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Volumn 10, Issue 2, 2010, Pages 210-228

Inhibitors of HDACs - Effective drugs against cancer?

Author keywords

Cancer; Chemotherapy; Gene expression; Histone deacetylase; Histone deacetylase inhibitor; SAHA; Translational research; VPA

Indexed keywords

ARYLBUTYRIC ACID DERIVATIVE; ATRAZINE; AZATHIOPRINE; BELINOSTAT; DEPSIPEPTIDE; DOXORUBICIN; EPIRUBICIN; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; PANOBINOSTAT; RETINOIC ACID; THEOPHYLLINE; VALPROIC ACID; VORINOSTAT;

EID: 77950640292     PISSN: 15680096     EISSN: None     Source Type: Journal    
DOI: 10.2174/156800910791054149     Document Type: Article
Times cited : (63)

References (155)
  • 1
    • 0007852927 scopus 로고
    • The presence of acetyl groups of histones
    • Phillips, D. M. The presence of acetyl groups of histones. Biochem. J. 1963, 87, 258-263.
    • (1963) Biochem. J. , vol.87 , pp. 258-263
    • Phillips, D.M.1
  • 2
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of rna synthesis
    • Allfrey, V. G.; Faulkner, R.; Mirsky, A. E. Acetylation and methylation of histones and their possible role in the regulation of rna synthesis. Proc. Natl. Acad. Sci. USA 1964, 51, 786-794.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 4
    • 33845877732 scopus 로고    scopus 로고
    • Defining an epigenetic code
    • Turner, B. M. Defining an epigenetic code. Nat. Cell Biol. 2007, 9, 2-6.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 2-6
    • Turner, B.M.1
  • 5
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci, S.; Pelicci, P. G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 2006, 6, 38-51.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 6
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: Past, present and future
    • Yoo, C. B.; Jones, P. A. Epigenetic therapy of cancer: past, present and future. Nat. Rev. Drug Discov. 2006, 5, 37-50.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 7
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: From bacteria and yeast to mice and men
    • Yang, X. J.; Seto, E. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. Mol. Cell Biol. 2008, 9, 206-218.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 8
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • 20090
    • Spange, S.; Wagner, T.; Heinzel, T.; Krämer, O. H. Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int. J. Biochem. Cell Biol. 20090, 41(1), 185-198.
    • Int. J. Biochem. Cell Biol. , vol.41 , Issue.1 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Krämer, O.H.4
  • 10
    • 61549116543 scopus 로고    scopus 로고
    • Histone deacetylases: Salesmen and customers in the post-translational modification market
    • Brandl, A.; Heinzel, T.; Kramer, O. H. Histone deacetylases: salesmen and customers in the post-translational modification market. Biol. Cell 2009, 101, 193-205.
    • (2009) Biol. Cell , vol.101 , pp. 193-205
    • Brandl, A.1    Heinzel, T.2    Kramer, O.H.3
  • 12
    • 47049127380 scopus 로고    scopus 로고
    • Pharmacodynamic markers for histone deacetylase inhibitor development
    • Heinzel, T.; Krämer, O. H. Pharmacodynamic markers for histone deacetylase inhibitor development. Drug Discov. Today 2008, 4, 277-283.
    • (2008) Drug Discov. Today , vol.4 , pp. 277-283
    • Heinzel, T.1    Krämer, O.H.2
  • 13
    • 38949086502 scopus 로고    scopus 로고
    • Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy
    • Weichert, W.; Roske, A.; Gekeler, V.; Beckers, T.; Stephan, C.; Jung, K.; Fritzsche, F. R.; Niesporek, S.; Denkert, C.; Dietel, M.; Kristiansen, G. Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy. Br. J. Cancer 2008, 98, 604-610.
    • (2008) Br. J. Cancer , vol.98 , pp. 604-610
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Stephan, C.5    Jung, K.6    Fritzsche, F.R.7    Niesporek, S.8    Denkert, C.9    Dietel, M.10    Kristiansen, G.11
  • 14
    • 50949104573 scopus 로고    scopus 로고
    • Expression of class I histone deacetylases indicates poor prognosis in endometrioid subtypes of ovarian and endometrial carcinomas
    • Weichert, W.; Denkert, C.; Noske, A.; Darb-Esfahani, S.; Dietel, M.; Kalloger, S. E.; Huntsman, D. G.; Kobel, M. Expression of class I histone deacetylases indicates poor prognosis in endometrioid subtypes of ovarian and endometrial carcinomas. Neoplasia 2008, 10, 1021-1027.
    • (2008) Neoplasia , vol.10 , pp. 1021-1027
    • Weichert, W.1    Denkert, C.2    Noske, A.3    Darb-Esfahani, S.4    Dietel, M.5    Kalloger, S.E.6    Huntsman, D.G.7    Kobel, M.8
  • 15
    • 70449675089 scopus 로고    scopus 로고
    • HDAC2: A critical factor in health and disease
    • Krämer, O. H. HDAC2: a critical factor in health and disease. Trends Pharmacol. Sci. 2009, 30, 647-655.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 647-655
    • Krämer, O.H.1
  • 17
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J. E.; Peart, M. J.; Johnstone, R. W. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 2006, 5, 769-784.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 19
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • Lee, K. K.; Workman, J. L. Histone acetyltransferase complexes: one size doesn't fit all. Nat. Rev. Mol. Cell Biol. 2007, 8, 284-295.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 20
    • 25144496904 scopus 로고    scopus 로고
    • The Sir 2 family of protein deacetylases
    • Denu, J. M. The Sir 2 family of protein deacetylases. Curr. Opin. Chem. Biol. 2005, 9, 431-440.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 431-440
    • Denu, J.M.1
  • 21
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins - Emerging roles in physiology, aging, and calorie restriction
    • Haigis, M. C.; Guarente, L. P. Mammalian sirtuins - emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006, 20, 2913-2921.
