Popa, C., Jones, S., and Dahler, A. (1999). Histone deacetylase inhibitors as potential anti-skin cancer agents. Cancer Res. 59:399-404.
    • (1999) Cancer Res. , vol.59 , pp. 399-404
    • Saunders, N.1    Dicker, A.2    Popa, C.3    Jones, S.4    Dahler, A.5
  • 147
    • 0031465731 scopus 로고    scopus 로고
    • p21/p53, cellular growth control and genomic integrity
    • El-Deiry, W.S. (1998). p21/p53, cellular growth control and genomic integrity. Curr. Top. Microbiol. Immunol. 227:121-137.
    • (1998) Curr. Top. Microbiol. Immunol. , vol.227 , pp. 121-137
    • El-Deiry, W.S.1
  • 148
    • 0029956387 scopus 로고    scopus 로고
    • Protective role of p21(Waf1/Cip1) against prostaglandin A2-mediated apoptosis of human colorectal carcinoma cells
    • Gorospe, M., Wang, X., Guyton, K.Z., and Holbrook, N.J. (1996). Protective role of p21(Waf1/Cip1) against prostaglandin A2-mediated apoptosis of human colorectal carcinoma cells. Mol. Cell. Biol. 16:6654-6660.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6654-6660
    • Gorospe, M.1    Wang, X.2    Guyton, K.Z.3    Holbrook, N.J.4
  • 149
    • 0030902111 scopus 로고    scopus 로고
    • p21(Waf1/Cip1) protects against p53-mediated apoptosis of human melanoma cells
    • Gorospe, M., Cirielli, C., Wang, X., Seth, P., Capogrossi, M.C., and Holbrook, N.J. (1997). p21(Waf1/Cip1) protects against p53-mediated apoptosis of human melanoma cells. Oncogene 14:929-935.
    • (1997) Oncogene , vol.14 , pp. 929-935
    • Gorospe, M.1    Cirielli, C.2    Wang, X.3    Seth, P.4    Capogrossi, M.C.5    Holbrook, N.J.6
  • 151
    • 0029996726 scopus 로고    scopus 로고
    • Resistance to apoptosis conferred by Cdk inhibitors during myocyte differentiation
    • Wang, J., and Walsh, K. (1996). Resistance to apoptosis conferred by Cdk inhibitors during myocyte differentiation. Science 273:359-361.
    • (1996) Science , vol.273 , pp. 359-361
    • Wang, J.1    Walsh, K.2
  • 152
    • 0029811984 scopus 로고    scopus 로고
    • Genetic determinants of p53-induced apoptosis and growth arrest
    • Polyak, K., Waldman, T., He, T.C., Kinzler, K.W., and Vogelstein, B. (1996). Genetic determinants of p53-induced apoptosis and growth arrest. Genes Dev. 10:1945-1952.
    • (1996) Genes Dev. , vol.10 , pp. 1945-1952
    • Polyak, K.1    Waldman, T.2    He, T.C.3    Kinzler, K.W.4    Vogelstein, B.5
  • 153
    • 0033008429 scopus 로고    scopus 로고
    • Quercetin inhibited DNA synthesis and induced apoptosis associated with increase in c-fos mRNA level and the upregulation of p21WAF1CIP1 mRNA and protein expression during liver regeneration after partial hepatectomy
    • Iwao, K., and Tsukamoto, I. (1999). Quercetin inhibited DNA synthesis and induced apoptosis associated with increase in c-fos mRNA level and the upregulation of p21WAF1CIP1 mRNA and protein expression during liver regeneration after partial hepatectomy. Biochim. Biophys. Acta 1427:112-120.
    • (1999) Biochim. Biophys. Acta , vol.1427 , pp. 112-120
    • Iwao, K.1    Tsukamoto, I.2
  • 154
    • 0035958630 scopus 로고    scopus 로고
    • Prolonged Jun N-terminal (JNK) activation and the upregulation of p53 and p21 preceded apoptosis in hepatocytes after partial hepatectomy and cisplatin
    • Kobayashi, K., and Tsukamoto, I. (2001). Prolonged Jun N-terminal (JNK) activation and the upregulation of p53 and p21 preceded apoptosis in hepatocytes after partial hepatectomy and cisplatin. Biochim. Biophys. Acta 1537:79-88.
