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Volumn 121, Issue , 2016, Pages 451-483

Inside HDACs with more selective HDAC inhibitors

Author keywords

Epigenetics; HDAC inhibitors; Histone acetylation; Molecular modelling; Synthesis

Indexed keywords

ANDROGEN RECEPTOR; BENZAMIDE DERIVATIVE; BENZIMIDAZOLE; BETA CYCLODEXTRIN; CARBONATE DEHYDRATASE; CARBOXYLIC ACID; CYCLOPEPTIDE; DIPEPTIDYL CARBOXYPEPTIDASE; DNA TOPOISOMERASE; ENTINOSTAT; ESTROGEN RECEPTOR; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 10; HISTONE DEACETYLASE 11; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 5; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE 7; HISTONE DEACETYLASE 8; HISTONE DEACETYLASE 9; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; LYSINE; MATRIX METALLOPROTEINASE; MONOPHENOL MONOOXYGENASE; VORINOSTAT; ZINC BINDING PROTEIN; ORGANIC COMPOUND;

EID: 84974674596     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (269)

References (178)
  • 1
    • 85027954125 scopus 로고    scopus 로고
    • DNA methylation profiling in the clinic: Applications and challenges
    • H. Heyn, M. Esteller, DNA methylation profiling in the clinic: applications and challenges, Nat. Rev. Genet. 13 (2012) 679, http://dx.doi.org/10.1038/nrg3270.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 679
    • Heyn, H.1    Esteller, M.2
  • 2
    • 84862649489 scopus 로고    scopus 로고
    • Comprehensive analysis of mRNA methylation reveals enrichment in 30 UTRs and near stop codons
    • K.D. Meyer, Y. Saletore, P. Zumbo, O. Elemento, C.E. Mason, S.R. Jaffrey, Comprehensive analysis of mRNA methylation reveals enrichment in 30 UTRs and near stop codons, Cell. 149 (2012) 1635, http://dx.doi.org/10.1016/j.cell.2012.05.003.
    • (2012) Cell. , vol.149 , pp. 1635
    • Meyer, K.D.1    Saletore, Y.2    Zumbo, P.3    Elemento, O.4    Mason, C.E.5    Jaffrey, S.R.6
  • 3
    • 84875149194 scopus 로고    scopus 로고
    • Regulation of nucleosome dynamics by histone modifications
    • G.E. Zentner, S. Henikoff, Regulation of nucleosome dynamics by histone modifications, Nat. Struct. Mol. Biol. 20 (2013) 259, http://dx.doi.org/10.1038/nsmb.2470.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 259
    • Zentner, G.E.1    Henikoff, S.2
  • 4
    • 84875183056 scopus 로고    scopus 로고
    • Structure and function of long noncoding RNAs in epigenetic regulation
    • T.R. Mercer, J.S. Mattick, Structure and function of long noncoding RNAs in epigenetic regulation, Nat. Struct. Mol. Biol. 20 (2013) 300, http://dx.doi.org/10.1038/nsmb.2480.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 300
    • Mercer, T.R.1    Mattick, J.S.2
  • 5
    • 85006184529 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis infection induces HDAC1-mediated suppression of IL-12B gene expression in macrophages
    • A. Chandran, C. Antony, L. Jose, S. Mundayoor, K. Natarajan, R.A. Kumar, Mycobacterium tuberculosis infection induces HDAC1-mediated suppression of IL-12B gene expression in macrophages, Front. Cell. Infect. Microbiol. 5 (2015) 90, http://dx.doi.org/10.3389/fcimb.2015.00090.
    • (2015) Front. Cell. Infect. Microbiol. , vol.5 , pp. 90
    • Chandran, A.1    Antony, C.2    Jose, L.3    Mundayoor, S.4    Natarajan, K.5    Kumar, R.A.6
  • 6
    • 79961207189 scopus 로고
    • Epigenetic control of gene regulation in plants
    • M. Lauria, V. Rossi, Epigenetic control of gene regulation in plants, Biochim. Biophys. Acta BBA e Gene Regul. Mech. 1809 (2011) 369, http://dx.doi.org/10.1016/j.bbagrm.2011.03.002.
    • (1809) Biochim. Biophys. Acta BBA e Gene Regul. Mech. , vol.2011 , pp. 369
    • Lauria, M.1    Rossi, V.2
  • 7
    • 84887682495 scopus 로고    scopus 로고
    • Parasite epigenetics and immune evasion: Lessons from budding yeast
    • B.A. Wyse, R. Oshidari, D.C. Jeffery, K.Y. Yankulov, Parasite epigenetics and immune evasion: lessons from budding yeast, Epigenetics Chromatin. 6 (2013) 1, http://dx.doi.org/10.1186/1756-8935-6-40.
    • (2013) Epigenetics Chromatin. , vol.6 , pp. 1
    • Wyse, B.A.1    Oshidari, R.2    Jeffery, D.C.3    Yankulov, K.Y.4
  • 8
    • 84860602436 scopus 로고    scopus 로고
    • Epigenetic tailoring for the production of anti-infective cytosporones from the marine fungus Leucostoma persoonii
    • J. Beau, N. Mahid, W.N. Burda, L. Harrington, L.N. Shaw, T. Mutka, et al., Epigenetic tailoring for the production of anti-infective cytosporones from the marine fungus Leucostoma persoonii, Mar. Drugs 10 (2012) 762, http://dx.doi.org/10.3390/md10040762.
    • (2012) Mar. Drugs , vol.10 , pp. 762
    • Beau, J.1    Mahid, N.2    Burda, W.N.3    Harrington, L.4    Shaw, L.N.5    Mutka, T.6
  • 9
    • 84926663899 scopus 로고    scopus 로고
    • Histone acylation beyond acetylation: Terra incognita in chromatin biology
    • S. Rousseaux, S. Khochbin, Histone acylation beyond acetylation: terra incognita in chromatin biology, Cell J. Yakhteh 17 (2015) 1.
    • (2015) Cell J. Yakhteh , vol.17 , pp. 1
    • Rousseaux, S.1    Khochbin, S.2
  • 11
  • 12
    • 84930687902 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation and its role in chromatin plasticity, cell differentiation, epigenetics
    • M.O. Hottiger, Nuclear ADP-ribosylation and its role in chromatin plasticity, cell differentiation, epigenetics, Annu. Rev. Biochem. 84 (2015) 227, http://dx.doi.org/10.1146/annurev-biochem-060614-034506.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 227
    • Hottiger, M.O.1
  • 13
    • 78650447665 scopus 로고    scopus 로고
    • B-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • K. Sakabe, Z. Wang, G.W. Hart, b-N-acetylglucosamine (O-GlcNAc) is part of the histone code, Proc. Natl. Acad. Sci. 107 (2010) 19915, http://dx.doi.org/10.1073/pnas.1009023107.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 19915
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 14
    • 84929598341 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents
    • M. Mottamal, S. Zheng, T.L. Huang, G. Wang, Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents, Molecules 20 (2015) 3898, http://dx.doi.org/10.3390/molecules20033898.
    • (2015) Molecules , vol.20 , pp. 3898
    • Mottamal, M.1    Zheng, S.2    Huang, T.L.3    Wang, G.4
  • 15
    • 34447509697 scopus 로고    scopus 로고
    • A new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma Expert
    • M. Duvic, J. Vu, Vorinostat: a new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma, Expert Opin. Investig. Drugs 16 (2007) 1111, http://dx.doi.org/10.1517/13543784.16.7.1111.
    • (2007) Opin. Investig. Drugs , vol.16 , Issue.1111
    • Duvic, M.1    Vu Vorinostat, J.2
  • 16
    • 77954884940 scopus 로고    scopus 로고
    • Romidepsin: A new therapy for cutaneous T-cell lymphoma and a potential therapy for solid tumors
    • C. Grant, F. Rahman, R. Piekarz, C. Peer, R. Frye, R.W. Robey, et al., Romidepsin: a new therapy for cutaneous T-cell lymphoma and a potential therapy for solid tumors, Expert Rev. Anticancer Ther. 10 (2010) 997, http://dx.doi.org/10.1586/era.10.88.
    • (2010) Expert Rev. Anticancer Ther. , vol.10 , pp. 997
    • Grant, C.1    Rahman, F.2    Piekarz, R.3    Peer, C.4    Frye, R.5    Robey, R.W.6
  • 17
    • 84928774345 scopus 로고    scopus 로고
    • Belinostat: First global approval
    • R. Poole, Belinostat: first global approval, Drugs 74 (2014) 1543, http://dx.doi.org/10.1007/s40265-014-0275-8.
    • (2014) Drugs , vol.74 , pp. 1543
    • Poole, R.1
  • 18
    • 84933522687 scopus 로고    scopus 로고
    • FDA approves new agent for multiple myeloma
    • M.P. Fenichel, FDA approves new agent for multiple myeloma, J. Natl. Cancer Inst. 107 (2015) djv165, http://dx.doi.org/10.1093/jnci/djv165.
    • (2015) J. Natl. Cancer Inst. , vol.107 , pp. 165
    • Fenichel, M.P.1
  • 19
    • 84877574817 scopus 로고    scopus 로고
    • The future of epigenetic therapy in solid tumours: Lessons from the past
    • N. Azad, C.A. Zahnow, C.M. Rudin, S.B. Baylin, The future of epigenetic therapy in solid tumours: lessons from the past, Nat. Rev. Clin. Oncol. 10 (2013) 256.
    • (2013) Nat. Rev. Clin. Oncol. , vol.10 , pp. 256
    • Azad, N.1    Zahnow, C.A.2    Rudin, C.M.3    Baylin, S.B.4
  • 20
    • 77950860448 scopus 로고    scopus 로고
    • Inside HDAC with HDAC inhibitors
    • P. Bertrand, Inside HDAC with HDAC inhibitors, Eur. J. Med. Chem. 45 (2010) 2095, http://dx.doi.org/10.1016/j.ejmech.2010.02.030.
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 2095
    • Bertrand, P.1
  • 21
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • S. Minucci, P.G. Pelicci, Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer, Nat. Rev. Cancer 6 (2006) 38, http://dx.doi.org/10.1038/nrc1779.
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.38
    • Minucci, S.1    Pelicci, P.G.2
  • 22
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure function and regulation to novel strategies for therapy and prevention
    • X.-J. Yang, E. Seto, HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention, Oncogene 26 (2007) 5310.
    • (2007) Oncogene , vol.26 , pp. 5310
    • Yang, X.-J.1    Seto, E.2
  • 23
    • 84879574177 scopus 로고    scopus 로고
    • The functional interactome landscape of the human histone deacetylase family
    • P. Joshi, T.M. Greco, A.J. Guise, Y. Luo, F. Yu, A.I. Nesvizhskii, et al., The functional interactome landscape of the human histone deacetylase family, Mol. Syst. Biol. 9 (2013), http://dx.doi.org/10.1038/msb.2013.26.
    • (2013) Mol. Syst. Biol. , vol.9
    • Joshi, P.1    Greco, T.M.2    Guise, A.J.3    Luo, Y.4    Yu, F.5    Nesvizhskii, A.I.6
  • 24
    • 84908265816 scopus 로고    scopus 로고
    • Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
    • K.J. Falkenberg, R.W. Johnstone, Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders, Nat. Rev. Drug Discov. 13 (2014) 673.
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 673
    • Falkenberg, K.J.1    Johnstone, R.W.2
  • 25
    • 39549088498 scopus 로고    scopus 로고
    • Class II histone deacetylases play pivotal roles in heat shock protein 90-mediated proteasomal degradation of vascular endothelial growth factor receptors
    • J.-H. Park, S.-H. Kim, M.-C. Choi, J. Lee, D.-Y. Oh, S.-A. Im, et al., Class II histone deacetylases play pivotal roles in heat shock protein 90-mediated proteasomal degradation of vascular endothelial growth factor receptors, Biochem. Biophys. Res. Commun. 368 (2008) 318, http://dx.doi.org/10.1016/j.bbrc.2008.01.056.
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 318
    • Park, J.-H.1    Kim, S.-H.2    Choi, M.-C.3    Lee, J.4    Oh, D.-Y.5    Im, S.-A.6
  • 26
    • 79953219078 scopus 로고    scopus 로고
    • Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner
    • D. Li, S. Xie, Y. Ren, L. Huo, J. Gao, D. Cui, et al., Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner, Protein Cell. 2 (2011) 150, http://dx.doi.org/10.1007/s13238-011-1015-4.
    • (2011) Protein Cell. , vol.2 , pp. 150
    • Li, D.1    Xie, S.2    Ren, Y.3    Huo, L.4    Gao, J.5    Cui, D.6
  • 27
    • 80054881600 scopus 로고    scopus 로고
    • Class IIb HDAC6 regulates endothelial cell migration and angiogenesis by deacetylation of cortactin
    • D. Kaluza, J. Kroll, S. Gesierich, T. Yao, R.A. Boon, E. Hergenreider, et al., Class IIb HDAC6 regulates endothelial cell migration and angiogenesis by deacetylation of cortactin, EMBO J. 30 (2011) 4142, http://dx.doi.org/10.1038/emboj.2011.298.
