메뉴 건너뛰기




Volumn 9, Issue 6, 2009, Pages 661-692

Histone deacetylase inhibitors: Design, structure-activity relationships and therapeutic implications for cancer

Author keywords

Benzamide; Cancer therapy; Cyclic peptide; HDAC isoform; Histone deacetylase (HDAC); Histone deacetylase inhibitor; Hydroxamate; Zinc binding group

Indexed keywords

3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; ADS 100380; ANTINEOPLASTIC AGENT; BENZAMIDE DERIVATIVE; CINNAMOHYDROXAMIC ACID DERIVATIVE; CRA 024781; CRA 026440; CYCLODEPSIPEPTIDE DERIVATIVE; DU 145; FLUDARABINE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE; IMATINIB; ISOTRETINOIN; KETONE DERIVATIVE; MIDOSTAURIN; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; NVP LBH 8589; PANOBINOSTAT; PLACEBO; RECOMBINANT TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; RETINOIC ACID; ROMIDEPSIN; TANESPIMYCIN; THIOL DERIVATIVE; TRASTUZUMAB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VORINOSTAT;

EID: 70349128205     PISSN: 18715206     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152009788679976     Document Type: Review
Times cited : (73)

References (196)
  • 1
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Krüppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • Zhang, W.; Bieker, J. Acetylation and modulation of erythroid Krüppel-like factor (EKLF) activity by interaction with histone acetyltransferases J. Proc. Natl. Acad. Sci. USA, 1998, 95, 9855-9860.
    • (1998) J. Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.2
  • 2
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin, M. J.; Kadonaga, J. T. What's up and down with histone deacetylation and transcription? Cell, 1997, 89(3), 325-328.
    • (1997) Cell , vol.89 , Issue.3 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 3
    • 0035377556 scopus 로고    scopus 로고
    • Protein modules that manipulate histone tails for chromatin regulation
    • Marmorstein, R. Protein modules that manipulate histone tails for chromatin regulation. Nat. Rev. Mol. Cell. Biol., 2001, 2(6), 422-432.
    • (2001) Nat. Rev. Mol. Cell. Biol , vol.2 , Issue.6 , pp. 422-432
    • Marmorstein, R.1
  • 5
    • 0037382605 scopus 로고    scopus 로고
    • Functional consequences of histone modifications
    • Iizuka, M.; Smith, M. M. Functional consequences of histone modifications. Curr. Opin. Genet. Dev., 2003, 13(2), 154-160.
    • (2003) Curr. Opin. Genet. Dev , vol.13 , Issue.2 , pp. 154-160
    • Iizuka, M.1    Smith, M.M.2
  • 6
    • 23844514827 scopus 로고    scopus 로고
    • Chromatin modifications as targets for new anticancer drugs
    • Schaefer, S.; Jung, M. Chromatin modifications as targets for new anticancer drugs. Arch. Pharm., 2005, 338, 347-357.
    • (2005) Arch. Pharm , vol.338 , pp. 347-357
    • Schaefer, S.1    Jung, M.2
  • 7
    • 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
  • 8
    • 20344392202 scopus 로고    scopus 로고
    • Epigenetics - An epicenter of gene regulation: Histones and histone-modifying enzymes A
    • Biel, M.; Wascholowski, V.; Giannis, Epigenetics - An epicenter of gene regulation: Histones and histone-modifying enzymes A. Angew. Chem., Int. Ed., 2005, 44, 3186-3216.
    • (2005) Angew. Chem., Int. Ed , vol.44 , pp. 3186-3216
    • Biel, M.1    Wascholowski, V.2    Giannis3
  • 9
    • 33646002067 scopus 로고    scopus 로고
    • Chemistry and biology of chromatin remodeling agents: State of art and future perspectives of HDAC inhibitors
    • Rodriquez, M.; Aquino, M.; Bruno, I.; De Martino, G.; Taddei, M.; Gomez-Paloma, L. Chemistry and biology of chromatin remodeling agents: state of art and future perspectives of HDAC inhibitors. Curr. Med. Chem., 2006, 13, 1119-1139.
    • (2006) Curr. Med. Chem , vol.13 , pp. 1119-1139
    • Rodriquez, M.1    Aquino, M.2    Bruno, I.3    De Martino, G.4    Taddei, M.5    Gomez-Paloma, L.6
  • 10
    • 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
  • 11
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J., 2000, 19, 1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 12
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo, J.; Nikoaev, A. Y.; Imai, S.; Chen, D.; Su, F.; Shiloh, A.; Guarente, L.; Gu, W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell, 2001, 107, 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikoaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 14
    • 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
  • 16
    • 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(19), 6170-6178.
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 6170-6178
    • Gantt, S.L.1    Gattis, S.G.2    Fierke, C.A.3
  • 18
  • 20
    • 3142562372 scopus 로고    scopus 로고
    • Somoza, J. R.; Skene, R. J.; Katz, B. A.; Mol, C.; Ho, J. D.; Jennings, A. J.; Luong, C.; Arvai, A.; Buggy, J. J.; Chi, E.; Tang, J.; Sang, B.-C..; Verner, E.; Wynands, R.; Leahy, E. M.; Dougan, D. R.; Snell, G.; Navre, M.; Knuth, M. W.; Swanson, R. V.; McRee, D.E.; Tari, L.W. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure, 2004, 12, 1325-1334.
    • Somoza, J. R.; Skene, R. J.; Katz, B. A.; Mol, C.; Ho, J. D.; Jennings, A. J.; Luong, C.; Arvai, A.; Buggy, J. J.; Chi, E.; Tang, J.; Sang, B.-C..; Verner, E.; Wynands, R.; Leahy, E. M.; Dougan, D. R.; Snell, G.; Navre, M.; Knuth, M. W.; Swanson, R. V.; McRee, D.E.; Tari, L.W. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure, 2004, 12, 1325-1334.
  • 21
    • 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
  • 22
    • 2942545807 scopus 로고    scopus 로고
    • On the function of the 14 A long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors
    • Wang, D.-F.; Wiest, O.; Helquist, P.; Lan-Hargest, H.-Y.; Wiech, N. L. On the function of the 14 A long internal cavity of histone deacetylase-like protein: implications for the design of histone deacetylase inhibitors. J. Med. Chem., 2004, 47, 3409-3417.
    • (2004) J. Med. Chem , vol.47 , pp. 3409-3417
    • Wang, D.-F.1    Wiest, O.2    Helquist, P.3    Lan-Hargest, H.-Y.4    Wiech, N.L.5
  • 24
    • 33646021957 scopus 로고    scopus 로고
    • Unexpected deacetylation mechanism suggested by a density functional theory QM/MM study of histone-deacetylase-like protein
    • Corminboeuf, C.; Hu, P.; Tuckerman, M. E.; Zhang, Y. Unexpected deacetylation mechanism suggested by a density functional theory QM/MM study of histone-deacetylase-like protein. J. Am. Chem. Soc., 2006, 128, 4530-4531.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4530-4531
    • Corminboeuf, C.1    Hu, P.2    Tuckerman, M.E.3    Zhang, Y.4
  • 25
    • 1542304635 scopus 로고    scopus 로고
    • Synthetic analogues relevant to the structure and function of zinc enzymes
    • Parkin, G. Synthetic analogues relevant to the structure and function of zinc enzymes. Chem. Rev., 2004, 104, 699-767.
    • (2004) Chem. Rev , vol.104 , pp. 699-767
    • Parkin, G.1
  • 26
    • 33745356936 scopus 로고    scopus 로고
    • 3-D QSAR studies on histone deacetylase inhibitors. A GOLPE/GRID approach on different series of compounds
    • Ragno, R.; Simeoni, S.; Valente, S.; Massa, S.; Mai, A. 3-D QSAR studies on histone deacetylase inhibitors. A GOLPE/GRID approach on different series of compounds. J. Chem. Inf. Model., 2006, 46, 1420-1430.
    • (2006) J. Chem. Inf. Model , vol.46 , pp. 1420-1430
    • Ragno, R.1    Simeoni, S.2    Valente, S.3    Massa, S.4    Mai, A.5
  • 27
    • 0032484989 scopus 로고    scopus 로고
    • Micromolded PDMS planar electrode allows patch clamp electrical recordings from cells
    • Brehm, A.; Miska, E. A.; McCance, D. J.; Reid, J. L.; Bannister, A. J.; Kouzarides, T. Micromolded PDMS planar electrode allows patch clamp electrical recordings from cells. Nature, 1998, 391, 597-604.
    • (1998) Nature , vol.391 , pp. 597-604
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 28
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters
    • Robertson, K. D.; Ait-Si-Ali, S.; Yokochi, T.; Wade, P. A.; Jones, P. L.; Wolffe, A. P. DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat. Genet., 2000, 25, 338-342.
    • (2000) Nat. Genet , vol.25 , pp. 338-342
    • Robertson, K.D.1    Ait-Si-Ali, S.2    Yokochi, T.3    Wade, P.A.4    Jones, P.L.5    Wolffe, A.P.6
  • 29
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao, H. Y.; Downes, M.; Ordentlich, P.; Evans, R. M. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev., 2000, 14, 55-66.
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 30
    • 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.; Kouzarides, T. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J., 1999, 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
  • 32
    • 18644365597 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors differentially stabilize acetylated p53 and induce cell cycle arrest or apoptosis in prostate cancer cells
    • 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 Differ., 2005, 12, 482-491.
