메뉴 건너뛰기




Volumn 67, Issue , 2016, Pages 18-42

Inhibitors of histone deacetylase as antitumor agents: A critical review

Author keywords

Anticancer activity; HDAC inhibitors; Histone deacetylase; Hydroxamic acids; Short chain fatty acids

Indexed keywords

ANTINEOPLASTIC AGENT; BELINOSTAT; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; PANOBINOSTAT; ROMIDEPSIN; SHORT CHAIN FATTY ACID; VORINOSTAT; FATTY ACID; HISTONE DEACETYLASE;

EID: 84970968588     PISSN: 00452068     EISSN: 10902120     Source Type: Journal    
DOI: 10.1016/j.bioorg.2016.05.005     Document Type: Review
Times cited : (184)

References (203)
  • 1
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome from genomic organization to genomic regulation
    • S. Khorasanizadeh The nucleosome from genomic organization to genomic regulation Cell 116 2004 259 272
    • (2004) Cell , vol.116 , pp. 259-272
    • Khorasanizadeh, S.1
  • 3
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • M.J. Pazin, and J.T. Kadonaga What's up and down with histone deacetylation and transcription? Cell 89 1997 325 328
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 4
    • 0035313803 scopus 로고    scopus 로고
    • Histone acetyltransferases: Function, structure, and catalysis
    • R. Marmorstein, and S.Y. Roth Histone acetyltransferases: function, structure, and catalysis Curr. Opin. Genet. Dev. 11 2001 155 161
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 155-161
    • Marmorstein, R.1    Roth, S.Y.2
  • 5
    • 70349311616 scopus 로고    scopus 로고
    • Histone acetyltransferases as emerging drug targets
    • F.J. Dekker, and H.J. Haisma Histone acetyltransferases as emerging drug targets Drug Discov. Today 14 2009 942 948
    • (2009) Drug Discov. Today , vol.14 , pp. 942-948
    • Dekker, F.J.1    Haisma, H.J.2
  • 8
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • I. Gregoretti, Y.-M. Lee, and H.V. Goodson Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis J. Mol. Biol. 338 2004 17 31
    • (2004) J. Mol. Biol. , vol.338 , pp. 17-31
    • Gregoretti, I.1    Lee, Y.-M.2    Goodson, H.V.3
  • 9
    • 84970979970 scopus 로고    scopus 로고
    • Mammalian sirtuins emerging roles in physiology, aging and calorie restriction
    • M.C. Haigis, and L.P. Guarente Mammalian sirtuins emerging roles in physiology, aging and calorie restriction Genes Dev. 69 2006 1702 1705
    • (2006) Genes Dev. , vol.69 , pp. 1702-1705
    • Haigis, M.C.1    Guarente, L.P.2
  • 12
    • 65449189558 scopus 로고    scopus 로고
    • Computational studies on histone deacetylases and the design of selective histone deacetylase inhibitors
    • D. Wang Computational studies on histone deacetylases and the design of selective histone deacetylase inhibitors Curr. Top. Med. Chem. 9 2009 241 256
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 241-256
    • Wang, D.1
  • 16
    • 34447340903 scopus 로고    scopus 로고
    • Zinc binding in HDAC inhibitors: A DFT study
    • D.-F. Wang, P. Helquist, and O. Wiest Zinc binding in HDAC inhibitors: a DFT study J. Org. Chem. 72 2007 5446 5449
    • (2007) J. Org. Chem. , vol.72 , pp. 5446-5449
    • Wang, D.-F.1    Helquist, P.2    Wiest, O.3
  • 17
    • 2942545807 scopus 로고    scopus 로고
    • On the function of the 14 Å long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors
    • D.-F. Wang, O. Wiest, P. Helquist, H.Y. Lan-Hargest, and N.L. Wiech On the function of the 14 Å long internal cavity of histone deacetylase-like protein: implications for the design of histone deacetylase inhibitors J. Med. Chem. 47 2004 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
  • 20
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • E. Verdin, F. Dequiedt, and H.G. Kasler Class II histone deacetylases: versatile regulators Trends Genet. 19 2003 286 293
    • (2003) Trends Genet. , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 21
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: From sequence to function, regulation, and clinical implication
    • X.J. Yang, and S. Gregoire Class II histone deacetylases: from sequence to function, regulation, and clinical implication Mol. Cell. Biol. 25 2005 2873 2884
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2873-2884
    • Yang, X.J.1    Gregoire, S.2
  • 24
    • 5444254467 scopus 로고    scopus 로고
    • Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates
    • D. Riester, D. Wegener, C. Hildmann, and A. Schwienhorst Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates Biochem. Biophys. Res. Commun. 324 2004 1116 1123
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1116-1123
    • Riester, D.1    Wegener, D.2    Hildmann, C.3    Schwienhorst, A.4
  • 27
    • 34248344283 scopus 로고    scopus 로고
    • Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains
    • L. Guo, A. Han, D.L. Bates, J. Cao, and L. Chen Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains Proc. Natl. Acad. Sci. U.S.A. 104 2007 4297 4302
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 4297-4302
    • Guo, L.1    Han, A.2    Bates, D.L.3    Cao, J.4    Chen, L.5
  • 28
    • 0037016696 scopus 로고    scopus 로고
    • Isolation and characterisation of mammalian HDAC 10, a novel histone deacetylase
    • H.Y. Kao, C.H. Lee, A. Komarov, C.C. Han, and R.M. Evan Isolation and characterisation of mammalian HDAC 10, a novel histone deacetylase J. Biol. Chem. 277 2002 187 193
    • (2002) J. Biol. Chem. , vol.277 , pp. 187-193
    • Kao, H.Y.1    Lee, C.H.2    Komarov, A.3    Han, C.C.4    Evan, R.M.5
  • 29
    • 9144269738 scopus 로고    scopus 로고
    • A tetradecapeptide-repeat domain controls the leptomycin B-resistant cytoplasmic retention of human histone deacetylase 6
    • N.R. Bertos, B. Gilquin, M. Chan, T.J. Yen, S. Khochbin, and X.J. Yang A tetradecapeptide-repeat domain controls the leptomycin B-resistant cytoplasmic retention of human histone deacetylase 6 J. Biol. Chem. 279 2004 48246 48254
    • (2004) J. Biol. Chem. , vol.279 , pp. 48246-48254
    • Bertos, N.R.1    Gilquin, B.2    Chan, M.3    Yen, T.J.4    Khochbin, S.5    Yang, X.J.6
  • 30
    • 0034885934 scopus 로고    scopus 로고
    • Class II histone deacetylases: Structure, function and regulation
    • N.R. Bertos, A.H. Wang, and X.J. Yang Class II histone deacetylases: structure, function and regulation Biochem. Cell Biol. 79 2001 243 252
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 243-252
    • Bertos, N.R.1    Wang, A.H.2    Yang, X.J.3
  • 31
    • 33646366933 scopus 로고    scopus 로고
    • Two catalytic domains are required for protein deacetylation
    • Y. Zhang, B. Gilquin, S. Khochbin, and P. Matthais Two catalytic domains are required for protein deacetylation J. Biol. Chem. 281 2006 2401 2404
    • (2006) J. Biol. Chem. , vol.281 , pp. 2401-2404