    • (2011) EMBO J. , vol.30 , pp. 4142
    • Kaluza, D.1    Kroll, J.2    Gesierich, S.3    Yao, T.4    Boon, R.A.5    Hergenreider, E.6
  • 28
    • 84958662906 scopus 로고    scopus 로고
    • HDAC6 regulates cellular viral RNA sensing by deacetylation of RIG-I
    • S.J. Choi, H. Lee, J. Kim, S.Y. Park, T. Kim, W. Lee, et al., HDAC6 regulates cellular viral RNA sensing by deacetylation of RIG-I, EMBO J. 35 (2016) 429, http://dx.doi.org/10.15252/embj.201592586.
    • (2016) EMBO J. , vol.35 , pp. 429
    • Choi, S.J.1    Lee, H.2    Kim, J.3    Park, S.Y.4    Kim, T.5    Lee, W.6
  • 29
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • A.G. Kazantsev, L.M. Thompson, Therapeutic application of histone deacetylase inhibitors for central nervous system disorders, Nat. Rev. Drug Discov. 7 (2008) 854, http://dx.doi.org/10.1038/nrd2681.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 854
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 30
    • 84869869682 scopus 로고    scopus 로고
    • HDAC inhibitor-based therapies: Can we interpret the code
    • M. New, H. Olzscha, N.B. La Thangue, HDAC inhibitor-based therapies: can we interpret the code Cancer Epigenetics 6 (2012) 637, http://dx.doi.org/10.1016/j.molonc.2012.09.003.
    • (2012) Cancer Epigenetics , vol.6 , pp. 637
    • New, M.1    Olzscha, H.2    La Thangue, N.B.3
  • 31
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein
    • J. Borrow, V.P. Stanton, J.M. Andresen, R. Becher, F.G. Behm, R.S.K. Chaganti, et al., The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein, Nat. Genet. 14 (1996) 33, http://dx.doi.org/10.1038/ng0996-33.
    • (1996) Nat. Genet. , vol.14 , pp. 33
    • Borrow, J.1    Stanton, V.P.2    Andresen, J.M.3    Becher, R.4    Behm, F.G.5    Chaganti, R.S.K.6
  • 32
    • 0025917413 scopus 로고
    • Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties
    • P.P. Pandolfi, F. Grignani, M. Alcalay, A. Mencarelli, A. Biondi, F. LoCoco, et al., Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties, Oncogene 6 (1991) 1285.
    • (1991) Oncogene , vol.6 , pp. 1285
    • Pandolfi, P.P.1    Grignani, F.2    Alcalay, M.3    Mencarelli, A.4    Biondi, A.5    LoCoco, F.6
  • 33
    • 35148885660 scopus 로고    scopus 로고
    • Reduced body size and decreased intestinal tumor rates in HDAC2-mutant mice
    • S. Zimmermann, F. Kiefer, M. Prudenziati, C. Spiller, J. Hansen, T. Floss, et al., Reduced body size and decreased intestinal tumor rates in HDAC2-mutant mice, Cancer Res. 67 (2007) 9047, http://dx.doi.org/10.1158/0008-5472.CAN-07-0312.
    • (2007) Cancer Res. , vol.67 , pp. 9047
    • Zimmermann, S.1    Kiefer, F.2    Prudenziati, M.3    Spiller, C.4    Hansen, J.5    Floss, T.6
  • 34
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets
    • O. Witt, H.E. Deubzer, T. Milde, I. Oehme, HDAC family: what are the cancer relevant targets Cancer Lett. 277 (2009) 8, http://dx.doi.org/10.1016/j.canlet.2008.08.016.
    • (2009) Cancer Lett. , vol.277 , pp. 8
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 35
    • 84949908674 scopus 로고    scopus 로고
    • Epigenetic treatment of solid tumours: A review of clinical trials
    • C. Nervi, E. De Marinis, G. Codacci-Pisanelli, Epigenetic treatment of solid tumours: a review of clinical trials, Clin. Epigenetics 7 (2015) 1, http://dx.doi.org/10.1186/s13148-015-0157-2.
    • (2015) Clin. Epigenetics , vol.7 , pp. 1
    • Nervi, C.1    De Marinis, E.2    Codacci-Pisanelli, G.3
  • 36
    • 84655163371 scopus 로고    scopus 로고
    • Combination epigenetic therapy has efficacy in patients with refractory advanced nonesmall cell lung cancer
    • R.A. Juergens, J. Wrangle, F.P. Vendetti, S.C. Murphy, M. Zhao, B. Coleman, et al., Combination epigenetic therapy has efficacy in patients with refractory advanced nonesmall cell lung cancer, Cancer Discov. 1 (2011) 598, http://dx.doi.org/10.1158/2159-8290.CD-11-0214.
    • (2011) Cancer Discov. , vol.1 , pp. 598
    • Juergens, R.A.1    Wrangle, J.2    Vendetti, F.P.3    Murphy, S.C.4    Zhao, M.5    Coleman, B.6
  • 37
    • 84943653412 scopus 로고    scopus 로고
    • Combined inhibition of BET family proteins and histone deacetylases as a potential epigenetics-based therapy for pancreatic ductal adenocarcinoma
    • P.K. Mazur, A. Herner, S.S. Mello, M. Wirth, S. Hausmann, F.J. Sanchez-Rivera, et al., Combined inhibition of BET family proteins and histone deacetylases as a potential epigenetics-based therapy for pancreatic ductal adenocarcinoma, Nat. Med. 21 (2015) 1163.
    • (2015) Nat. Med. , vol.21 , pp. 1163
    • Mazur, P.K.1    Herner, A.2    Mello, S.S.3    Wirth, M.4    Hausmann, S.5    Sanchez-Rivera, F.J.6
  • 38
    • 84871171710 scopus 로고    scopus 로고
    • Structural basis for sirtuin activity and inhibition
    • H. Yuan, R. Marmorstein, Structural basis for sirtuin activity and inhibition, J. Biol. Chem. 287 (2012) 42428, http://dx.doi.org/10.1074/jbc.R112.372300.
    • (2012) J. Biol. Chem. , vol.287 , pp. 42428
    • Yuan, H.1    Marmorstein, R.2
  • 39
    • 84942372058 scopus 로고    scopus 로고
    • The multifaceted functions of sirtuins in cancer
    • A. Chalkiadaki, L. Guarente, The multifaceted functions of sirtuins in cancer, Nat. Rev. Cancer 15 (2015) 608.
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 608
    • Chalkiadaki, A.1    Guarente, L.2
  • 40
    • 48249102000 scopus 로고    scopus 로고
    • Phylogeny.fr: Robust phylogenetic analysis for the non-specialist
    • A. Dereeper, V. Guignon, G. Blanc, S. Audic, S. Buffet, F. Chevenet, et al., Phylogeny.fr: robust phylogenetic analysis for the non-specialist, Nucleic Acids Res. 36 (2008) W465, http://dx.doi.org/10.1093/nar/gkn180.
    • (2008) Nucleic Acids Res. , vol.36 , pp. W465
    • Dereeper, A.1    Guignon, V.2    Blanc, G.3    Audic, S.4    Buffet, S.5    Chevenet, F.6
  • 41
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • J. Castresana, Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis, Mol. Biol. Evol. 17 (2000) 540.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 540
    • Castresana, J.1
  • 42
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • S. Guindon, J.-F. Dufayard, V. Lefort, M. Anisimova, W. Hordijk, O. Gascuel, New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0, Syst. Biol. 59 (2010) 307, http://dx.doi.org/10.1093/sysbio/syq010.
    • (2010) Syst. Biol. , vol.59 , pp. 307
    • Guindon, S.1    Dufayard, J.-F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 43
    • 33745256005 scopus 로고    scopus 로고
    • Approximate likelihood-ratio test for branches: A fast, accurate, powerful alternative
    • M. Anisimova, O. Gascuel, Approximate likelihood-ratio test for branches: a fast, accurate, powerful alternative, Syst. Biol. 55 (2006) 539, http://dx.doi.org/10.1080/10635150600755453.
    • (2006) Syst Biol. , vol.55 , pp. 539
    • Anisimova, M.1    Gascuel, O.2
  • 44
    • 33750314083 scopus 로고    scopus 로고
    • TreeDyn: Towards dynamic graphics and annotations for analyses of trees
    • F. Chevenet, C. Brun, A.-L. Ba~nuls, B. Jacq, R. Christen, TreeDyn: towards dynamic graphics and annotations for analyses of trees, BMC Bioinforma. 7 (2006) 1, http://dx.doi.org/10.1186/1471-2105-7-439.
    • (2006) BMC Bioinforma. , vol.7 , pp. 1
    • Chevenet, F.1    Brun, C.2    Banuls, A.-L.3    Jacq, B.4    Christen, R.5
  • 45
    • 84869880178 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • B. Barneda-Zahonero, M. Parra, Histone deacetylases and cancer, Cancer Epigenetics 6 (2012) 579, http://dx.doi.org/10.1016/j.molonc.2012.07.003.
    • (2012) Cancer Epigenetics , vol.6 , pp. 579
    • Barneda-Zahonero, B.1    Parra, M.2
  • 47
    • 44349114629 scopus 로고    scopus 로고
    • HDAC inhibitors correct frataxin deficiency in a friedreich ataxia mouse model
    • M. Rai, E. Soragni, K. Jenssen, R. Burnett, D. Herman, G. Coppola, et al., HDAC inhibitors correct frataxin deficiency in a friedreich ataxia mouse model, PLoS ONE 3 (2008) e1958, http://dx.doi.org/10.1371/journal.pone.0001958.
    • (2008) PLoS ONE , vol.3 , pp. e1958
    • Rai, M.1    Soragni, E.2    Jenssen, K.3    Burnett, R.4    Herman, D.5    Coppola, G.6
  • 48
    • 84929359403 scopus 로고    scopus 로고
    • Histone deacetylase 10 suppresses proliferation and invasion by inhibiting the phosphorylation of b-catenin and serves as an independent prognostic factor for human clear cell renal cell carcinoma
    • W. Fan, J. Huang, H. Xiao, Histone deacetylase 10 suppresses proliferation and invasion by inhibiting the phosphorylation of b-catenin and serves as an independent prognostic factor for human clear cell renal cell carcinoma, Int. J. Clin. Exp. Med. 8 (2015) 3734.
    • (2015) Int. J. Clin. Exp. Med. , vol.8 , pp. 3734
    • Fan, W.1    Huang, J.2    Xiao, H.3
  • 49
    • 84941584627 scopus 로고    scopus 로고
    • Histone deacetylase 10 regulates DNA mismatch repair and may involve the deacetylation of MutS Homolog 2
    • R. Radhakrishnan, Y. Li, S. Xiang, F. Yuan, Z. Yuan, E. Telles, et al., Histone deacetylase 10 regulates dna mismatch repair and may involve the deacetylation of MutS Homolog 2, J. Biol. Chem. 290 (2015) 22795, http://dx.doi.org/10.1074/jbc.M114.612945.
    • (2015) J. Biol. Chem. , vol.290 , pp. 22795
    • Radhakrishnan, R.1    Li, Y.2    Xiang, S.3    Yuan, F.4    Yuan, Z.5    Telles, E.6
  • 50
    • 84944600409 scopus 로고    scopus 로고
    • Histone deacetylase 10 regulates the cell cycle G2/M phase transition via a novel Let-7eHMGA2ecyclin A2 pathway
    • Y. Li, L. Peng, E. Seto, Histone deacetylase 10 regulates the cell cycle G2/M phase transition via a novel Let-7eHMGA2ecyclin A2 pathway, Mol. Cell. Biol. 35 (2015) 3547, http://dx.doi.org/10.1128/MCB.00400-15.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 3547
    • Li, Y.1    Peng, L.2    Seto, E.3
  • 51
    • 84952864384 scopus 로고    scopus 로고
    • Growth attenuation is associated with histone deacetylase 10-induced autophagy in the liver
    • G. Pinto, B. Shtaif, M. Phillip, G. Gat-Yablonski, Growth attenuation is associated with histone deacetylase 10-induced autophagy in the liver, J. Nutr. Biochem. 27 (2016) 171, http://dx.doi.org/10.1016/j.jnutbio.2015.08.031.
    • (2016) J. Nutr. Biochem. , vol.27 , pp. 171
    • Pinto, G.1    Shtaif, B.2    Phillip, M.3    Gat-Yablonski, G.4
  • 52
    • 43949130430 scopus 로고    scopus 로고
    • Structural origin of selectivity in class II-selective histone deacetylase inhibitors
    • G. Estiu, E. Greenberg, C.B. Harrison, N.P. Kwiatkowski, R. Mazitschek, J.E. Bradner, et al., Structural origin of selectivity in class II-selective histone deacetylase inhibitors, J. Med. Chem. 51 (2008) 2898, http://dx.doi.org/10.1021/jm7015254.
    • (2008) J. Med. Chem. , vol.51 , pp. 2898
    • Estiu, G.1    Greenberg, E.2    Harrison, C.B.3    Kwiatkowski, N.P.4    Mazitschek, R.5    Bradner, J.E.6
  • 53
    • 84894031215 scopus 로고    scopus 로고
    • Mutagenesis studies of the 14 Å internal cavity of histone deacetylase 1: Insights toward the acetate-escape hypothesis and selective inhibitor design
    • M.K. Wambua, D.A. Nalawansha, A.T. Negmeldin, M.K.H. Pflum, Mutagenesis studies of the 14 Å internal cavity of histone deacetylase 1: insights toward the acetate-escape hypothesis and selective inhibitor design, J. Med. Chem. 57 (2014) 642, http://dx.doi.org/10.1021/jm401837e.
