메뉴 건너뛰기




Volumn 2, Issue 2, 2010, Pages 307-324

Small-molecule chromatin-modifying agents: Therapeutic applications

Author keywords

cancer; chromatin remodeling; epigenetics; histone deacetylase; infectious disease; neurodegenerative disease; sirtuin

Indexed keywords

17 DEMETHOXY 17 (2 DIMETHYLAMINOETHYLAMINO)GELDANAMYCIN; 4 PHENYLBUTYRIC ACID; ANILIDE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIMALARIAL AGENT; APICIDIN; BELINOSTAT; FLUOROURACIL; GIVINOSTAT; HEAT SHOCK PROTEIN 90 INHIBITOR; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; IMATINIB; MC 1568; MC 1575; MC 1714; MC 1716; MC 2113; MC 2211; MGCD 290; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; PANOBINOSTAT; PIVALOYLOXYMETHYL BUTYRATE; PYRROLE DERIVATIVE; PYRROLYL HYDROXAMATE; RETINOIC ACID; RETINOID DERIVATIVE; ROMIDEPSIN; SB 939; SIRTUIN; TAMOXIFEN; TRICHOSTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID; VORINOSTAT; WR 301801; WR 308292; WR 308298;

EID: 77954139965     PISSN: 17501911     EISSN: 1750192X     Source Type: Journal    
DOI: 10.2217/epi.10.7     Document Type: Review
Times cited : (29)

References (160)
  • 1
    • 33847047461 scopus 로고    scopus 로고
    • Epigenetics: A landscape takes shape
    • Goldberg AD, Allis CD, Bernstein E. Epigenetics: a landscape takes shape. Cell 128(4), 635-638 (2007).
    • (2007) Cell , vol.128 , Issue.4 , pp. 635-638
    • Goldberg, A.D.1    Allis, C.D.2    Bernstein, E.3
  • 2
    • 56149090684 scopus 로고    scopus 로고
    • Epi-drugs to fght cancer: From chemistry to cancer treatment, the road ahead
    • Mai A, Altucci L: Epi-drugs to fght cancer: from chemistry to cancer treatment, the road ahead. Int. J. Biochem. Cell Biol. 41(1), 199-213 (2009).
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , Issue.1 , pp. 199-213
    • Mai, A.1    Altucci, L.2
  • 3
    • 34250316675 scopus 로고    scopus 로고
    • The therapeutic uses of chromatin-modifying agents
    • Mai A: The therapeutic uses of chromatin-modifying agents. Expert Opin. Ther. Targets 11(6), 835-851 (2007).
    • (2007) Expert Opin. Ther. Targets , vol.11 , Issue.6 , pp. 835-851
    • Mai, A.1
  • 4
    • 67649379393 scopus 로고    scopus 로고
    • Histone acetyltransferase inhibitors and preclinical studies
    • Manzo F, Tambaro FP, Mai A, Altucci L: Histone acetyltransferase inhibitors and preclinical studies. Expert Opin. Ther. Pat. 19(6), 761-774 (2009).
    • (2009) Expert Opin. Ther. Pat , vol.19 , Issue.6 , pp. 761-774
    • Manzo, F.1    Tambaro, F.P.2    Mai, A.3    Altucci, L.4
  • 5
    • 65449142086 scopus 로고    scopus 로고
    • Non-cancer uses of histone deacetylase inhibitors: Effects on infectious diseases and b-hemoglobinopathies
    • Rotili D, Simonetti G, Savarino A, Palamara AT, Migliaccio AR, Mai A: Non-cancer uses of histone deacetylase inhibitors: effects on infectious diseases and b-hemoglobinopathies. Curr. Top. Med. Chem. 9(3), 272-291 (2009).