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 79-88
    • Kobayashi, K.1    Tsukamoto, I.2
  • 156
  • 157
  • 158
    • 0033166302 scopus 로고    scopus 로고
    • Interferon gamma induces the expression of p21waf-1 and arrests macrophage cell cycle, preventing induction of apoptosis
    • Xaus, J., Cardo, M., Valledor, A.F., Soler, C., Lloberas, J., and Celada, A. (1999). Interferon gamma induces the expression of p21waf-1 and arrests macrophage cell cycle, preventing induction of apoptosis. Immunity 11:103-113.
    • (1999) Immunity , vol.11 , pp. 103-113
    • Xaus, J.1    Cardo, M.2    Valledor, A.F.3    Soler, C.4    Lloberas, J.5    Celada, A.6
  • 159
    • 0035921430 scopus 로고    scopus 로고
    • Simple keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targetting modulation
    • Gilbert, S., Loranger, A., Daigle, N., and Marceau, N. (2001). Simple keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targetting modulation. J. Cell. Biol. 154:763-773.
    • (2001) J. Cell. Biol. , vol.154 , pp. 763-773
    • Gilbert, S.1    Loranger, A.2    Daigle, N.3    Marceau, N.4
  • 160
    • 1542742110 scopus 로고    scopus 로고
    • Additive effects of p53, p21 and Rb deletion in triple knockout primary hepatocytes
    • Sheahan, S., Bellamy, C.O.C., Treanor, L., Harrison, D.J., and Prost, S. (2004). Additive effects of p53, p21 and Rb deletion in triple knockout primary hepatocytes. Oncogene 23:1489-1497.
    • (2004) Oncogene , vol.23 , pp. 1489-1497
    • Sheahan, S.1    Bellamy, C.O.C.2    Treanor, L.3    Harrison, D.J.4    Prost, S.5
  • 162
    • 0033799041 scopus 로고    scopus 로고
    • Induction of apoptosis in normal cultured rat hepatocytes and in Hep3B, a human hepatoma cell line
    • Lamboley, C., Bringuier, A.-F., and Feldmann, G. (2000). Induction of apoptosis in normal cultured rat hepatocytes and in Hep3B, a human hepatoma cell line. Cell Biol. Toxicol. 16:185-200.
    • (2000) Cell Biol. Toxicol. , vol.16 , pp. 185-200
    • Lamboley, C.1    Bringuier, A.-F.2    Feldmann, G.3
  • 163
    • 0036186764 scopus 로고    scopus 로고
    • Alteration of liver cell function and proliferation: Differentiation between adaptation and toxicity
    • Williams, G.M., and Iatropoulos, M.J. (2002). Alteration of liver cell function and proliferation: Differentiation between adaptation and toxicity. Toxicol. Pathol. 30:41-53.
    • (2002) Toxicol. Pathol. , vol.30 , pp. 41-53
    • Williams, G.M.1    Iatropoulos, M.J.2
  • 164
    • 0033999998 scopus 로고    scopus 로고
    • Development and utilization of primary hepatocyte culture systems to evaluate metabolism, DNA binding and DNA repair of xenobiotics
    • Casciano, D.A. (2000). Development and utilization of primary hepatocyte culture systems to evaluate metabolism, DNA binding and DNA repair of xenobiotics. Drug Metab. Rev. 32:1-13.
    • (2000) Drug Metab. Rev. , vol.32 , pp. 1-13
    • Casciano, D.A.1
  • 166
    • 0023951517 scopus 로고
    • The polyploidization growth pattern of normal rat liver is replaced by divisional diploid growth in hepatocellular nodules and carcinomas
    • Saeter, G., Schwarze, P.E., Nesland, J.M., Juul, N., Pettersen, E.O., and Seglen, P.O. (1988). The polyploidization growth pattern of normal rat liver is replaced by divisional diploid growth in hepatocellular nodules and carcinomas. Carcinogenesis 9:939-945.
    • (1988) Carcinogenesis , vol.9 , pp. 939-945
    • Saeter, G.1    Schwarze, P.E.2    Nesland, J.M.3    Juul, N.4    Pettersen, E.O.5    Seglen, P.O.6
  • 167
    • 0030798347 scopus 로고    scopus 로고
    • DNA ploidy and autophagic protein degradation as determinants of hepatocellular growth and survival
    • Seglen, P.O. (1997). DNA ploidy and autophagic protein degradation as determinants of hepatocellular growth and survival. Cell Biol. Toxicol. 13:301-315.