    • (2005) Cell Death Differ , vol.12 , pp. 482-491
    • Roy, S.1    Packman, K.2    Jeffrey, R.3    Tenniswood, M.4
  • 34
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto, H.; Hawke, D.; Kobayashi, R.; Verreault, A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature, 2005, 436, 294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 37
    • 2342603414 scopus 로고    scopus 로고
    • Expression of keratinocyte growth factor and its receptor in human breast cancer: Its inhibitory role in the induction of apoptosis possibly through the overexpression of Bcl-2
    • Zhu, P.; Martin, E.; Mengwasser, J.; Schlag, P.; Janssen, K. P.; Gottlicher, M. Expression of keratinocyte growth factor and its receptor in human breast cancer: its inhibitory role in the induction of apoptosis possibly through the overexpression of Bcl-2. Cancer Cell, 2004, 5, 455-464.
    • (2004) Cancer Cell , vol.5 , pp. 455-464
    • Zhu, P.1    Martin, E.2    Mengwasser, J.3    Schlag, P.4    Janssen, K.P.5    Gottlicher, M.6
  • 38
    • 0033634946 scopus 로고    scopus 로고
    • Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers
    • Lin, R. J.; Evans, R. M. Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers. Mol. Cell, 2000, 5, 821-830.
    • (2000) Mol. Cell , vol.5 , pp. 821-830
    • Lin, R.J.1    Evans, R.M.2
  • 39
    • 0034817075 scopus 로고    scopus 로고
    • Amann, J. M.; Nip, J.; Strom, D. K.; Lutterbach, B.; Harada, H.; Lenny, N.; Downing, J. R.; Meyers, S.; Hiebert, S. W. ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol. Cell Biol., 2001, 21, 6470-6483.
    • Amann, J. M.; Nip, J.; Strom, D. K.; Lutterbach, B.; Harada, H.; Lenny, N.; Downing, J. R.; Meyers, S.; Hiebert, S. W. ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol. Cell Biol., 2001, 21, 6470-6483.
  • 40
    • 0032516221 scopus 로고    scopus 로고
    • Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein
    • David, G.; Alland, L.; Hong, S. H.; Wong, C. W.; DePinho, R. A.; Dejean, A. Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein. Oncogene, 1998, 16, 2549-2556.
    • (1998) Oncogene , vol.16 , pp. 2549-2556
    • David, G.1    Alland, L.2    Hong, S.H.3    Wong, C.W.4    DePinho, R.A.5    Dejean, A.6
  • 41
    • 0032531688 scopus 로고    scopus 로고
    • The LAZ3(BCL-6) oncoprotein recruits a SMRT/ mSIN3A/histone deacetylase containing complex to mediate transcriptional repression
    • Dhordain, P.; Lin, R. J.; Quief, S.; Lantoine, D.; Kerckaert, J. P.; Evans, R. M.; Albagli, O. The LAZ3(BCL-6) oncoprotein recruits a SMRT/ mSIN3A/histone deacetylase containing complex to mediate transcriptional repression. Nucl. Acids Res., 1998, 26, 4645-4651.
    • (1998) Nucl. Acids Res , vol.26 , pp. 4645-4651
    • Dhordain, P.1    Lin, R.J.2    Quief, S.3    Lantoine, D.4    Kerckaert, J.P.5    Evans, R.M.6    Albagli, O.7
  • 42
    • 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
  • 43
    • 33645950778 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Multifunctional anticancer agents
    • Liu, T.; Kuljaca, S.; Tee, A.; Marshall, G. M. Histone deacetylase inhibitors: Multifunctional anticancer agents Cancer Treat. Rev., 2006, 32, 157-165.
    • (2006) Cancer Treat. Rev , vol.32 , pp. 157-165
    • Liu, T.1    Kuljaca, S.2    Tee, A.3    Marshall, G.M.4
  • 44
    • 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
  • 45
    • 0034665124 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo
    • Butler, L. M.; Agus, D. B.; Scher, H. I.; Higgins, B.; Rose, A.; Cordon-Cardo, C.; Thaler, H. T.; Rifkind, R. A.; Marks, P. A.; Richon, V. M. Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo. Cancer Res., 2000, 60, 5165-5170.
    • (2000) Cancer Res , vol.60 , pp. 5165-5170
    • Butler, L.M.1    Agus, D.B.2    Scher, H.I.3    Higgins, B.4    Rose, A.5    Cordon-Cardo, C.6    Thaler, H.T.7    Rifkind, R.A.8    Marks, P.A.9    Richon, V.M.10
  • 46
    • 0034252183 scopus 로고    scopus 로고
    • Histone acetylation modifiers in the pathogenesis of malignant disease
    • Mahlknecht, U.; Hoelzner, D. Histone acetylation modifiers in the pathogenesis of malignant disease. Mol. Med., 2000, 6, 623-644
    • (2000) Mol. Med , vol.6 , pp. 623-644
    • Mahlknecht, U.1    Hoelzner, D.2
  • 48
    • 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.; Hodin, R. A. p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc. Natl. Acad. Sci. USA, 1998, 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
  • 50
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone, R. W.; Licht, J. D. Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target? Cancer Cell, 2003, 4, 13-18.
    • (2003) Cancer Cell , vol.4 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 51
    • 0033590071 scopus 로고    scopus 로고
    • The retinoblastoma gene family in differentiation and development
    • Lipinski, M. M.; Jacks, T. The retinoblastoma gene family in differentiation and development. Oncogene 1999, 18, 7873-7882.
    • (1999) Oncogene , vol.18 , pp. 7873-7882
    • Lipinski, M.M.1    Jacks, T.2
  • 52
    • 0035834786 scopus 로고    scopus 로고
    • Kwon, S. H.; Ahn, S. H.; Kim, Y. K.; Bae, G.-U.; Yoon, J. W.; Hong, S.; Lee, H. Y.; Lee, Y.-W.; Lee, H.-W.; Han, J.-W. Activation of p21(WAF1-Cip1) transcription through Sp1 sites by histone deacetylase inhibitor apicidin - Involvement of protein kinase C. J. Biol. Chem., 2001, 276, 42084-42090. 53 Druesne-Pecollo, N.; Pagniez, A.; Thomas, M.; Cherbuy, C.; Duée, P. H.; Martel, P.; Chaumontet, C. Diallyl disulfide increases CDKN1A promoter-associated histone acetylation in human colon tumor cell lines. J. Agric. Food Chem., 2006, 54, 7503-7507.
    • Kwon, S. H.; Ahn, S. H.; Kim, Y. K.; Bae, G.-U.; Yoon, J. W.; Hong, S.; Lee, H. Y.; Lee, Y.-W.; Lee, H.-W.; Han, J.-W. Activation of p21(WAF1-Cip1) transcription through Sp1 sites by histone deacetylase inhibitor apicidin - Involvement of protein kinase C. J. Biol. Chem., 2001, 276, 42084-42090. 53 Druesne-Pecollo, N.; Pagniez, A.; Thomas, M.; Cherbuy, C.; Duée, P. H.; Martel, P.; Chaumontet, C. Diallyl disulfide increases CDKN1A promoter-associated histone acetylation in human colon tumor cell lines. J. Agric. Food Chem., 2006, 54, 7503-7507.
  • 53
    • 18944403682 scopus 로고    scopus 로고
    • Regulation of tissue-specific and extracellular matrix-related genes by a class I histone deacetylase
    • Whetstine, J. R.; Ceron, J.; Ladd, B.; Dufourcq, P.; Reinke, V.; Shi, Y. Regulation of tissue-specific and extracellular matrix-related genes by a class I histone deacetylase. Mol. Cell, 2005, 18, 483-490.
    • (2005) Mol. Cell , vol.18 , pp. 483-490
    • Whetstine, J.R.1    Ceron, J.2    Ladd, B.3    Dufourcq, P.4    Reinke, V.5    Shi, Y.6
  • 54
    • 4143057046 scopus 로고    scopus 로고
    • Topoisomerase II and histone deacetylase inhibitors delay the G2/M transition by triggering the p38 MAPK checkpoint pathway
    • Mikhailov, A.; Shinohara, M.; Rieder, C. L. Topoisomerase II and histone deacetylase inhibitors delay the G2/M transition by triggering the p38 MAPK checkpoint pathway. J. Cell Biol., 2004, 166, 517-526.
    • (2004) J. Cell Biol , vol.166 , pp. 517-526
    • Mikhailov, A.1    Shinohara, M.2    Rieder, C.L.3
  • 55
    • 2442430362 scopus 로고    scopus 로고
    • Expression of the metastasis-associated MTA1 protein and its relationship to deacetylation of the histone H4 in esophageal squamous cell carcinomas
    • Toh, Y.; Ohga, T.; Endo, K.; Adachi, E.; Kusumoto, H.; Haraguchi, M.; Okamura, T.; Nicolson, G. L. Expression of the metastasis-associated MTA1 protein and its relationship to deacetylation of the histone H4 in esophageal squamous cell carcinomas. Int. J. Cancer, 2004, 110, 362-367.
    • (2004) Int. J. Cancer , vol.110 , pp. 362-367
    • Toh, Y.1    Ohga, T.2    Endo, K.3    Adachi, E.4    Kusumoto, H.5    Haraguchi, M.6    Okamura, T.7    Nicolson, G.L.8
  • 56
    • 0142088869 scopus 로고    scopus 로고
    • Histone deacetylase 1 represses the small GTPase RhoB expression in human nonsmall lung carcinoma cell line
    • Wang, S.; Yan-Neale, Y.; Fischer, D.; Zeremski, M.; Cai, R.; Zhu, J.; Asselbergs, F.; Hampton, G.; Cohen, D. Histone deacetylase 1 represses the small GTPase RhoB expression in human nonsmall lung carcinoma cell line. Oncogene, 2003, 22, 6204-6213.