    • (2009) Curr. Top. Med. Chem , vol.9 , Issue.3 , pp. 272-291
    • Rotili, D.1    Simonetti, G.2    Savarino, A.3    Palamara, A.T.4    Migliaccio, A.R.5    Mai, A.6
  • 6
    • 70349780606 scopus 로고    scopus 로고
    • The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors
    • Spannhoff A, Hauser AT, Heinke R, Sippl W, Jung M: The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. ChemMedChem 4(10), 1568-1582 (2009).
    • (2009) ChemMedChem , vol.4 , Issue.10 , pp. 1568-1582
    • Spannhoff, A.1    Hauser, A.T.2    Heinke, R.3    Sippl, W.4    Jung, M.5
  • 7
    • 55949109901 scopus 로고    scopus 로고
    • Cancer treatment of the future: Inhibitors of histone methyltransferases
    • Spannhoff A, Sippl W, Jung M: Cancer treatment of the future: inhibitors of histone methyltransferases. Int. J. Biochem. Cell Biol. 41(1), 4-11 (2009).
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , Issue.1 , pp. 4-11
    • Spannhoff, A.1    Sippl, W.2    Jung, M.3
  • 8
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland M, Montgomery RL, Olson EN: The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet. 10(1), 32-42 (2009).
    • (2009) Nat. Rev. Genet , vol.10 , Issue.1 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 9
    • 70349311616 scopus 로고    scopus 로고
    • Histone acetyl transferases as emerging drug targets
    • Dekker FJ, Haisma HJ: Histone acetyl transferases as emerging drug targets. Drug Discov. Today 14(19-20), 942-948 (2009).
    • (2009) Drug Discov. Today , vol.14 , Issue.19-20 , pp. 942-948
    • Dekker, F.J.1    Haisma, H.J.2
  • 10
    • 70649108817 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and neurodegenerative disorders: Holding the promise
    • Mai A, Rotili D, Valente S, Kazantsev AG: Histone deacetylase inhibitors and neurodegenerative disorders: holding the promise. Curr. Pharm. Des. 15(34), 3940-3957 (2009).
    • (2009) Curr. Pharm. des , vol.15 , Issue.34 , pp. 3940-3957
    • Mai, A.1    Rotili, D.2    Valente, S.3    Kazantsev, A.G.4
  • 11
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifcations and their function
    • Kouzarides T: Chromatin modifcations and their function. Cell 128(4), 693-705 (2007).
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 13
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M: Histone acetylation in chromatin structure and transcription. Nature 389(6649), 349-352 (1997).
    • (1997) Nature , vol.389 , Issue.6649 , pp. 349-352
    • Grunstein, M.1
  • 14
    • 33746457753 scopus 로고    scopus 로고
    • Enhanced histone acetylation and transcription: A dynamic perspective
    • Clayton AL, Hazzalin CA, Mahadevan LC: Enhanced histone acetylation and transcription: a dynamic perspective. Mol. Cell 23(3), 289-296 (2006).
    • (2006) Mol. Cell , vol.23 , Issue.3 , pp. 289-296
    • Clayton, A.L.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 15
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specifc histone acetylation and deacetylation
    • Shahbazian MD, Grunstein M: Functions of site-specifc histone acetylation and deacetylation. Annu. Rev. Biochem. 76, 75-100 (2007).
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 16
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifcations by linked binding modules
    • Ruthenburg AJ, Li H, Patel DJ, Allis CD: Multivalent engagement of chromatin modifcations by linked binding modules. Nat. Rev. Mol. Cell Biol. 8(12), 983-994 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , Issue.12 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    Allis, C.D.4
  • 17
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger CM, Schreiber SL: Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem. Biol. 9(1), 3-16 (2002).
    • (2002) Chem. Biol , vol.9 , Issue.1 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 18
    • 16844362441 scopus 로고    scopus 로고
    • Histone deacetylation in epigenetics: An attractive target for anticancer therapy
    • Mai A, Massa S, Rotili D et al.: Histone deacetylation in epigenetics: an attractive target for anticancer therapy. Med. Res. Rev. 25(3), 261-309 (2005).