    • (2014) J. Med. Chem. , vol.57 , pp. 642
    • Wambua, M.K.1    Nalawansha, D.A.2    Negmeldin, A.T.3    Pflum, M.K.H.4
  • 54
    • 84940036821 scopus 로고    scopus 로고
    • Histone deacetylase 4 (HDAC4) inhibitors: A promising treatment for Huntington's disease
    • A.F. Abdel-Magid, Histone deacetylase 4 (HDAC4) inhibitors: a promising treatment for Huntington's disease, ACS Med. Chem. Lett. 4 (2013) 692, http://dx.doi.org/10.1021/ml4002216.
    • (2013) ACS Med. Chem. Lett. , vol.4 , pp. 692
    • Abdel-Magid, A.F.1
  • 55
    • 84883155892 scopus 로고    scopus 로고
    • Development and therapeutic implications of selective histone deacetylase 6 inhibitors
    • J.H. Kalin, J.A. Bergman, Development and therapeutic implications of selective histone deacetylase 6 inhibitors, J. Med. Chem. 56 (2013) 6297, http://dx.doi.org/10.1021/jm4001659.
    • (2013) J. Med. Chem. , vol.56 , pp. 6297
    • Kalin, J.H.1    Bergman, J.A.2
  • 56
    • 82955173014 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Emerging mechanisms of resistance
    • R.W. Robey, A.R. Chakraborty, A. Basseville, V. Luchenko, J. Bahr, Z. Zhan, et al., Histone deacetylase inhibitors: emerging mechanisms of resistance, Mol. Pharm. 8 (2011) 2021, http://dx.doi.org/10.1021/mp200329f.
    • (2011) Mol. Pharm. , vol.8 , pp. 2021
    • Robey, R.W.1    Chakraborty, A.R.2    Basseville, A.3    Luchenko, V.4    Bahr, J.5    Zhan, Z.6
  • 59
    • 84884685624 scopus 로고    scopus 로고
    • Structural basis for the inhibition of histone deacetylase 8 (HDAC8) a key epigenetic player in the blood fluke Schistosoma mansoni
    • M. Marek, S. Kannan, A.-T. Hauser, M. Moraes Moureo, S. Caby, V. Cura, et al., Structural basis for the inhibition of histone deacetylase 8 (HDAC8), a key epigenetic player in the blood fluke Schistosoma mansoni, PLoS Pathog. 9 (2013) e1003645, http://dx.doi.org/10.1371/journal.ppat.1003645.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003645
    • Marek, M.1    Kannan, S.2    Hauser, A.-T.3    Moraes Moureo, M.4    Caby, S.5    Cura, V.6
  • 60
    • 84962198274 scopus 로고    scopus 로고
    • Structure-based design and synthesis of novel inhibitors targeting HDAC8 from Schistosoma mansoni for the treatment of schistosomiasis
    • T. Heimburg, A. Chakrabarti, J. Lancelot, M. Marek, J. Melesina, A.-T. Hauser, et al., Structure-based design and synthesis of novel inhibitors targeting HDAC8 from Schistosoma mansoni for the treatment of schistosomiasis, J. Med. Chem. 59 (2016) 2423, http://dx.doi.org/10.1021/acs.jmedchem.5b01478.
    • (2016) J. Med. Chem. , vol.59 , pp. 2423
    • Heimburg, T.1    Chakrabarti, A.2    Lancelot, J.3    Marek, M.4    Melesina, J.5    Hauser, A.-T.6
  • 61
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • M.S. Finnin, J.R. Donigian, A. Cohen, V.M. Richon, R.A. Rifkind, P.A. Marks, et al., Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors, Nature 401 (1999) 188, http://dx.doi.org/10.1038/43710.
    • (1999) Nature , vol.401 , pp. 188
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3    Richon, V.M.4    Rifkind, R.A.5    Marks, P.A.6
  • 62
    • 77955808765 scopus 로고    scopus 로고
    • A proton-shuttle reaction mechanism for histone deacetylase 8 and the catalytic role of metal ions
    • R. Wu, S. Wang, N. Zhou, Z. Cao, Y. Zhang, A proton-shuttle reaction mechanism for histone deacetylase 8 and the catalytic role of metal ions, J. Am. Chem. Soc. 132 (2010) 9471, http://dx.doi.org/10.1021/ja103932d.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9471
    • Wu, R.1    Wang, S.2    Zhou, N.3    Cao, Z.4    Zhang, Y.5
  • 63
    • 79954998200 scopus 로고    scopus 로고
    • Zinc chelation with hydroxamate in histone deacetylases modulated by water access to the linker binding channel
    • R. Wu, Z. Lu, Z. Cao, Y. Zhang, Zinc chelation with hydroxamate in histone deacetylases modulated by water access to the linker binding channel, J. Am. Chem. Soc. 133 (2011) 6110, http://dx.doi.org/10.1021/ja111104p.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6110
    • Wu, R.1    Lu, Z.2    Cao, Z.3    Zhang, Y.4
  • 64
    • 84878388412 scopus 로고    scopus 로고
    • Quantum polarized ligand docking investigation to understand the significance of protonation states in histone deacetylase inhibitors
    • S. Kalyaanamoorthy, Y.-P.P. Chen, Quantum polarized ligand docking investigation to understand the significance of protonation states in histone deacetylase inhibitors, J. Mol. Graph. Model. 44 (2013) 44, http://dx.doi.org/10.1016/j.jmgm.2013.05.002.
    • (2013) J. Mol. Graph. Model. , vol.44 , pp. 44
    • Kalyaanamoorthy, S.1    Chen, Y.-P.P.2
  • 65
    • 84906330653 scopus 로고    scopus 로고
    • Inhibition and mechanism of HDAC8 revisited
    • K. Chen, X. Zhang, Y.-D. Wu, O. Wiest, Inhibition and mechanism of HDAC8 revisited, J. Am. Chem. Soc. 136 (2014) 11636, http://dx.doi.org/10.1021/ja501548p.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 11636
    • Chen, K.1    Zhang, X.2    Wu, Y.-D.3    Wiest, O.4
  • 67
    • 84916243697 scopus 로고    scopus 로고
    • Thermodynamics of binding of structurally similar ligands to histone deacetylase 8 sheds light on challenges in the rational design of potent and isozyme-selective inhibitors of the enzyme
    • R.K. Singh, T. Suzuki, T. Mandal, N. Balsubramanian, M. Haldar, D.J. Mueller, J.A. Strode, G. Cook, S. Mallik, D.K. Srivastava, Thermodynamics of Binding of Structurally Similar Ligands to Histone Deacetylase 8 Sheds Light on Challenges in the Rational Design of Potent and Isozyme-Selective Inhibitors of the Enzyme, Biochemistry 53 (2014) 7445, http://dx.doi.org/10.1021/bi500711x.
    • (2014) Biochemistry , vol.53 , pp. 7445
    • Singh, R.K.1    Suzuki, T.2    Mandal, T.3    Balsubramanian, N.4    Haldar, M.5    Mueller, D.J.6    Strode, J.A.7    Cook, G.8    Mallik, S.9    Srivastava, D.K.10
  • 68
    • 84903128207 scopus 로고    scopus 로고
    • Kinetic method for the large-scale analysis of the binding mechanism of histone deacetylase inhibitors
    • C. Meyners, M.G.J. Baud, M.J. Fuchter, F.-J. Meyer-Almes, Kinetic method for the large-scale analysis of the binding mechanism of histone deacetylase inhibitors, Anal. Biochem. 460 (2014) 39, http://dx.doi.org/10.1016/j.ab.2014.05.014.
    • (2014) Anal. Biochem. , vol.460 , pp. 39
    • Meyners, C.1    Baud, M.G.J.2    Fuchter, M.J.3    Meyer-Almes, F.-J.4
  • 69
    • 33846695065 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor assay based on fluorescence resonance energy transfer
    • D. Riester, C. Hildmann, A. Schwienhorst, F.-J. Meyer-Almes, Histone deacetylase inhibitor assay based on fluorescence resonance energy transfer, Anal. Biochem. 362 (2007) 136, http://dx.doi.org/10.1016/j.ab.2006.12.019.
    • (2007) Anal. Biochem. , vol.362 , pp. 136
    • Riester, D.1    Hildmann, C.2    Schwienhorst, A.3    Meyer-Almes, F.-J.4
  • 70
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor-ligand complexes and its effect on biological function
    • P.J. Tummino, R.A. Copeland, Residence time of receptor-ligand complexes and its effect on biological function, Biochem. (Mosc.) 47 (2008) 5481, http://dx.doi.org/10.1021/bi8002023.
    • (2008) Biochem. (Mosc.) , vol.47 , pp. 5481
    • Tummino, P.J.1    Copeland, R.A.2
  • 71
    • 84893699626 scopus 로고    scopus 로고
    • Divergent kinetics differentiate the mechanism of action of two HDAC inhibitors
    • A.M. Kral, N. Ozerova, J. Close, J. Jung, M. Chenard, J. Fleming, et al., Divergent kinetics differentiate the mechanism of action of two HDAC inhibitors, Biochem. (Mosc.) 53 (2014) 725, http://dx.doi.org/10.1021/bi400936h.
    • (2014) Biochem. (Mosc.) , vol.53 , pp. 725
    • Kral, A.M.1    Ozerova, N.2    Close, J.3    Jung, J.4    Chenard, M.5    Fleming, J.6
  • 72
    • 84893407575 scopus 로고    scopus 로고
    • Docking ligands into flexible and solvated macromolecules. 6. Development and application to the docking of HDACs and other zinc metalloenzymes inhibitors
    • J. Pottel, E. Therrien, J.L. Gleason, N. Moitessier, Docking ligands into flexible and solvated macromolecules. 6. Development and application to the docking of HDACs and other zinc metalloenzymes inhibitors, J. Chem. Inf. Model 54 (2014) 254, http://dx.doi.org/10.1021/ci400550m.
    • (2014) J. Chem. Inf. Model , vol.54 , pp. 254
    • Pottel, J.1    Therrien, E.2    Gleason, J.L.3    Moitessier, N.4
  • 73
    • 84874039614 scopus 로고    scopus 로고
    • Discovering the binding modes of natural products with histone deacetylase 1
    • Lei Zhang, Minyong Li, Lihui Zhang, Wenfang Xu, Discovering the binding modes of natural products with histone deacetylase 1, Med. Chem. 9 (2013) 126, http://dx.doi.org/10.2174/1573406411309010126.
    • (2013) Med. Chem. , vol.9 , pp. 126
    • Zhang, L.1    Li, M.2    Zhang, L.3    Xu, W.4
  • 74
    • 84864035147 scopus 로고    scopus 로고
    • In silico modification of suberoylanilide hydroxamic acid (SAHA) as potential inhibitor for class II histone deacetylase (HDAC)
    • U.S. Tambunan, N. Bramantya, A.A. Parikesit, In silico modification of suberoylanilide hydroxamic acid (SAHA) as potential inhibitor for class II histone deacetylase (HDAC), BMC Bioinforma. 12 (2011) 1, http://dx.doi.org/10.1186/1471-2105-12-S13-S23.
    • (2011) BMC Bioinforma. , vol.12 , pp. 1
    • Tambunan, U.S.1    Bramantya, N.2    Parikesit, A.A.3
  • 75
    • 77957920371 scopus 로고    scopus 로고
    • Identification of a better Homo sapiens Class II HDAC inhibitor through binding energy calculations and descriptor analysis
    • U.S.F. Tambunan, E.K. Wulandari, Identification of a better Homo sapiens Class II HDAC inhibitor through binding energy calculations and descriptor analysis, BMC Bioinforma. 11 (2010) 1, http://dx.doi.org/10.1186/1471-2105-11-S7-S16.
    • (2010) BMC Bioinforma. , vol.11 , pp. 1
    • Tambunan, U.S.F.1    Wulandari, E.K.2
  • 76
    • 80051599485 scopus 로고    scopus 로고
    • Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases
    • K.E. Cole, D.P. Dowling, M.A. Boone, A.J. Phillips, D.W. Christianson, Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases, J. Am. Chem. Soc. 133 (2011) 12474, http://dx.doi.org/10.1021/ja205972n.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 12474
    • Cole, K.E.1    Dowling, D.P.2    Boone, M.A.3    Phillips, A.J.4    Christianson, D.W.5
  • 77
    • 84889251209 scopus 로고    scopus 로고
    • Loop interactions and dynamics tune the enzymatic activity of the human histone deacetylase 8
    • M.B.A. Kunze, D.W. Wright, N.D. Werbeck, J. Kirkpatrick, P.V. Coveney, D.F. Hansen, Loop interactions and dynamics tune the enzymatic activity of the human histone deacetylase 8, J. Am. Chem. Soc. 135 (2013) 17862, http://dx.doi.org/10.1021/ja408184x.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 17862
    • Kunze, M.B.A.1    Wright, D.W.2    Werbeck, N.D.3    Kirkpatrick, J.4    Coveney, P.V.5    Hansen, D.F.6
  • 78
    • 84961291691 scopus 로고    scopus 로고
    • Variable active site loop conformations accommodate the binding of macrocyclic largazole analogues to HDAC8
    • C. Decroos, D.J. Clausen, B.E. Haines, O. Wiest, R.M. Williams, D.W. Christianson, Variable active site loop conformations accommodate the binding of macrocyclic largazole analogues to HDAC8, Biochem. (Mosc.) 54 (2015) 2126, http://dx.doi.org/10.1021/acs.biochem.5b00010.