    • (2003) Oncogene , vol.22 , pp. 6204-6213
    • Wang, S.1    Yan-Neale, Y.2    Fischer, D.3    Zeremski, M.4    Cai, R.5    Zhu, J.6    Asselbergs, F.7    Hampton, G.8    Cohen, D.9
  • 57
    • 3142702962 scopus 로고    scopus 로고
    • Invasion of v-Fos(FBR)-transformed cells is dependent upon histone deacetylase activity and suppression of histone deacetylase regulated genes
    • Joseph, J.; Mudduluru, G.; Antony, S.; Vashistha, S.; Ajitkumar, P.; Somasundaram, K. Invasion of v-Fos(FBR)-transformed cells is dependent upon histone deacetylase activity and suppression of histone deacetylase regulated genes. Oncogene, 2004, 23, 5284-5292.
    • (2004) Oncogene , vol.23 , pp. 5284-5292
    • Joseph, J.1    Mudduluru, G.2    Antony, S.3    Vashistha, S.4    Ajitkumar, P.5    Somasundaram, K.6
  • 62
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity
    • Kato, H.; Tamamizu-Kato, S.; Shibasaki, F. Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity. J. Biol. Chem., 2004, 279, 41966-41974.
    • (2004) J. Biol. Chem , vol.279 , pp. 41966-41974
    • Kato, H.1    Tamamizu-Kato, S.2    Shibasaki, F.3
  • 63
    • 0037462884 scopus 로고    scopus 로고
    • Butyrate impairs intestinal tumor cell-induced angiogenesis by inhibiting HIF-1alpha nuclear translocation
    • Zgouras, D.; Wachtershauser, A.; Frings, D.; Stein, J. Butyrate impairs intestinal tumor cell-induced angiogenesis by inhibiting HIF-1alpha nuclear translocation. Biochem. Biophys. Res. Commun., 2003, 300, 832-838.
    • (2003) Biochem. Biophys. Res. Commun , vol.300 , pp. 832-838
    • Zgouras, D.1    Wachtershauser, A.2    Frings, D.3    Stein, J.4
  • 64
    • 1642312811 scopus 로고    scopus 로고
    • Modulation of angiogenesis-related protein synthesis by valproic acid
    • Zgouras, D.; Becker, U.; Loitsch, S.; Stein. Modulation of angiogenesis-related protein synthesis by valproic acid J. Biochem. Biophys. Res. Commun., 2004, 316, 693-697.
    • (2004) J. Biochem. Biophys. Res. Commun , vol.316 , pp. 693-697
    • Zgouras, D.1    Becker, U.2    Loitsch, S.3    Stein4
  • 66
    • 4644364508 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584
    • Qian, D. Z.; Wang, X.; Kachhap, S. K.; Kato, Y.; Wei, Y.; Zhang, L.; Atadja, P.; Pili, R. The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584. Cancer Res., 2004, 64, 6626-6634.
    • (2004) Cancer Res , vol.64 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3    Kato, Y.4    Wei, Y.5    Zhang, L.6    Atadja, P.7    Pili, R.8
  • 68
    • 20044390016 scopus 로고    scopus 로고
    • Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors
    • Ngo, L.; Holmgren, A.; Jiang, X.; Marks, P. A. Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proc. Natl. Acad. Sci. USA, 2005, 102, 673-678.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 673-678
    • Ngo, L.1    Holmgren, A.2    Jiang, X.3    Marks, P.A.4
  • 69
    • 20544471104 scopus 로고    scopus 로고
    • Ozone therapy effects on biomarkers and lung function in asthma
    • Marks, P. A.; Jiang, X.-J. Ozone therapy effects on biomarkers and lung function in asthma. Cell Cycle, 2005, 4, 549-554.
    • (2005) Cell Cycle , vol.4 , pp. 549-554
    • Marks, P.A.1    Jiang, X.-J.2
  • 70
    • 31644442355 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors require caspase activity to induce apoptosis in lung and prostate carcinoma cells
    • Sonnemann, H.; Hartwig, M.; Plath, A.; Kumar, K. S.; Muller, C.; Beck, J. F. Histone deacetylase inhibitors require caspase activity to induce apoptosis in lung and prostate carcinoma cells. Cancer Lett., 2006, 232, 148-160.
    • (2006) Cancer Lett , vol.232 , pp. 148-160
    • Sonnemann, H.1    Hartwig, M.2    Plath, A.3    Kumar, K.S.4    Muller, C.5    Beck, J.F.6
  • 71
    • 33845352223 scopus 로고    scopus 로고
    • Bim plays a crucial role in synergistic induction of apoptosis by the histone deacetylase inhibitor SBHA and TRAIL in melanoma cells
    • Gillespie, S.; Borrow, J.; Xu, D. Z.; Hersey, P. Bim plays a crucial role in synergistic induction of apoptosis by the histone deacetylase inhibitor SBHA and TRAIL in melanoma cells. Apoptosis, 2006, 11, 2251-2261.
    • (2006) Apoptosis , vol.11 , pp. 2251-2261
    • Gillespie, S.1    Borrow, J.2    Xu, D.Z.3    Hersey, P.4
  • 73
    • 33750288048 scopus 로고    scopus 로고
    • Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor
    • Xu, W. S.; Ngo, L.; Perez, G.; Dokmanovic, M.; Marks, P. A. Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor. Proc. Natl. Acad. Sci. USA, 2006, 103, 15540-15545.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15540-15545
    • Xu, W.S.1    Ngo, L.2    Perez, G.3    Dokmanovic, M.4    Marks, P.A.5
  • 74
    • 33644875208 scopus 로고    scopus 로고
    • Komatsu, N.; Kawamata, N.; Takeuchi, S.; Yin, D.; Chien, W. W.; Miller, C. W.; Koeffler, H. P. SAHA, a HDAC inhibitor, has profound anti-growth activity against non-small cell lung cancer cells. Oncol. Reports, 2006, 15, 187-191.
    • Komatsu, N.; Kawamata, N.; Takeuchi, S.; Yin, D.; Chien, W. W.; Miller, C. W.; Koeffler, H. P. SAHA, a HDAC inhibitor, has profound anti-growth activity against non-small cell lung cancer cells. Oncol. Reports, 2006, 15, 187-191.
  • 75
    • 22744459936 scopus 로고    scopus 로고
    • A new simple and high-yield synthesis of suberoylanilide hydroxamic acid and its inhibitory effect alone or in combination with retinoids on proliferation of human prostate cancer cells
    • Gediya, L. K.; Chopra, P.; Purushottamachar, P.; Maheshwari, N.; Njar, C. O. A new simple and high-yield synthesis of suberoylanilide hydroxamic acid and its inhibitory effect alone or in combination with retinoids on proliferation of human prostate cancer cells. J. Med. Chem., 2005, 48, 5047-5051.
    • (2005) J. Med. Chem , vol.48 , pp. 5047-5051
    • Gediya, L.K.1    Chopra, P.2    Purushottamachar, P.3    Maheshwari, N.4    Njar, C.O.5
  • 76
    • 33747836834 scopus 로고    scopus 로고
    • Activation of mitochondrial pathway is crucial for tumor selective induction of apoptosis by LAQ824
    • Wang, S. W.; Yan-Neale, Y.; Cai, R.; Alimov, I.; Cohen, D. Activation of mitochondrial pathway is crucial for tumor selective induction of apoptosis by LAQ824. Cell Cycle, 2006, 5, 1662-1668.
    • (2006) Cell Cycle , vol.5 , pp. 1662-1668
    • Wang, S.W.1    Yan-Neale, Y.2    Cai, R.3    Alimov, I.4    Cohen, D.5
  • 77
    • 30044434594 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide
    • Rosato, R. R.; Maggio, S. C.; Almenara, J. A.; Payne, S. G.; Atadja, P.; Spiegel, S.; Dent, P.; Grant, S. The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide. Mol. Pharmacol., 2006, 69, 216-225.
    • (2006) Mol. Pharmacol , vol.69 , pp. 216-225
    • Rosato, R.R.1    Maggio, S.C.2    Almenara, J.A.3    Payne, S.G.4    Atadja, P.5    Spiegel, S.6    Dent, P.7    Grant, S.8
  • 78
    • 33645817023 scopus 로고    scopus 로고
    • Anticancer activity of MS-275, a novel histone deacetylase inhibitor, against human endometrial cancer cells
    • Takai, N.; Ueda, T.; Nishida, M.; Nasu, K.; Narahara, H. Anticancer activity of MS-275, a novel histone deacetylase inhibitor, against human endometrial cancer cells. Anticancer Res., 2006, 26, 939-945.
    • (2006) Anticancer Res , vol.26 , pp. 939-945
    • Takai, N.1    Ueda, T.2    Nishida, M.3    Nasu, K.4    Narahara, H.5
  • 79
    • 33646839799 scopus 로고    scopus 로고
    • Sequence-dependent interaction between cisplatin and histone deacetylase inhibitors in human oral squamous cell carcinoma cells
    • Sato, T.; Suzuki, M.; Sato, Y.; Echigo, S.; Rikiishi, H. Sequence-dependent interaction between cisplatin and histone deacetylase inhibitors in human oral squamous cell carcinoma cells. Int. J. Oncol., 2006, 28, 1233-1241.