    • (1997) Cell Biol. Toxicol. , vol.13 , pp. 301-315
    • Seglen, P.O.1
  • 168
    • 0033455394 scopus 로고    scopus 로고
    • Hepatic regeneration-Revisiting the myth of Prometheus
    • Ankoma-Sey, V. (1999) Hepatic regeneration-Revisiting the myth of Prometheus. News Physiol. Sci. 14:149-155,
    • (1999) News Physiol. Sci. , vol.14 , pp. 149-155
    • Ankoma-Sey, V.1
  • 169
    • 0030098001 scopus 로고    scopus 로고
    • Transcriptional control of liver regeneration
    • Taub, R. (1996). Transcriptional control of liver regeneration. FASEB J. 10:413-427.
    • (1996) FASEB J. , vol.10 , pp. 413-427
    • Taub, R.1
  • 171
    • 0024217256 scopus 로고
    • Transient expression of c-fos and constant expression of c-myc in freshly isolated and cultured normal adult rat hepatocytes
    • Etienne, P.L., Baffet, G., Desvergne, B., Boisnard-Rissel, M., Glaise, D., and Guguen-Guillouzo, C. (1988). Transient expression of c-fos and constant expression of c-myc in freshly isolated and cultured normal adult rat hepatocytes. Oncogene Res. 3:255-262.
    • (1988) Oncogene Res. , vol.3 , pp. 255-262
    • Etienne, P.L.1    Baffet, G.2    Desvergne, B.3    Boisnard-Rissel, M.4    Glaise, D.5    Guguen-Guillouzo, C.6
  • 172
    • 0029973363 scopus 로고    scopus 로고
    • Growth factor dependence of progression through G1 and S phases of adult rat hepatocytes in vitro
    • Loyer, P., Cariou, S., Glaise, D., Bilodeau, M., Baffet, G., and Guguen-Guillouzo, C. (1996). Growth factor dependence of progression through G1 and S phases of adult rat hepatocytes in vitro. J. Biol. Chem. 271:11484-11492.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11484-11492
    • Loyer, P.1    Cariou, S.2    Glaise, D.3    Bilodeau, M.4    Baffet, G.5    Guguen-Guillouzo, C.6
  • 173
    • 0027336491 scopus 로고
    • Mammalian G1 cyclins
    • Sherr, C.J. (1993). Mammalian G1 cyclins. Cell 73:1059-1065.
    • (1993) Cell , vol.73 , pp. 1059-1065
    • Sherr, C.J.1
  • 174
    • 0028171292 scopus 로고
    • G1 phase progression: Cycling on cue
    • Sherr, C.J. (1994). G1 phase progression: Cycling on cue. Cell 79:551-555.
    • (1994) Cell , vol.79 , pp. 551-555
    • Sherr, C.J.1
  • 175
    • 0025982958 scopus 로고
    • Role for cyclin A in the dependence of mitosis on completion of DNA replication
    • Walker, D.H., and Maller, J.L. (1991). Role for cyclin A in the dependence of mitosis on completion of DNA replication. Nature 354:314-317.
    • (1991) Nature , vol.354 , pp. 314-317
    • Walker, D.H.1    Maller, J.L.2
  • 176
    • 0030998797 scopus 로고    scopus 로고
    • Regulation of CDK/cyclin complexes during the cell cycle
    • Arrellano, M., and Moreno, S. (1997). Regulation of CDK/cyclin complexes during the cell cycle. Int. J. Biochem. Cell Biol. 29:559-573.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 559-573
    • Arrellano, M.1    Moreno, S.2
  • 178
    • 0026452949 scopus 로고
    • Defects in a cell cycle checkpoint may be responsible for the genomic instability of cancer cells
    • Hartwell, L.H. (1992). Defects in a cell cycle checkpoint may be responsible for the genomic instability of cancer cells. Cell 71:543-546.
    • (1992) Cell , vol.71 , pp. 543-546
    • Hartwell, L.H.1
  • 179
    • 0024425887 scopus 로고
    • Checkpoints: Controls that ensure the order of cell cycle events
    • Hartwell, L.H., and Weinert, T.A. (1989). Checkpoints: Controls that ensure the order of cell cycle events. Science 246:629-634.