    • (2015) Biochem. (Mosc.) , vol.54 , pp. 2126
    • Decroos, C.1    Clausen, D.J.2    Haines, B.E.3    Wiest, O.4    Williams, R.M.5    Christianson, D.W.6
  • 79
    • 84891304904 scopus 로고    scopus 로고
    • Design synthesis, biological evaluation of potent and selective class IIa histone deacetylase (HDAC) inhibitors as a potential therapy for Huntington's disease
    • R.W. Bürli, C.A. Luckhurst, O. Aziz, K.L. Matthews, D. Yates, K.A. Lyons, et al., Design, synthesis, biological evaluation of potent and selective class IIa histone deacetylase (HDAC) inhibitors as a potential therapy for Huntington's disease, J. Med. Chem. 56 (2013) 9934, http://dx.doi.org/10.1021/jm4011884.
    • (2013) J Med. Chem. , vol.56 , pp. 9934
    • Bürli, R.W.1    Luckhurst, C.A.2    Aziz, O.3    Matthews, K.L.4    Yates, D.5    Lyons, K.A.6
  • 81
    • 84865466261 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Structure-based modeling and isoform-selectivity prediction
    • L. Silvestri, F. Ballante, A. Mai, G.R. Marshall, R. Ragno, Histone deacetylase inhibitors: structure-based modeling and isoform-selectivity prediction, J. Chem. Inf. Model 52 (2012) 2215, http://dx.doi.org/10.1021/ci300160y.
    • (2012) J. Chem. Inf. Model , vol.52 , pp. 2215
    • Silvestri, L.1    Ballante, F.2    Mai, A.3    Marshall, G.R.4    Ragno, R.5
  • 82
    • 77956182637 scopus 로고    scopus 로고
    • Ligand and structure based pharmacophore modeling to facilitate novel histone deacetylase 8 inhibitor design
    • S. Thangapandian, S. John, S. Sakkiah, K.W. Lee, Ligand and structure based pharmacophore modeling to facilitate novel histone deacetylase 8 inhibitor design, Eur. J. Med. Chem. 45 (2010) 4409, http://dx.doi.org/10.1016/j.ejmech.2010.06.024.
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 4409
    • Thangapandian, S.1    John, S.2    Sakkiah, S.3    Lee, K.W.4
  • 83
    • 84878551168 scopus 로고    scopus 로고
    • Structural basis for the design and synthesis of selective HDAC inhibitors
    • S.D. Micco, M.G. Chini, S. Terracciano, I. Bruno, R. Riccio, G. Bifulco, Structural basis for the design and synthesis of selective HDAC inhibitors, Bioorg. Med. Chem. 21 (2013) 3795, http://dx.doi.org/10.1016/j.bmc.2013.04.036.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 3795
    • Micco, S.D.1    Chini, M.G.2    Terracciano, S.3    Bruno, I.4    Riccio, R.5    Bifulco, G.6
  • 84
    • 84928652393 scopus 로고    scopus 로고
    • Enhancing the sensitivity of pharmacophore-based virtual screening by incorporating customized ZBG features: A case study using histone deacetylase 8
    • X. Hou, J. Du, R. Liu, Y. Zhou, M. Li, W. Xu, et al., Enhancing the sensitivity of pharmacophore-based virtual screening by incorporating customized ZBG features: a case study using histone deacetylase 8, J. Chem. Inf. Model 55 (2015) 861, http://dx.doi.org/10.1021/ci500762z.
    • (2015) J. Chem. Inf. Model , vol.55 , pp. 861
    • Hou, X.1    Du, J.2    Liu, R.3    Zhou, Y.4    Li, M.5    Xu, W.6
  • 85
    • 84886506966 scopus 로고    scopus 로고
    • Investigating the selectivity of metalloenzyme inhibitors
    • J.A. Day, S.M. Cohen, Investigating the selectivity of metalloenzyme inhibitors, J. Med. Chem. 56 (2013) 7997, http://dx.doi.org/10.1021/jm401053m.
    • (2013) J. Med. Chem. , vol.56 , pp. 7997
    • Day, J.A.1    Cohen, S.M.2
  • 87
    • 84877701677 scopus 로고    scopus 로고
    • 3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition
    • V. Patil, Q.H. Sodji, J.R. Kornacki, M. Mrksich, A.K. Oyelere, 3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition, J. Med. Chem. 56 (2013) 3492, http://dx.doi.org/10.1021/jm301769u.
    • (2013) J. Med. Chem. , vol.56 , pp. 3492
    • Patil, V.1    Sodji, Q.H.2    Kornacki, J.R.3    Mrksich, M.4    Oyelere, A.K.5
  • 88
    • 84891318832 scopus 로고    scopus 로고
    • Synthesis and structureeactivity relationship of 3-hydroxypyridine-2-thione-based histone deacetylase inhibitors
    • Q.H. Sodji, V. Patil, J.R. Kornacki, M. Mrksich, A.K. Oyelere, Synthesis and structureeactivity relationship of 3-hydroxypyridine-2-thione-based histone deacetylase inhibitors, J. Med. Chem. 56 (2013) 9969, http://dx.doi.org/10.1021/jm401225q.
    • (2013) J. Med. Chem. , vol.56 , pp. 9969
    • Sodji, Q.H.1    Patil, V.2    Kornacki, J.R.3    Mrksich, M.4    Oyelere, A.K.5
  • 89
    • 77950679234 scopus 로고    scopus 로고
    • A structure-based virtual screening approach toward the discovery of histone deacetylase inhibitors: Identification of promising zinc-chelating groups
    • H. Park, S. Kim, Y.E. Kim, S.-J. Lim, A structure-based virtual screening approach toward the discovery of histone deacetylase inhibitors: identification of promising zinc-chelating groups, ChemMedChem. 5 (2010) 591, http://dx.doi.org/10.1002/cmdc.200900500.
    • (2010) Chem Med Chem. , vol.5 , pp. 591
    • Park, H.1    Kim, S.2    Kim, Y.E.3    Lim, S.-J.4
  • 90
    • 84925643353 scopus 로고    scopus 로고
    • Computational design of a time-dependent histone deacetylase 2 selective inhibitor
    • J. Zhou, M. Li, N. Chen, S. Wang, H.-B. Luo, Y. Zhang, et al., Computational design of a time-dependent histone deacetylase 2 selective inhibitor, ACS Chem. Biol. 10 (2015) 687, http://dx.doi.org/10.1021/cb500767c.
    • (2015) ACS Chem. Biol. , vol.10 , pp. 687
    • Zhou, J.1    Li, M.2    Chen, N.3    Wang, S.4    Luo, H.-B.5    Zhang, Y.6
  • 91
    • 84942825718 scopus 로고    scopus 로고
    • Investigation on the ZBG-functionality of phenyl-4-yl-acrylohydroxamic acid derivatives as histone deacetylase inhibitors
    • L. Musso, R. Cincinelli, V. Zuco, F. Zunino, A. Nurisso, M. Cuendet, et al., Investigation on the ZBG-functionality of phenyl-4-yl-acrylohydroxamic acid derivatives as histone deacetylase inhibitors, Bioorg. Med. Chem. Lett. 25 (2015) 4457, http://dx.doi.org/10.1016/j.bmcl.2015.09.006.
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 4457
    • Musso, L.1    Cincinelli, R.2    Zuco, V.3    Zunino, F.4    Nurisso, A.5    Cuendet, M.6
  • 92
    • 84907214942 scopus 로고    scopus 로고
    • Design synthesis, 3D pharmacophore, QSAR, docking studies of carboxylic acid derivatives as histone deacetylase inhibitors and cytotoxic agents
    • M.M. Abdel-Atty, N.A. Farag, S.E. Kassab, R.A.T. Serya, K.A.M. Abouzid, Design, synthesis, 3D pharmacophore, QSAR, docking studies of carboxylic acid derivatives as histone deacetylase inhibitors and cytotoxic agents, Bioorg. Chem. 57 (2014) 65, http://dx.doi.org/10.1016/j.bioorg.2014.08.006.
    • (2014) Bioorg Chem. , vol.57 , pp. 65
    • Abdel-Atty, M.M.1    Farag, N.A.2    Kassab, S.E.3    Serya, R.A.T.4    Abouzid, K.A.M.5
  • 93
    • 71049156256 scopus 로고    scopus 로고
    • Identification of Novel, selective, stable inhibitors of class II histone deacetylases. Validation studies of the inhibition of the enzymatic activity of hdac4 by small molecules as a novel approach for cancer therapy
    • J.M. Ontoria, S. Altamura, A. Di Marco, F. Ferrigno, R. Laufer, E. Muraglia, et al., Identification of Novel, selective, stable inhibitors of class II histone deacetylases. Validation studies of the inhibition of the enzymatic activity of hdac4 by small molecules as a novel approach for cancer therapy, J. Med. Chem. 52 (2009) 6782, http://dx.doi.org/10.1021/jm900555u.
    • (2009) J. Med. Chem. , vol.52 , pp. 6782
    • Ontoria, J.M.1    Altamura, S.2    Di Marco, A.3    Ferrigno, F.4    Laufer, R.5    Muraglia, E.6
  • 94
    • 84861592477 scopus 로고    scopus 로고
    • Appraisal of GABA and PABA as linker: Design and synthesis of novel benzamide based histone deacetylase inhibitors
    • H. Rajak, P. Kumar, P. Parmar, B.S. Thakur, R. Veerasamy, P.C. Sharma, et al., Appraisal of GABA and PABA as linker: design and synthesis of novel benzamide based histone deacetylase inhibitors, Eur. J. Med. Chem. 53 (2012) 390, http://dx.doi.org/10.1016/j.ejmech.2012.03.058.
    • (2012) Eur. J. Med. Chem. , vol.53 , pp. 390
    • Rajak, H.1    Kumar, P.2    Parmar, P.3    Thakur, B.S.4    Veerasamy, R.5    Sharma, P.C.6
  • 95
    • 84904962606 scopus 로고    scopus 로고
    • 1,3,4-Oxadiazole-containing histone deacetylase inhibitors: Anticancer activities in cancer cells
    • S. Valente, D. Trisciuoglio, T. De Luca, A. Nebbioso, D. Labella, A. Lenoci, et al., 1,3,4-Oxadiazole-containing histone deacetylase inhibitors: anticancer activities in cancer cells, J. Med. Chem. 57 (2014) 6259, http://dx.doi.org/10.1021/jm500303u.
    • (2014) J. Med. Chem. , vol.57 , pp. 6259
    • Valente, S.1    Trisciuoglio, D.2    De Luca, T.3    Nebbioso, A.4    Labella, D.5    Lenoci, A.6
  • 96
    • 84865662814 scopus 로고    scopus 로고
    • Rationale for the development of 2-aminobenzamide histone deacetylase inhibitors as therapeutics for friedreich ataxia
    • E. Soragni, C. Xu, H.L. Plasterer, V. Jacques, J.R. Rusche, J.M. Gottesfeld, Rationale for the development of 2-aminobenzamide histone deacetylase inhibitors as therapeutics for friedreich ataxia, J. Child. Neurol. 27 (2012) 1164, http://dx.doi.org/10.1177/0883073812448533.
    • (2012) J. Child. Neurol. , vol.27 , pp. 1164
    • Soragni, E.1    Xu, C.2    Plasterer, H.L.3    Jacques, V.4    Rusche, J.R.5    Gottesfeld, J.M.6
  • 97
    • 84881434208 scopus 로고    scopus 로고
    • Discovery of potent, isoform-selective inhibitors of histone deacetylase containing chiral heterocyclic capping groups and a N-(2-Aminophenyl) benzamide binding unit
    • C.M. Marson, C.J. Matthews, E. Yiannaki, S.J. Atkinson, P.E. Soden, L. Shukla, et al., Discovery of potent, isoform-selective inhibitors of histone deacetylase containing chiral heterocyclic capping groups and a N-(2-Aminophenyl) benzamide binding unit, J. Med. Chem. 56 (2013) 6156, http://dx.doi.org/10.1021/jm400634n.
    • (2013) J Med. Chem. , vol.56 , pp. 6156
    • Marson, C.M.1    Matthews, C.J.2    Yiannaki, E.3    Atkinson, S.J.4    Soden, P.E.5    Shukla, L.6
  • 98
    • 84885189972 scopus 로고    scopus 로고
    • Synthesis and HDAC inhibitory activity of isosteric thiazoline-oxazole largazole analogs
    • J.M. Guerra-Bubb, A.A. Bowers, W.B. Smith, R. Paranal, G. Estiu, O. Wiest, et al., Synthesis and HDAC inhibitory activity of isosteric thiazoline-oxazole largazole analogs, Bioorg. Med. Chem. Lett. 23 (2013) 6025, http://dx.doi.org/10.1016/j.bmcl.2013.06.012.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 6025
    • Guerra-Bubb, J.M.1    Bowers, A.A.2    Smith, W.B.3    Paranal, R.4    Estiu, G.5    Wiest, O.6
  • 99
  • 100
    • 77953740289 scopus 로고    scopus 로고
    • Synthesis and biological characterization of the histone deacetylase inhibitor largazole and C7-modified analogues
    • J.A. Souto, E. Vaz, I. Lepore, A.-C. Poppler, G. Franci, R.-Alvarez, et al., Synthesis and biological characterization of the histone deacetylase inhibitor largazole and C7-modified analogues, J. Med. Chem. 53 (2010) 4654, http://dx.doi.org/10.1021/jm100244y.