    • (2006) Int. J. Oncol , vol.28 , pp. 1233-1241
    • Sato, T.1    Suzuki, M.2    Sato, Y.3    Echigo, S.4    Rikiishi, H.5
  • 82
    • 33845231990 scopus 로고    scopus 로고
    • Ornithine decarboxylase activity in tumor cell lines correlates with sensitivity to cell death induced by histone deacetylase inhibitors
    • Saunders, L. R.; Verdin, E. Ornithine decarboxylase activity in tumor cell lines correlates with sensitivity to cell death induced by histone deacetylase inhibitors. Mol. Cancer Ther., 2006, 5, 2777-2785.
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2777-2785
    • Saunders, L.R.1    Verdin, E.2
  • 84
    • 85036838999 scopus 로고    scopus 로고
    • Lichenstein, H.; Jeffers, M. Combination therapies using HDAC inhibitors. WO 2006/082428.
    • Lichenstein, H.; Jeffers, M. Combination therapies using HDAC inhibitors. WO 2006/082428.
  • 85
    • 33845209109 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and paclitaxel cause synergistic effects on apoptosis and microtubule stabilization in papillary serous endometrial cancer cells
    • Dowdy, S. C.; Jiang, S. J.; Zhou, X. C.; Hou, X. N.; Jin, F.; Podratz, K. C.; Jiang, S. W. Histone deacetylase inhibitors and paclitaxel cause synergistic effects on apoptosis and microtubule stabilization in papillary serous endometrial cancer cells. Mol. Cancer Ther., 2006, 5, 2767-2776.
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2767-2776
    • Dowdy, S.C.1    Jiang, S.J.2    Zhou, X.C.3    Hou, X.N.4    Jin, F.5    Podratz, K.C.6    Jiang, S.W.7
  • 86
    • 32644438678 scopus 로고    scopus 로고
    • Up-regulation of MDR1 and induction of doxorubicin resistance by histone deacetylase inhibitor depsipeptide (FK228) and ATRA in acute promyelocytic leukemia cells
    • Tabe, Y.; Konopleva, M.; Contractor, R.; Munsell, M.; Schober, W. D.; Jin, L.; Tsutsumi-Ishii, Y.; Nagaoka, I.; Igari, J.; Andreeff, M. Up-regulation of MDR1 and induction of doxorubicin resistance by histone deacetylase inhibitor depsipeptide (FK228) and ATRA in acute promyelocytic leukemia cells. Blood, 2006, 107, 1546-1554.
    • (2006) Blood , vol.107 , pp. 1546-1554
    • Tabe, Y.1    Konopleva, M.2    Contractor, R.3    Munsell, M.4    Schober, W.D.5    Jin, L.6    Tsutsumi-Ishii, Y.7    Nagaoka, I.8    Igari, J.9    Andreeff, M.10
  • 87
    • 33750463070 scopus 로고    scopus 로고
    • Cytotoxic effects of histone deacetylase inhibitor FK228 (depsipeptide, formally named FR901228) in combination with conventional anti-leukemia/lymphoma agents against human leukemia/lymphoma cell lines
    • Kano, Y.; Akutsu, M.; Tsunoda, S.; Izumi, T.; Kobayashi, H.; Mano, H.; Furakawa, Y. Cytotoxic effects of histone deacetylase inhibitor FK228 (depsipeptide, formally named FR901228) in combination with conventional anti-leukemia/lymphoma agents against human leukemia/lymphoma cell lines. Invest. New Drugs, 2007, 25, 31-40.
    • (2007) Invest. New Drugs , vol.25 , pp. 31-40
    • Kano, Y.1    Akutsu, M.2    Tsunoda, S.3    Izumi, T.4    Kobayashi, H.5    Mano, H.6    Furakawa, Y.7
  • 88
    • 33748376365 scopus 로고    scopus 로고
    • Duvic Vorinostat (suberoylanilide hydroxamic acid, SAHA) is clinically active in advanced cutaneous T-cell lymphoma (CTCL): Results of a phase IIb trial M
    • Abstract 7500
    • Olsen, E.; Kim, Y. H.; Kuzel, T.; Pacheco, T. R.; Foss, F.; Parker, S.; Wang, J. G.; Frankel, S. R.; Lis, J.; Duvic Vorinostat (suberoylanilide hydroxamic acid, SAHA) is clinically active in advanced cutaneous T-cell lymphoma (CTCL): Results of a phase IIb trial M. J. Clin. Oncol., 2006, 24, 422S Abstract 7500.
    • (2006) J. Clin. Oncol , vol.24
    • Olsen, E.1    Kim, Y.H.2    Kuzel, T.3    Pacheco, T.R.4    Foss, F.5    Parker, S.6    Wang, J.G.7    Frankel, S.R.8    Lis, J.9
  • 89
    • 33947190411 scopus 로고    scopus 로고
    • A phase I study of vorinostat (suberoylanilide hydroxamic acid, SAHA) in combination with 5-fluorouracil, leucovorin, and oxaliplatin (FOLFOX) in patients with advanced colorectal cancer (CRC)
    • Fakih, M. G.; Pendyala, L.; Toth, K.; Creaven, P.; Soehnlein, N.; Litwin, A.; Trump, D. A phase I study of vorinostat (suberoylanilide hydroxamic acid, SAHA) in combination with 5-fluorouracil, leucovorin, and oxaliplatin (FOLFOX) in patients with advanced colorectal cancer (CRC). J. Clin. Oncol., 2006, 24, 168S.
    • (2006) J. Clin. Oncol , vol.24
    • Fakih, M.G.1    Pendyala, L.2    Toth, K.3    Creaven, P.4    Soehnlein, N.5    Litwin, A.6    Trump, D.7
  • 90
    • 33846664820 scopus 로고    scopus 로고
    • Phase I study of vorinostat, a histone deacetylase (HDAC) inhibitor, in combination with carboplatin (Cb) and paclitaxel (P) for patients with advanced solid malignancies (NCI #6922)
    • Ramalingam, S.; Parise, R. A.; Egorin, M. J.; Argiris, A.; Stoller, R.; Beattie, L.; Aparicio, A.; Newman, E. M.; Zweibel, J.; Belani, C. P. Phase I study of vorinostat, a histone deacetylase (HDAC) inhibitor, in combination with carboplatin (Cb) and paclitaxel (P) for patients with advanced solid malignancies (NCI #6922). J. Clin. Oncol., 2006, 24, 98S.
    • (2006) J. Clin. Oncol , vol.24
    • Ramalingam, S.1    Parise, R.A.2    Egorin, M.J.3    Argiris, A.4    Stoller, R.5    Beattie, L.6    Aparicio, A.7    Newman, E.M.8    Zweibel, J.9    Belani, C.P.10
  • 91
    • 33748360764 scopus 로고    scopus 로고
    • Munshi, A.; Tanaka, T.; Hobbs, M. L.; Tucker, S. L.; Richon, V. M.; Meyn, R. E. Vorinostat, a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol. Cancer Ther., 2006, 5, 1967-1974.
    • Munshi, A.; Tanaka, T.; Hobbs, M. L.; Tucker, S. L.; Richon, V. M.; Meyn, R. E. Vorinostat, a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol. Cancer Ther., 2006, 5, 1967-1974.
  • 94
    • 38749084421 scopus 로고    scopus 로고
    • A phase 1 pharmacokinetic (PK) and pharmacodynamic (PD) study of the histone deacetylase (HDAC) inhibitor PXD101 in patients (pts) with advanced solid tumours
    • Steele, N.; Vidal, J.; Plumb, J.; Attard, G.; Rasmussen, A.; Buhl-Jensen, P.; Brown, R.; Blagden, S.; Evans, J.; de Bono, J. A phase 1 pharmacokinetic (PK) and pharmacodynamic (PD) study of the histone deacetylase (HDAC) inhibitor PXD101 in patients (pts) with advanced solid tumours. J. Clin. Oncol., 2005, 23, 200S.
    • (2005) J. Clin. Oncol , vol.23
    • Steele, N.1    Vidal, J.2    Plumb, J.3    Attard, G.4    Rasmussen, A.5    Buhl-Jensen, P.6    Brown, R.7    Blagden, S.8    Evans, J.9    de Bono, J.10
  • 95
    • 35848937484 scopus 로고    scopus 로고
    • A phase I study of the histone deacetylase (HDAC) inhibitor PXD101 in patients with advanced hematological tumors
    • Hansen, M.; Gimsing, P.; Rasmussen, A.; Buhl-Jensen, P.; Knudsen, L. M. A phase I study of the histone deacetylase (HDAC) inhibitor PXD101 in patients with advanced hematological tumors. J. Clin. Oncol., 2005, 23, 225S.