    • (1989) Science , vol.246 , pp. 629-634
    • Hartwell, L.H.1    Weinert, T.A.2
  • 182
    • 0032899038 scopus 로고    scopus 로고
    • Retinoblastoma proteins meets chromatin
    • Brehm, A., and Kouzarides, T. (1999). Retinoblastoma proteins meets chromatin. TIBS 24:142-145.
    • (1999) TIBS , vol.24 , pp. 142-145
    • Brehm, A.1    Kouzarides, T.2
  • 183
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1 phase progression
    • Sherr, C.J., and Roberts, J.M. (1999). CDK inhibitors: Positive and negative regulators of G1 phase progression. Genes Dev. 13:1501-1512.
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 186
    • 0031736586 scopus 로고    scopus 로고
    • Cell cycle regulators and human hepatocarcinogenesis
    • Hui, A.M., Makuuchi, M., and Li, X. (1998). Cell cycle regulators and human hepatocarcinogenesis. Hepato-Gastroenterology 45:1635-1642.
    • (1998) Hepato-Gastroenterology , vol.45 , pp. 1635-1642
    • Hui, A.M.1    Makuuchi, M.2    Li, X.3
  • 187
    • 0026041836 scopus 로고
    • Aberrations of the tumor suppressor p53 and retinoblastoma genes in human hepatocellular carcinomas
    • Murakami, Y., Hayashi, K., Hirohashi, S. and Sekiya, T. (1991). Aberrations of the tumor suppressor p53 and retinoblastoma genes in human hepatocellular carcinomas. Cancer Res. 51:5520-5525.
    • (1991) Cancer Res. , vol.51 , pp. 5520-5525
    • Murakami, Y.1    Hayashi, K.2    Hirohashi, S.3    Sekiya, T.4
  • 188
    • 0027207612 scopus 로고
    • p53 gene mutation and integrated hepatitis B viral DNA sequences in human liver cancer cell lines
    • Hsu, I.C., Tokiwa, T., Bennett, W., Metcalf, R.A., Welsh, J.A., Sun, T., and Harris, C.C. (1993). p53 gene mutation and integrated hepatitis B viral DNA sequences in human liver cancer cell lines. Carcinogenesis 14:987-992.
    • (1993) Carcinogenesis , vol.14 , pp. 987-992
    • Hsu, I.C.1    Tokiwa, T.2    Bennett, W.3    Metcalf, R.A.4    Welsh, J.A.5    Sun, T.6    Harris, C.C.7
  • 189
    • 0032885751 scopus 로고    scopus 로고
    • Nuclear accumulation of mutated beta-catenin in hepatocellular carcinoma is associated with increased cell proliferation
    • Nhieu, J.T., Renard, C.A., Wei, Y., Cherqui, D., Zafrani, E.S., and Buenida, M.A. (1999). Nuclear accumulation of mutated beta-catenin in hepatocellular carcinoma is associated with increased cell proliferation. Am. J. Pathol. 155:703-710.
    • (1999) Am. J. Pathol. , vol.155 , pp. 703-710
    • Nhieu, J.T.1    Renard, C.A.2    Wei, Y.3    Cherqui, D.4    Zafrani, E.S.5    Buenida, M.A.6
  • 190
    • 0030801640 scopus 로고    scopus 로고
    • Alteration of cell cycle-related genes in hepatocarcinogenesis
    • Nishida, N., Fukuda, Y., Ishizaki, K., and Nakao, K. (1997). Alteration of cell cycle-related genes in hepatocarcinogenesis. Histol. Histopathol. 12:1019-1025.
    • (1997) Histol. Histopathol. , vol.12 , pp. 1019-1025
    • Nishida, N.1    Fukuda, Y.2    Ishizaki, K.3    Nakao, K.4
  • 191
    • 0027848777 scopus 로고
    • Gap junctional intercellular communication and cell proliferation during rat liver carcinogenesis
    • Yamasaki, H., Krutovskikh, V., Mesnil, M., Columbano, A., Tsuda, H., and Ito, N. (1993) Gap junctional intercellular communication and cell proliferation during rat liver carcinogenesis. Environ. Health Perspect. 101(Suppl. 5):191-197.