    • Zhang, Y.1    Gilquin, B.2    Khochbin, S.3    Matthais, P.4
  • 32
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC 11, a novel member of human deacetylase family
    • L. Gao, M.A. Cueto, F. Asselberg, and P. Atadja Cloning and functional characterization of HDAC 11, a novel member of human deacetylase family J. Biol. Chem. 277 2002 25748 25755
    • (2002) J. Biol. Chem. , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselberg, F.3    Atadja, P.4
  • 33
    • 65449166411 scopus 로고    scopus 로고
    • Novel structural insights into class i and class II histone deacetylases
    • R. Ficner Novel structural insights into class I and class II histone deacetylases Curr. Top. Med. Chem. 9 2009 235 240
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 235-240
    • Ficner, R.1
  • 35
    • 80053627793 scopus 로고    scopus 로고
    • Expression of histone deacetylase 1 correlates with a poor prognosis in patients with adenocarcinoma of the lung
    • Y. Minamiya, T. Ono, H. Saito, N. Takahashi, M. Ito, M. Mitsui, S. Motoyama, and J. Ogawa Expression of histone deacetylase 1 correlates with a poor prognosis in patients with adenocarcinoma of the lung Lung Cancer 74 2011 300 304
    • (2011) Lung Cancer , vol.74 , pp. 300-304
    • Minamiya, Y.1    Ono, T.2    Saito, H.3    Takahashi, N.4    Ito, M.5    Mitsui, M.6    Motoyama, S.7    Ogawa, J.8
  • 37
    • 41549159879 scopus 로고    scopus 로고
    • Class i histone deacetylase expression has independent prognostic impact in human colorectal cancer: Specific role of class i histone deacetylases in vitro and in vivo
    • W. Weichert, A. Roske, S. Neisporek, A. Noske, A.C. Buckendahl, M. Dietel, V. Gekeler, M. Boehm, T. Beckers, and C. Demkert Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: specific role of class I histone deacetylases in vitro and in vivo Clin. Cancer Res. 14 2008 1669 1677
    • (2008) Clin. Cancer Res. , vol.14 , pp. 1669-1677
    • Weichert, W.1    Roske, A.2    Neisporek, S.3    Noske, A.4    Buckendahl, A.C.5    Dietel, M.6    Gekeler, V.7    Boehm, M.8    Beckers, T.9    Demkert, C.10
  • 38
    • 37049001617 scopus 로고    scopus 로고
    • Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma
    • T. Rikimaru, A. Taketomi, Y. Yamashita, K. Shirabe, T. Hamatsu, M. Shimada, and Y. Maehara Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma Oncology 72 2007 69 74
    • (2007) Oncology , vol.72 , pp. 69-74
    • Rikimaru, T.1    Taketomi, A.2    Yamashita, Y.3    Shirabe, K.4    Hamatsu, T.5    Shimada, M.6    Maehara, Y.7
  • 40
    • 38549157208 scopus 로고    scopus 로고
    • Association of patterns of class i histone deacetylase expression with patient prognosis in gastric cancer: A retrospective analysis
    • W. Weichert, A. Roske, V. Gekeler, T. Beckers, M.P. Ebert, M. Pross, M. Dietel, C. Denkert, and C. Rocken Association of patterns of class I histone deacetylase expression with patient prognosis in gastric cancer: a retrospective analysis Lancet Oncol. 9 2008 139 148
    • (2008) Lancet Oncol. , vol.9 , pp. 139-148
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Ebert, M.P.5    Pross, M.6    Dietel, M.7    Denkert, C.8    Rocken, C.9
  • 41
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • O. Witt, H.E. Deubzer, T. Milde, and I. Oehme HDAC family: what are the cancer relevant targets? Cancer Lett. 277 2009 8 21
    • (2009) Cancer Lett. , vol.277 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 42
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • W.S. Xu, R.B. Parmigiani, and P.A. Marks Histone deacetylase inhibitors: molecular mechanisms of action Oncogene 26 2007 5541 5552
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 43
    • 67449127083 scopus 로고    scopus 로고
    • Cytotoxicity mediated by histone deacetylase inhibitors in cancer cells: Mechanisms and potential clinical implications
    • D.S. Schrumps Cytotoxicity mediated by histone deacetylase inhibitors in cancer cells: mechanisms and potential clinical implications Clin. Cancer Res. 15 2009 3947 3954
    • (2009) Clin. Cancer Res. , vol.15 , pp. 3947-3954
    • Schrumps, D.S.1
  • 46
    • 0034682037 scopus 로고    scopus 로고
    • Cell-cycle inhibitors: Three families united by a common cause
    • A. Vidal, and A. Koff Cell-cycle inhibitors: three families united by a common cause Gene 247 2000 1 15
    • (2000) Gene , vol.247 , pp. 1-15
    • Vidal, A.1    Koff, A.2
  • 48
    • 22144434077 scopus 로고    scopus 로고
    • The effects of histone deacetylase inhibitors on heterochromatin: Implications for anticancer therapy?
    • A. Taddei, D. Roche, W.A. Bickmore, and G. Almouzni The effects of histone deacetylase inhibitors on heterochromatin: implications for anticancer therapy? EMBO Rep. 6 2005 520 524
    • (2005) EMBO Rep. , vol.6 , pp. 520-524
    • Taddei, A.1    Roche, D.2    Bickmore, W.A.3    Almouzni, G.4
  • 49
    • 79955678223 scopus 로고    scopus 로고
    • Developing histone deacetylase inhibitors as anti-cancer therapeutics
    • R. Venugopal, and T.R.J. Evans Developing histone deacetylase inhibitors as anti-cancer therapeutics Curr. Med. Chem. 18 2011 1658 1671
    • (2011) Curr. Med. Chem. , vol.18 , pp. 1658-1671
    • Venugopal, R.1    Evans, T.R.J.2
  • 50
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • A.A. Ruefli, M.J. Ausserlechner, D. Bernhard, V.R. Sutton, K.M. Tainton, R. Kofler, M.J. Symth, and R.W. Johnstone The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species Proc. Natl. Acad. Sci. U.S.A. 98 2001 10833 10838
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3    Sutton, V.R.4    Tainton, K.M.5    Kofler, R.6    Symth, M.J.7    Johnstone, R.W.8
  • 52
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2 and downregulates thioredoxin
    • L.M. Butler, X. Zhou, W.S. Xu, H.I. Scher, R.A. Rifkind, P.A. Marks, and V.M. Richon The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2 and downregulates thioredoxin Proc. Natl. Acad. Sci. U.S.A. 99 2002 11700 11705
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3    Scher, H.I.4    Rifkind, R.A.5    Marks, P.A.6    Richon, V.M.7
  • 53
    • 77957091318 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair
    • J.H. Lee, M.L. Choy, L. Ngo, S.S. Foster, and P.A. Marks Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair Proc. Natl. Acad. Sci. U.S.A. 107 2010 14639 14644
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14639-14644
    • Lee, J.H.1    Choy, M.L.2    Ngo, L.3    Foster, S.S.4    Marks, P.A.5
  • 57
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase Inhibitors and the promise of epigenetic (and more) treatments for cancer
    • S. Minucci, and P.G. Pelicci Histone deacetylase Inhibitors and the promise of epigenetic (and more) treatments for cancer Nat. Rev. Cancer 6 2006 38 51