    • (2005) Med. Res. Rev , vol.25 , Issue.3 , pp. 261-309
    • Mai, A.1    Massa, S.2    Rotili, D.3
  • 19
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
    • Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN: Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89(3), 349-356 (1997).
    • (1997) Cell , vol.89 , Issue.3 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 20
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • Verdin E, Dequiedt F, Kasler HG: Class II histone deacetylases: versatile regulators. Trends Genet. 19(5), 286-293 (2003).
    • (2003) Trends Genet , vol.19 , Issue.5 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 21
    • 34547919621 scopus 로고    scopus 로고
    • Class IIa histone deacetylases: Regulating the regulators
    • Martin M, Kettmann R, Dequiedt F: Class IIa histone deacetylases: regulating the regulators. Oncogene 26(37), 5450-5467 (2007).
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5450-5467
    • Martin, M.1    Kettmann, R.2    Dequiedt, F.3
  • 22
    • 67650090545 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Potential in cancer therapy
    • Marks PA, Xu WS: Histone deacetylase inhibitors: potential in cancer therapy. J. Cell. Biochem. 107(4), 600-608 (2009).
    • (2009) J. Cell. Biochem , vol.107 , Issue.4 , pp. 600-608
    • Marks, P.A.1    Xu, W.S.2
  • 23
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • Witt O, Deubzer HE, Milde T, Oehme I: HDAC family: what are the cancer relevant targets? Cancer Lett. 277(1), 8-21 (2009).
    • (2009) Cancer Lett , vol.277 , Issue.1 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 24
    • 0036165434 scopus 로고    scopus 로고
    • MEF2: A calcium-dependent regulator of cell division, differentiation and death
    • McKinsey TA, Zhang CL, Olson EN: MEF2: a calcium-dependent regulator of cell division, differentiation and death. Trends Biochem. Sci. 27(1), 40-47 (2002).
    • (2002) Trends Biochem. Sci , vol.27 , Issue.1 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 25
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C, Guardiola A, Shao R et al.: HDAC6 is a microtubule-associated deacetylase. Nature 417(6887), 455-458 (2002).
    • (2002) Nature , vol.417 , Issue.6887 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 26
    • 57849096553 scopus 로고    scopus 로고
    • The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance
    • Villagra A, Cheng F, Wang HW et al.: The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance. Nat. Immunol. 10(1), 92-100 (2009).
    • (2009) Nat. Immunol , vol.10 , Issue.1 , pp. 92-100
    • Villagra, A.1    Cheng, F.2    Wang, H.W.3
  • 27
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden JE, Peart MJ, Johnstone RW: Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 5(9), 769-784 (2006).
    • (2006) Nat. Rev. Drug Discov , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 28
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG: Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 6(1), 38-51 (2006).
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 29
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak MA, Seto E: Histone deacetylases and cancer. Oncogene 26(37), 5420-5432 (2007).
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 30
    • 43249120953 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Mechanisms and clinical signifcance in cancer: HDAC inhibitor-induced apoptosis
    • Shankar S, Srivastava RK: Histone deacetylase inhibitors: mechanisms and clinical signifcance in cancer: HDAC inhibitor-induced apoptosis. Adv. Exp. Med. Biol. 615, 261-298 (2008).
    • (2008) Adv. Exp. Med. Biol , vol.615 , pp. 261-298
    • Shankar, S.1    Srivastava, R.K.2
  • 31
    • 0032188989 scopus 로고    scopus 로고
    • Caspases mediate retinoic acid-induced degradation of the acute promyelocytic leukemia PML/RARa fusion protein
    • Nervi C, Ferrara FF, Fanelli M et al.: Caspases mediate retinoic acid-induced degradation of the acute promyelocytic leukemia PML/RARa fusion protein. Blood 92(7), 2244-2251 (1998).
