참고문헌
- Marks PA, Richon VM, Rifkind RA. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J Natl Cancer Inst 2000;92:1210-1216 https://doi.org/10.1093/jnci/92.15.1210
- Marks PA, Rifkind RA, Richon VM, et al. Histone deacetylases and cancer: Causes and therapies. Nat Rev Cancer 2001;1:194-202 https://doi.org/10.1038/35106079
- Marks PA, Jiang X. Histone deacetylase inhibitors in programmed cell death and cancer therapy. Cell Cycle 2005;25:552-563
- Thiagalingam S, Cheng KH, Lee HJ, Minerva NA. Histone deactylases: unique players in shaping the epigenetic histone code. Ann N Y Acad Sci 2003;983:84-100 https://doi.org/10.1111/j.1749-6632.2003.tb05964.x
- Antonelllo Mai, Silvio Massa, Dante Rotili, et al. Histone Deacetylation in Epigenetics: An attractive target for anticancer therapy. Medicinal Research Rev 2005;25:261-309 https://doi.org/10.1002/med.20024
- Yang XY, Seto E. Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression. Curr Opin Genet Nev 2003;13:143-153 https://doi.org/10.1016/S0959-437X(03)00015-7
- Gray SG, Ekstrom TJ. The human histone deacetylase family. Exp Cell Res 2001;262:75-83 https://doi.org/10.1006/excr.2000.5080
- Grozinger CM, Hassig CA, Schreiber SL. Three proteins define a class of human histone deacetylase related to yeast Hda1p. Proc Natl Acad Sci USA 1999;96:4868-4873 https://doi.org/10.1073/pnas.96.9.4868
- Bertos NR, Wang AH, Yang XY. Class II histone deacetylase: Structure, function, and regulation. Biochem Cell Biol 2001;79:243-252 https://doi.org/10.1139/bcb-79-3-243
- Fische W, Kiermer V, Dequiedt F, et al. The emerging role of class II histone deactylase. Biochem Cell Biol 2001;79:339-348
-
Luo J, Nikolaev AY, Imai S, et al. Negative control of p53 by Sir2
$\alpha$ promotes cell survival under stress. Cell 2001;107:137-148 https://doi.org/10.1016/S0092-8674(01)00524-4 -
Vaziri H, Dessain SK, Ng Eaton E, et al.
$hSIR2^{SIRT1}$ functions as an NAD-dependent p53 deacetylase. Cell 2001;107:149-159 https://doi.org/10.1016/S0092-8674(01)00527-X - Park JH, Jung Y, Kim TY, et al. Class I histone deacetyalse-selective novel synthetic inhibitors potentially inhibit human tumor proliferation. Clin Cancer Res 2004;10:5271- 5281 https://doi.org/10.1158/1078-0432.CCR-03-0709
- Insinga A, Monestiroli S, Ronzoni S, et al. Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of death receptor pathway. Nat Med 2005;11:71-76 https://doi.org/10.1038/nm1160
- Nebbiosso A, Clarke N, Voltz E, et al. Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells. Nat Med 2005;11:77-84 https://doi.org/10.1038/nm1161
- Liu F, Dowling M, Yang XJ, Kao GD. Caspase-mediated specific cleavage of human histone deacetylase 4. J Biol Chem 2004;13:34537-34546 https://doi.org/10.1074/jbc.M402475200
- Bakin RE, Jung MO. Cytoplasmic sequestration of HDAC7 from mitochondrial and nuclear compartments upon initiation of apoptosis. J Biol Chem 2004;279:51218-51225 https://doi.org/10.1074/jbc.M409271200
- Medina V, Edmonds B, Young GP, James R, Appleton S, Zalewski PD. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res 1997;57:3697-3707
- Kao GD, McKenna WG, Guenther MG, Muschel RJ, Lazar MA, Yen TJ. Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response. J Cell Biol 2003;160:1017-1027 https://doi.org/10.1083/jcb.200209065
-
Camphausen K, Burgan W, Cerra M, et al. Enhanced radiation-induced cell killing and prolongation of
$\gamma$ H2AX foci expression by the histone deacetylase inhibitor MS-275. Cancer Res 2004;64:316-321 https://doi.org/10.1158/0008-5472.CAN-03-2630 - Camphausen K, Scott T, Sproull M, Tofilon PJ. Enhancement of xenograft radiosenstivity by histone deacetylase inhibitor MS275 and Correlation with histone hyperacetylation. Clin Cancer Res 2004;10:6066-6071 https://doi.org/10.1158/1078-0432.CCR-04-0537
- Biade S, Stobbe CC, Boyd JT, Chapman JD. Chemical agents that promote chromatin compaction radiosensitize tumour cells. Int J Radiat Biol 2001;77:1033-1042 https://doi.org/10.1080/09553000110066068
- Kim JH, Shin JH, Kim IH. Susceptibility and radiosensitization of human glioblastoma cells to trichostatin A, a histone deacetylase inhibitor. Int J Radiat Oncol Biol Phys 2004;62:1348-1354
- Kim JH, Shin JH, Chie EK, et al. Trichostatin A, a histone deacetylase inhibitor, potentiated cytotoxic effect of inonizing radiation in human head and neck cancer cell lines. J Korean Soc Ther Radiol Oncol 2004:22:138-144