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 58
    • 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
    • R.R. Rosato, S.C. Maggio, J.A. Almenara, S.G. Payne, P. Atadja, S. Spiegel, P. Dent, and S. Gant 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. 69 2006 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    Gant, S.8
  • 60
    • 31544466465 scopus 로고    scopus 로고
    • Bmf is a possible mediator in histone deacetylase inhibitors FK228 and CBHA-induced apoptosis
    • Y. Zhang, M. Adachi, R. Kawamura, and K. Imai Bmf is a possible mediator in histone deacetylase inhibitors FK228 and CBHA-induced apoptosis Cell Death Differ. 13 2006 129 140
    • (2006) Cell Death Differ. , vol.13 , pp. 129-140
    • Zhang, Y.1    Adachi, M.2    Kawamura, R.3    Imai, K.4
  • 61
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Y. Shao, Z. Gao, P.A. Marks, and X. Jiang Apoptotic and autophagic cell death induced by histone deacetylase inhibitors Proc. Natl. Acad. Sci. U.S.A. 101 2004 18030 18035
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4
  • 62
    • 84904062324 scopus 로고    scopus 로고
    • Combined autophagy and HDAC inhibition: A phase i safety, tolerability, pharmacokinetic, and pharmacodynamic analysis of hydroxychloroquine in combination with the HDAC inhibitor vorinostat in patients with advanced solid tumors
    • D. Mahalingam, M. Mita, J. Sarantopoulos, L. Wood, R.K. Amaravadi, L.E. Davis, A.C. Mita, T.J. Curiel, C.M. Espitia, S.T. Nawrocki, F.J. Giles, and J.S. Carew Combined autophagy and HDAC inhibition: a phase I safety, tolerability, pharmacokinetic, and pharmacodynamic analysis of hydroxychloroquine in combination with the HDAC inhibitor vorinostat in patients with advanced solid tumors Autophagy 10 2014 1403 1414
    • (2014) Autophagy , vol.10 , pp. 1403-1414
    • Mahalingam, D.1    Mita, M.2    Sarantopoulos, J.3    Wood, L.4    Amaravadi, R.K.5    Davis, L.E.6    Mita, A.C.7    Curiel, T.J.8    Espitia, C.M.9    Nawrocki, S.T.10    Giles, F.J.11    Carew, J.S.12
  • 63
    • 24744434639 scopus 로고    scopus 로고
    • Induction of polyploidy by histone deacetylase inhibitor: A pathway for antitumor effects
    • W.S. Xu, G. Perez, L. Ngo, C.Y. Gui, and P.A. Marks Induction of polyploidy by histone deacetylase inhibitor: a pathway for antitumor effects Cancer Res. 65 2005 7832 7839
    • (2005) Cancer Res. , vol.65 , pp. 7832-7839
    • Xu, W.S.1    Perez, G.2    Ngo, L.3    Gui, C.Y.4    Marks, P.A.5
  • 65
    • 33751249589 scopus 로고    scopus 로고
    • Effects of histone deacetylase inhibitors on HIF-1
    • D. Liang, X. Kong, and N. Sang Effects of histone deacetylase inhibitors on HIF-1 Cell Cycle 5 2006 2430 2435
    • (2006) Cell Cycle , vol.5 , pp. 2430-2435
    • Liang, D.1    Kong, X.2    Sang, N.3
  • 66
    • 0036458731 scopus 로고    scopus 로고
    • Histone deacetylases inhibitors potently repress CXCR4 chemokine receptor expression and function in acute lymphoblastic leukemia
    • R. Crazzolara, K. Johrer, R.W. Johnstone, R. Greil, R. Kofler, B. Meister, and D. Bernhard Histone deacetylases inhibitors potently repress CXCR4 chemokine receptor expression and function in acute lymphoblastic leukemia Br. J. Haematol. 119 2002 965 969
    • (2002) Br. J. Haematol. , vol.119 , pp. 965-969
    • Crazzolara, R.1    Johrer, K.2    Johnstone, R.W.3    Greil, R.4    Kofler, R.5    Meister, B.6    Bernhard, D.7
  • 68
    • 0034548836 scopus 로고    scopus 로고
    • Up-regulation of co-stimulatory/adhesion molecules by histone deacetylase inhibitors in acute myeloid leukemia cells
    • T. Maeda, M. Towatari, H. Kosugi, and H. Saito Up-regulation of co-stimulatory/adhesion molecules by histone deacetylase inhibitors in acute myeloid leukemia cells Blood 96 2000 3847 3856
    • (2000) Blood , vol.96 , pp. 3847-3856
    • Maeda, T.1    Towatari, M.2    Kosugi, H.3    Saito, H.4
  • 71
    • 28244502269 scopus 로고    scopus 로고
    • Cancer cells become susceptible to natural cell killing after exposure to histone deacetylase inhibitors due to glycogen synthase kinase-3-dependent expression of MHC class-I-related chain A and B
    • S. Skov, M.T. Pedersen, L. Andresen, P.T. Straten, A. Woetmann, and N. Odum Cancer cells become susceptible to natural cell killing after exposure to histone deacetylase inhibitors due to glycogen synthase kinase-3-dependent expression of MHC class-I-related chain A and B Cancer Res. 65 2005 11136 11145
    • (2005) Cancer Res. , vol.65 , pp. 11136-11145
    • Skov, S.1    Pedersen, M.T.2    Andresen, L.3    Straten, P.T.4    Woetmann, A.5    Odum, N.6
  • 72
    • 1642415712 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect
    • P. Reddy, Y. Maeda, K. Hotary, C. Liu, L.L. Reznikov, C.A. Dinarello, and J.L.M. Ferrara Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect Proc. Natl. Acad. Sci. U.S.A. 101 2004 3921 3926
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3921-3926
    • Reddy, P.1    Maeda, Y.2    Hotary, K.3    Liu, C.4    Reznikov, L.L.5    Dinarello, C.A.6    Ferrara, J.L.M.7
  • 76
    • 84856259087 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity in human endometrial stromal cells promotes extracellular matrix remodelling and limits embryo invasion
    • C. Estella, I. Herrer, S.P. Atkinson, A. Quiñonero, S. Martínez, A. Pellicer, and C. Simon Inhibition of histone deacetylase activity in human endometrial stromal cells promotes extracellular matrix remodelling and limits embryo invasion PLoS ONE 7 2012 e30508
    • (2012) PLoS ONE , vol.7 , pp. e30508
    • Estella, C.1    Herrer, I.2    Atkinson, S.P.3    Quiñonero, A.4    Martínez, S.5    Pellicer, A.6    Simon, C.7
  • 77
    • 84865660690 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor, apicidin, inhibits human ovarian cancer cell migration via class II histone deacetylase 4 silencing
    • M.Y. Ahn, D.O. Kang, Y.J. Na, S. Yoon, W.S. Choi, K.W. Kang, H.Y. Chung, J.H. Jung, D.S. Min, and H.S. Kim Histone deacetylase inhibitor, apicidin, inhibits human ovarian cancer cell migration via class II histone deacetylase 4 silencing Cancer Lett. 325 2012 189 199
    • (2012) Cancer Lett. , vol.325 , pp. 189-199
    • Ahn, M.Y.1    Kang, D.O.2    Na, Y.J.3    Yoon, S.4    Choi, W.S.5    Kang, K.W.6    Chung, H.Y.7    Jung, J.H.8    Min, D.S.9    Kim, H.S.10
  • 79
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Z.L. Yuan, Y.J. Guan, D. Chatterjee, and Y.E. Chin Stat3 dimerization regulated by reversible acetylation of a single lysine residue Science 307 2005 269 273
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 80
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • L. Chen, W. Fische, E. Verdin, and W.C. Greene Duration of nuclear NF-κB action regulated by reversible acetylation Science 293 2001 1653 1657