    • (2005) J. Clin. Oncol , vol.23
    • Hansen, M.1    Gimsing, P.2    Rasmussen, A.3    Buhl-Jensen, P.4    Knudsen, L.M.5
  • 96
    • 10744229917 scopus 로고    scopus 로고
    • Remiszewski, S. W.; Sambucetti, L. C.; Bair, K. W.; Bontempo, J.; Cesarz, D.; Chadramouli, N.; Chen, R.; Cheung, M.; Cornell-Kennon, S.; Dean, K.; Diamantidis, G.; France, D.; Green, M. A.; Howell, K. L.; Kashi, R.; Kwon, P.; Lassota, P.; Martin, M. S.; Mou, Y.; Perez, L. B.; Sharma, S.; Smith, T.; Sorensen, E.; Taplin, F.; Trogani, N.; Versace, R.; Walker, H.; Weltchek-Engler, S.; Wood, A.; Wu, A.; Atadja, P. N-hydroxy-3-phenyl-2-propenamides as novel inhibitors of human histone deacetylase with in vivo anti-tumor activity: discovery of (2E)-N-hydroxy-3-[4-(2-hydroxyethyl)[2-(1H-indol-3-yl) ethyl]amino]methyl]phenyl]-2-propenamide (NVP-LAQ824). J. Med. Chem., 2003, 46, 4609-4624.
    • Remiszewski, S. W.; Sambucetti, L. C.; Bair, K. W.; Bontempo, J.; Cesarz, D.; Chadramouli, N.; Chen, R.; Cheung, M.; Cornell-Kennon, S.; Dean, K.; Diamantidis, G.; France, D.; Green, M. A.; Howell, K. L.; Kashi, R.; Kwon, P.; Lassota, P.; Martin, M. S.; Mou, Y.; Perez, L. B.; Sharma, S.; Smith, T.; Sorensen, E.; Taplin, F.; Trogani, N.; Versace, R.; Walker, H.; Weltchek-Engler, S.; Wood, A.; Wu, A.; Atadja, P. N-hydroxy-3-phenyl-2-propenamides as novel inhibitors of human histone deacetylase with in vivo anti-tumor activity: discovery of (2E)-N-hydroxy-3-[4-(2-hydroxyethyl)[2-(1H-indol-3-yl) ethyl]amino]methyl]phenyl]-2-propenamide (NVP-LAQ824). J. Med. Chem., 2003, 46, 4609-4624.
  • 97
    • 0141953928 scopus 로고    scopus 로고
    • The discovery of NVP-LAQ824: From concept to clinic
    • Remiszewski, S. W. The discovery of NVP-LAQ824: from concept to clinic. Curr. Med. Chem., 2003, 10, 2393-2402.
    • (2003) Curr. Med. Chem , vol.10 , pp. 2393-2402
    • Remiszewski, S.W.1
  • 98
    • 44449092402 scopus 로고    scopus 로고
    • A phase 1, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase inhibitor LAQ824 in patients with hematologic malignancies
    • Ottmann, O. G.; Deangelo, D. J.; Stone, R. M.; Pfeifer, H.; Atadja, P.; Peng, B.; Scott, J. W.; Dugan, M.; Sonneveld, P. A phase 1, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase inhibitor LAQ824 in patients with hematologic malignancies. J. Clin. Oncol., 2004, 22, 201S.
    • (2004) J. Clin. Oncol , vol.22
    • Ottmann, O.G.1    Deangelo, D.J.2    Stone, R.M.3    Pfeifer, H.4    Atadja, P.5    Peng, B.6    Scott, J.W.7    Dugan, M.8    Sonneveld, P.9
  • 99
    • 25144508608 scopus 로고    scopus 로고
    • A phase I, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase (HDAC) inhibitor LAQ824 in patients with advanced solid tumors
    • Rowinsky, E. K.; Pacey, S.; Patnaik, A.; O'Donnell, A.; Mita, M. M.; Atadja, P.; Peng, B.; Dugan, M.; Scott, J. W.; de Bono, J. S. A phase I, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase (HDAC) inhibitor LAQ824 in patients with advanced solid tumors. J. Clin. Oncol., 2004, 22, 200S.
    • (2004) J. Clin. Oncol , vol.22
    • Rowinsky, E.K.1    Pacey, S.2    Patnaik, A.3    O'Donnell, A.4    Mita, M.M.5    Atadja, P.6    Peng, B.7    Dugan, M.8    Scott, J.W.9    de Bono, J.S.10
  • 100
    • 33745687975 scopus 로고    scopus 로고
    • Results of cardiac monitoring during phase I trials of a novel histone deacetylase (HDAC) inhibitor LBH589 in patients with advanced solid tumors and hematologic malignancies
    • Fischer, T.; Patnaik, A.; Bhalla, K.; Beck, J.; Morganroth, J.; Laird, G. H.; Sharma, S.; Scott, J. W.; Dugan, M.; Giles, F. Results of cardiac monitoring during phase I trials of a novel histone deacetylase (HDAC) inhibitor LBH589 in patients with advanced solid tumors and hematologic malignancies. J. Clin. Oncol., 2005, 23, 218S.
    • (2005) J. Clin. Oncol , vol.23
    • Fischer, T.1    Patnaik, A.2    Bhalla, K.3    Beck, J.4    Morganroth, J.5    Laird, G.H.6    Sharma, S.7    Scott, J.W.8    Dugan, M.9    Giles, F.10
  • 101
    • 85036807867 scopus 로고    scopus 로고
    • Beck, J.; Fischer, George, D.; Huber, C.; Calvo, E.; Atadja, P.; Peng, B.; Kwong, C.; Sharma, S.; Patnaik, A. HDAC inhibition in cancer therapy: an increasingly intriguing tale of chemistry, biology and clinical benefit. J. Clin. Oncol., 2007, 23, 16S, Abstr. 3418.
    • Beck, J.; Fischer, George, D.; Huber, C.; Calvo, E.; Atadja, P.; Peng, B.; Kwong, C.; Sharma, S.; Patnaik, A. HDAC inhibition in cancer therapy: an increasingly intriguing tale of chemistry, biology and clinical benefit. J. Clin. Oncol., 2007, 23, 16S, Abstr. 3418.
  • 102
    • 34248366845 scopus 로고    scopus 로고
    • Two novel histone deacetylase inhibitors NVP-LAQ824 and NVP-LBH589 are active against biliary tract cancer and potentiate the efficacy of gemcitabine
    • Wiedemann, M.; Bluethner, T.; Niederhagen, M.; Schoppmeyer, K.; Moessner, J.; Caca, K. Two novel histone deacetylase inhibitors NVP-LAQ824 and NVP-LBH589 are active against biliary tract cancer and potentiate the efficacy of gemcitabine. J. Clin. Oncol., 2006, 24, 214S.
    • (2006) J. Clin. Oncol , vol.24
    • Wiedemann, M.1    Bluethner, T.2    Niederhagen, M.3    Schoppmeyer, K.4    Moessner, J.5    Caca, K.6
  • 103
    • 34247555807 scopus 로고    scopus 로고
    • Combined effects of novel tyrosine kinase inhibitor AMN107 and histone deacetylase inhibitor LBH589 against unmutated or mutant Bcr-Abl-expressing human leukemia cells
    • Fiskus, W.; Pranpat, M.; Balasis, M.; Atadja, P.; Manley, P.; Giles, F.; Bhalla, K. Combined effects of novel tyrosine kinase inhibitor AMN107 and histone deacetylase inhibitor LBH589 against unmutated or mutant Bcr-Abl-expressing human leukemia cells. J. Clin. Oncol., 2006, 24, 359S.
    • (2006) J. Clin. Oncol , vol.24
    • Fiskus, W.1    Pranpat, M.2    Balasis, M.3    Atadja, P.4    Manley, P.5    Giles, F.6    Bhalla, K.7
  • 107
    • 85036817323 scopus 로고    scopus 로고
    • Donovan, E. A.; Sparreboom, A.; Figg, W.; Trepel, J.; Maynard, K.; Zwiebel, J.; Melillo, G.; Gutierrez, M.; Doroshow, J.; Kummar, S. Phase I trial of the oral histone deacetylase inhibitor MS-275 administered with food. ASCO Meeting Abstracts. June 20 2006, 13036.
    • Donovan, E. A.; Sparreboom, A.; Figg, W.; Trepel, J.; Maynard, K.; Zwiebel, J.; Melillo, G.; Gutierrez, M.; Doroshow, J.; Kummar, S. Phase I trial of the oral histone deacetylase inhibitor MS-275 administered with food. ASCO Meeting Abstracts. June 20 2006, 13036.
  • 109
    • 34248334530 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of the histone deacetylase inhibitor MS-275 in combination with 13-cis retinoic acid in patients with advanced solid tumors
    • Pili, R.; Rudek, M.; Altiok, S.; Qian, D.; Zhao, M.; Donehower, R.; Anderson, A.; Halter, M.; McFarland, H.; Zwiebel, J.; Carducci, M. Phase I pharmacokinetic and pharmacodynamic study of the histone deacetylase inhibitor MS-275 in combination with 13-cis retinoic acid in patients with advanced solid tumors. J. Clin. Oncol., 2006, 24, 134S.
    • (2006) J. Clin. Oncol , vol.24
    • Pili, R.1    Rudek, M.2    Altiok, S.3    Qian, D.4    Zhao, M.5    Donehower, R.6    Anderson, A.7    Halter, M.8    McFarland, H.9    Zwiebel, J.10    Carducci, M.11
  • 110
    • 31944444233 scopus 로고    scopus 로고
    • The benzamide MS-275 is a potent, long-lasting brain region-selective inhibitor of histone deacetylases
    • Simonini, M. V.; Camargo, L. M.; Dong, E.; Maloku, E.; Costa, E.; Guidotti, A. The benzamide MS-275 is a potent, long-lasting brain region-selective inhibitor of histone deacetylases. Proc. Natl. Acad. Sci. USA, 2006, 103, 1587-1592.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1587-1592
    • Simonini, M.V.1    Camargo, L.M.2    Dong, E.3    Maloku, E.4    Costa, E.5    Guidotti, A.6
  • 111
    • 33845357791 scopus 로고    scopus 로고
    • Clinical activity and safety of the histone deacetylase inhibitor MGCD0103: Results of a phase I study in patients with leukemia or myelodysplastic syndromes (MDS)
    • Garcia-Manero, G.; Minden, M.; Estrov, Z.; Verstovsek, S.; Newsome, W. M.; Reid, G.; Besterman, J.; Li, Z.; Pearce, L.; Martell, R. Clinical activity and safety of the histone deacetylase inhibitor MGCD0103: Results of a phase I study in patients with leukemia or myelodysplastic syndromes (MDS). J. Clin. Oncol., 2006, 24, 337S.