    • (1998) Blood , vol.92 , Issue.7 , pp. 2244-2251
    • Nervi, C.1    Ferrara, F.F.2    Fanelli, M.3
  • 32
    • 0029919406 scopus 로고    scopus 로고
    • The PML/RAR a oncoprotein is a direct molecular target of retinoic acid in acute promyelocytic leukemia cells
    • Raelson JV, Nervi C, Rosenauer A et al.: The PML/RAR a oncoprotein is a direct molecular target of retinoic acid in acute promyelocytic leukemia cells. Blood 88(8), 2826-2832 (1996).
    • (1996) Blood , vol.88 , Issue.8 , pp. 2826-2832
    • Raelson, J.V.1    Nervi, C.2    Rosenauer, A.3
  • 33
    • 0033592948 scopus 로고    scopus 로고
    • Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor a (RARa) and oncogenic RARa fusion proteins
    • Zhu J, Gianni M, Kopf E et al.: Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor a (RARa) and oncogenic RARa fusion proteins. Proc. Natl Acad. Sci. USA 96(26), 14807-14812 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.26 , pp. 14807-14812
    • Zhu, J.1    Gianni, M.2    Kopf, E.3
  • 34
    • 0033104901 scopus 로고    scopus 로고
    • Constitutive degradation of PML/RARa through the proteasome pathway mediates retinoic acid resistance
    • Fanelli M, Minucci S, Gelmetti V, Nervi C, Gambacorti-Passerini C, Pelicci PG: Constitutive degradation of PML/RARa through the proteasome pathway mediates retinoic acid resistance. Blood 93(5), 1477-1481 (1999).
    • (1999) Blood , vol.93 , Issue.5 , pp. 1477-1481
    • Fanelli, M.1    Minucci, S.2    Gelmetti, V.3    Nervi, C.4    Gambacorti-Passerini, C.5    Pelicci, P.G.6
  • 35
    • 0033037274 scopus 로고    scopus 로고
    • PIC-1/SUMO-1-modifed PML-retinoic acid receptor a mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • Sternsdorf T, Puccetti E, Jensen K et al.: PIC-1/SUMO-1-modifed PML-retinoic acid receptor a mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Mol. Cell. Biol. 19(7), 5170-5178 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , Issue.7 , pp. 5170-5178
    • Sternsdorf, T.1    Puccetti, E.2    Jensen, K.3
  • 36
    • 0032402135 scopus 로고    scopus 로고
    • Trivalent antimonials induce degradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells
    • Muller S, Miller WH Jr, Dejean A: Trivalent antimonials induce degradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells. Blood 92(11), 4308-4316 (1998).
    • (1998) Blood , vol.92 , Issue.11 , pp. 4308-4316
    • Muller, S.1    Miller Jr., W.H.2    Dejean, A.3
  • 37
    • 1342266237 scopus 로고    scopus 로고
    • The PML-RARa fusion protein and targeted therapy for acute promyelocytic leukemia
    • Jing Y: The PML-RARa fusion protein and targeted therapy for acute promyelocytic leukemia. Leuk. Lymphoma 45(4), 639-648 (2004).
    • (2004) Leuk. Lymphoma , vol.45 , Issue.4 , pp. 639-648
    • Jing, Y.1
  • 38
    • 0034730198 scopus 로고    scopus 로고
    • Retinoic acid (RA) and As2O3 treatment in transgenic models of acute promyelocytic leukemia (APL) unravel the distinct nature of the leukemogenic process induced by the PML-RARa and PLZF-RARa oncoproteins
    • Rego EM, He LZ, Warrell RP Jr, Wang ZG, Pandolf PP: Retinoic acid (RA) and As2O3 treatment in transgenic models of acute promyelocytic leukemia (APL) unravel the distinct nature of the leukemogenic process induced by the PML-RARa and PLZF-RARa oncoproteins. Proc. Natl Acad. Sci. USA 97(18), 10173-10178 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.18 , pp. 10173-10178
    • Rego, E.M.1    He, L.Z.2    Warrell Jr., R.P.3    Wang, Z.G.4    Pandolf, P.P.5
  • 39
    • 17144458786 scopus 로고    scopus 로고
    • Fusion proteins of the retinoic acid receptor-a recruit histone deacetylase in promyelocytic leukaemia
    • Grignani F, De Matteis S, Nervi C et al.: Fusion proteins of the retinoic acid receptor-a recruit histone deacetylase in promyelocytic leukaemia. Nature 391(6669), 815-818 (1998).