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fische, W.2    Verdin, E.3    Greene, W.C.4
  • 81
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • P. Bali, M. Pranpat, J. Bradner, M. Balasis, W. Fiskus, F. Guo, K. Rocha, S. Kumaraswamy, S. Boyapalle, P. Atadja, E. Seto, and K. Bhalla Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors J. Biol. Chem. 280 2005 26729 26734
    • (2005) J. Biol. Chem. , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 83
    • 1542289920 scopus 로고    scopus 로고
    • Deacetylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases
    • M.H. Brush, A. Guardiola, J.H. Connor, T.P. Yao, and S. Shenolikar Deacetylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases J. Biol. Chem. 279 2004 7685 7691
    • (2004) J. Biol. Chem. , vol.279 , pp. 7685-7691
    • Brush, M.H.1    Guardiola, A.2    Connor, J.H.3    Yao, T.P.4    Shenolikar, S.5
  • 84
    • 33644663872 scopus 로고    scopus 로고
    • Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes
    • C.S. Chen, S.C. Weng, P.H. Tseng, H.P. Lin, and C.S. Chen Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes J. Biol. Chem. 280 2005 38879 38887
    • (2005) J. Biol. Chem. , vol.280 , pp. 38879-38887
    • Chen, C.S.1    Weng, S.C.2    Tseng, P.H.3    Lin, H.P.4    Chen, C.S.5
  • 85
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Y. Kawaguchi, J.J. Kovacs, A. McLaurin, J.M. Vance, A. Ito, and T.P. Yao The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress Cell 115 2003 727 738
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 86
    • 84929598341 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents
    • M. Mottamal, S. Zheng, T.L. Huang, and G. Wang Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents Molecules 20 2015 3898 3941
    • (2015) Molecules , vol.20 , pp. 3898-3941
    • Mottamal, M.1    Zheng, S.2    Huang, T.L.3    Wang, G.4
  • 87
    • 35748981538 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Latest developments, trends and medicinal chemistry perspective
    • K.V. Balakin, Y.A. Ivanenkov, A.S. Kiselyov, and S.E. Tkachenko Histone deacetylase inhibitors in cancer therapy: latest developments, trends and medicinal chemistry perspective Anti-Cancer Agents Med. Chem. 7 2007 576 592
    • (2007) Anti-Cancer Agents Med. Chem. , vol.7 , pp. 576-592
    • Balakin, K.V.1    Ivanenkov, Y.A.2    Kiselyov, A.S.3    Tkachenko, S.E.4
  • 88
    • 47249100271 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: New compounds and clinical update of benzamide-type agents
    • O. Moradei, A. Vaisburg, and R.E. Martell Histone deacetylase inhibitors in cancer therapy: new compounds and clinical update of benzamide-type agents Curr. Top. Med. Chem. 8 2008 841 858
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 841-858
    • Moradei, O.1    Vaisburg, A.2    Martell, R.E.3
  • 90
    • 84878002317 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: An attractive strategy for cancer therapy
    • J. Li, G. Li, and W. Xu Histone deacetylase inhibitors: an attractive strategy for cancer therapy Curr. Med. Chem. 20 2013 1856 1886
    • (2013) Curr. Med. Chem. , vol.20 , pp. 1856-1886
    • Li, J.1    Li, G.2    Xu, W.3
  • 92
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • V.G. Allfrey, R. Faulkner, and A.E. Mirsky Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis Proc. Natl. Acad. Sci. U.S.A. 51 1964 786 794
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 93
    • 0013900616 scopus 로고
    • RNA synthesis and histone acetylation during the course of gene activation in lymphocytes
    • B.G. Pogo, V.G. Allfrey, and A.E. Mirsky RNA synthesis and histone acetylation during the course of gene activation in lymphocytes Proc. Natl. Acad. Sci. U.S.A. 55 1966 805 812
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.55 , pp. 805-812
    • Pogo, B.G.1    Allfrey, V.G.2    Mirsky, A.E.3
  • 94
    • 0017767153 scopus 로고
    • N-butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
    • M.G. Riggs, R.G. Whittaker, J.R. Neumann, and V.M. Ingram N-butyrate causes histone modification in HeLa and Friend erythroleukaemia cells Nature 268 1977 462 464
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 95
    • 0015841745 scopus 로고
    • Growth inhibition and morphological changes caused by lipophilic acids in mammalian cells
    • G. Ginsburg, D. Salomon, T. Sreevalsan, and E. Freese Growth inhibition and morphological changes caused by lipophilic acids in mammalian cells Proc. Natl. Acad. Sci. U.S.A. 70 1973 2457 2461
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 2457-2461
    • Ginsburg, G.1    Salomon, D.2    Sreevalsan, T.3    Freese, E.4
  • 96
    • 0016734084 scopus 로고
    • Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells
    • A. Leder, and P. Leder Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells Cell 5 1975 319 322
    • (1975) Cell , vol.5 , pp. 319-322
    • Leder, A.1    Leder, P.2
  • 98
    • 0017291238 scopus 로고
    • Effect of sodium butyrate on mammalian cells in culture: A review
    • K.N. Prasad, and K. Sinha Effect of sodium butyrate on mammalian cells in culture: a review Vitro 12 1976 125 132
    • (1976) Vitro , vol.12 , pp. 125-132
    • Prasad, K.N.1    Sinha, K.2
  • 99
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: Past, present and future
    • C.B. Yoo, and P.A. Jones Epigenetic therapy of cancer: past, present and future Nat. Rev. Drug Discov. 5 2006 37 50
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 101
    • 34248644319 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors - Turning epigenic mechanisms of gene regulation into tools of therapeutic intervention in malignant and other diseases
    • D. Riester, C. Hildmann, and A. Schwienhorst Histone deacetylase inhibitors - turning epigenic mechanisms of gene regulation into tools of therapeutic intervention in malignant and other diseases Appl. Microbiol. Biotechnol. 75 2007 499 514
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 499-514
    • Riester, D.1    Hildmann, C.2    Schwienhorst, A.3
  • 103
    • 0028260120 scopus 로고
    • Butyrate as a differentiating agent: Pharmacokinetics, analogues and current status
    • H.L. Newmark, J.R. Lupton, and C.W. Young Butyrate as a differentiating agent: pharmacokinetics, analogues and current status Cancer Lett. 78 1994 1 5
    • (1994) Cancer Lett. , vol.78 , pp. 1-5
    • Newmark, H.L.1    Lupton, J.R.2    Young, C.W.3
  • 104
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • R.P. Warrell Jr., L.Z. He, V. Richon, E. Calleja, and P.P. Pandolfi Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase J. Natl. Cancer Inst. 90 1998 1621 1625