    • (2010) J. Med. Chem. , vol.53 , pp. 4654
    • Souto, J.A.1    Vaz, E.2    Lepore, I.3    Poppler, A.-C.4    Franci, G.5    Alvarez, R.6
  • 101
    • 80455162618 scopus 로고    scopus 로고
    • Largazole and analogues with modified metal-binding motifs targeting histone deacetylases: Synthesis and biological evaluation
    • P. Bhansali, C.L. Hanigan, R.A. Casero, L.M.V. Tillekeratne, Largazole and analogues with modified metal-binding motifs targeting histone deacetylases: synthesis and biological evaluation, J. Med. Chem. 54 (2011) 7453, http://dx.doi.org/10.1021/jm200432a.
    • (2011) J. Med. Chem. , vol.54 , pp. 7453
    • Bhansali, P.1    Hanigan, C.L.2    Casero, R.A.3    Tillekeratne, L.M.V.4
  • 102
    • 84907811029 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of largazole analogues with modified surface recognition cap groups
    • P. Bhansali, C.L. Hanigan, L. Perera, R.A.C. Jr., L.M.V. Tillekeratne, Synthesis and biological evaluation of largazole analogues with modified surface recognition cap groups, Eur. J. Med. Chem. 86 (2014) 528, http://dx.doi.org/10.1016/j.ejmech.2014.09.009.
    • (2014) Eur. J. Med. Chem. , vol.86 , pp. 528
    • Bhansali, P.1    Hanigan, C.L.2    Perera, R.A.C.L.3    Tillekeratne, L.M.V.4
  • 103
    • 78649527328 scopus 로고    scopus 로고
    • An aldol-based build/couple/pair strategy for the synthesis of mediumand large-sized rings: Discovery of macrocyclic histone deacetylase inhibitors
    • L.A. Marcaurelle, E. Comer, S. Dandapani, J.R. Duvall, B. Gerard, S. Kesavan, et al., An aldol-based build/couple/pair strategy for the synthesis of mediumand large-sized rings: discovery of macrocyclic histone deacetylase inhibitors, J. Am. Chem. Soc. 132 (2010) 16962, http://dx.doi.org/10.1021/ja105119r.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 16962
    • Marcaurelle, L.A.1    Comer, E.2    Dandapani, S.3    Duvall, J.R.4    Gerard, B.5    Kesavan, S.6
  • 104
    • 77951207678 scopus 로고    scopus 로고
    • Synthesis and biological activity of cyclotetrapeptide analogues of the natural HDAC inhibitor FR235222
    • S. Terracciano, S.D. Micco, G. Bifulco, P. Gallinari, R. Riccio, I. Bruno, Synthesis and biological activity of cyclotetrapeptide analogues of the natural HDAC inhibitor FR235222, Bioorg. Med. Chem. 18 (2010) 3252, http://dx.doi.org/10.1016/j.bmc.2010.03.022.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 3252
    • Terracciano, S.1    Micco, S.D.2    Bifulco, G.3    Gallinari, P.4    Riccio, R.5    Bruno, I.6
  • 105
    • 84905098006 scopus 로고    scopus 로고
    • Design and synthesis of CHAP31, trapoxin B and HC-toxin based bicyclic tetrapeptides disulfide as potent histone deacetylase inhibitors
    • M.A. Hoque, M.N. Islam, M.S. Islam, T. Kato, N. Nishino, A. Ito, et al., Design and synthesis of CHAP31, trapoxin B and HC-toxin based bicyclic tetrapeptides disulfide as potent histone deacetylase inhibitors, Bioorg. Med. Chem. 22 (2014) 3850, http://dx.doi.org/10.1016/j.bmc.2014.06.029.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 3850
    • Hoque, M.A.1    Islam, M.N.2    Islam, M.S.3    Kato, T.4    Nishino, N.5    Ito, A.6
  • 106
    • 84883180983 scopus 로고    scopus 로고
    • Total Synthesis and Full Histone deacetylase inhibitory profiling of azumamides AeE as well as b2-epi-Azumamide e and b3-epi-Azumamide
    • J.S. Villadsen, H.M. Stephansen, A.R. Maolanon, P. Harris, C.A. Olsen, Total Synthesis and Full Histone deacetylase inhibitory profiling of azumamides AeE as well as b2-epi-Azumamide E and b3-epi-Azumamide E, J. Med. Chem. 56 (2013) 6512, http://dx.doi.org/10.1021/jm4008449.
    • (2013) E J. Med. Chem. , vol.56 , pp. 6512
    • Villadsen, J.S.1    Stephansen, H.M.2    Maolanon, A.R.3    Harris, P.4    Olsen, C.A.5
  • 107
    • 84913573143 scopus 로고    scopus 로고
    • Methyl effect in azumamides provides insight into histone deacetylase inhibition by macrocycles
    • A.R. Maolanon, J.S. Villadsen, N.J. Christensen, C. Hoeck, T. Friis, P. Harris, et al., Methyl effect in azumamides provides insight into histone deacetylase inhibition by macrocycles, J. Med. Chem. 57 (2014) 9644, http://dx.doi.org/10.1021/jm501399d.
    • (2014) J. Med. Chem. , vol.57 , pp. 9644
    • Maolanon, A.R.1    Villadsen, J.S.2    Christensen, N.J.3    Hoeck, C.4    Friis, T.5    Harris, P.6
  • 108
    • 84925233415 scopus 로고    scopus 로고
    • An efficient synthesis of SK-658 and its analogs as potent histone deacetylase inhibitors
    • M.S. Islam, M.N. Islam, M.A. Hoque, N. Nishino, T. Kato, H.-J. Kim, et al., An efficient synthesis of SK-658 and its analogs as potent histone deacetylase inhibitors, Bioorg. Chem. 59 (2015) 145, http://dx.doi.org/10.1016/j.bioorg.2015.02.009.
    • (2015) Bioorg. Chem. , vol.59 , pp. 145
    • Islam, M.S.1    Islam, M.N.2    Hoque, M.A.3    Nishino, N.4    Kato, T.5    Kim, H.-J.6
  • 109
    • 84900392663 scopus 로고    scopus 로고
    • Late-Stage C-H coupling enables rapid identification of HDAC inhibitors: Synthesis and evaluation of NCH-31 analogues
    • H. Sekizawa, K. Amaike, Y. Itoh, T. Suzuki, K. Itami, J. Yamaguchi, Late-Stage C-H coupling enables rapid identification of HDAC inhibitors: synthesis and evaluation of NCH-31 analogues, ACS Med. Chem. Lett. 5 (2014) 582-586.
    • (2014) ACS Med. Chem. Lett. , vol.5 , pp. 582-586
    • Sekizawa, H.1    Amaike, K.2    Itoh, Y.3    Suzuki, T.4    Itami, K.5    Yamaguchi, J.6
  • 110
    • 84911919415 scopus 로고    scopus 로고
    • Superacid and thiol-ene reactions for access to psammaplin analogues with HDAC inhibition activities
    • F.E. Bahhaj, J. D-esir-e, C. Blanquart, N. Martinet, V. Zwick, C. Sim~oes-Pires, et al., Superacid and thiol-ene reactions for access to psammaplin analogues with HDAC inhibition activities, Tetrahedron. 70 (2014) 9702, http://dx.doi.org/10.1016/j.tet.2014.10.053.
    • (2014) Tetrahedron , vol.70 , pp. 9702
    • Bahhaj, F.E.1    Desire, J.2    Blanquart, C.3    Martinet, N.4    Zwick, V.5    Simoes-Pires, C.6
  • 111
    • 84881368436 scopus 로고    scopus 로고
    • Identification of novel HDAC inhibitors through cell based screening and their evaluation as potential anticancer agents
    • T. Wang, M. Sepulveda, P. Gonzales, S. Gately, Identification of novel HDAC inhibitors through cell based screening and their evaluation as potential anticancer agents, Bioorg. Med. Chem. Lett. 23 (2013) 4790, http://dx.doi.org/10.1016/j.bmcl.2013.07.001.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 4790
    • Wang, T.1    Sepulveda, M.2    Gonzales, P.3    Gately, S.4
  • 113
    • 84877577635 scopus 로고    scopus 로고
    • Design, syn thesis, biological evaluation of novel histone deacetylase 1 inhibitors through click chemistry
    • Q. Sun, Y. Yao, C. Liu, H. Li, H. Yao, X. Xue, et al., Design, synthesis, biological evaluation of novel histone deacetylase 1 inhibitors through click chemistry, Bioorg. Med. Chem. Lett. 23 (2013) 3295, http://dx.doi.org/10.1016/j.bmcl.2013.03.102.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 3295
    • Sun, Q.1    Yao, Y.2    Liu, C.3    Li, H.4    Yao, H.5    Xue, X.6
  • 114
    • 80052934367 scopus 로고    scopus 로고
    • Synthesis and evaluation of aliphatic-chain hydroxamates capped with osthole derivatives as histone deacetylase inhibitors
    • W.-J. Huang, C.-C. Chen, S.-W. Chao, C.-C. Yu, C.-Y. Yang, J.-H. Guh, et al., Synthesis and evaluation of aliphatic-chain hydroxamates capped with osthole derivatives as histone deacetylase inhibitors, Eur. J. Med. Chem. 46 (2011) 4042, http://dx.doi.org/10.1016/j.ejmech.2011.06.002.
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 4042
    • Huang, W.-J.1    Chen, C.-C.2    Chao, S.-W.3    Yu, C.-C.4    Yang, C.-Y.5    Guh, J.-H.6
  • 115
    • 84925234100 scopus 로고    scopus 로고
    • Design, synthesis and preliminary evaluation of a series of histone deacetylase inhibitors carrying a benzodiazepine ring
    • L. Guandalini, M. Balliu, C. Cellai, M.V. Martino, A. Nebbioso, C. Mercurio, et al., Design, synthesis and preliminary evaluation of a series of histone deacetylase inhibitors carrying a benzodiazepine ring, Eur. J. Med. Chem. 66 (2013) 56, http://dx.doi.org/10.1016/j.ejmech.2013.05.017.
    • (2013) Eur. J. Med. Chem. , vol.66 , pp. 56
    • Guandalini, L.1    Balliu, M.2    Cellai, C.3    Martino, M.V.4    Nebbioso, A.5    Mercurio, C.6
  • 116
    • 84896706991 scopus 로고    scopus 로고
    • Design, synthesis and preliminary bioactivity studies of 1,2-dihydrobenzo [d]isothiazol-3-one-1,1-dioxide hydroxamic acid derivatives as novel histone deacetylase inhibitors
    • L. Han, L. Wang, X. Hou, H. Fu, W. Song, W. Tang, et al., Design, synthesis and preliminary bioactivity studies of 1,2-dihydrobenzo [d]isothiazol-3-one-1,1-dioxide hydroxamic acid derivatives as novel histone deacetylase inhibitors, Bioorg. Med. Chem. 22 (2014) 1529, http://dx.doi.org/10.1016/j.bmc.2014.01.045.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 1529
    • Han, L.1    Wang, L.2    Hou, X.3    Fu, H.4    Song, W.5    Tang, W.6
  • 117
    • 84907859411 scopus 로고    scopus 로고
    • Design, synthesis, biological evaluation of 1, 3-disubstituted-pyrazole derivatives as new class i and IIb histone deacetylase inhibitors
    • Y. Yao, C. Liao, Z. Li, Z. Wang, Q. Sun, C. Liu, et al., Design, synthesis, biological evaluation of 1, 3-disubstituted-pyrazole derivatives as new class I and IIb histone deacetylase inhibitors, Eur. J. Med. Chem. 86 (2014) 639, http://dx.doi.org/10.1016/j.ejmech.2014.09.024.