    • (2006) J. Clin. Oncol , vol.24
    • Garcia-Manero, G.1    Minden, M.2    Estrov, Z.3    Verstovsek, S.4    Newsome, W.M.5    Reid, G.6    Besterman, J.7    Li, Z.8    Pearce, L.9    Martell, R.10
  • 112
    • 34248370087 scopus 로고    scopus 로고
    • Phase I study of isotype-selective histone deacetylase (HDAC) inhibitor MGCD0103 given as three-times weekly oral dose in patients (pts) with advanced solid tumors
    • Carducci, M.; Siu, L. L.; Sullivan, R.; Maclean, M.; Kalita, A.; Chen, E. X.; Pili, R.; Martell, R. E.; Besterman, J.; Reid, G. K. Phase I study of isotype-selective histone deacetylase (HDAC) inhibitor MGCD0103 given as three-times weekly oral dose in patients (pts) with advanced solid tumors. J. Clin. Oncol., 2006, 24, 122S.
    • (2006) J. Clin. Oncol , vol.24
    • Carducci, M.1    Siu, L.L.2    Sullivan, R.3    Maclean, M.4    Kalita, A.5    Chen, E.X.6    Pili, R.7    Martell, R.E.8    Besterman, J.9    Reid, G.K.10
  • 113
    • 34249331091 scopus 로고    scopus 로고
    • Phase I trials of the oral histone deacetylase (HOAC) inhibitor MGCD0103 given either daily or 3x weekly for 14 days every 3 weeks in patients (pts) with advanced solid tumors
    • Gelmon, K.; Tolcher, A.; Carducci, M.; Reid, G. K.; Li, Z.; Kalita, A.; Callejas, V.; Longstreth, J.; Besterman, J. M.; Siu, L. L. Phase I trials of the oral histone deacetylase (HOAC) inhibitor MGCD0103 given either daily or 3x weekly for 14 days every 3 weeks in patients (pts) with advanced solid tumors. J. Clin. Oncol., 2005, 23, 228S.
    • (2005) J. Clin. Oncol , vol.23
    • Gelmon, K.1    Tolcher, A.2    Carducci, M.3    Reid, G.K.4    Li, Z.5    Kalita, A.6    Callejas, V.7    Longstreth, J.8    Besterman, J.M.9    Siu, L.L.10
  • 114
    • 85036837773 scopus 로고    scopus 로고
    • Li, Z.; Zhou, N.; Fournel, M.; Kalita, A.; Trachy-Bourget, M.-C.; Yan, P. T.; Lu, A.; Elowe, N.; Hou, Y.; Liu, J.; Bonfils, C.; Robert, M.-F.; Leit, S.; Raeppel, S.; Frechette, S.; Rahil, G.; Wang, J.; Delorme, D.; Moradei, O.; MacLeod, R.; Besterman, J. M. 83 Anti-tumor activities of MGCD0103, a novel isotype-selective histone deacetylase inhibitor. Eur. J. Cancer Suppl. 16th EORTC-NCI-AACR Symp. Mol. Targets Cancer Ther., 2004, 2(8), Abstr 83.
    • Li, Z.; Zhou, N.; Fournel, M.; Kalita, A.; Trachy-Bourget, M.-C.; Yan, P. T.; Lu, A.; Elowe, N.; Hou, Y.; Liu, J.; Bonfils, C.; Robert, M.-F.; Leit, S.; Raeppel, S.; Frechette, S.; Rahil, G.; Wang, J.; Delorme, D.; Moradei, O.; MacLeod, R.; Besterman, J. M. 83 Anti-tumor activities of MGCD0103, a novel isotype-selective histone deacetylase inhibitor. Eur. J. Cancer Suppl. 16th EORTC-NCI-AACR Symp. Mol. Targets Cancer Ther., 2004, 2(8), Abstr 83.
  • 115
    • 85036808464 scopus 로고    scopus 로고
    • Molife, R.; Patterson, S.; Riggs, C.; Higano, C.; Stadler, W. M.; Dearnley, D.; Parker, C.; McCulloch, W.; Shalaurov, A.; de Bono, J. S. Phase II study of FK228 in patients with hormone refractory prostate cancer (HRPC). ASCO Meeting Abstracts. June 20, 2006, 14554.
    • Molife, R.; Patterson, S.; Riggs, C.; Higano, C.; Stadler, W. M.; Dearnley, D.; Parker, C.; McCulloch, W.; Shalaurov, A.; de Bono, J. S. Phase II study of FK228 in patients with hormone refractory prostate cancer (HRPC). ASCO Meeting Abstracts. June 20, 2006, 14554.
  • 116
    • 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
  • 118
    • 67649985963 scopus 로고    scopus 로고
    • International multicenter phase II study of the HDAC inhibitor (HDACi) depsipeptide (FK228) in cutaneous T-cell lymphoma (CTCL): Interim report
    • Whittaker, S.; McCulloch, W.; Robak, T.; Baran, E.; Prentice, A. International multicenter phase II study of the HDAC inhibitor (HDACi) depsipeptide (FK228) in cutaneous T-cell lymphoma (CTCL): Interim report. J. Clin. Oncol., 2006, 24, 136S.
    • (2006) J. Clin. Oncol , vol.24
    • Whittaker, S.1    McCulloch, W.2    Robak, T.3    Baran, E.4    Prentice, A.5
  • 119
    • 85036838950 scopus 로고    scopus 로고
    • Piekarz, R. L.; Frye, R.; Turner, M.; Wright, J.; Leonard, J.; Allen, S.; Bates, S. E. Update on the phase II trial and correlative studies of depsipeptide in patients with cutaneous T-cell lymphoma and relapsed peripheral T-cell lymphoma. ASCO Meeting Abstracts. Jul 15, 2004, Abstr. 3028.
    • Piekarz, R. L.; Frye, R.; Turner, M.; Wright, J.; Leonard, J.; Allen, S.; Bates, S. E. Update on the phase II trial and correlative studies of depsipeptide in patients with cutaneous T-cell lymphoma and relapsed peripheral T-cell lymphoma. ASCO Meeting Abstracts. Jul 15, 2004, Abstr. 3028.
  • 120
    • 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.; Mutoh, S. Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo. Biochem. Pharmacol., 2002, 6, 1079-1090.
    • (2002) Biochem. Pharmacol , vol.6 , pp. 1079-1090
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6    Mutoh, S.7
  • 122
    • 0028258610 scopus 로고    scopus 로고
    • Ueda, H.; Nakajima, H.; Hori, Y.; Fujita, T.; Mishimura, M.; Goto, T.; Okuhara, M. F. FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968. I. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity. J. Antibiot., 1994, 47, 301-310.
    • Ueda, H.; Nakajima, H.; Hori, Y.; Fujita, T.; Mishimura, M.; Goto, T.; Okuhara, M. F. FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968. I. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity. J. Antibiot., 1994, 47, 301-310.
  • 125
    • 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. R.; 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.R.2    Piekarz, R.L.3    Kayastha, G.L.4    Fojo, T.5    Bates, S.E.6
  • 126
    • 0020644885 scopus 로고
    • Sulfation and glucuronidation as competing pathways in the metabolism of hydroxamic acids: The role of N,O-sulfonation in chemical carcinogenesis of aromatic amines
    • Meerman, J. H. Sulfation and glucuronidation as competing pathways in the metabolism of hydroxamic acids: the role of N,O-sulfonation in chemical carcinogenesis of aromatic amines. Environ. Health Perspect., 1983, 49, 27-32.
    • (1983) Environ. Health Perspect , vol.49 , pp. 27-32
    • Meerman, J.H.1
  • 132
    • 33749430243 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of cyclic amide/imidebearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors
    • Shinji, C.; Maeda, S.; Imai, K.; Yoshida, M.; Hashimoto, Y.; Miyachi, H. Design, synthesis, and evaluation of cyclic amide/imidebearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors. Bioorg. Med. Chem., 2006, 14, 7625-7651.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 7625-7651
    • Shinji, C.1    Maeda, S.2    Imai, K.3    Yoshida, M.4    Hashimoto, Y.5    Miyachi, H.6
  • 135
    • 85036814895 scopus 로고    scopus 로고
    • Cho, J.-W.; Lim, S.-C. Oxazole hydroxamic acid derivatives and use thereof. WO 2006/075888.
    • Cho, J.-W.; Lim, S.-C. Oxazole hydroxamic acid derivatives and use thereof. WO 2006/075888.
  • 136
    • 85036826988 scopus 로고    scopus 로고
    • Guidi, A.; Dimoulas, T. N-Hydroxyamides omega-substituted with tricyclic groups as histone deacetylase inhibitors, their preparation and use in pharmaceutical formulations. WO 2006/097449 Menarini International Operations SA.