    • (1998) J. Natl. Cancer Inst. , vol.90 , pp. 1621-1625
    • Warrell, R.P.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 106
    • 33645233142 scopus 로고    scopus 로고
    • Structure-activity relationship between carboxylic acids and T cell cycle blockade
    • K.M. Gilbert, A. De Loose, J.L. Valentine, and E.K. Fifer Structure-activity relationship between carboxylic acids and T cell cycle blockade Life Sci. 78 2006 2159 2165
    • (2006) Life Sci. , vol.78 , pp. 2159-2165
    • Gilbert, K.M.1    De Loose, A.2    Valentine, J.L.3    Fifer, E.K.4
  • 108
    • 53949087611 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: The anticancer, antimetastatic and antiangiogenic activities of AN-7 are superior to those of the clinically tested AN-9 (Pivanex)
    • N. Tarasenko, A. Nudelman, I. Tarasenko, M. Entin-Meer, D. Hass-Kogan, A. Inbal, and A. Rephaeli Histone deacetylase inhibitors: the anticancer, antimetastatic and antiangiogenic activities of AN-7 are superior to those of the clinically tested AN-9 (Pivanex) Clin. Exp. Metastasis 25 2008 703 716
    • (2008) Clin. Exp. Metastasis , vol.25 , pp. 703-716
    • Tarasenko, N.1    Nudelman, A.2    Tarasenko, I.3    Entin-Meer, M.4    Hass-Kogan, D.5    Inbal, A.6    Rephaeli, A.7
  • 109
    • 0033819869 scopus 로고    scopus 로고
    • Prodrugs of butyric acid from bench to bedside: Synthetic design, mechanisms of action, and clinical applications
    • A. Rephaeli, R. Zhuk, and A. Nudelman Prodrugs of butyric acid from bench to bedside: synthetic design, mechanisms of action, and clinical applications Drug Dev. Res. 50 2000 379 391
    • (2000) Drug Dev. Res. , vol.50 , pp. 379-391
    • Rephaeli, A.1    Zhuk, R.2    Nudelman, A.3
  • 111
    • 56149090684 scopus 로고    scopus 로고
    • Epi-drugs to fight cancer: From chemistry to cancer treatment, the road ahead
    • A. Mai, and L. Altucci Epi-drugs to fight cancer: from chemistry to cancer treatment, the road ahead Int. J. Biochem. Cell Biol. 41 2009 199 213
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 199-213
    • Mai, A.1    Altucci, L.2
  • 112
    • 33645969256 scopus 로고    scopus 로고
    • SLC5A8 (SMCT1)-mediated transport of butyrate forms the basis for the tumor suppressive function of the transporter
    • N. Gupta, P.M. Martin, P.D. Prasad, and V. Ganapathy SLC5A8 (SMCT1)-mediated transport of butyrate forms the basis for the tumor suppressive function of the transporter Life Sci. 78 2006 2419 2425
    • (2006) Life Sci. , vol.78 , pp. 2419-2425
    • Gupta, N.1    Martin, P.M.2    Prasad, P.D.3    Ganapathy, V.4
  • 113
    • 57749111596 scopus 로고    scopus 로고
    • Nutrient transporters in cancer: Relevance to Warburg hypothesis and beyond
    • V. Ganapathy, M. Thangaraju, and P.D. Prasad Nutrient transporters in cancer: relevance to Warburg hypothesis and beyond Pharmacol. Therapeut. 121 2009 29 40
    • (2009) Pharmacol. Therapeut. , vol.121 , pp. 29-40
    • Ganapathy, V.1    Thangaraju, M.2    Prasad, P.D.3
  • 115
    • 58149097138 scopus 로고    scopus 로고
    • Targeting proinvasive oncogenes with short chain fatty acid-hexosamine analogues inhibits the mobility of metastatic MDA-MB-231 breast cancer cells
    • C.T. Campbell, U. Aich, C.A. Weier, J.J. Wang, S.S. Choi, M.M. Wen, K. Maisel, S.G. Sampathkumar, and M.J. Yarema Targeting proinvasive oncogenes with short chain fatty acid-hexosamine analogues inhibits the mobility of metastatic MDA-MB-231 breast cancer cells J. Med. Chem. 51 2008 8135 8147
    • (2008) J. Med. Chem. , vol.51 , pp. 8135-8147
    • Campbell, C.T.1    Aich, U.2    Weier, C.A.3    Wang, J.J.4    Choi, S.S.5    Wen, M.M.6    Maisel, K.7    Sampathkumar, S.G.8    Yarema, M.J.9
  • 117
    • 36148956147 scopus 로고    scopus 로고
    • Transport of butyryl-l-carnitine, a potential prodrug, via the carnitine transporter OCTN2 and the amino acid transporter ATB(0,+)
    • S.R. Srinivas, P.D. Prasad, N.S. Umapathy, V. Ganapathy, and P.S. Shekhawat Transport of butyryl-l-carnitine, a potential prodrug, via the carnitine transporter OCTN2 and the amino acid transporter ATB(0,+) Am. J. Physiol. Gastrointest. Liver Physiol. 293 2007 G1046 G1053
    • (2007) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.293 , pp. G1046-G1053
    • Srinivas, S.R.1    Prasad, P.D.2    Umapathy, N.S.3    Ganapathy, V.4    Shekhawat, P.S.5
  • 118
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-cell lymphoma
    • B.S. Mann, J.R. Johnson, M.H. Cohen, R. Justice, and R. Pazdur FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma Oncologist 12 2007 1247 1252
    • (2007) Oncologist , vol.12 , pp. 1247-1252
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 119
    • 84970964617 scopus 로고    scopus 로고
    • FDA Approves Beleodaq to Treat Rare (accessed 12.10.15)
    • FDA Approves Beleodaq to Treat Rare, Aggressive Form of Non-Hodgkin Lymphoma. < http://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/ucm403929.html > (accessed 12.10.15).
    • Aggressive Form of Non-Hodgkin Lymphoma
  • 120
    • 85006193518 scopus 로고    scopus 로고
    • Panobinostat or the treatment of multiple myeloma: The evidence to date
    • H. Bailey, D.D. Stenehjem, and S. Sharma Panobinostat or the treatment of multiple myeloma: the evidence to date J. Blood Med. 6 2015 269 276
    • (2015) J. Blood Med. , vol.6 , pp. 269-276
    • Bailey, H.1    Stenehjem, D.D.2    Sharma, S.3
  • 121
    • 71449109387 scopus 로고    scopus 로고
    • New patented histone deacetylase inhibitors
    • H. Wang, and B.W. Dymock New patented histone deacetylase inhibitors Expert Opin. Ther. Patents 19 2009 1727 1757
    • (2009) Expert Opin. Ther. Patents , vol.19 , pp. 1727-1757
    • Wang, H.1    Dymock, B.W.2
  • 122
    • 77955480670 scopus 로고    scopus 로고
    • Strategies in developing promising histone deacetylase inhibitors
    • L. Zhang, H. Fang, and W. Xu Strategies in developing promising histone deacetylase inhibitors Med. Res. Rev. 30 2010 585 602
    • (2010) Med. Res. Rev. , vol.30 , pp. 585-602
    • Zhang, L.1    Fang, H.2    Xu, W.3
  • 123
  • 126
  • 127
    • 77955355838 scopus 로고    scopus 로고
    • Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A
    • K.V. Butler, J. Kalin, C. Brochier, G. Vistoli, B. Langley, and A.P. Kozikowski Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A J. Am. Chem. Soc. 132 2010 10842 10846
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10842-10846
    • Butler, K.V.1    Kalin, J.2    Brochier, C.3    Vistoli, G.4    Langley, B.5    Kozikowski, A.P.6
  • 130
    • 1942534547 scopus 로고    scopus 로고
    • Stereodefined and polyunsaturated inhibitors of histone deacetylase based on (2E,4E)-5-arylpenta-2.; 4-dienoic acid hydroxyamides