    • (2006) Genes Dev. , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 22
    • 0035313803 scopus 로고    scopus 로고
    • Histone acetyltransferases: Function, structure, and catalysis
    • Marmorstein, R.; Roth, S. Y. Histone acetyltransferases: function, structure, and catalysis. Curr. Opin. Genet. Dev. 2001, 11, 155-161.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 155-161
    • Marmorstein, R.1    Roth, S.Y.2
  • 23
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger, C. M.; Schreiber, S. L. Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem. Biol. 2002, 9, 3-16.
    • (2002) Chem. Biol. , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 24
    • 67449100866 scopus 로고    scopus 로고
    • Histone deacetylase 2 expression predicts poorer prognosis in oral cancer patients
    • Chang, H. H.; Chiang, C. P.; Hung, H. C.; Lin, C. Y.; Deng, Y. T.; Kuo, M. Y. Histone deacetylase 2 expression predicts poorer prognosis in oral cancer patients. Oral Oncol. 2009, 45(7), 610-614.
    • (2009) Oral Oncol. , vol.45 , Issue.7 , pp. 610-614
    • Chang, H.H.1    Chiang, C.P.2    Hung, H.C.3    Lin, C.Y.4    Deng, Y.T.5    Kuo, M.Y.6
  • 26
    • 65249141665 scopus 로고    scopus 로고
    • Clinical and biological effects of valproic acid as a histone deacetylase inhibitor on tumor and surrogate tissues: Phase I/II trial of valproic acid and epirubicin/FEC
    • Münster, P.; Marchion, D.; Bicaku, E.; Lacevic, M.; Kim, J.; Centeno, B.; Daud, A.; Neuger, A.; Minton, S.; Sullivan, D. Clinical and biological effects of valproic acid as a histone deacetylase inhibitor on tumor and surrogate tissues: phase I/II trial of valproic acid and epirubicin/FEC. Clin. Cancer Res. 2009, 15, 2488-2496.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 2488-2496
    • Münster, P.1    Marchion, D.2    Bicaku, E.3    Lacevic, M.4    Kim, J.5    Centeno, B.6    Daud, A.7    Neuger, A.8    Minton, S.9    Sullivan, D.10
  • 28
    • 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.; Beppu, T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 1990, 265, 17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 31
    • 0842325787 scopus 로고    scopus 로고
    • Histone deacetylase is a target of valproic acid-mediated cellular differentiation
    • Gurvich, N.; Tsygankova, O. M.; Meinkoth, J. L.; Klein, P. S. Histone deacetylase is a target of valproic acid-mediated cellular differentiation. Cancer Res. 2004, 64, 1079-1086.
    • (2004) Cancer Res. , vol.64 , pp. 1079-1086
    • Gurvich, N.1    Tsygankova, O.M.2    Meinkoth, J.L.3    Klein, P.S.4
  • 32
    • 33847258674 scopus 로고    scopus 로고
    • Discovery and development of SAHA as an anticancer agent
    • Marks, P. A. Discovery and development of SAHA as an anticancer agent. Oncogene 2007, 26, 1351-1356.
    • (2007) Oncogene , vol.26 , pp. 1351-1356
    • Marks, P.A.1
  • 33
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu, W. S.; Parmigiani, R. B.; Marks, P. A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007, 26, 5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 35
    • 34447101115 scopus 로고    scopus 로고
    • MS-275, a potent orally available inhibitor of histone deacetylases - The development of an anticancer agent
    • Hess-Stumpp, H.; Bracker, T. U.; Henderson, D.; Politz, O. MS-275, a potent orally available inhibitor of histone deacetylases - the development of an anticancer agent. Int. J. Biochem. Cell Biol. 2007, 39, 1388-1405.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1388-1405
    • Hess-Stumpp, H.1    Bracker, T.U.2    Henderson, D.3    Politz, O.4
  • 37
    • 47249100271 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: New compounds and clinical update of benzamide-type agents
    • Moradei, O.; Vaisburg, A.; Martell, R. E. Histone deacetylase inhibitors in cancer therapy: new compounds and clinical update of benzamide-type agents. Curr. Top. Med. Chem. 2008, 8, 841-858.
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 841-858
    • Moradei, O.1    Vaisburg, A.2    Martell, R.E.3
  • 41
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty, S. J.; Koeller, K. M.; Wong, J. C.; Grozinger, C. M.; Schreiber, S. L. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. USA 2003, 100, 4389-4394.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 43
    • 59649092334 scopus 로고    scopus 로고
    • Zn(II)-dependent histone deacetylase inhibitors: Suberoylanilide hydroxamic acid and trichostatin a
    • Codd, R.; Braich, N.; Liu, J.; Soe, C. Z.; Pakchung, A. A. Zn(II)-dependent histone deacetylase inhibitors: Suberoylanilide hydroxamic acid and trichostatin A. Int. J. Biochem. Cell Biol. 2009, 41(4), 736-739.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , Issue.4 , pp. 736-739
    • Codd, R.1    Braich, N.2    Liu, J.3    Soe, C.Z.4    Pakchung, A.A.5
  • 44
    • 45749142120 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Bieliauskas, A. V.; Pflum, M. K. Isoform-selective histone deacetylase inhibitors. Chem. Soc. Rev. 2008, 37, 1402-1413.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1402-1413
    • Bieliauskas, A.V.1    Pflum, M.K.2
  • 47
    • 27444435580 scopus 로고    scopus 로고
    • Toward selective histone deacetylase inhibitor design: Homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases
    • Wang, D. F.; Helquist, P.; Wiech, N. L.; Wiest, O. Toward selective histone deacetylase inhibitor design: homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases. J. Med. Chem. 2005, 48, 6936-6947.