    • (1998) Nature , vol.391 , Issue.6669 , pp. 815-818
    • Grignani, F.1    De Matteis, S.2    Nervi, C.3
  • 40
    • 0031723957 scopus 로고    scopus 로고
    • Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO
    • Gelmetti V, Zhang J, Fanelli M, Minucci S, Pelicci PG, Lazar MA: Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO. Mol. Cell. Biol. 18(12), 7185-7191 (1998).
    • (1998) Mol. Cell. Biol , vol.18 , Issue.12 , pp. 7185-7191
    • Gelmetti, V.1    Zhang, J.2    Fanelli, M.3    Minucci, S.4    Pelicci, P.G.5    Lazar, M.A.6
  • 41
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin MS, Donigian JR, Cohen A et al.: Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401(6749), 188-193 (1999).
    • (1999) Nature , vol.401 , Issue.6749 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3
  • 42
    • 3142562372 scopus 로고    scopus 로고
    • Structural snapshots of human HDAC8 provide insights into the class i histone deacetylases
    • Somoza JR, Skene RJ, Katz BA et al.: Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure 12(7), 1325-1334 (2004).
    • (2004) Structure , vol.12 , Issue.7 , pp. 1325-1334
    • Somoza, J.R.1    Skene, R.J.2    Katz, B.A.3
  • 43
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
    • Vannini A, Volpari C, Filocamo G et al.: Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc. Natl Acad. Sci. USA 101(42), 15064-15069 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.42 , pp. 15064-15069
    • Vannini, A.1    Volpari, C.2    Filocamo, G.3
  • 45
    • 55549094833 scopus 로고    scopus 로고
    • Structural and functional ana lysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain
    • Bottomley MJ, Lo Surdo P, Di Giovine P et al.: Structural and functional ana lysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain. J. Biol. Chem. 283(39), 26694-26704 (2008).
    • (2008) J. Biol. Chem , vol.283 , Issue.39 , pp. 26694-26704
    • Bottomley, M.J.1    Lo Surdo, P.2    Di Giovine, P.3
  • 46
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class i histone deacetylases
    • Furumai R, Matsuyama A, Kobashi N et al.: FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res. 62(17), 4916-4921 (2002).
    • (2002) Cancer Res , vol.62 , Issue.17 , pp. 4916-4921
    • Furumai, R.1    Matsuyama, A.2    Kobashi, N.3
  • 47
    • 27444435580 scopus 로고    scopus 로고
    • Toward selective histone deacetylase inhibitor design: Homology modeling, docking studies, and molecular dynamics simulations of human class i histone deacetylases
    • Wang DF, Helquist P, Wiech NL, Wiest O: Toward selective histone deacetylase inhibitor design: homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases. J. Med. Chem. 48(22), 6936-6947 (2005).
    • (2005) J. Med. Chem , vol.48 , Issue.22 , pp. 6936-6947
    • Wang, D.F.1    Helquist, P.2    Wiech, N.L.3    Wiest, O.4
  • 48
    • 52449112167 scopus 로고    scopus 로고
    • Residues in the 11 A channel of histone deacetylase 1 promote catalytic activity: Implications for designing isoform-selective histone deacetylase inhibitors
    • Weerasinghe SV, Estiu G, Wiest O, Pfum MK: Residues in the 11 A channel of histone deacetylase 1 promote catalytic activity: implications for designing isoform-selective histone deacetylase inhibitors. J. Med. Chem. 51(18), 5542-5551 (2008).