    • C.M. Marson, N. Serradji, A.S. Rioja, S.P. Gaustaud, J.P. Alao, R.C. Coombes, and D.M. Vigushin Stereodefined and polyunsaturated inhibitors of histone deacetylase based on (2E,4E)-5-arylpenta-2.; 4-dienoic acid hydroxyamides Bioorg. Med. Chem. Lett. 14 2004 2477 2481
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 2477-2481
    • Marson, C.M.1    Serradji, N.2    Rioja, A.S.3    Gaustaud, S.P.4    Alao, J.P.5    Coombes, R.C.6    Vigushin, D.M.7
  • 132
    • 0037140821 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors: N-hydroxycarboxamides possessing a terminal bicyclic aryl group
    • S. Uesato, M. Kitagawa, Y. Nagaoka, T. Maeda, H. Kuwajima, and T. Yamori Novel histone deacetylase inhibitors: N-hydroxycarboxamides possessing a terminal bicyclic aryl group Bioorg. Med. Chem. Lett. 12 2002 1347 1349
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1347-1349
    • Uesato, S.1    Kitagawa, M.2    Nagaoka, Y.3    Maeda, T.4    Kuwajima, H.5    Yamori, T.6
  • 136
    • 0345358526 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors: Design, synthesis, enzyme inhibition, and binding mode study of SAHA-based non-hydroxamates
    • T. Suzuki, Y. Nagano, A. Matsuura, A. Kohara, S. Ninomiya, K. Kohda, and N. Miyata Novel histone deacetylase inhibitors: design, synthesis, enzyme inhibition, and binding mode study of SAHA-based non-hydroxamates Bioorg. Med. Chem. Lett. 13 2003 4321 4326
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 4321-4326
    • Suzuki, T.1    Nagano, Y.2    Matsuura, A.3    Kohara, A.4    Ninomiya, S.5    Kohda, K.6    Miyata, N.7
  • 137
    • 20344391371 scopus 로고    scopus 로고
    • Design and synthesis of non-hydroxamate histone deacetylase inhibitors: Identification of a selective histone acetylating agent
    • T. Suzuki, A. Matsuura, A. Kouketsu, S. Hisakawa, H. Nakagawa, and N. Miyata Design and synthesis of non-hydroxamate histone deacetylase inhibitors: identification of a selective histone acetylating agent Bioorg. Med. Chem. Lett. 13 2005 4332 4342
    • (2005) Bioorg. Med. Chem. Lett. , vol.13 , pp. 4332-4342
    • Suzuki, T.1    Matsuura, A.2    Kouketsu, A.3    Hisakawa, S.4    Nakagawa, H.5    Miyata, N.6
  • 139
    • 33749430243 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of -cyclic amide/imide-bearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors
    • C. Shinji, S. Maeda, K. Imai, M. Yoshida, Y. Hashimoto, and H. Miyachi Design, synthesis and evaluation of -cyclic amide/imide-bearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors Bioorg. Med. Chem. Lett. 14 2006 7625 7651
    • (2006) Bioorg. Med. Chem. Lett. , vol.14 , pp. 7625-7651
    • Shinji, C.1    Maeda, S.2    Imai, K.3    Yoshida, M.4    Hashimoto, Y.5    Miyachi, H.6
  • 141
    • 25144444434 scopus 로고    scopus 로고
    • Exploring the connection unit in the HDAC inhibitor pharmacophore model: Novel uracil-HDAC inhibitors based hydroxamates
    • A. Mai, S. Massa, D. Rotili, R. Pezzi, P. Bottoni, R. Scatena, J. Meraner, and G. Brosch Exploring the connection unit in the HDAC inhibitor pharmacophore model: novel uracil-HDAC inhibitors based hydroxamates Bioorg. Med. Chem. Lett. 15 2005 4656 4661
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 4656-4661
    • Mai, A.1    Massa, S.2    Rotili, D.3    Pezzi, R.4    Bottoni, P.5    Scatena, R.6    Meraner, J.7    Brosch, G.8
  • 147
    • 35148834194 scopus 로고    scopus 로고
    • Antiproliferative activities of a library of hybrids between indanones and HDAC inhibitor SAHA and MS-275 analogues
    • C. Charrier, J. Roche, J.-P. Gesson, and P. Bertrand Antiproliferative activities of a library of hybrids between indanones and HDAC inhibitor SAHA and MS-275 analogues Bioorg. Med. Chem. Lett. 17 2007 6142 6146
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 6142-6146
    • Charrier, C.1    Roche, J.2    Gesson, J.-P.3    Bertrand, P.4
  • 148
    • 65649113311 scopus 로고    scopus 로고
    • Synthesis and modeling of new benzofuranone histone deacetylase inhibitors that stimulate tumor suppressor gene expression
    • C. Charrier, J. Clarhaut, J.-P. Gesson, G. Estiu, O. Wiest, J. Roche, and P. Bertrand Synthesis and modeling of new benzofuranone histone deacetylase inhibitors that stimulate tumor suppressor gene expression J. Med. Chem. 52 2009 3112 3115
    • (2009) J. Med. Chem. , vol.52 , pp. 3112-3115
    • Charrier, C.1    Clarhaut, J.2    Gesson, J.-P.3    Estiu, G.4    Wiest, O.5    Roche, J.6    Bertrand, P.7
  • 149
    • 43049104161 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap
    • P.C. Chen, V. Patil, W. Guerrant, P. Green, and A.K. Oyelere Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap Bioorg. Med. Chem. Lett. 16 2008 4839 4853
    • (2008) Bioorg. Med. Chem. Lett. , vol.16 , pp. 4839-4853
    • Chen, P.C.1    Patil, V.2    Guerrant, W.3    Green, P.4    Oyelere, A.K.5
  • 150
    • 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, D.D. Billadeau, and A.P. Kozikowski Synthesis and biological evaluation of triazol-4-ylphenyl-bearing histone deacetylase inhibitors as anticancer agents J. Med. Chem. 53 2010 1347 1356
    • (2010) J. Med. Chem. , vol.53 , pp. 1347-1356
    • He, R.1    Chen, Y.2    Chen, Y.3    Ougolkov, A.V.4    Zhang, J.S.5    Savoy, D.N.6    Billadeau, D.D.7    Kozikowski, A.P.8
  • 155
    • 65149094611 scopus 로고    scopus 로고
    • Isoxazole moiety in the linker region of HDAC inhibitors adjacent to the Zn-chelating group: Effects on HDAC biology and antiproliferative activity
    • S. Tapadar, R. He, D.N. Luchini, D.D. Billadeau, and A.P. Kozikowski Isoxazole moiety in the linker region of HDAC inhibitors adjacent to the Zn-chelating group: effects on HDAC biology and antiproliferative activity Bioorg. Med. Chem. Lett. 19 2009 3023 3026
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 3023-3026
    • Tapadar, S.1    He, R.2    Luchini, D.N.3    Billadeau, D.D.4    Kozikowski, A.P.5
  • 157
    • 70349761276 scopus 로고    scopus 로고
    • Design, synthesis and preliminary biological evaluation of N-hydroxy-4-(3-phenylpropanamido)benzamide (HPPB) derivatives as novel histone deacetylase inhibitors
    • J. Jiao, H. Fang, X. Wang, P. Guan, Y. Yuan, and W. Xu Design, synthesis and preliminary biological evaluation of N-hydroxy-4-(3-phenylpropanamido)benzamide (HPPB) derivatives as novel histone deacetylase inhibitors Eur. J. Med. Chem. 44 2009 4470 4476
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 4470-4476
    • Jiao, J.1    Fang, H.2    Wang, X.3    Guan, P.4    Yuan, Y.5    Xu, W.6
  • 165
    • 84861571256 scopus 로고    scopus 로고
    • Structure and property based design, synthesis and biological evaluation of γ-lactam based HDAC inhibitors: Part II