    • Guidi, A.; Dimoulas, T. N-Hydroxyamides omega-substituted with tricyclic groups as histone deacetylase inhibitors, their preparation and use in pharmaceutical formulations. WO 2006/097449 Menarini International Operations SA.
  • 139
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Mrris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem., 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Mrris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 140
    • 0033839257 scopus 로고    scopus 로고
    • First non-radioactive assay for in vitro screening of histone deacetylase inhibitors
    • Hoffmann, K.; Brosch, G.; Loidl, P.; Jung, M. First non-radioactive assay for in vitro screening of histone deacetylase inhibitors. Pharmazie, 2000, 55, 601-606.
    • (2000) Pharmazie , vol.55 , pp. 601-606
    • Hoffmann, K.1    Brosch, G.2    Loidl, P.3    Jung, M.4
  • 143
    • 26444441453 scopus 로고    scopus 로고
    • Alkyl-substituted polyaminohydroxamic acids: A novel class of targeted histone deacetylase inhibitors
    • Varghese, S.; Gupta, D.; Baran, T.; Jiemjit, A.; Gore, S. D.; Casero, Jr., R. A.; Woster, P. M. Alkyl-substituted polyaminohydroxamic acids: a novel class of targeted histone deacetylase inhibitors. J. Med. Chem., 2005, 48, 6350-6365.
    • (2005) J. Med. Chem , vol.48 , pp. 6350-6365
    • Varghese, S.1    Gupta, D.2    Baran, T.3    Jiemjit, A.4    Gore, S.D.5    Casero Jr., R.A.6    Woster, P.M.7
  • 144
    • 1942534547 scopus 로고    scopus 로고
    • Stereodefined and polyunsaturated inhibitors of histone deacetylase based on (2E,4E)-5-arylpenta-2,4-dienoic acid hydroxyamides
    • Marson, C. M.; Serradji, N.; Rioja, A. S.; Gastaud, S. P.; Alao, J. P.; Coombes, R. C.; Vigushin, D. M. Stereodefined and polyunsaturated inhibitors of histone deacetylase based on (2E,4E)-5-arylpenta-2,4-dienoic acid hydroxyamides. Bioorg. Med. Chem. Lett., 2004, 14, 2477-2481.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 2477-2481
    • Marson, C.M.1    Serradji, N.2    Rioja, A.S.3    Gastaud, S.P.4    Alao, J.P.5    Coombes, R.C.6    Vigushin, D.M.7
  • 145
    • 85036826338 scopus 로고    scopus 로고
    • Wiech, N. L.; Lan-Hargest, H.-Y. Histone deacetylase inhibitors. WO 2006/ 052916.
    • Wiech, N. L.; Lan-Hargest, H.-Y. Histone deacetylase inhibitors. WO 2006/ 052916.
  • 146
    • 85036808637 scopus 로고    scopus 로고
    • Belvedere, S.; Miller, T. A. Histone deacetylase inhibitors. WO 2006/ 020004.
    • Belvedere, S.; Miller, T. A. Histone deacetylase inhibitors. WO 2006/ 020004.
  • 147
    • 85036816016 scopus 로고    scopus 로고
    • Ishibashi, N.; Sawada, Y. Hydroxyamide compounds having activity as inhibitors of histone deacetylase. WO 2006/016680.
    • Ishibashi, N.; Sawada, Y. Hydroxyamide compounds having activity as inhibitors of histone deacetylase. WO 2006/016680.
  • 149
    • 85036819252 scopus 로고    scopus 로고
    • Deng, W.; Chen, D. Bicyclic heterocycles hydroxamate compounds useful as histone deacetylase (HDAC) inhibitors. WO 2006/101456.
    • Deng, W.; Chen, D. Bicyclic heterocycles hydroxamate compounds useful as histone deacetylase (HDAC) inhibitors. WO 2006/101456.
  • 150
    • 85036811772 scopus 로고    scopus 로고
    • Maier, T.; Baer, T. Sulfonylpyrroles as histone deacetylase inhibitors. WO 2006/105979.
    • Maier, T.; Baer, T. Sulfonylpyrroles as histone deacetylase inhibitors. WO 2006/105979.
  • 151
    • 85036802921 scopus 로고    scopus 로고
    • Maier, T.; Baer, T. N-Sulfonylpyrroles as histone deacetylase inhibitors. WO 2006/097474.
    • Maier, T.; Baer, T. N-Sulfonylpyrroles as histone deacetylase inhibitors. WO 2006/097474.
  • 152
    • 85036818541 scopus 로고    scopus 로고
    • Moffat, D. F. C.; Patel, S. R. Histone deacetylase inhibitors. WO 2006/ 123121.
    • Moffat, D. F. C.; Patel, S. R. Histone deacetylase inhibitors. WO 2006/ 123121.
  • 153
    • 85036821745 scopus 로고    scopus 로고
    • Angibaud, P. R.; Marconnet-Decrane, L., Substituted aminopropenyl piperidine or morpholine derivatives as novel inhibitors of histone deacetylase. WO 2006/122926.
    • Angibaud, P. R.; Marconnet-Decrane, L., Substituted aminopropenyl piperidine or morpholine derivatives as novel inhibitors of histone deacetylase. WO 2006/122926.
  • 154
    • 85036818870 scopus 로고    scopus 로고
    • Verdonck, M. G. C.; Angibaud, P. R. Substituted indolyl alkyl amino derivatives as novel inhibitors of histone deacetylase. WO 2006/010750.
    • Verdonck, M. G. C.; Angibaud, P. R. Substituted indolyl alkyl amino derivatives as novel inhibitors of histone deacetylase. WO 2006/010750.
  • 155
    • 85036831561 scopus 로고    scopus 로고
    • Anandan, S. K.; Xiao, X.-Y. Fused heterocyclic compounds useful as inhibitors of histone deacetylase. WO 2006/088949.
    • Anandan, S. K.; Xiao, X.-Y. Fused heterocyclic compounds useful as inhibitors of histone deacetylase. WO 2006/088949.
  • 158
    • 85036816370 scopus 로고    scopus 로고
    • Methot, J.; Miller, T. A. Benzothiophene hydroxamic acid derivatives with carbamate, urea, amide and sulfonamide substitutions. WO 2006/ 115833 Merck & Co Inc.
    • Methot, J.; Miller, T. A. Benzothiophene hydroxamic acid derivatives with carbamate, urea, amide and sulfonamide substitutions. WO 2006/ 115833 Merck & Co Inc.
  • 159
    • 85036823923 scopus 로고    scopus 로고
    • Hubbs, J. L.; Kattar, S. Benzothiophene hydroxamic acid derivatives. WO 2006/115835 Merck & Co Inc.
    • Hubbs, J. L.; Kattar, S. Benzothiophene hydroxamic acid derivatives. WO 2006/115835 Merck & Co Inc.
  • 160
    • 27744496468 scopus 로고    scopus 로고
    • Non-hydroxamate histone deacetylase inhibitors
    • Suzuki, T.; Miyata, N. Non-hydroxamate histone deacetylase inhibitors. Curr. Med. Chem., 2005, 12, 2867-80.
    • (2005) Curr. Med. Chem , vol.12 , pp. 2867-2880
    • Suzuki, T.1    Miyata, N.2
  • 161
    • 33646548906 scopus 로고    scopus 로고
    • Rational design of non-hydroxamate histone deacetylase inhibitors
    • Suzuki, T.; Miyata, N. Rational design of non-hydroxamate histone deacetylase inhibitors. Mini-Rev. Med. Chem., 2006, 6, 515-526.
    • (2006) Mini-Rev. Med. Chem , vol.6 , pp. 515-526
    • Suzuki, T.1    Miyata, N.2
  • 162
    • 85036846184 scopus 로고    scopus 로고
    • Leit de Moradei, S. M.; Tessier, P. Inhibitors of histone deacetylase. WO 2006/102760 MethylGene, Inc.
    • Leit de Moradei, S. M.; Tessier, P. Inhibitors of histone deacetylase. WO 2006/102760 MethylGene, Inc.
  • 165
    • 20344391371 scopus 로고    scopus 로고
    • Design and synthesis of non-hydroxamate histone deacetylase inhibitors: Identification of a selective histone acetylating agent
    • Suzuki, T.; Matsuura, A.; Kouketsu, A.; Hisakawa, S.; Nakagawa, H.; Miyata, N. Design and synthesis of non-hydroxamate histone deacetylase inhibitors: identification of a selective histone acetylating agent. Bioorg. Med. Chem., 2005, 13, 4332-4342.
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 4332-4342
    • Suzuki, T.1    Matsuura, A.2    Kouketsu, A.3    Hisakawa, S.4    Nakagawa, H.5    Miyata, N.6
  • 166
    • 85036820434 scopus 로고    scopus 로고
    • Malecha, J.; Noble, S. Novel inhibitors of histone deacetylase for the treatment of disease. WO 2006/063294.
    • Malecha, J.; Noble, S. Novel inhibitors of histone deacetylase for the treatment of disease. WO 2006/063294.
  • 167
    • 85036826906 scopus 로고    scopus 로고
    • Ahmed, S.; Combet, C. Mercaptoamides as histone deacetylase inhibitors. WO 2006/028972.
    • Ahmed, S.; Combet, C. Mercaptoamides as histone deacetylase inhibitors. WO 2006/028972.