    • (2005) J. Med. Chem. , vol.48 , pp. 6936-6947
    • Wang, D.F.1    Helquist, P.2    Wiech, N.L.3    Wiest, O.4
  • 48
    • 33646548638 scopus 로고    scopus 로고
    • Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion
    • Gantt, S. L.; Gattis, S. G.; Fierke, C. A. Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry 2006, 45, 6170-6178.
    • (2006) Biochemistry , vol.45 , pp. 6170-6178
    • Gantt, S.L.1    Gattis, S.G.2    Fierke, C.A.3
  • 49
    • 33845514708 scopus 로고    scopus 로고
    • Will broad-spectrum histone deacetylase inhibitors be superseded by more specific compounds?
    • Karagiannis, T. C.; El-Osta, A. Will broad-spectrum histone deacetylase inhibitors be superseded by more specific compounds? Leukemia 2007, 21, 61-65.
    • (2007) Leukemia , vol.21 , pp. 61-65
    • Karagiannis, T.C.1    El-Osta, A.2
  • 50
    • 43749109171 scopus 로고    scopus 로고
    • A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas
    • Balasubramanian, S.; Ramos, J.; Luo, W.; Sirisawad, M.; Verner, E.; Buggy, J. J. A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas. Leukemia 2008, 22, 1026-1034.
    • (2008) Leukemia , vol.22 , pp. 1026-1034
    • Balasubramanian, S.1    Ramos, J.2    Luo, W.3    Sirisawad, M.4    Verner, E.5    Buggy, J.J.6
  • 51
    • 49349098483 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Mechanisms of cell death and promise in combination cancer therapy
    • Carew, J. S.; Giles, F. J.; Nawrocki, S. T. Histone deacetylase inhibitors: mechanisms of cell death and promise in combination cancer therapy. Cancer Lett. 2008, 269, 7-17.
    • (2008) Cancer Lett. , vol.269 , pp. 7-17
    • Carew, J.S.1    Giles, F.J.2    Nawrocki, S.T.3
  • 52
    • 67449127083 scopus 로고    scopus 로고
    • Cytotoxicity mediated by histone deacetylase inhibitors in cancer cells: Mechanisms and potential clinical implications
    • Schrump, D. S. Cytotoxicity mediated by histone deacetylase inhibitors in cancer cells: mechanisms and potential clinical implications. Clin. Cancer Res. 2009, 15, 3947-3957.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 3947-3957
    • Schrump, D.S.1
  • 53
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane, A. A.; Chabner, B. A. Histone deacetylase inhibitors in cancer therapy. J. Clin. Oncol. 2009, 27, 5459-5468.
    • (2009) J. Clin. Oncol. , vol.27 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 54
    • 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.; Davidsen, S. K. 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. 2003, 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
  • 55
    • 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.; Verdin, E. The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr. 1996, 5, 245-253.
    • (1996) Gene Expr. , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 56
    • 3042566927 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor Trichostatin a modulates CD4+ T cell responses
    • Moreira, J. M.; Scheipers, P.; Sorensen, P. The histone deacetylase inhibitor Trichostatin A modulates CD4+ T cell responses. BMC Cancer 2003, 3, 30.
    • (2003) BMC Cancer , vol.3 , pp. 30
    • Moreira, J.M.1    Scheipers, P.2    Sorensen, P.3
  • 57
    • 21744442937 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor valproic acid alters sensitivity towards all trans retinoic acid in acute myeloblastic leukemia cells
    • Trus, M. R.; Yang, L.; Suarez Saiz, F.; Bordeleau, L.; Jurisica, I.; Minden, M. D. The histone deacetylase inhibitor valproic acid alters sensitivity towards all trans retinoic acid in acute myeloblastic leukemia cells. Leukemia 2005, 19, 1161-1168.
    • (2005) Leukemia , vol.19 , pp. 1161-1168
    • Trus, M.R.1    Yang, L.2    Suarez Saiz, F.3    Bordeleau, L.4    Jurisica, I.5    Minden, M.D.6
  • 60
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: Role in the control of protein stability
    • Caron, C.; Boyault, C.; Khochbin, S. Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability. Bioessays 2005, 27, 408-415.
    • (2005) Bioessays , vol.27 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 61
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak, M. A.; Sengupta, N.; Zhang, X.; Seto, E. Acetylation and deacetylation of non-histone proteins. Gene 2005, 363, 15-23.
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 63
    • 67349142662 scopus 로고    scopus 로고
    • HDAC inhibitors in models of inflammation-related tumorigenesis
    • Glauben, R.; Sonnenberg, E.; Zeitz, M.; Siegmund, B. HDAC inhibitors in models of inflammation-related tumorigenesis. Cancer Lett. 2009, 280, 154-159.
    • (2009) Cancer Lett. , vol.280 , pp. 154-159
    • Glauben, R.1    Sonnenberg, E.2    Zeitz, M.3    Siegmund, B.4
  • 64
    • 40949085551 scopus 로고    scopus 로고
    • HDAC2 deficiency sensitizes colon cancer cells to TNFalpha-induced apoptosis through inhibition of NF-kappaB activity
    • Kaler, P.; Sasazuki, T.; Shirasawa, S.; Augenlicht, L.; Klampfer, L. HDAC2 deficiency sensitizes colon cancer cells to TNFalpha-induced apoptosis through inhibition of NF-kappaB activity. Exp. Cell Res. 2008, 314, 1507-1518.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1507-1518
    • Kaler, P.1    Sasazuki, T.2    Shirasawa, S.3    Augenlicht, L.4    Klampfer, L.5
  • 67
    • 33744938927 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress the inducibility of nuclear factorkappaB by tumor necrosis factor-alpha receptor-1 down-regulation
    • Imre, G.; Gekeler, V.; Leja, A.; Beckers, T.; Boehm, M. Histone deacetylase inhibitors suppress the inducibility of nuclear factorkappaB by tumor necrosis factor-alpha receptor-1 down-regulation. Cancer Res. 2006, 66, 5409-5418.