    • C. Lee, E. Choi, M. Cho, B. Lee, J.S. Oh, J.S. Kang, S.K. Park, K. Lee, H.M. Kim, and G. Han Structure and property based design, synthesis and biological evaluation of γ-lactam based HDAC inhibitors: part II Bioorg. Med. Chem. Lett. 22 2012 4189 4192
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 4189-4192
    • Lee, C.1    Choi, E.2    Cho, M.3    Lee, B.4    Oh, J.S.5    Kang, J.S.6    Park, S.K.7    Lee, K.8    Kim, H.M.9    Han, G.10
  • 168
    • 80052555163 scopus 로고    scopus 로고
    • 2,5-Disubstituted-1,3,4-oxadiazoles/thiadiazole as surface recognition moiety: Design and synthesis of novel hydroxamic acid based histone deacetylase inhibitors
    • H. Rajak, A. Agarawal, P. Parmar, B.S. Thakur, R. Veerasamy, P.C. Sharma, and M.D. Kharya 2,5-Disubstituted-1,3,4-oxadiazoles/thiadiazole as surface recognition moiety: design and synthesis of novel hydroxamic acid based histone deacetylase inhibitors Bioorg. Med. Chem. Lett. 21 2011 5735 5738
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 5735-5738
    • Rajak, H.1    Agarawal, A.2    Parmar, P.3    Thakur, B.S.4    Veerasamy, R.5    Sharma, P.C.6    Kharya, M.D.7
  • 169
    • 84908428873 scopus 로고    scopus 로고
    • Improved antiproliferative activity of 1,3,4-thiadiazole-containing histone deacetylase (HDAC) inhibitors by introduction of the heteroaromatic surface recognition motif
    • P. Guan, L. Wang, X. Hou, Y. Wan, W. Xu, W. Tang, and H. Fang Improved antiproliferative activity of 1,3,4-thiadiazole-containing histone deacetylase (HDAC) inhibitors by introduction of the heteroaromatic surface recognition motif Bioorg. Med. Chem. 22 2014 5766 5775
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 5766-5775
    • Guan, P.1    Wang, L.2    Hou, X.3    Wan, Y.4    Xu, W.5    Tang, W.6    Fang, H.7
  • 170
    • 84937403780 scopus 로고    scopus 로고
    • Discovery, bioactivity and docking simulation of Vorinostat analogues containing 1,2,4-oxadiazole moiety as potent histone deacetylase inhibitors and antitumor agents
    • J. Cai, H. Wei, K.H. Hong, X. Wu, X. Zong, M. Cao, P. Wang, L. Li, C. Sun, B. Chen, G. Zhou, J. Chen, and M. Ji Discovery, bioactivity and docking simulation of Vorinostat analogues containing 1,2,4-oxadiazole moiety as potent histone deacetylase inhibitors and antitumor agents Bioorg. Med. Chem. 23 2015 3457 3471
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 3457-3471
    • Cai, J.1    Wei, H.2    Hong, K.H.3    Wu, X.4    Zong, X.5    Cao, M.6    Wang, P.7    Li, L.8    Sun, C.9    Chen, B.10    Zhou, G.11    Chen, J.12    Ji, M.13
  • 171
    • 84907859411 scopus 로고    scopus 로고
    • Design, synthesis and 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, Y. Yang, Z. Tu, and S. Jiang Design, synthesis and biological evaluation of 1,3-disubstituted-pyrazole derivatives as new class I and IIb histone deacetylase inhibitors Eur. J. Med. Chem. 86 2014 639 652
    • (2014) Eur. J. Med. Chem. , vol.86 , pp. 639-652
    • Yao, Y.1    Liao, C.2    Li, Z.3    Wang, Z.4    Sun, Q.5    Liu, C.6    Yang, Y.7    Tu, Z.8    Jiang, S.9
  • 175
    • 78650513499 scopus 로고    scopus 로고
    • Design and synthesis of aryl ether and sulfone hydroxamic acids as potent histone deacetylase (HDAC) inhibitors
    • C. Pabba, B.T. Gregg, D.B. Kitchen, Z.J. Chen, and A. Judkins Design and synthesis of aryl ether and sulfone hydroxamic acids as potent histone deacetylase (HDAC) inhibitors Bioorg. Med. Chem. Lett. 21 2011 324 328
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 324-328
    • Pabba, C.1    Gregg, B.T.2    Kitchen, D.B.3    Chen, Z.J.4    Judkins, A.5
  • 176
    • 84872106590 scopus 로고    scopus 로고
    • Synthesis and antitumor activity of novel diaryl ether hydroxamic acids derivatives as potential HDAC inhibitors
    • Y. Zhu, X. Chen, Z. Wu, Y. Zheng, Y. Chen, W. Tang, and T. Lu Synthesis and antitumor activity of novel diaryl ether hydroxamic acids derivatives as potential HDAC inhibitors Arch. Pharm. Res. 35 2012 1723 1732
    • (2012) Arch. Pharm. Res. , vol.35 , pp. 1723-1732
    • Zhu, Y.1    Chen, X.2    Wu, Z.3    Zheng, Y.4    Chen, Y.5    Tang, W.6    Lu, T.7
  • 177
    • 84927914516 scopus 로고    scopus 로고
    • Novel hybrids from N-hydroxyarylamide and indole ring through click chemistry as histone deacetylase inhibitors with potent antitumor activities
    • M. Cai, J. Hu, J.L. Tian, H. Yan, C.G. Zheng, and W.L. Hu Novel hybrids from N-hydroxyarylamide and indole ring through click chemistry as histone deacetylase inhibitors with potent antitumor activities Chin. Chem. Lett. 26 2015 675 680
    • (2015) Chin. Chem. Lett. , vol.26 , pp. 675-680
    • Cai, M.1    Hu, J.2    Tian, J.L.3    Yan, H.4    Zheng, C.G.5    Hu, W.L.6
  • 178
    • 84908668147 scopus 로고    scopus 로고
    • Development of 3-hydroxycinnamide-based HDAC inhibitors with potent in vitro and in vivo anti-tumor activity
    • X. Li, J. Hou, X. Li, Y. Jiang, X. Liu, W. Mu, Y. Jin, Y. Zhang, and W. Xu Development of 3-hydroxycinnamide-based HDAC inhibitors with potent in vitro and in vivo anti-tumor activity Eur. J. Med. Chem. 89 2015 628 637
    • (2015) Eur. J. Med. Chem. , vol.89 , pp. 628-637
    • Li, X.1    Hou, J.2    Li, X.3    Jiang, Y.4    Liu, X.5    Mu, W.6    Jin, Y.7    Zhang, Y.8    Xu, W.9
  • 179
    • 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, H. Sun, and Q. You Novel N-hydroxyfurylacrylamide-based histone deacetylase (HDAC) inhibitors with branched CAP group (Part 2) Bioorg. Med. Chem. 21 2013 5339 5354
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 5339-5354
    • Feng, T.1    Wang, H.2    Su, H.3    Lu, H.4    Yu, L.5    Zhang, X.6    Sun, H.7    You, Q.8
  • 180
    • 84945975040 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of saccharin based N-hydroxybenzamides as histone deacetylase (HDAC) inhibitors
    • H. Fu, L. Han, X. Hou, Y. Dun, L. Wang, X. Gong, and H. Fang Design, synthesis and biological evaluation of saccharin based N-hydroxybenzamides as histone deacetylase (HDAC) inhibitors Bioorg. Med. Chem. 23 2015 5774 5781
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 5774-5781
    • Fu, H.1    Han, L.2    Hou, X.3    Dun, Y.4    Wang, L.5    Gong, X.6    Fang, H.7
  • 181
    • 84899459604 scopus 로고    scopus 로고
    • Search for novel histone deacetylase inhibitors. Part II: Design and synthesis of novel isoferulic acid derivatives
    • W. Lu, F. Wang, T. Zhang, J. Dong, H. Gao, P. Su, Y. Shi, and J. Zhang Search for novel histone deacetylase inhibitors. Part II: design and synthesis of novel isoferulic acid derivatives Bioorg. Med. Chem. 22 2014 2707 2713
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 2707-2713
    • Lu, W.1    Wang, F.2    Zhang, T.3    Dong, J.4    Gao, H.5    Su, P.6    Shi, Y.7    Zhang, J.8
  • 187
    • 84939879982 scopus 로고    scopus 로고