  • 168
    • 33645847864 scopus 로고    scopus 로고
    • Carbonyl- and sulfur-containing analogs of suberoylanilide hydroxamic acid: Potent inhibition of histone deacetylases
    • Gu, W.; Nusinzon, I.; Smith, Jr., R. D.; Horvath, C. M.; Silverman, R. B. Carbonyl- and sulfur-containing analogs of suberoylanilide hydroxamic acid: Potent inhibition of histone deacetylases. Bioorg. Med. Chem., 2006, 14, 3320-3329.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 3320-3329
    • Gu, W.1    Nusinzon, I.2    Smith Jr., R.D.3    Horvath, C.M.4    Silverman, R.B.5
  • 170
    • 85036843012 scopus 로고    scopus 로고
    • Stokes, E. S. E.; Carr, G. N-(2-Aminophenyl)-4-(5-((ethylamino) methyl) 1,3-thiazol-2-yl) benzamide and N-(2-aminophenyl)-4-(5-((isopropylamino) methyl) 1,3-thiazol-2-yl) benzamide as HDAC inhibitors. WO 2006/064246 AstraZeneca AB, AstraZeneca UK Ltd.
    • Stokes, E. S. E.; Carr, G. N-(2-Aminophenyl)-4-(5-((ethylamino) methyl) 1,3-thiazol-2-yl) benzamide and N-(2-aminophenyl)-4-(5-((isopropylamino) methyl) 1,3-thiazol-2-yl) benzamide as HDAC inhibitors. WO 2006/064246 AstraZeneca AB, AstraZeneca UK Ltd.
  • 171
    • 85036827735 scopus 로고    scopus 로고
    • Hubbs, J. L.; Mampreian, D. Benzothiophene derivatives. WO 2006/115845 Merck & Co Inc.
    • Hubbs, J. L.; Mampreian, D. Benzothiophene derivatives. WO 2006/115845 Merck & Co Inc.
  • 172
    • 85036812186 scopus 로고    scopus 로고
    • Bressi, J. C.; Brown, J. W. Histone deacetylase inhibitors. WO 2006/ 066133 Takeda San Diego Inc.
    • Bressi, J. C.; Brown, J. W. Histone deacetylase inhibitors. WO 2006/ 066133 Takeda San Diego Inc.
  • 174
    • 85036823009 scopus 로고    scopus 로고
    • Davis, D.; Kim, H. M. Silanol derivatives as inhibitors of histone deacetylase. WO 2006/069096.
    • Davis, D.; Kim, H. M. Silanol derivatives as inhibitors of histone deacetylase. WO 2006/069096.
  • 175
    • 85036824165 scopus 로고    scopus 로고
    • Attenni, B.; Ferrigno, F. Heterocycle derivatives as histone deacetylase (HDAC) inhibitors. WO 2006/061638.
    • Attenni, B.; Ferrigno, F. Heterocycle derivatives as histone deacetylase (HDAC) inhibitors. WO 2006/061638.
  • 176
    • 85036818952 scopus 로고    scopus 로고
    • Chakravarty, P. K.; Colletti, S. L. Amide derivatives as inhibitors of histone deacetylase. WO 2006/005955.
    • Chakravarty, P. K.; Colletti, S. L. Amide derivatives as inhibitors of histone deacetylase. WO 2006/005955.
  • 178
    • 33845925314 scopus 로고    scopus 로고
    • Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from alpha-aminosuberic acid
    • Kahnberg, P.; Lucke, A. J.; Glenn, M. P.; Boyle, G. M.; Tyndall, J. D. A.; Parsons, P. G.; Fairlie, D. P. Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from alpha-aminosuberic acid. J. Med. Chem., 2006, 49, 7611-7622.
    • (2006) J. Med. Chem , vol.49 , pp. 7611-7622
    • Kahnberg, P.1    Lucke, A.J.2    Glenn, M.P.3    Boyle, G.M.4    Tyndall, J.D.A.5    Parsons, P.G.6    Fairlie, D.P.7
  • 179
    • 85036810355 scopus 로고    scopus 로고
    • Belvedere, S.; Hamblett, C. L. Histone deacetylase inhibitors. WO 2006/ 017216.
    • Belvedere, S.; Hamblett, C. L. Histone deacetylase inhibitors. WO 2006/ 017216.
  • 180
    • 85036819287 scopus 로고    scopus 로고
    • Belvedere, S.; Methot, J. L. Histone deacetylase inhibitors. 2006/017215.
    • Belvedere, S.; Methot, J. L. Histone deacetylase inhibitors. 2006/017215.
  • 182
    • 0035024737 scopus 로고    scopus 로고
    • Histone deacetylase: A target for anti-proliferative and antiprotozoal agents
    • Meinke, P. T.; Liberator, P. Histone deacetylase: a target for anti-proliferative and antiprotozoal agents. Curr. Med. Chem., 2001, 8, 211-215.
    • (2001) Curr. Med. Chem , vol.8 , pp. 211-215
    • Meinke, P.T.1    Liberator, P.2
  • 184
    • 0037300480 scopus 로고    scopus 로고
    • FR235222, a fungal metabolite, is a novel immunosuppressant that inhibits mammalian histone deacetylase (HDAC) II. Biological activities in animal models
    • Mori, H.; Urano, Y.; Abe, F.; Furukawa, S.; Furukawa, S.; Sakai, F.; Hino, M.; Fujii, T. FR235222, a fungal metabolite, is a novel immunosuppressant that inhibits mammalian histone deacetylase (HDAC) II. Biological activities in animal models. J. Antibiot., 2003, 56, 80-86.
    • (2003) J. Antibiot , vol.56 , pp. 80-86
    • Mori, H.1    Urano, Y.2    Abe, F.3    Furukawa, S.4    Furukawa, S.5    Sakai, F.6    Hino, M.7    Fujii, T.8
  • 185
    • 25444469045 scopus 로고    scopus 로고
    • Total synthesis of cyclic tetrapeptide FR235222, a potent immunosuppressant that inhibits mammalian histone deacetylases
    • Xie, W.; Zou, B.; Pei, D.; Ma, D. Total synthesis of cyclic tetrapeptide FR235222, a potent immunosuppressant that inhibits mammalian histone deacetylases. Org. Lett., 2005, 7, 2775-2777.
    • (2005) Org. Lett , vol.7 , pp. 2775-2777
    • Xie, W.1    Zou, B.2    Pei, D.3    Ma, D.4
  • 186
    • 33645892015 scopus 로고    scopus 로고
    • Chlamydocin analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases
    • Bhuiyan, M. P. I.; Kato, T.; Okauchi, T.; Nishino, N.; Maeda, S.; Nihino, T. G.; Yoshida, M. Chlamydocin analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases. Bioorg. Med. Chem., 2006, 14, 3438-3446.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 3438-3446
    • Bhuiyan, M.P.I.1    Kato, T.2    Okauchi, T.3    Nishino, N.4    Maeda, S.5    Nihino, T.G.6    Yoshida, M.7
  • 189
    • 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.; Kochbin, S.; Yoshida, M.; Horinouchi, S. Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc. Natl. Acad. Sci. USA, 2001, 98, 87-92.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Kochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 191
    • 33746894565 scopus 로고    scopus 로고
    • Highly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate
    • Suzuki, T.; Kouketsu, A.; Itoh, Y.; Hisakawa, S.; Maeda, S.; Yoshida, M.; Nakagawa, H.; Miyata, N. Highly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate. J. Med. Chem., 2006, 49, 4809-4812.
    • (2006) J. Med. Chem , vol.49 , pp. 4809-4812
    • Suzuki, T.1    Kouketsu, A.2    Itoh, Y.3    Hisakawa, S.4    Maeda, S.5    Yoshida, M.6    Nakagawa, H.7    Miyata, N.8
  • 192
    • 20944435415 scopus 로고    scopus 로고
    • Mai, A.; Massa, S.; Pezzi, R; Simeoni, S.; Rotili, D.; Nebbioso, A.; Scognamiglio, A.; Altucci, L.; Loidl, P.; Brosch, G. Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. J. Med. Chem., 2005, 48, 3344-3353.
    • Mai, A.; Massa, S.; Pezzi, R; Simeoni, S.; Rotili, D.; Nebbioso, A.; Scognamiglio, A.; Altucci, L.; Loidl, P.; Brosch, G. Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. J. Med. Chem., 2005, 48, 3344-3353.
  • 194
    • 0942265466 scopus 로고    scopus 로고
    • Total synthesis of spiruchostatin A, a potent histone deacetylase inhibitor
    • Yurek-George, A.; Habens, F.; Brimmell, M.; Packham, G.; Ganesan, A. Total synthesis of spiruchostatin A, a potent histone deacetylase inhibitor. J. Am. Chem. Soc., 2004, 126, 1030-1031.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 1030-1031
    • Yurek-George, A.1    Habens, F.2    Brimmell, M.3    Packham, G.4    Ganesan, A.5
  • 196
    • 85036842083 scopus 로고    scopus 로고
    • Characterisation of spiruchostatin A as an inhibitor of histone deacetylases (HDAC) in breast cancer
    • Packham, G.; Crabb, S. J.; Carey, K.; Yurek-George, A.; Johnson, P. W.; Ganesan, A. Characterisation of spiruchostatin A as an inhibitor of histone deacetylases (HDAC) in breast cancer. Clin. Cancer Res., 2005, 11, 9138S.
    • (2005) Clin. Cancer Res , vol.11
    • Packham, G.1    Crabb, S.J.2    Carey, K.3    Yurek-George, A.4    Johnson, P.W.5    Ganesan, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.