- Bristow RG, Benchimol S, Hill RP. The 53 gene as a modifier of intrinsic radiosensitivity: implication for radiotherapy. Radiotherapy and Oncology 1996;40:197-223 https://doi.org/10.1016/0167-8140(96)01806-3
- Schwartz JL, Russell KJ. The effect of functional inactivation of TP53 by HPV-E6 transformation on the induction of chromosome aberration by gamma rays in human tumor cells. Radiat Res 1999;151:385-390 https://doi.org/10.2307/3579824
- Schwartz JL, Jordan R, Kaufmann WK, et al. Evidence for the expression of radiation-induced petetially lethral damage being a p53-dependent process. Int J Radiat Biol 2000;76:1037-1043 https://doi.org/10.1080/09553000050111505
- Kim IA, Yang YJ, Yoon SC, et al. Potential of adenoviral p53 gene therapy and irradiation for the treatment of malignant gliomas. Int J Oncol 2001;19:1041-1047
- Roy S, Packman K, Jeffrey R, Tenniswood M. Histone deacetylase inhibitors differentially stabilize acetylated p53 and induce cell cycle arrest or apoptosis in prostate cancer cells. Cell Death & Differentiation. Advance online publication Mar 2005;cdd4401581 https://doi.org/10.1038/sj.cdd.4401581
- Liu L, Scolnick DM, Trievel RC, et al. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol Cell Biol 1999;19:1202-1209 https://doi.org/10.1128/MCB.19.2.1202
- Luo J, Su F, Chen D, Shiloh A, Gu W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 2000;408:377-381 https://doi.org/10.1038/35042612
- Li M, Luo J, Brooks CL, Gu W. Acetylation of p53 inhibits its ubiquitination by mdm2. J Biol Chem 2002;277:50607-50611 https://doi.org/10.1074/jbc.C200578200
- Luo J, Li M, Tang Y, et al. Acetylaton of p53 augments its site-specific DNA bind both in vitro and in vivo. Proc Natl Acad Sci USA 2004;101:2259-2264 https://doi.org/10.1073/pnas.0308762101
- Ito A, Lai CH, Zhao X, et al. p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2. EMBO J 2001;20:1331-1340 https://doi.org/10.1093/emboj/20.6.1331
- Grunstein M. Histone acetylation and chromatin structure and transcription. Nature 1997;389:349-352 https://doi.org/10.1038/38664
- Bernstein BT, Tong T, Schreiber S. Genomwide studies of histone deacetylase function in yeast. Proc Natl Acad Sci USA 2000;97:13708-13713 https://doi.org/10.1073/pnas.250477697
- Glaser KJ, Li J, Staver RQ, et al. Role of class I and Class II histone deacetylases in carcinoma cells using siRNA. Biochem Biophys Res Comm 2003;310:529-536 https://doi.org/10.1016/j.bbrc.2003.09.043
- Henderson C, Mizzau M, Paroni G, Maestro R, Schneider C, Brancolini C. Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J Biol Chem 2003;278:12579-12589 https://doi.org/10.1074/jbc.M213093200
- Joseph J, Wajapeyee N, Somasundaram K. Role of p53 status in chemosensitivity determination of cancer cells against histone deacetylase inhibitor sodium butyrate. Int J Cancer 2005;115:11-18 https://doi.org/10.1002/ijc.20842
- Kudo N, Wolff B, Sekimoto T, et al. Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. Exp Cell Res 1998;242:540-547 https://doi.org/10.1006/excr.1998.4136
- Kudo N, Matsumori N, Taoka H, et al. Leptomycin B inactivates CRM1/expotin 1 by covalent modification at a cystein residue in the central conserved region. Proc Natl Acad Sci USA 1999.96:9112-9117 https://doi.org/10.1002/ijc.22591
- Lain S, Xirodima D, Lain DP. Accumulating active p53 in the nucleus by inhibition of nuclear export: a novel strategy to promote the p53 tumor suppressor function. Exp Cell Res 1999;253:315-324 https://doi.org/10.1006/excr.1999.4672
- Honda R, Tanaka H, Yasuda H. Oncoprotein mdm2 is ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 1997;420:25-27 https://doi.org/10.1016/S0014-5793(97)01480-4
- Kubbuttat MH, Jones SN, Vousden KH. Regulation of p53 stability by mdm2. Nature 1997;387:299-303 https://doi.org/10.1038/387299a0
- Nakamura S, Roth JA, Mukhopadhyay T. Multiple lysine mutations in the C-terminal domain of p53 interfere with MDM2-dependent protein degradation and ubiquitination. Mol Cell Biol 2000;20:9391-9398 https://doi.org/10.1128/MCB.20.24.9391-9398.2000
- Hietanen S, Lain S, Krausz E, et al. Activation of p53 in cervical carcinoma cells by small molecules. Proc Natl Acad Sci USA 2000;97:8501-8506 https://doi.org/10.1073/pnas.97.15.8501
- Lain DP, Lain S. Therapeutic exploration of the p53 pathway. Trends Mol Med 2002;8:S38-S42 https://doi.org/10.1016/S1471-4914(01)02221-3
- Liang SH, Clarke MF. Regulation of p53 localization. Eur J Biochem 2001;268:2779-2783 https://doi.org/10.1046/j.1432-1327.2001.02227.x