    • (2014) Eur. J. Med. Chem. , vol.86 , pp. 639
    • Yao, Y.1    Liao, C.2    Li, Z.3    Wang, Z.4    Sun, Q.5    Liu, C.6
  • 118
    • 84891489942 scopus 로고    scopus 로고
    • Synthesis and anticancer activities of thieno[3,2-d]pyrimidines as novel HDAC inhibitors
    • Q. Tan, Z. Zhang, J. Hui, Y. Zhao, L. Zhu, Synthesis and anticancer activities of thieno [3,2-d]pyrimidines as novel HDAC inhibitors, Bioorg. Med. Chem. 22 (2014) 358, http://dx.doi.org/10.1016/j.bmc.2013.11.021.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 358
    • Tan, Q.1    Zhang, Z.2    Hui, J.3    Zhao, Y.4    Zhu, L.5
  • 119
    • 84908461603 scopus 로고    scopus 로고
    • Design synthesis and biological evaluation of 4-anilinothieno[2,3-d]pyrimidine-based hydroxamic acid derivatives as novel histone deacetylase inhibitors
    • W. Yang, L. Li, X. Ji, X. Wu, M. Su, L. Sheng, et al., Design, synthesis and biological evaluation of 4-anilinothieno [2,3-d]pyrimidine-based hydroxamic acid derivatives as novel histone deacetylase inhibitors, Bioorg. Med. Chem. 22 (2014) 6146, http://dx.doi.org/10.1016/j.bmc.2014.08.030.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 6146
    • Yang, W.1    Li, L.2    Ji, X.3    Wu, X.4    Su, M.5    Sheng, L.6
  • 120
    • 84929378676 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors induce growth arrest, apoptosis, differentiation in sarcoma cancer stem cells
    • G.D. Pompo, M. Salerno, D. Rotili, S. Valente, C. Zwergel, S. Avnet, et al., Novel histone deacetylase inhibitors induce growth arrest, apoptosis, differentiation in sarcoma cancer stem cells, J. Med. Chem. 58 (2015) 4073, http://dx.doi.org/10.1021/acs.jmedchem.5b00126.
    • (2015) J Med. Chem. , vol.58 , pp. 4073
    • Pompo, G.D.1    Salerno, M.2    Rotili, D.3    Valente, S.4    Zwergel, C.5    Avnet, S.6
  • 121
    • 84887259628 scopus 로고    scopus 로고
    • New benzothiazole/thiazole-containing hydroxamic acids as potent histone deacetylase inhibitors and antitumor agents
    • T.T. Tung, D.T.K. Oanh, P.T.P. Dung, V.T.M. Hue, S.H. Park, B.W. Han, et al., New benzothiazole/thiazole-containing hydroxamic acids as potent histone deacetylase inhibitors and antitumor agents, Med. Chem. 9 (2013) 1051.
    • (2013) Med. Chem. , vol.9 , pp. 1051
    • Tung, T.T.1    Oanh, D.T.K.2    Dung, P.T.P.3    Hue, V.T.M.4    Park, S.H.5    Han, B.W.6
  • 122
    • 77951103831 scopus 로고    scopus 로고
    • Modified cap group suberoylanilide hydroxamic acid histone deacetylase inhibitor derivatives reveal improved selective antileukemic activity
    • C. Salmi-Smail, A. Fabre, F. Dequiedt, A. Restouin, R. Castellano, S. Garbit, et al., Modified cap group suberoylanilide hydroxamic acid histone deacetylase inhibitor derivatives reveal improved selective antileukemic activity, J. Med. Chem. 53 (2010) 3038, http://dx.doi.org/10.1021/jm901358y.
    • (2010) J. Med. Chem. , vol.53 , pp. 3038
    • Salmi-Smail, C.1    Fabre, A.2    Dequiedt, F.3    Restouin, A.4    Castellano, R.5    Garbit, S.6
  • 123
    • 77249176625 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of Triazol-4-ylphenyl-Bearing histone deacetylase inhibitors as anticancer agents
    • R. He, Y. Chen, Y. Chen, A.V. Ougolkov, J.-S. Zhang, D.N. Savoy, et al., Synthesis and biological evaluation of Triazol-4-ylphenyl-Bearing histone deacetylase inhibitors as anticancer agents, J. Med. Chem. 53 (2010) 1347, http://dx.doi.org/10.1021/jm901667k.
    • (2010) J. Med. Chem. , vol.53 , pp. 1347
    • He, R.1    Chen, Y.2    Chen, Y.3    Ougolkov, A.V.4    Zhang, J.-S.5    Savoy, D.N.6
  • 124
    • 84913554345 scopus 로고    scopus 로고
    • Design and optimization of novel hydroxamate-based histone deacetylase inhibitors of bissubstituted aromatic amides bearing potent activities against tumor growth and metastasis
    • F. Yang, T. Zhang, H. Wu, Y. Yang, N. Liu, A. Chen, et al., Design and optimization of novel hydroxamate-based histone deacetylase inhibitors of bissubstituted aromatic amides bearing potent activities against tumor growth and metastasis, J. Med. Chem. 57 (2014) 9357, http://dx.doi.org/10.1021/jm5012148.
    • (2014) J. Med. Chem. , vol.57 , pp. 9357
    • Yang, F.1    Zhang, T.2    Wu, H.3    Yang, Y.4    Liu, N.5    Chen, A.6
  • 125
    • 84872823252 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors with a novel connecting unit linker region reveal a selectivity profile for HDAC4 and HDAC5 with improved activity against chemoresistant cancer cells
    • L. Marek, A. Hamacher, F.K. Hansen, K. Kuna, H. Gohlke, M.U. Kassack, et al., Histone deacetylase (HDAC) inhibitors with a novel connecting unit linker region reveal a selectivity profile for HDAC4 and HDAC5 with improved activity against chemoresistant cancer cells, J. Med. Chem. 56 (2013) 427, http://dx.doi.org/10.1021/jm301254q.
    • (2013) J. Med. Chem. , vol.56 , pp. 427
    • Marek, L.1    Hamacher, A.2    Hansen, F.K.3    Kuna, K.4    Gohlke, H.5    Kassack, M.U.6
  • 126
    • 84902147732 scopus 로고    scopus 로고
    • Discovery of HDAC inhibitors with potent activity against multiple malaria parasite life cycle stages
    • F.K. Hansen, S.D.M. Sumanadasa, K. Stenzel, S. Duffy, S. Meister, L. Marek, et al., Discovery of HDAC inhibitors with potent activity against multiple malaria parasite life cycle stages, Eur. J. Med. Chem. 82 (2014) 204, http://dx.doi.org/10.1016/j.ejmech.2014.05.050.
    • (2014) Eur. J. Med. Chem. , vol.82 , pp. 204
    • Hansen, F.K.1    Sumanadasa, S.D.M.2    Stenzel, K.3    Duffy, S.4    Meister, S.5    Marek, L.6
  • 127
    • 80052925413 scopus 로고    scopus 로고
    • The structural requirements of histone deacetylase inhibitors: Suberoylanilide hydroxamic acid analogs modified at the C3 position display isoform selectivity
    • S.E. Choi, S.V.W. Weerasinghe, M.K.H. Pflum, The structural requirements of histone deacetylase inhibitors: suberoylanilide hydroxamic acid analogs modified at the C3 position display isoform selectivity, Bioorg. Med. Chem. Lett. 21 (2011) 6139, http://dx.doi.org/10.1016/j.bmcl.2011.08.027.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 6139
    • Choi, S.E.1    Weerasinghe, S.V.W.2    Pflum, M.K.H.3
  • 128
    • 84869085767 scopus 로고    scopus 로고
    • The structural requirements of histone deacetylase inhibitors: Suberoylanilide hydroxamic acid analogs modified at the C6 position
    • S.E. Choi, M.K.H. Pflum, The structural requirements of histone deacetylase inhibitors: suberoylanilide hydroxamic acid analogs modified at the C6 position, Bioorg. Med. Chem. Lett. 22 (2012) 7084, http://dx.doi.org/10.1016/j.bmcl.2012.09.093.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 7084
    • Choi, S.E.1    Pflum, M.K.H.2
  • 130
    • 84886742463 scopus 로고    scopus 로고
    • Novel isatin-based hydroxamic acids as histone deacetylase inhibitors and antitumor agents
    • N.-H. Nam, T.L. Huong, D.T.M. Dung, P.T.P. Dung, D.T.K. Oanh, D. Quyen, et al., Novel isatin-based hydroxamic acids as histone deacetylase inhibitors and antitumor agents, Eur. J. Med. Chem. 70 (2013) 477, http://dx.doi.org/10.1016/j.ejmech.2013.10.045.
    • (2013) Eur. J. Med. Chem. , vol.70 , pp. 477
    • Nam, N.-H.1    Huong, T.L.2    Dung, D.T.M.3    Dung, P.T.P.4    Oanh, D.T.K.5    Quyen, D.6
  • 131
  • 133
    • 79952357878 scopus 로고    scopus 로고
    • Discovery of N-hydroxy-4-(3-phenylpropanamido)benzamide derivative 5j, a novel histone deacetylase inhibitor, as a potential therapeutic agent for human breast cancer
    • J. Feng, H. Fang, X. Wang, Y. Jia, L. Zhang, J. Jiao, et al., Discovery of N-hydroxy-4-(3-phenylpropanamido)benzamide derivative 5j, a novel histone deacetylase inhibitor, as a potential therapeutic agent for human breast cancer, Cancer Biol. Ther. 11 (2011) 477.
    • (2011) Cancer Biol Ther. , vol.11 , pp. 477
    • Feng, J.1    Fang, H.2    Wang, X.3    Jia, Y.4    Zhang, L.5    Jiao, J.6
  • 134
    • 84879048463 scopus 로고    scopus 로고
    • Discovery of the first histone deacetylase 6/8 dual inhibitors
    • D.E. Olson, F.F. Wagner, T. Kaya, J.P. Gale, N. Aidoud, E.L. Davoine, et al., Discovery of the first histone deacetylase 6/8 dual inhibitors, J. Med. Chem. 56 (2013) 4816, http://dx.doi.org/10.1021/jm400390r.
    • (2013) J. Med. Chem. , vol.56 , pp. 4816
    • Olson, D.E.1    Wagner, F.F.2    Kaya, T.3    Gale, J.P.4    Aidoud, N.5    Davoine, E.L.6
  • 135
    • 84925841614 scopus 로고    scopus 로고
    • Design and synthesis of orally bioavailable aminopyrrolidinone histone deacetylase 6 inhibitors
    • X. Lin, W. Chen, Z. Qiu, L. Guo, W. Zhu, W. Li, et al., Design and synthesis of orally bioavailable aminopyrrolidinone histone deacetylase 6 inhibitors, J. Med. Chem. 58 (2015) 2809, http://dx.doi.org/10.1021/jm502011f.
    • (2015) J. Med. Chem. , vol.58 , pp. 2809
    • Lin, X.1    Chen, W.2    Qiu, Z.3    Guo, L.4    Zhu, W.5    Li, W.6
  • 136
    • 84896700010 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors with enhanced enzymatic inhibition effects and potent in vitro and in vivo antitumor activities
    • L. Zhang, Y. Zhang, C.J. Chou, E.S. Inks, X. Wang, X. Li, et al., Histone deacetylase inhibitors with enhanced enzymatic inhibition effects and potent in vitro and in vivo antitumor activities, ChemMedChem. 9 (2014) 638, http://dx.doi.org/10.1002/cmdc.201300297.
    • (2014) Chem Med Chem. , vol.9 , pp. 638
    • Zhang, L.1    Zhang, Y.2    Chou, C.J.3    Inks, E.S.4    Wang, X.5    Li, X.6
  • 137
    • 84969246377 scopus 로고    scopus 로고
    • Design, synthesis, pharmacological evaluation of novel N-acylhydrazone derivatives as potent histone deacetylase 6/8 dual inhibitors
    • D.A. Rodrigues, G.-A. Ferreira-Silva, A.C.S. Ferreira, R.A. Fernandes, J.K. Kwee, C.M.R. Sant'Anna, et al., Design, synthesis, pharmacological evaluation of novel N-acylhydrazone derivatives as potent histone deacetylase 6/8 dual inhibitors, J. Med. Chem. 59 (2016) 655, http://dx.doi.org/10.1021/acs.jmedchem.5b01525.
    • (2016) J. Med. Chem. , vol.59 , pp. 655
    • Rodrigues, D.A.1    Ferreira-Silva, G.A.2    Ferreira, A.C.S.3    Fernandes, R.A.4    Kwee, J.K.5    Sant'Anna, C.M.R.6
  • 138
    • 84885006253 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors derived from 4-(Aminomethyl)-N-hydroxybenzamide with high selectivity for the HDAC6 isoform
    • C. Blackburn, C. Barrett, J. Chin, K. Garcia, K. Gigstad, A. Gould, et al., Potent histone deacetylase inhibitors derived from 4-(Aminomethyl)-N-hydroxybenzamide with high selectivity for the HDAC6 isoform, J. Med. Chem. 56 (2013) 7201, http://dx.doi.org/10.1021/jm400385r.
    • (2013) J. Med. Chem. , vol.56 , pp. 7201
    • Blackburn, C.1    Barrett, C.2    Chin, J.3    Garcia, K.4    Gigstad, K.5    Gould, A.6
  • 139
    • 84907897779 scopus 로고    scopus 로고
    • Identification of a novel aminotetralin class of HDAC6 and HDAC8 selective inhibitors
    • G. Tang, J.C. Wong, W. Zhang, Z. Wang, N. Zhang, Z. Peng, et al., Identification of a novel aminotetralin class of HDAC6 and HDAC8 selective inhibitors, J. Med. Chem. 57 (2014) 8026, http://dx.doi.org/10.1021/jm5008962.