    • (2006) Cancer Res. , vol.66 , pp. 5409-5418
    • Imre, G.1    Gekeler, V.2    Leja, A.3    Beckers, T.4    Boehm, M.5
  • 69
    • 1842557733 scopus 로고    scopus 로고
    • Regulation of mammalian epithelial differentiation and intestine development by class I histone deacetylases
    • Tou, L.; Liu, Q.; Shivdasani, R. A. Regulation of mammalian epithelial differentiation and intestine development by class I histone deacetylases. Mol. Cell Biol. 2004, 24, 3132-3139.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3132-3139
    • Tou, L.1    Liu, Q.2    Shivdasani, R.A.3
  • 71
    • 33749572938 scopus 로고    scopus 로고
    • Valproate inhibition of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells
    • Hrzenjak, A.; Moinfar, F.; Kremser, M. L.; Strohmeier, B.; Staber, P. B.; Zatloukal, K.; Denk, H. Valproate inhibition of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells. Mol. Cancer Ther. 2006, 5, 2203-2210.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 2203-2210
    • Hrzenjak, A.1    Moinfar, F.2    Kremser, M.L.3    Strohmeier, B.4    Staber, P.B.5    Zatloukal, K.6    Denk, H.7
  • 73
    • 33846109370 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce the degradation of the t(8;21) fusion oncoprotein
    • Yang, G.; Thompson, M. A.; Brandt, S. J.; Hiebert, S. W. Histone deacetylase inhibitors induce the degradation of the t(8;21) fusion oncoprotein. Oncogene 2007, 26, 91-101.
    • (2007) Oncogene , vol.26 , pp. 91-101
    • Yang, G.1    Thompson, M.A.2    Brandt, S.J.3    Hiebert, S.W.4
  • 74
    • 43249104204 scopus 로고    scopus 로고
    • Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RAR{alpha}
    • Krämer, O. H.; Müller, S.; Buchwald, M.; Reichardt, S.; Heinzel, T. Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RAR{alpha}. FASEB J. 2008, 22(5), 1369-1379.
    • (2008) FASEB J. , vol.22 , Issue.5 , pp. 1369-1379
    • Krämer, O.H.1    Müller, S.2    Buchwald, M.3    Reichardt, S.4    Heinzel, T.5
  • 77
    • 61549123363 scopus 로고    scopus 로고
    • Phase II study of belinostat (PXD101), a histone deacetylase inhibitor, for second line therapy of advanced malignant pleural mesothelioma
    • Ramalingam, S. S.; Belani, C. P.; Ruel, C.; Frankel, P.; Gitlitz, B.; Koczywas, M.; Espinoza-Delgado, I.; Gandara, D. Phase II study of belinostat (PXD101), a histone deacetylase inhibitor, for second line therapy of advanced malignant pleural mesothelioma. J. Thorac. Oncol. 2009, 4, 97-101.
    • (2009) J. Thorac. Oncol. , vol.4 , pp. 97-101
    • Ramalingam, S.S.1    Belani, C.P.2    Ruel, C.3    Frankel, P.4    Gitlitz, B.5    Koczywas, M.6    Espinoza-Delgado, I.7    Gandara, D.8
  • 78
    • 34548748173 scopus 로고    scopus 로고
    • The pharmaceutical potential of histone deacetylase inhibitors
    • Elaut, G.; Rogiers, V.; Vanhaecke, T. The pharmaceutical potential of histone deacetylase inhibitors. Curr. Pharm. Des. 2007, 13, 2584-2620.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2584-2620
    • Elaut, G.1    Rogiers, V.2    Vanhaecke, T.3
  • 80
  • 83
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • Bradbury, C. A.; Khanim, F. L.; Hayden, R.; Bunce, C. M.; White, D. A.; Drayson, M. T.; Craddock, C.; Turner, B. M. Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 2005, 19, 1751-1759.
    • (2005) Leukemia , vol.19 , pp. 1751-1759
    • Bradbury, C.A.1    Khanim, F.L.2    Hayden, R.3    Bunce, C.M.4    White, D.A.5    Drayson, M.T.6    Craddock, C.7    Turner, B.M.8
  • 87
    • 44049101802 scopus 로고    scopus 로고
    • Identification of predictive biomarkers for the histone deacetylase inhibitor belinostat in a panel of human cancer cell lines
    • Dejligbjerg, M.; Grauslund, M.; Christensen, I. J.; Tjornelund, J.; Buhl Jensen, P.; Sehested, M. Identification of predictive biomarkers for the histone deacetylase inhibitor belinostat in a panel of human cancer cell lines. Cancer Biomark. 2008, 4, 101-109.
    • (2008) Cancer Biomark. , vol.4 , pp. 101-109
    • Dejligbjerg, M.1    Grauslund, M.2    Christensen, I.J.3    Tjornelund, J.4    Buhl Jensen, P.5    Sehested, M.6
  • 89
    • 40449140444 scopus 로고    scopus 로고
    • Modulation of TRAIL-induced apoptosis by HDAC inhibitors
    • Fulda, S. Modulation of TRAIL-induced apoptosis by HDAC inhibitors. Curr. Cancer Drug Targets 2008, 8, 132-140.