    • 1,3,5-Triazine inhibitors of histone deacetylases: Synthesis and biological activity
    • X. Zhao, Q. Tan, Z. Zhang, and Y. Zhao 1,3,5-Triazine inhibitors of histone deacetylases: synthesis and biological activity Med. Chem. Res. 23 2014 5188 5196
    • (2014) Med. Chem. Res. , vol.23 , pp. 5188-5196
    • Zhao, X.1    Tan, Q.2    Zhang, Z.3    Zhao, Y.4
  • 188
    • 84937521120 scopus 로고    scopus 로고
    • Design, synthesis and preliminary biological evaluation of indoline-2,3-dione derivatives as HDAC inhibitors
    • K. Jin, S. Li, X. Li, J. Zhang, W. Xu, and X. Li Design, synthesis and preliminary biological evaluation of indoline-2,3-dione derivatives as HDAC inhibitors Bioorg. Med. Chem. 23 2015 4728 4736
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 4728-4736
    • Jin, K.1    Li, S.2    Li, X.3    Zhang, J.4    Xu, W.5    Li, X.6
  • 189
    • 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, and L. Zhu Synthesis and anticancer activities of thieno[3,2-d]pyrimidines as novel HDAC inhibitors Bioorg. Med. Chem. 22 2014 358 365
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 358-365
    • Tan, Q.1    Zhang, Z.2    Hui, J.3    Zhao, Y.4    Zhu, L.5
  • 190
    • 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, Y. Zang, J. Li, and H. Liu 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 6155
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 6146-6155
    • Yang, W.1    Li, L.2    Ji, X.3    Wu, X.4    Su, M.5    Sheng, L.6    Zang, Y.7    Li, J.8    Liu, H.9
  • 191
    • 84937817680 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of novel histone deacetylases inhibitors with nitric oxide releasing activity
    • W. Duan, J. Hou, X. Chu, X. Li, J. Zhang, J. Li, W. Xu, and Y. Zhang Synthesis and biological evaluation of novel histone deacetylases inhibitors with nitric oxide releasing activity Bioorg. Med. Chem. 23 2015 4481 4488
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 4481-4488
    • Duan, W.1    Hou, J.2    Chu, X.3    Li, X.4    Zhang, J.5    Li, J.6    Xu, W.7    Zhang, Y.8
  • 192
    • 84937973886 scopus 로고    scopus 로고
    • Design, synthesis and preliminary bioactivity evaluations of substituted quinoline hydroxamic acid derivatives as novel histone deacetylase (HDAC) inhibitors
    • L. Wang, X. Hou, H. Fu, X. Pan, W. Xu, W. Tang, and H. Fang Design, synthesis and preliminary bioactivity evaluations of substituted quinoline hydroxamic acid derivatives as novel histone deacetylase (HDAC) inhibitors Bioorg. Med. Chem. 23 2015 4364 4374
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 4364-4374
    • Wang, L.1    Hou, X.2    Fu, H.3    Pan, X.4    Xu, W.5    Tang, W.6    Fang, H.7
  • 193
    • 84946496563 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of isoquinoline-based derivatives as novel histone deacetylase inhibitors
    • W. Yang, L. Li, Y. Wang, X. Wu, T. Li, N. Yang, M. Su, L. Sheng, M. Zheng, Y. Zang, J. Li, and H. Liu Design, synthesis and biological evaluation of isoquinoline-based derivatives as novel histone deacetylase inhibitors Bioorg. Med. Chem. 23 2015 5881 5890
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 5881-5890
    • Yang, W.1    Li, L.2    Wang, Y.3    Wu, X.4    Li, T.5    Yang, N.6    Su, M.7    Sheng, L.8    Zheng, M.9    Zang, Y.10    Li, J.11    Liu, H.12
  • 197
    • 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, and T. Kurz 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 427 436
    • (2013) J. Med. Chem. , vol.56 , pp. 427-436
    • Marek, L.1    Hamacher, A.2    Hansen, F.K.3    Kuna, K.4    Gohlke, H.5    Kassack, M.U.6    Kurz, T.7
  • 198
    • 84902549707 scopus 로고    scopus 로고
    • Design and synthesis of novel and highly-active pan-histone deacetylase (pan-HDAC) inhibitors
    • T. Tashima, H. Murata, and H. Kodama Design and synthesis of novel and highly-active pan-histone deacetylase (pan-HDAC) inhibitors Bioorg. Med. Chem. 22 2014 3720 3731
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 3720-3731
    • Tashima, T.1    Murata, H.2    Kodama, H.3
  • 199
    • 84907227111 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of b-boswellic acid based HDAC inhibitors as inducers of cancer cell death
    • S. Sharma, M. Ahmad, J.A. Bhat, A. Kumar, M. Kumar, M.A. Zargar, A. Hamid, and B.A. Shah Design, synthesis and biological evaluation of b-boswellic acid based HDAC inhibitors as inducers of cancer cell death Bioorg. Med. Chem. Lett. 24 2014 4729 4734
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 4729-4734
    • Sharma, S.1    Ahmad, M.2    Bhat, J.A.3    Kumar, A.4    Kumar, M.5    Zargar, M.A.6    Hamid, A.7    Shah, B.A.8
  • 200
    • 84945931288 scopus 로고    scopus 로고
    • Hybrids from 4-anilinoquinazoline and hydroxamic acid as dual inhibitors of vascular endothelial growth factor receptor-2 and histone deacetylase
    • F.W. Peng, T.T. Wu, Z.W. Ren, J.Y. Xue, and L. Shi Hybrids from 4-anilinoquinazoline and hydroxamic acid as dual inhibitors of vascular endothelial growth factor receptor-2 and histone deacetylase Bioorg. Med. Chem. Lett. 25 2015 5137 5141
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 5137-5141
    • Peng, F.W.1    Wu, T.T.2    Ren, Z.W.3    Xue, J.Y.4    Shi, L.5
  • 201
    • 84908277134 scopus 로고    scopus 로고
    • 1-Arylsulfonyl-5-(N-hydroxyacrylamide)tetrahydroquinolines as potent histone deacetylase inhibitors suppressing the growth of prostate cancer cells
    • Y.M. Liu, H.Y. Lee, C.H. Chen, C.H. Lee, L.T. Wang, S.L. Pan, M.J. Lai, T.K. Yeh, and J.P. Liou 1-Arylsulfonyl-5-(N-hydroxyacrylamide)tetrahydroquinolines as potent histone deacetylase inhibitors suppressing the growth of prostate cancer cells Eur. J. Med. Chem. 89 2015 320 330
    • (2015) Eur. J. Med. Chem. , vol.89 , pp. 320-330
    • Liu, Y.M.1    Lee, H.Y.2    Chen, C.H.3    Lee, C.H.4    Wang, L.T.5    Pan, S.L.6    Lai, M.J.7    Yeh, T.K.8    Liou, J.P.9
  • 203
    • 84949623954 scopus 로고    scopus 로고
    • Cross metathesis with hydroxamate and benzamide BOC-protected alkenes to access HDAC inhibitors and their biological evaluation highlighted intrinsic activity of BOC-protected dihydroxamates
    • V. Zwick, A. Nurisso, C. Simoes-Pires, S. Bouchet, N. Martinet, A. Lehotzky, J. Ovadi, M. Cuendet, C. Blanquart, and P. Bertrand Cross metathesis with hydroxamate and benzamide BOC-protected alkenes to access HDAC inhibitors and their biological evaluation highlighted intrinsic activity of BOC-protected dihydroxamates Bioorg. Med. Chem. Lett. 26 2016 154 159
    • (2016) Bioorg. Med. Chem. Lett. , vol.26 , pp. 154-159
    • Zwick, V.1    Nurisso, A.2    Simoes-Pires, C.3    Bouchet, S.4    Martinet, N.5    Lehotzky, A.6    Ovadi, J.7    Cuendet, M.8    Blanquart, C.9    Bertrand, P.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.