    • (2014) J. Med. Chem. , vol.57 , pp. 8026
    • Tang, G.1    Wong, J.C.2    Zhang, W.3    Wang, Z.4    Zhang, N.5    Peng, Z.6
  • 140
    • 84879415316 scopus 로고    scopus 로고
    • Benzofused hydroxamic acids: Useful fragments for the preparation of histone deacetylase inhibitors. Part 1: Hit identification
    • E. Marastoni, S. Bartoli, M. Berettoni, A. Cipollone, A. Ettorre, C.I. Fincham, et al., Benzofused hydroxamic acids: useful fragments for the preparation of histone deacetylase inhibitors. Part 1: hit identification, Bioorg. Med. Chem. Lett. 23 (2013) 4091, http://dx.doi.org/10.1016/j.bmcl.2013.05.053.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 4091
    • Marastoni, E.1    Bartoli, S.2    Berettoni, M.3    Cipollone, A.4    Ettorre, A.5    Fincham, C.I.6
  • 141
    • 84921998819 scopus 로고    scopus 로고
    • Influence of the adamantyl moiety on the activity of biphenylacrylohydroxamic acid-based HDAC inhibitors
    • R. Cincinelli, L. Musso, G. Giannini, V. Zuco, M.D. Cesare, F. Zunino, et al., Influence of the adamantyl moiety on the activity of biphenylacrylohydroxamic acid-based HDAC inhibitors, Eur. J. Med. Chem. 79 (2014) 251, http://dx.doi.org/10.1016/j.ejmech.2014.04.021.
    • (2014) Eur. J. Med. Chem. , vol.79 , pp. 251
    • Cincinelli, R.1    Musso, L.2    Giannini, G.3    Zuco, V.4    Cesare, M.D.5    Zunino, F.6
  • 143
    • 84886949366 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of di-substituted cinnamic hydroxamic acids bearing urea/thiourea unit as potent histone deacetylase inhibitors
    • C. Ning, Y. Bi, Y. He, W. Huang, L. Liu, Y. Li, et al., Design, synthesis and biological evaluation of di-substituted cinnamic hydroxamic acids bearing urea/thiourea unit as potent histone deacetylase inhibitors, Bioorg. Med. Chem. Lett. 23 (2013) 6432, http://dx.doi.org/10.1016/j.bmcl.2013.09.051.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 6432
    • Ning, C.1    Bi, Y.2    He, Y.3    Huang, W.4    Liu, L.5    Li, Y.6
  • 144
    • 77950686302 scopus 로고    scopus 로고
    • Synthesis of N-hydroxycinnamides capped with a naturally occurring moiety as inhibitors of histone deacetylase
    • W.-J. Huang, C.-C. Chen, S.-W. Chao, S.-S. Lee, F.-L. Hsu, Y.-L. Lu, et al., Synthesis of N-hydroxycinnamides capped with a naturally occurring moiety as inhibitors of histone deacetylase, ChemMedChem. 5 (2010) 598, http://dx.doi.org/10.1002/cmdc.200900494.
    • (2010) Chem Med Chem. , vol.5 , pp. 598
    • Huang, W.-J.1    Chen, C.-C.2    Chao, S.-W.3    Lee, S.-S.4    Hsu, F.-L.5    Lu, Y.-L.6
  • 145
    • 84918530742 scopus 로고    scopus 로고
    • Syntheses and discovery of a novel class of cinnamic hydroxamates as histone deacetylase inhibitors by multimodality molecular imaging in living subjects
    • C.T. Chan, J. Qi, W. Smith, R. Paranol, R. Mazitschek, N. West, et al., Syntheses and discovery of a novel class of cinnamic hydroxamates as histone deacetylase inhibitors by multimodality molecular imaging in living subjects, Cancer Res. 74 (2014) 7475, http://dx.doi.org/10.1158/0008-5472.CAN-14-0197.
    • (2014) Cancer Res. , vol.74 , pp. 7475
    • Chan, C.T.1    Qi, J.2    Smith, W.3    Paranol, R.4    Mazitschek, R.5    West, N.6
  • 146
    • 84899565467 scopus 로고    scopus 로고
    • Discovery of the first NHydroxycinnamamide-based histone deacetylase 1/3 dual inhibitors with potent oral antitumor activity
    • X. Li, E.S. Inks, X. Li, J. Hou, C.J. Chou, J. Zhang, et al., Discovery of the first NHydroxycinnamamide-based histone deacetylase 1/3 dual inhibitors with potent oral antitumor activity, J. Med. Chem. 57 (2014) 3324, http://dx.doi.org/10.1021/jm401877m.
    • (2014) J. Med. Chem. , vol.57 , pp. 3324
    • Li, X.1    Inks, E.S.2    Li, X.3    Hou, J.4    Chou, C.J.5    Zhang, J.6
  • 147
    • 84901263366 scopus 로고    scopus 로고
    • Azaindolylsulfonamides, with a more selective inhibitory effect on histone deacetylase 6 activity, exhibit antitumor activity in colorectal cancer HCT116 cells
    • H.-Y. Lee, A.-C. Tsai, M.-C. Chen, P.-J. Shen, Y.-C. Cheng, C.-C. Kuo, et al., Azaindolylsulfonamides, with a more selective inhibitory effect on histone deacetylase 6 activity, exhibit antitumor activity in colorectal cancer HCT116 cells, J. Med. Chem. 57 (2014) 4009, http://dx.doi.org/10.1021/jm401899x.
    • (2014) J Med. Chem. , vol.57 , pp. 4009
    • Lee, H.-Y.1    Tsai, A.-C.2    Chen, M.-C.3    Shen, P.-J.4    Cheng, Y.-C.5    Kuo, C.-C.6
  • 148
    • 84945914020 scopus 로고    scopus 로고
    • Lightcontrolled histone deacetylase (hdac) inhibitors: Towards photopharmacological chemotherapy
    • W. Szymanski, M.E. Ourailidou, W.A. Velema, F.J. Dekker, B.L. Feringa, Lightcontrolled histone deacetylase (hdac) inhibitors: towards photopharmacological chemotherapy, Chem.dEur. J. 21 (2015) 16517, http://dx.doi.org/10.1002/chem.201502809.
    • (2015) Chem. D Eur. J. , vol.21 , pp. 16517
    • Szymanski, W.1    Ourailidou, M.E.2    Velema, W.A.3    Dekker, F.J.4    Feringa, B.L.5
  • 149
    • 84877577078 scopus 로고    scopus 로고
    • Design synthesis and biological evaluation of indeno [1,2-d]thiazole derivatives as potent histone deacetylase inhibitors
    • M. Zhou, C. Ning, R. Liu, Y. He, N. Yu, Design, synthesis and biological evaluation of indeno [1,2-d]thiazole derivatives as potent histone deacetylase inhibitors, Bioorg. Med. Chem. Lett. 23 (2013) 3200, http://dx.doi.org/10.1016/j.bmcl.2013.04.004.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 3200
    • Zhou, M.1    Ning, C.2    Liu, R.3    He, Y.4    Yu, N.5
  • 150
    • 79960188498 scopus 로고    scopus 로고
    • Optimization of the in vitro cardiac safety of hydroxamate-based histone deacetylase inhibitors
    • M.D. Shultz, X. Cao, C.H. Chen, Y.S. Cho, N.R. Davis, J. Eckman, et al., Optimization of the in vitro cardiac safety of hydroxamate-based histone deacetylase inhibitors, J. Med. Chem. 54 (2011) 4752, http://dx.doi.org/10.1021/jm200388e.
    • (2011) J. Med. Chem. , vol.54 , pp. 4752
    • Shultz, M.D.1    Cao, X.2    Chen, C.H.3    Cho, Y.S.4    Davis, N.R.5    Eckman, J.6
  • 151
    • 84877045821 scopus 로고    scopus 로고
    • Synthesis and biological characterization of spiro[2H-(13)-benzoxazine-2,40-piperidine] based histone deacetylase inhibitors
    • F. Thaler, M. Varasi, A. Abate, G. Carenzi, A. Colombo, C. Bigogno, et al., Synthesis and biological characterization of spiro [2H-(1,3)-benzoxazine-2,40-piperidine] based histone deacetylase inhibitors, Eur. J. Med. Chem. 64 (2013) 273, http://dx.doi.org/10.1016/j.ejmech.2013.03.061.
    • (2013) Eur. J. Med. Chem. , vol.64 , pp. 273
    • Thaler, F.1    Varasi, M.2    Abate, A.3    Carenzi, G.4    Colombo, A.5    Bigogno, C.6
  • 152
    • 79960163508 scopus 로고    scopus 로고
    • Discovery of (2E)-3-2-Butyl-1-[2-(diethylamino)ethyl]-1H-benzimidazol-5-yl-N-hydroxyacrylamide (SB939), an orally active histone deacetylase inhibitor with a superior preclinical profile
    • H. Wang, N. Yu, D. Chen, K.C.L. Lee, P.L. Lye, J.W.W. Chang, et al., Discovery of (2E)-3-2-Butyl-1-[2-(diethylamino)ethyl]-1H-benzimidazol-5-yl-N-hydroxyacrylamide (SB939), an orally active histone deacetylase inhibitor with a superior preclinical profile, J. Med. Chem., 54, 2011. 4694
    • (2011) J. Med. Chem. , vol.54 , pp. 4694
    • Wang, H.1    Yu, N.2    Chen, D.3    Lee, K.C.L.4    Lye, P.L.5    Chang, J.W.W.6
  • 153
    • 77249133651 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of N-hydroxyphenylacrylamides and N-hydroxypyridin-2-ylacrylamides as novel histone deacetylase inhibitors
    • F. Thaler, A. Colombo, A. Mai, R. Amici, C. Bigogno, R. Boggio, et al., Synthesis and biological evaluation of N-hydroxyphenylacrylamides and N-hydroxypyridin-2-ylacrylamides as novel histone deacetylase inhibitors, J. Med. Chem. 53 (2010) 822, http://dx.doi.org/10.1021/jm901502p.
    • (2010) J. Med. Chem. , vol.53 , pp. 822
    • Thaler, F.1    Colombo, A.2    Mai, A.3    Amici, R.4    Bigogno, C.5    Boggio, R.6
  • 154
    • 84894034702 scopus 로고    scopus 로고
    • Improved synthesis and structural reassignment of MC1568: A class IIa selective HDAC inhibitor
    • C.L. Fleming, T.D. Ashton, V. Gaur, S.L. McGee, F.M. Pfeffer, Improved synthesis and structural reassignment of MC1568: a class IIa selective HDAC inhibitor, J. Med. Chem. 57 (2014) 1132, http://dx.doi.org/10.1021/jm401945k.
    • (2014) J. Med. Chem. , vol.57 , pp. 1132
    • Fleming, C.L.1    Ashton, T.D.2    Gaur, V.3    McGee, S.L.4    Pfeffer, F.M.5
  • 155
    • 84881369198 scopus 로고    scopus 로고
    • Novel N-hydroxyfurylacrylamide-based histone deacetylase (HDAC) inhibitors with branched CAP group (Part 2)
    • T. Feng, H. Wang, H. Su, H. Lu, L. Yu, X. Zhang, et al., Novel N-hydroxyfurylacrylamide-based histone deacetylase (HDAC) inhibitors with branched CAP group (Part 2), Bioorg. Med. Chem. 21 (2013) 5339, http://dx.doi.org/10.1016/j.bmc.2013.06.009.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 5339
    • Feng, T.1    Wang, H.2    Su, H.3    Lu, H.4    Yu, L.5    Zhang, X.6
  • 156
    • 84902549707 scopus 로고    scopus 로고
    • Design and synthesis of novel and highlyactive pan-histone deacetylase (pan-HDAC) inhibitors
    • T. Tashima, H. Murata, H. Kodama, Design and synthesis of novel and highlyactive pan-histone deacetylase (pan-HDAC) inhibitors, Bioorg. Med. Chem. 22 (2014) 3720, http://dx.doi.org/10.1016/j.bmc.2014.05.001.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 3720
    • Tashima, T.1    Murata, H.2    Kodama, H.3
  • 157
    • 84859789575 scopus 로고    scopus 로고
    • Discovery and extensive in vitro evaluations of NK-HDAC-1: A chiral histone deacetylase inhibitor as a promising lead
    • J. Hou, Z. Li, Q. Fang, C. Feng, H. Zhang, W. Guo, et al., Discovery and extensive in vitro evaluations of NK-HDAC-1: a chiral histone deacetylase inhibitor as a promising lead, J. Med. Chem. 55 (2012) 3066, http://dx.doi.org/10.1021/jm201496g.
    • (2012) J. Med. Chem. , vol.55 , pp. 3066
    • Hou, J.1    Li, Z.2    Fang, Q.3    Feng, C.4    Zhang, H.5    Guo, W.6
  • 158
    • 78149415398 scopus 로고    scopus 로고
    • Coumarin-suberoylanilide hydroxamic acid as a fluorescent probe for determining binding affinities and off-rates of histone deacetylase inhibitors
    • R.K. Singh, T. Mandal, N. Balasubramanian, G. Cook, D.K. Srivastava, Coumarin-suberoylanilide hydroxamic acid as a fluorescent probe for determining binding affinities and off-rates of histone deacetylase inhibitors, Anal. Biochem. 408 (2011) 309, http://dx.doi.org/10.1016/j.ab.2010.08.040.