    • (2008) Curr. Cancer Drug Targets , vol.8 , pp. 132-140
    • Fulda, S.1
  • 90
    • 36849058762 scopus 로고    scopus 로고
    • Deciphering AP-1 function in tumorigenesis: Fra-ternizing on target promoters
    • Verde, P.; Casalino, L.; Talotta, F.; Yaniv, M.; Weitzman, J. B. Deciphering AP-1 function in tumorigenesis: fra-ternizing on target promoters. Cell Cycle 2007, 6, 2633-2639.
    • (2007) Cell Cycle , vol.6 , pp. 2633-2639
    • Verde, P.1    Casalino, L.2    Talotta, F.3    Yaniv, M.4    Weitzman, J.B.5
  • 91
    • 0030956308 scopus 로고    scopus 로고
    • Hydroxyurea for treatment of unresectable and recurrent meningiomas. I. Inhibition of primary human meningioma cells in culture and in meningioma transplants by induction of the apoptotic pathway
    • Schrell, U. M.; Rittig, M. G.; Anders, M.; Kiesewetter, F.; Marschalek, R.; Koch, U. H.; Fahlbusch, R. Hydroxyurea for treatment of unresectable and recurrent meningiomas. I. Inhibition of primary human meningioma cells in culture and in meningioma transplants by induction of the apoptotic pathway. J. Neurosurg. 1997, 86, 845-852.
    • (1997) J. Neurosurg. , vol.86 , pp. 845-852
    • Schrell, U.M.1    Rittig, M.G.2    Anders, M.3    Kiesewetter, F.4    Marschalek, R.5    Koch, U.H.6    Fahlbusch, R.7
  • 92
    • 0035050818 scopus 로고    scopus 로고
    • Molecular remission following high-dose hydroxyurea and fludarabine plus cytarabine in a patient with simultaneous acute myeloid leukemia and low-grade lymphoma
    • Montefusco, E.; Fazi, F.; Cordone, I.; Ariola, C.; Nanni, M.; Spadea, A.; Spiriti, M. A.; Fenu, S.; Mandelli, F.; Petti, M. C. Molecular remission following high-dose hydroxyurea and fludarabine plus cytarabine in a patient with simultaneous acute myeloid leukemia and low-grade lymphoma. Leuk. Lymphoma 2001, 40, 671-674.
    • (2001) Leuk. Lymphoma , vol.40 , pp. 671-674
    • Montefusco, E.1    Fazi, F.2    Cordone, I.3    Ariola, C.4    Nanni, M.5    Spadea, A.6    Spiriti, M.A.7    Fenu, S.8    Mandelli, F.9    Petti, M.C.10
  • 93
    • 33745823841 scopus 로고    scopus 로고
    • Ribonucleotide reductase inhibitors and future drug design
    • Shao, J.; Zhou, B.; Chu, B.; Yen, Y. Ribonucleotide reductase inhibitors and future drug design. Curr. Cancer Drug Targets 2006, 6, 409-431.
    • (2006) Curr. Cancer Drug Targets , vol.6 , pp. 409-431
    • Shao, J.1    Zhou, B.2    Chu, B.3    Yen, Y.4
  • 94
    • 38749121729 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and hydroxyurea modulate the cell cycle and cooperatively induce apoptosis
    • Krämer, O. H.; Knauer, S. K.; Zimmermann, D.; Stauber, R. H.; Heinzel, T. Histone deacetylase inhibitors and hydroxyurea modulate the cell cycle and cooperatively induce apoptosis. Oncogene 2008, 27, 732-740.
    • (2008) Oncogene , vol.27 , pp. 732-740
    • Krämer, O.H.1    Knauer, S.K.2    Zimmermann, D.3    Stauber, R.H.4    Heinzel, T.5
  • 96
    • 0038079767 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1
    • Rosato, R. R.; Almenara, J. A.; Grant, S. The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1. Cancer Res. 2003, 63, 3637-3645.
    • (2003) Cancer Res. , vol.63 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 97
    • 1842481018 scopus 로고    scopus 로고
    • Abrogation of p21 expression by flavopiridol enhances depsipeptide-mediated apoptosis in malignant pleural mesothelioma cells
    • Nguyen, D. M.; Schrump, W. D.; Chen, G. A.; Tsai, W.; Nguyen, P.; Trepel, J. B.; Schrump, D. S. Abrogation of p21 expression by flavopiridol enhances depsipeptide-mediated apoptosis in malignant pleural mesothelioma cells. Clin. Cancer Res. 2004, 10, 1813-1825.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 1813-1825
    • Nguyen, D.M.1    Schrump, W.D.2    Chen, G.A.3    Tsai, W.4    Nguyen, P.5    Trepel, J.B.6    Schrump, D.S.7
  • 98
    • 77950643012 scopus 로고    scopus 로고
    • Redefining the role of interferon in the treatment of malignant diseases
    • Bracarda, S.; Eggermont, A. M.; Samuelsson, J. Redefining the role of interferon in the treatment of malignant diseases. Eur. J. Cancer 2009.
    • (2009) Eur. J. Cancer
    • Bracarda, S.1    Eggermont, A.M.2    Samuelsson, J.3
  • 99
    • 71849101259 scopus 로고    scopus 로고
    • Phosphorylation-acetylation switch in the regulation of STAT1 signaling
    • Krämer, O. H.; Heinzel, T. Phosphorylation-acetylation switch in the regulation of STAT1 signaling. Mol. Cell Endocrinol. 2010, 315(1-2), 40-48.