    • (1993) Environ. Health Perspect. , vol.101 , Issue.5 SUPPL. , pp. 191-197
    • Yamasaki, H.1    Krutovskikh, V.2    Mesnil, M.3    Columbano, A.4    Tsuda, H.5    Ito, N.6
  • 192
    • 0028177936 scopus 로고
    • Multiple mechanisms are responsible for altered expression of gap junction genes during oncogenesis in rat liver
    • Neveu, M.J., Hully, J.R., Babcock, K.L., Hertzberg, E.L., Nicholson, B.J., Paul, D.L., and Pilot, H.C. (1994). Multiple mechanisms are responsible for altered expression of gap junction genes during oncogenesis in rat liver. J. Cell Sci. 107:83-95.
    • (1994) J. Cell Sci. , vol.107 , pp. 83-95
    • Neveu, M.J.1    Hully, J.R.2    Babcock, K.L.3    Hertzberg, E.L.4    Nicholson, B.J.5    Paul, D.L.6    Pilot, H.C.7
  • 193
    • 0027682801 scopus 로고
    • Amplification of the c-myc gene in human hepatocellular carcinoma: Biological significance
    • Peng, S.Y., Lai, P.L., and Hsu, H.C. (1993). Amplification of the c-myc gene in human hepatocellular carcinoma: Biological significance. J. Formos. Med. Assoc. 92:866-870.
    • (1993) J. Formos. Med. Assoc. , vol.92 , pp. 866-870
    • Peng, S.Y.1    Lai, P.L.2    Hsu, H.C.3
  • 195
    • 0027970838 scopus 로고
    • Chromosomal translocations in human cancer
    • Rabbitts, T.H. (1994). Chromosomal translocations in human cancer. Nature 372:143-149.
    • (1994) Nature , vol.372 , pp. 143-149
    • Rabbitts, T.H.1
  • 197
    • 0028071555 scopus 로고
    • Mutations in the p53 tumor suppressor gene: Clues to cancer etiology and molecular pathogenesis
    • Greenblatt, M.S., Bennett, W.P., Hollstein, M., and Harris, C.C. (1994). Mutations in the p53 tumor suppressor gene: Clues to cancer etiology and molecular pathogenesis. Cancer Res. 54:4855-4878.
    • (1994) Cancer Res. , vol.54 , pp. 4855-4878
    • Greenblatt, M.S.1    Bennett, W.P.2    Hollstein, M.3    Harris, C.C.4
  • 198
    • 0031055839 scopus 로고    scopus 로고
    • Reduced p21(WAF1/CIP1) expression and p53 mutation in hepatocellular carcinomas
    • Hui, A.M., Kanai, Y., Sakamoto, M., Tsuda, H., and Hirohashi, S. (1997). Reduced p21(WAF1/CIP1) expression and p53 mutation in hepatocellular carcinomas. Hepatology 25:575-579.
    • (1997) Hepatology , vol.25 , pp. 575-579
    • Hui, A.M.1    Kanai, Y.2    Sakamoto, M.3    Tsuda, H.4    Hirohashi, S.5
  • 200
    • 0021910677 scopus 로고
    • Ultraviolet light-induced DNA repair synthesis in hepatocytes from species of differing longevities
    • Maslansky, C.J., and Williams, G.M. (1985). Ultraviolet light-induced DNA repair synthesis in hepatocytes from species of differing longevities. Mech Ageing Dev. 29:191-203.
    • (1985) Mech Ageing Dev. , vol.29 , pp. 191-203
    • Maslansky, C.J.1    Williams, G.M.2
  • 201
    • 0019128241 scopus 로고
    • Cell cycle-specific mutagenesis at the hypoxanthine phosphoribosyltransferase locus in adult rat liver epithelial cells
    • Tong, C., Fazio, M., and Williams, G.M. (1980). Cell cycle-specific mutagenesis at the hypoxanthine phosphoribosyltransferase locus in adult rat liver epithelial cells. Proc. Natl. Acad. Sci. USA 77:7377-7379.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7377-7379
    • Tong, C.1    Fazio, M.2    Williams, G.M.3
  • 202
    • 0032540934 scopus 로고    scopus 로고
    • Reexpression of C/EBP alpha induces CYP2B6, CYP2C9 and CYP2D6 genes in HepG2 cells
    • Jover, R., Bort, R., Goméz-Lechon, M.J., and Castell, J.V. (1998). Reexpression of C/EBP alpha induces CYP2B6, CYP2C9 and CYP2D6 genes in HepG2 cells. FEBS Lett 431:227-230.