    • (2011) Anal. Biochem. , vol.408 , pp. 309
    • Singh, R.K.1    Mandal, T.2    Balasubramanian, N.3    Cook, G.4    Srivastava, D.K.5
  • 159
    • 80052768852 scopus 로고    scopus 로고
    • Histone deacetylase cytoplasmic trapping by a novel fluorescent HDAC inhibitor
    • Y. Kong, M. Jung, K. Wang, S. Grindrod, A. Velena, S.A. Lee, et al., Histone deacetylase cytoplasmic trapping by a novel fluorescent HDAC inhibitor, Mol. Cancer Ther. 10 (2011) 1591, http://dx.doi.org/10.1158/1535-7163.MCT-10-0779.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 1591
    • Kong, Y.1    Jung, M.2    Wang, K.3    Grindrod, S.4    Velena, A.5    Lee, S.A.6
  • 160
    • 84865212342 scopus 로고    scopus 로고
    • Fluorescent analogs of the marine natural product psammaplin A: Synthesis and biological activity
    • F. Hentschel, F. Sasse, T. Lindel, Fluorescent analogs of the marine natural product psammaplin A: synthesis and biological activity, Org. Biomol. Chem. 10 (2012) 7120, http://dx.doi.org/10.1039/C2OB25909E.
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 7120
    • Hentschel, F.1    Sasse, F.2    Lindel, T.3
  • 161
    • 84936763373 scopus 로고    scopus 로고
    • An HDAC-Targeted Imaging Probe LBH589eCy5.5 for tumor detection and therapy evaluation
    • Q. Meng, Z. Liu, F. Li, J. Ma, H. Wang, Y. Huan, et al., An HDAC-Targeted Imaging Probe LBH589eCy5.5 for tumor detection and therapy evaluation, Mol. Pharm. 12 (2015) 2469, http://dx.doi.org/10.1021/acs.molpharmaceut.5b00167.
    • (2015) Mol. Pharm. , vol.12 , pp. 2469
    • Meng, Q.1    Liu, Z.2    Li, F.3    Ma, J.4    Wang, H.5    Huan, Y.6
  • 162
    • 84881385613 scopus 로고    scopus 로고
    • Histone-deacetylasetargeted fluorescent ruthenium(II) polypyridyl complexes as potent anticancer agents
    • R.-R. Ye, Z.-F. Ke, C.-P. Tan, L. He, L.-N. Ji, Z.-W. Mao, Histone-deacetylasetargeted fluorescent ruthenium(II) polypyridyl complexes as potent anticancer agents, Chem. e Eur. J. 19 (2013) 10160, http://dx.doi.org/10.1002/chem.201300814.
    • (2013) Chem. e Eur. J. , vol.19 , pp. 10160
    • Ye, R.-R.1    Ke, Z.-F.2    Tan, C.-P.3    He, L.4    Ji, L.-N.5    Mao, Z.-W.6
  • 163
    • 84865790010 scopus 로고    scopus 로고
    • Development of a fluorogenic probe with a transesterification switch for detection of histone deacetylase activity
    • R. Baba, Y. Hori, S. Mizukami, K. Kikuchi, Development of a fluorogenic probe with a transesterification switch for detection of histone deacetylase activity, J. Am. Chem. Soc. 134 (2012) 14310, http://dx.doi.org/10.1021/ja306045j.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 14310
    • Baba, R.1    Hori, Y.2    Mizukami, S.3    Kikuchi, K.4
  • 164
    • 79959631545 scopus 로고    scopus 로고
    • The synthesis and evaluation of N1-(4-(2-[18F]-fluoroethyl)phenyl)-N8-hydroxyoctanediamide ([18F]-FESAHA) A PET radiotracer designed for the delineation of histone deacetylase expression in cancer
    • B.M. Zeglis, N. Pillarsetty, V. Divilov, R.A. Blasberg, J.S. Lewis, The synthesis and evaluation of N1-(4-(2-[18F]-FESAHA), A PET radiotracer designed for the delineation of histone deacetylase expression in cancer, Nucl. Med. Biol. 38 (2011) 683, http://dx.doi.org/10.1016/j.nucmedbio.2010.12.008.
    • (2011) Nucl. Med. Biol. , vol.38 , pp. 683
    • Zeglis, B.M.1    Pillarsetty, N.2    Divilov, V.3    Blasberg, R.A.4    Lewis, J.S.5
  • 165
    • 84884246930 scopus 로고    scopus 로고
    • Novel 64Cu-Labeled CUDC-101 for in vivo PET imaging of histone deacetylases
    • Q. Meng, F. Li, S. Jiang, Z. Li, Novel 64Cu-Labeled CUDC-101 for in vivo PET imaging of histone deacetylases, ACS Med. Chem. Lett. 4 (2013) 858, http://dx.doi.org/10.1021/ml400191z.
    • (2013) ACS Med. Chem. Lett. , vol.4 , pp. 858
    • Meng, Q.1    Li, F.2    Jiang, S.3    Li, Z.4
  • 166
    • 84879622267 scopus 로고    scopus 로고
    • Class i HDAC imaging using [3H] CI-994 autoradiography
    • Y. Wang, Y.-L. Zhang, K. Hennig, J.P. Gale, Y. Hong, A. Cha, et al., Class I HDAC imaging using [3H]CI-994 autoradiography, Epigenetics 8 (2013) 756, http://dx.doi.org/10.4161/epi.25202.
    • (2013) Epigenetics , vol.8 , pp. 756
    • Wang, Y.1    Zhang, Y.-L.2    Hennig, K.3    Gale, J.P.4    Hong, Y.5    Cha, A.6
  • 167
    • 84908031655 scopus 로고    scopus 로고
    • Design, synthesis, evaluation of hydroxamic acid-based molecular probes for in vivo imaging of histone deacetylase (HDAC) in brain
    • C. Wang, T.E. Eessalu, V.N. Barth, C.H. Mitch, F.F. Wagner, Y. Hong, et al., Design, synthesis, evaluation of hydroxamic acid-based molecular probes for in vivo imaging of histone deacetylase (HDAC) in brain, Am. J. Nucl. Med. Mol. Imaging 4 (2014) 29.
    • (2014) Am. J. Nucl. Med. Mol. Imaging , vol.4 , pp. 29
    • Wang, C.1    Eessalu, T.E.2    Barth, V.N.3    Mitch, C.H.4    Wagner, F.F.5    Hong, Y.6
  • 168
    • 84867573822 scopus 로고    scopus 로고
    • Characterizing the disposition, metabolism, excretion of an orally active pan-deacetylase inhibitor, panobinostat, via trace radiolabeled 14C material in advanced cancer patients
    • S. Clive, M. Woo, T. Nydam, L. Kelly, M. Squier, M. Kagan, Characterizing the disposition, metabolism, excretion of an orally active pan-deacetylase inhibitor, panobinostat, via trace radiolabeled 14C material in advanced cancer patients, Cancer Chemother. Pharmacol. 70 (2012) 513, http://dx.doi.org/10.1007/s00280-012-1940-9.
    • (2012) Cancer Chemother Pharmacol. , vol.70 , pp. 513
    • Clive, S.1    Woo, M.2    Nydam, T.3    Kelly, L.4    Squier, M.5    Kagan, M.6
  • 169
    • 84888882303 scopus 로고    scopus 로고
    • Radionuclide labeling and evaluation of candidate radioligands for PET imaging of histone deacetylase in the brain
    • Y.J. Seo, L. Muench, A. Reid, J. Chen, Y. Kang, J.M. Hooker, et al., Radionuclide labeling and evaluation of candidate radioligands for PET imaging of histone deacetylase in the brain, Bioorg. Med. Chem. Lett. 23 (2013) 6700, http://dx.doi.org/10.1016/j.bmcl.2013.10.038.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 6700
    • Seo, Y.J.1    Muench, L.2    Reid, A.3    Chen, J.4    Kang, Y.5    Hooker, J.M.6
  • 170
    • 84904417032 scopus 로고    scopus 로고
    • Image-guided synthesis reveals potent blood-brain barrier permeable histone deacetylase inhibitors ACS
    • Y.J. Seo, Y. Kang, L. Muench, A. Reid, S. Caesar, L. Jean, et al., Image-guided synthesis reveals potent blood-brain barrier permeable histone deacetylase inhibitors, ACS Chem. Neurosci. 5 (2014) 588, http://dx.doi.org/10.1021/cn500021p.
    • (2014) Chem. Neurosci. , vol.5 , pp. 588
    • Seo, Y.J.1    Kang, Y.2    Muench, L.3    Reid, A.4    Caesar, S.5    Jean, L.6
  • 171
    • 84883557495 scopus 로고    scopus 로고
    • Whole-body pharmacokinetics of HDAC inhibitor drugs, butyric acid, valproic acid and 4-phenylbutyric acid measured with carbon-11 labeled analogs by PET
    • S.W. Kim, J.M. Hooker, N. Otto, K. Win, L. Muench, C. Shea, et al., Whole-body pharmacokinetics of HDAC inhibitor drugs, butyric acid, valproic acid and 4-phenylbutyric acid measured with carbon-11 labeled analogs by PET, Nucl. Med. Biol. 40 (2013) 912, http://dx.doi.org/10.1016/j.nucmedbio.2013.06.007.
    • (2013) Nucl. Med. Biol. , vol.40 , pp. 912
    • Kim, S.W.1    Hooker, J.M.2    Otto, N.3    Win, K.4    Muench, L.5    Shea, C.6
  • 172
    • 84885858940 scopus 로고    scopus 로고
    • The discovery and optimization of novel dual inhibitors of topoisomerase II and histone deacetylase
    • X. Zhang, B. Bao, X. Yu, L. Tong, Y. Luo, Q. Huang, et al., The discovery and optimization of novel dual inhibitors of topoisomerase ii and histone deacetylase, Bioorg. Med. Chem. 21 (2013) 6981, http://dx.doi.org/10.1016/j.bmc.2013.09.023.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 6981
    • Zhang, X.1    Bao, B.2    Yu, X.3    Tong, L.4    Luo, Y.5    Huang, Q.6
  • 173
    • 84857406206 scopus 로고    scopus 로고
    • Dual targeting of histone deacetylase and topoisomerase II with novel bifunctional inhibitors
    • W. Guerrant, V. Patil, J.C. Canzoneri, A.K. Oyelere, Dual targeting of histone deacetylase and topoisomerase II with novel bifunctional inhibitors, J. Med. Chem. 55 (2012) 1465, http://dx.doi.org/10.1021/jm200799p.
    • (2012) J. Med. Chem. , vol.55 , pp. 1465
    • Guerrant, W.1    Patil, V.2    Canzoneri, J.C.3    Oyelere, A.K.4
  • 174
    • 84887981384 scopus 로고    scopus 로고
    • Selectively targeting prostate cancer with antiandrogen equipped histone deacetylase inhibitors
    • B.E. Gryder, M.J. Akbashev, M.K. Rood, E.D. Raftery, W.M. Meyers, P. Dillard, et al., Selectively targeting prostate cancer with antiandrogen equipped histone deacetylase inhibitors, ACS Chem. Biol. 8 (2013) 2550, http://dx.doi.org/10.1021/cb400542w.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2550
    • Gryder, B.E.1    Akbashev, M.J.2    Rood, M.K.3    Raftery, E.D.4    Meyers, W.M.5    Dillard, P.6
  • 175
    • 84880856474 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors equipped with estrogen receptor modulation activity
    • B.E. Gryder, M.K. Rood, K.A. Johnson, V. Patil, E.D. Raftery, L.-P.D. Yao, et al., Histone deacetylase inhibitors equipped with estrogen receptor modulation activity, J. Med. Chem. 56 (2013) 5782, http://dx.doi.org/10.1021/jm400467w.
    • (2013) J. Med. Chem. , vol.56 , pp. 5782
    • Gryder, B.E.1    Rood, M.K.2    Johnson, K.A.3    Patil, V.4    Raftery, E.D.5    Yao, L.-P.D.6
  • 176
    • 84896696956 scopus 로고    scopus 로고
    • A chimeric SERMehistone deacetylase inhibitor approach to breast cancer therapy
    • H.K. Patel, M.I. Siklos, H. Abdelkarim, E.L. Mendonca, A. Vaidya, P.A. Petukhov, et al., A chimeric SERMehistone deacetylase inhibitor approach to breast cancer therapy, ChemMedChem. 9 (2014) 602, http://dx.doi.org/10.1002/cmdc.201300270.
    • (2014) Chem Med Chem. , vol.9 , pp. 602
    • Patel, H.K.1    Siklos, M.I.2    Abdelkarim, H.3    Mendonca, E.L.4    Vaidya, A.5    Petukhov, P.A.6
  • 177
    • 77949353758 scopus 로고    scopus 로고
    • Discovery of 7-(4-(3-Ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide (CUDC-101) as a potent multi-acting HDAC, EGFR, HER2 inhibitor for the treatment of cancer
    • X. Cai, H.-X. Zhai, J. Wang, J. Forrester, H. Qu, L. Yin, et al., Discovery of 7-(4-(3-Ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide (CUDC-101) as a potent multi-acting HDAC, EGFR, HER2 inhibitor for the treatment of cancer, J. Med. Chem. 53 (2010) 2000, http://dx.doi.org/10.1021/jm901453q.
    • (2000) J Med. Chem. , vol.53 , pp. 2010
    • Cai, X.1    Zhai, H.-X.2    Wang, J.3    Forrester, J.4    Qu, H.5    Yin, L.6


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