    • (2010) Mol. Cell Endocrinol. , vol.315 , Issue.1-2 , pp. 40-48
    • Krämer, O.H.1    Heinzel, T.2
  • 100
    • 33645839013 scopus 로고    scopus 로고
    • Signal transducers and activators of transcription (STATs): Novel targets of chemopreventive and chemotherapeutic drugs
    • Klampfer, L. Signal transducers and activators of transcription (STATs): Novel targets of chemopreventive and chemotherapeutic drugs. Curr. Cancer Drug Targets 2006, 6, 107-121.
    • (2006) Curr. Cancer Drug Targets , vol.6 , pp. 107-121
    • Klampfer, L.1
  • 101
    • 3142721913 scopus 로고    scopus 로고
    • Requirement of histone deacetylase activity for signaling by STAT1
    • Klampfer, L.; Huang, J.; Swaby, L. A.; Augenlicht, L. Requirement of histone deacetylase activity for signaling by STAT1. J. Biol. Chem. 2004, 279, 30358-30368.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30358-30368
    • Klampfer, L.1    Huang, J.2    Swaby, L.A.3    Augenlicht, L.4
  • 103
    • 33645069138 scopus 로고    scopus 로고
    • Increased MDR1 expression in normal and malignant peripheral blood mononuclear cells obtained from patients receiving depsipeptide (FR901228, FK228, NSC630176)
    • Robey, R. W.; Zhan, Z.; Piekarz, R. L.; Kayastha, G. L.; Fojo, T.; Bates, S. E. Increased MDR1 expression in normal and malignant peripheral blood mononuclear cells obtained from patients receiving depsipeptide (FR901228, FK228, NSC630176). Clin. Cancer Res. 2006, 12, 1547-1555.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 1547-1555
    • Robey, R.W.1    Zhan, Z.2    Piekarz, R.L.3    Kayastha, G.L.4    Fojo, T.5    Bates, S.E.6
  • 104
    • 38449122336 scopus 로고    scopus 로고
    • The histone deacetylase inhibitors suberoylanilide hydroxamic (Vorinostat) and valproic acid induce irreversible and MDR1-independent resistance in human colon cancer cells
    • Fedier, A.; Dedes, K. J.; Imesch, P.; Von Bueren, A. O.; Fink, D. The histone deacetylase inhibitors suberoylanilide hydroxamic (Vorinostat) and valproic acid induce irreversible and MDR1-independent resistance in human colon cancer cells. Int. J. Oncol. 2007, 31, 633-641.
    • (2007) Int. J. Oncol. , vol.31 , pp. 633-641
    • Fedier, A.1    Dedes, K.J.2    Imesch, P.3    Von Bueren, A.O.4    Fink, D.5
  • 105
    • 37549022694 scopus 로고    scopus 로고
    • DNA methyltransferase and histone deacetylase inhibitors in the treatment of myelodysplastic syndromes
    • Griffiths, E. A.; Gore, S. D. DNA methyltransferase and histone deacetylase inhibitors in the treatment of myelodysplastic syndromes. Semin. Hematol. 2008, 45, 23-30.
    • (2008) Semin. Hematol. , vol.45 , pp. 23-30
    • Griffiths, E.A.1    Gore, S.D.2
  • 111
    • 38449099535 scopus 로고    scopus 로고
    • The epigenetic modifier, valproic acid, enhances radiation sensitivity
    • Karagiannis, T. C.; Kn, H.; El-Osta, A. The epigenetic modifier, valproic acid, enhances radiation sensitivity. Epigenetics 2006, 1, 131-137.
    • (2006) Epigenetics , vol.1 , pp. 131-137
    • Karagiannis, T.C.1    Kn, H.2    El-Osta, A.3
  • 112
    • 67349285731 scopus 로고    scopus 로고
    • Enhancing the apoptotic and therapeutic effects of HDAC inhibitors
    • Frew, A. J.; Johnstone, R. W.; Bolden, J. E. Enhancing the apoptotic and therapeutic effects of HDAC inhibitors. Cancer Lett. 2009, 280, 125-133.
    • (2009) Cancer Lett. , vol.280 , pp. 125-133
    • Frew, A.J.1    Johnstone, R.W.2    Bolden, J.E.3
  • 113
    • 29744454120 scopus 로고    scopus 로고
    • The histone deacetylase (HDAC) inhibitor valproic acid as monotherapy or in combination with all-trans retinoic acid in patients with acute myeloid leukemia
    • Kuendgen, A.; Schmid, M.; Schlenk, R.; Knipp, S.; Hildebrandt, B.; Steidl, C.; Germing, U.; Haas, R.; Dohner, H.; Gattermann, N. The histone deacetylase (HDAC) inhibitor valproic acid as monotherapy or in combination with all-trans retinoic acid in patients with acute myeloid leukemia. Cancer 2006, 106, 112-119.
    • (2006) Cancer , vol.106 , pp. 112-119
    • Kuendgen, A.1    Schmid, M.2    Schlenk, R.3    Knipp, S.4    Hildebrandt, B.5    Steidl, C.6    Germing, U.7    Haas, R.8    Dohner, H.9    Gattermann, N.10
  • 115
    • 3142692649 scopus 로고    scopus 로고
    • Valproic acid inhibits proliferation and induces apoptosis in acute myeloid leukemia cells expressing P-gp and MRP1
    • Tang, R.; Faussat, A. M.; Majdak, P.; Perrot, J. Y.; Chaoui, D.; Legrand, O.; Marie, J. P. Valproic acid inhibits proliferation and induces apoptosis in acute myeloid leukemia cells expressing P-gp and MRP1. Leukemia 2004, 18, 1246-1251.