    • (1998) FEBS Lett , vol.431 , pp. 227-230
    • Jover, R.1    Bort, R.2    Goméz-Lechon, M.J.3    Castell, J.V.4
  • 203
    • 0028914210 scopus 로고
    • Expression of the liver-enriched transcription factors C/EBP alpha, C/EBP beta, HNF-1 and HNF-4 in preneoplastic nodules and hepatocellular carcinoma in rat liver
    • Flodby, P., Liao, D.Z., Blanck, A., Xanthopoulos, K.G., and Hallstrom, I.P. (1995). Expression of the liver-enriched transcription factors C/EBP alpha, C/EBP beta, HNF-1 and HNF-4 in preneoplastic nodules and hepatocellular carcinoma in rat liver. Mol. Carcinogen. 12:103-109.
    • (1995) Mol. Carcinogen. , vol.12 , pp. 103-109
    • Flodby, P.1    Liao, D.Z.2    Blanck, A.3    Xanthopoulos, K.G.4    Hallstrom, I.P.5
  • 204
    • 0036618423 scopus 로고    scopus 로고
    • Decreased expression of the CCAAT/enhancer binding protein alpha gene involved in hepatocyte proliferation in human hepatocellular carcinomas
    • Tomizawa, M., Wang, Y.Q., Ebara, M., Saisho, H., Watanabe, K., Nakagawa, A., and Tagawa, M. (2002). Decreased expression of the CCAAT/enhancer binding protein alpha gene involved in hepatocyte proliferation in human hepatocellular carcinomas. Int. J. Mol. Med. 9:597-600.
    • (2002) Int. J. Mol. Med. , vol.9 , pp. 597-600
    • Tomizawa, M.1    Wang, Y.Q.2    Ebara, M.3    Saisho, H.4    Watanabe, K.5    Nakagawa, A.6    Tagawa, M.7
  • 205
    • 0036892569 scopus 로고    scopus 로고
    • Major phase I biotransformation pathways of trichostatin A in rat hepatocytes and in rat and human liver microsomes
    • Elaut, G., Török, G., Vinken, M., Laus, G., Papeleu, P., Tourwé, D., and Rogiers, V. (2002). Major phase I biotransformation pathways of trichostatin A in rat hepatocytes and in rat and human liver microsomes. Drug Metab. Dispos. 30:1320-1328.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1320-1328
    • Elaut, G.1    Török, G.2    Vinken, M.3    Laus, G.4    Papeleu, P.5    Tourwé, D.6    Rogiers, V.7
  • 206
    • 0036554730 scopus 로고    scopus 로고
    • End points in cancer clinical trials and the drug approval process
    • Schilsky, R.L. (2002). End points in cancer clinical trials and the drug approval process. Clin. Cancer Res. 8:935-938.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 935-938
    • Schilsky, R.L.1
  • 209
    • 1542331640 scopus 로고    scopus 로고
    • Toward an HDAC6 inhibitor: Synthesis and conformational analysis of cyclic hexapeptide hydroxamic acid designed from α-tubulin sequence
    • Jose, B., Okamura, S., Kato, T., Nishino, N., Sumida, Y., and Yoshida, M. (2004). Toward an HDAC6 inhibitor: Synthesis and conformational analysis of cyclic hexapeptide hydroxamic acid designed from α-tubulin sequence. Bioorg. Med. Chem. 12:1351-1356.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 1351-1356
    • Jose, B.1    Okamura, S.2    Kato, T.3    Nishino, N.4    Sumida, Y.5    Yoshida, M.6
  • 212
    • 0034885012 scopus 로고    scopus 로고
    • Role of drug metabolism in drug discovery and development
    • Kumar, G.N., and Surapaneni, S. (2001). Role of drug metabolism in drug discovery and development. Med. Res. Rev. 21:397-411.
    • (2001) Med. Res. Rev. , vol.21 , pp. 397-411
    • Kumar, G.N.1    Surapaneni, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.