    • (2004) Leukemia , vol.18 , pp. 1246-1251
    • Tang, R.1    Faussat, A.M.2    Majdak, P.3    Perrot, J.Y.4    Chaoui, D.5    Legrand, O.6    Marie, J.P.7
  • 116
    • 0036721055 scopus 로고    scopus 로고
    • Anti-tumor mechanisms of valproate: A novel role for an old drug
    • Blaheta, R. A.; Cinatl, J., Jr. Anti-tumor mechanisms of valproate: a novel role for an old drug. Med. Res. Rev. 2002, 22, 492-511.
    • (2002) Med. Res. Rev. , vol.22 , pp. 492-511
    • Blaheta, R.A.1    Cinatl Jr., J.2
  • 117
    • 21744444434 scopus 로고    scopus 로고
    • Evolving anticancer drug valproic acid: Insights into the mechanism and clinical studies
    • Blaheta, R. A.; Michaelis, M.; Driever, P. H.; Cinatl, J., Jr. Evolving anticancer drug valproic acid: insights into the mechanism and clinical studies. Med. Res. Rev. 2005, 25, 383-397.
    • (2005) Med. Res. Rev. , vol.25 , pp. 383-397
    • Blaheta, R.A.1    Michaelis, M.2    Driever, P.H.3    Cinatl Jr., J.4
  • 118
    • 34548176264 scopus 로고    scopus 로고
    • Valproic acid for the treatment of myeloid malignancies
    • Kuendgen, A.; Gattermann, N. Valproic acid for the treatment of myeloid malignancies. Cancer 2007, 110, 943-954.
    • (2007) Cancer , vol.110 , pp. 943-954
    • Kuendgen, A.1    Gattermann, N.2
  • 119
    • 0038555374 scopus 로고    scopus 로고
    • Short-chain fatty acid inhibitors of histone deacetylases: Promising anticancer therapeutics?
    • Chen, J. S.; Faller, D. V.; Spanjaard, R. A. Short-chain fatty acid inhibitors of histone deacetylases: promising anticancer therapeutics? Curr. Cancer Drug Targets 2003, 3, 219-236.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 219-236
    • Chen, J.S.1    Faller, D.V.2    Spanjaard, R.A.3
  • 120
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell, R. P., Jr.; He, L. Z.; Richon, V.; Calleja, E.; Pandolfi, P. P. Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J. Natl. Cancer Inst. 1998, 90, 1621-1625.
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 1621-1625
    • Warrell Jr., R.P.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 122
    • 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.; Klein, P. S. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 2001, 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
  • 123
    • 26944443973 scopus 로고    scopus 로고
    • Prolonged molecular remission in PMLRARalpha-positive acute promyelocytic leukemia treated with minimal chemotherapy followed by maintenance including the histone deacetylase inhibitor sodium valproate
    • McMullin, M. F.; Nugent, E.; Thompson, A.; Hull, D.; Jones, F. G.; Grimwade, D. Prolonged molecular remission in PMLRARalpha-positive acute promyelocytic leukemia treated with minimal chemotherapy followed by maintenance including the histone deacetylase inhibitor sodium valproate. Leukemia 2005, 19, 1676-1677.
    • (2005) Leukemia , vol.19 , pp. 1676-1677
    • McMullin, M.F.1    Nugent, E.2    Thompson, A.3    Hull, D.4    Jones, F.G.5    Grimwade, D.6
  • 124
    • 4444309863 scopus 로고    scopus 로고
    • Treatment of myelodysplastic syndromes with valproic acid alone or in combination with all-trans retinoic acid
    • Kuendgen, A.; Strupp, C.; Aivado, M.; Bernhardt, A.; Hildebrandt, B.; Haas, R.; Germing, U.; Gattermann, N. Treatment of myelodysplastic syndromes with valproic acid alone or in combination with all-trans retinoic acid. Blood 2004, 104, 1266-1269.
    • (2004) Blood , vol.104 , pp. 1266-1269
    • Kuendgen, A.1    Strupp, C.2    Aivado, M.3    Bernhardt, A.4    Hildebrandt, B.5    Haas, R.6    Germing, U.7    Gattermann, N.8
  • 126
    • 29144481615 scopus 로고    scopus 로고
    • Results of a phase 2 study of valproic acid alone or in combination with alltrans retinoic acid in 75 patients with myelodysplastic syndrome and relapsed or refractory acute myeloid leukemia
    • Kuendgen, A.; Knipp, S.; Fox, F.; Strupp, C.; Hildebrandt, B.; Steidl, C.; Germing, U.; Haas, R.; Gattermann, N. Results of a phase 2 study of valproic acid alone or in combination with alltrans retinoic acid in 75 patients with myelodysplastic syndrome and relapsed or refractory acute myeloid leukemia. Ann. Hematol. 2005, 84(Suppl 1), 61-66.
    • (2005) Ann. Hematol. , vol.84 , Issue.SUPPL. 1 , pp. 61-66
    • Kuendgen, A.1    Knipp, S.2    Fox, F.3    Strupp, C.4    Hildebrandt, B.5    Steidl, C.6    Germing, U.7    Haas, R.8    Gattermann, N.9
  • 133
    • 58149377828 scopus 로고    scopus 로고
    • Multicenter phase II trial of the histone deacetylase inhibitor pyridylmethyl-N-{4-[(2-aminophenyl)-carbamoyl]-benzyl}-carbamate in pretreated metastatic melanoma
    • Hauschild, A.; Trefzer, U.; Garbe, C.; Kaehler, K. C.; Ugurel, S.; Kiecker, F.; Eigentler, T.; Krissel, H.; Schott, A.; Schadendorf, D. Multicenter phase II trial of the histone deacetylase inhibitor pyridylmethyl-N-{4-[(2- aminophenyl)-carbamoyl]-benzyl}-carbamate in pretreated metastatic melanoma. Melanoma Res. 2008, 18, 274-278.
    • (2008) Melanoma Res. , vol.18 , pp. 274-278
    • Hauschild, A.1    Trefzer, U.2    Garbe, C.3    Kaehler, K.C.4    Ugurel, S.5    Kiecker, F.6    Eigentler, T.7    Krissel, H.8    Schott, A.9    Schadendorf, D.10
  • 136
    • 51449095189 scopus 로고    scopus 로고
    • Promising antitumor activity with MGCD0103, a novel isotype-selective histone deacetylase inhibitor
    • Le Tourneau, C.; Siu, L. L. Promising antitumor activity with MGCD0103, a novel isotype-selective histone deacetylase inhibitor. Expert Opin Investig. Drugs 2008, 17, 1247-1254.
    • (2008) Expert Opin Investig. Drugs , vol.17 , pp. 1247-1254
    • Le Tourneau, C.1    Siu, L.L.2
  • 137
    • 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.; Bates, S. E. Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report. Blood 2001, 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
  • 138
    • 0036889625 scopus 로고    scopus 로고
    • Arginine butyrate increases the cytotoxicity of DAB(389)IL-2 in leukemia and lymphoma cells by upregulation of IL-2Rbeta gene
    • Shao, R. H.; Tian, X.; Gorgun, G.; Urbano, A. G.; Foss, F. M. Arginine butyrate increases the cytotoxicity of DAB(389)IL-2 in leukemia and lymphoma cells by upregulation of IL-2Rbeta gene. Leuk. Res. 2002, 26, 1077-1083.
    • (2002) Leuk. Res. , vol.26 , pp. 1077-1083
    • Shao, R.H.1    Tian, X.2    Gorgun, G.3    Urbano, A.G.4    Foss, F.M.5
  • 140
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • Zhang, C. L.; McKinsey, T. A.; Chang, S.; Antos, C. L.; Hill, J. A.; Olson, E. N. Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell 2002, 110, 479-488.
    • (2002) Cell , vol.110 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3    Antos, C.L.4    Hill, J.A.5    Olson, E.N.6
  • 146
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-cell lymphoma
    • Mann, B. S.; Johnson, J. R.; Cohen, M. H.; Justice, R.; Pazdur, R. FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma. Oncologist 2007, 12, 1247-1252.
    • (2007) Oncologist , vol.12 , pp. 1247-1252
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 149
    • 38149140216 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor vorinostat (Zolinza, suberoylanilide hydroxamic acid, SAHA) in patients with recurrent and/or metastatic head and neck cancer
    • Blumenschein, G. R., Jr.; Kies, M. S.; Papadimitrakopoulou, V. A.; Lu, C.; Kumar, A. J.; Ricker, J. L.; Chiao, J. H.; Chen, C.; Frankel, S. R. Phase II trial of the histone deacetylase inhibitor vorinostat (Zolinza, suberoylanilide hydroxamic acid, SAHA) in patients with recurrent and/or metastatic head and neck cancer. Invest. New Drugs 2008, 26, 81-87.
    • (2008) Invest. New Drugs , vol.26 , pp. 81-87
    • Blumenschein Jr., G.R.1    Kies, M.S.2    Papadimitrakopoulou, V.A.3    Lu, C.4    Kumar, A.J.5    Ricker, J.L.6    Chiao, J.H.7    Chen, C.8    Frankel, S.R.9
  • 150
    • 33244458274 scopus 로고    scopus 로고
    • Potential role of histone deacetylase inhibitors in mesothelioma: Clinical experience with suberoylanilide hydroxamic acid
    • Krug, L. M.; Curley, T.; Schwartz, L.; Richardson, S.; Marks, P.; Chiao, J.; Kelly, W. K. Potential role of histone deacetylase inhibitors in mesothelioma: clinical experience with suberoylanilide hydroxamic acid. Clin. Lung Cancer 2006, 7, 257-261.
    • (2006) Clin. Lung Cancer , vol.7 , pp. 257-261
    • Krug, L.M.1    Curley, T.2    Schwartz, L.3    Richardson, S.4    Marks, P.5    Chiao, J.6    Kelly, W.K.7
  • 152
  • 154
    • 49349104503 scopus 로고    scopus 로고
    • A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia
    • Gimsing, P.; Hansen, M.; Knudsen, L. M.; Knoblauch, P.; Christensen, I. J.; Ooi, C. E.; Buhl-Jensen, P. A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia. Eur. J. Haematol. 2008, 81, 170-176.
    • (2008) Eur. J. Haematol. , vol.81 , pp. 170-176
    • Gimsing, P.1    Hansen, M.2    Knudsen, L.M.3    Knoblauch, P.4    Christensen, I.J.5    Ooi, C.E.6    Buhl-Jensen, P.7
  • 155
    • 31444438952 scopus 로고    scopus 로고
    • Pilot study of combination transcriptional modulation therapy with sodium phenylbutyrate and 5-azacytidine in patients with acute myeloid leukemia or myelodysplastic syndrome
    • Maslak, P.; Chanel, S.; Camacho, L. H.; Soignet, S.; Pandolfi, P. P.; Guernah, I.; Warrell, R.; Nimer, S. Pilot study of combination transcriptional modulation therapy with sodium phenylbutyrate and 5-azacytidine in patients with acute myeloid leukemia or myelodysplastic syndrome. Leukemia 2006, 20, 212-217.
    • (2006) Leukemia , vol.20 , pp. 212-217
    • Maslak, P.1    Chanel, S.2    Camacho, L.H.3    Soignet, S.4    Pandolfi, P.P.5    Guernah, I.6    Warrell, R.7    Nimer, S.8


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