    • (2008) J. Med. Chem , vol.51 , Issue.18 , pp. 5542-5551
    • Weerasinghe, S.V.1    Estiu, G.2    Wiest, O.3    Pfum, M.K.4
  • 49
    • 2942545807 scopus 로고    scopus 로고
    • On the function of the 14 A long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors
    • Wang DF, Wiest O, Helquist P, Lan-Hargest HY, Wiech NL: On the function of the 14 A long internal cavity of histone deacetylase-like protein: implications for the design of histone deacetylase inhibitors. J. Med. Chem. 47(13), 3409-3417 (2004).
    • (2004) J. Med. Chem , vol.47 , Issue.13 , pp. 3409-3417
    • Wang, D.F.1    Wiest, O.2    Helquist, P.3    Lan-Hargest, H.Y.4    Wiech, N.L.5
  • 50
    • 70349240449 scopus 로고    scopus 로고
    • Sodium butyrate induces human colon carcinoma HT-29 cell apoptosis through a mitochondrial pathway
    • Wang L, Luo HS, Xia H: Sodium butyrate induces human colon carcinoma HT-29 cell apoptosis through a mitochondrial pathway. J. Int. Med. Res. 37(3), 803-811 (2009).
    • (2009) J. Int. Med. Res , vol.37 , Issue.3 , pp. 803-811
    • Wang, L.1    Luo, H.S.2    Xia, H.3
  • 51
    • 66449127641 scopus 로고    scopus 로고
    • Valproic acid causes dose-and time-dependent changes in nuclear structure in prostate cancer cells in vitro and in vivo
    • Kortenhorst MS, Isharwal S, van Diest PJ et al.: Valproic acid causes dose-and time-dependent changes in nuclear structure in prostate cancer cells in vitro and in vivo. Mol. Cancer Ther. 8(4), 802-808 (2009).
    • (2009) Mol. Cancer Ther , vol.8 , Issue.4 , pp. 802-808
    • Kortenhorst, M.S.1    Isharwal, S.2    Van Diest, P.J.3
  • 52
    • 3843151628 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor pivaloyloxymethyl butyrate (Pivanex, AN-9) in advanced non-small cell lung cancer
    • Reid T, Valone F, Lipera W et al.: Phase II trial of the histone deacetylase inhibitor pivaloyloxymethyl butyrate (Pivanex, AN-9) in advanced non-small cell lung cancer. Lung Cancer 45(3), 381-386 (2004).
    • (2004) Lung Cancer , vol.45 , Issue.3 , pp. 381-386
    • Reid, T.1    Valone, F.2    Lipera, W.3
  • 53
    • 37849019672 scopus 로고    scopus 로고
    • Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors
    • Khan N, Jeffers M, Kumar S et al.: Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors. Biochem. J. 409(2), 581-589 (2008).
    • (2008) Biochem. J , vol.409 , Issue.2 , pp. 581-589
    • Khan, N.1    Jeffers, M.2    Kumar, S.3
  • 55
    • 77649171884 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
    • Tan J, Cang S, Ma Y, Petrillo RL, Liu D: Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents. J. Hematol. Oncol. 3, 5 (2010).
    • (2010) J. Hematol. Oncol , vol.3 , pp. 5
    • Tan, J.1    Cang, S.2    Ma, Y.3    Petrillo, R.L.4    Liu, D.5
  • 56
    • 67449127082 scopus 로고    scopus 로고
    • Clinical studies of histone deacetylase inhibitors
    • Prince HM, Bishton MJ, Harrison SJ: Clinical studies of histone deacetylase inhibitors. Clin. Cancer Res. 15(12), 3958-3969 (2009).
    • (2009) Clin. Cancer Res , vol.15 , Issue.12 , pp. 3958-3969
    • Prince, H.M.1    Bishton, M.J.2    Harrison, S.J.3
  • 57
    • 67449138841 scopus 로고    scopus 로고
    • Epigenetic modifers: Basic understanding and clinical development
    • Piekarz RL, Bates SE: Epigenetic modifers: basic understanding and clinical development. Clin. Cancer Res. 15(12), 3918-3926 (2009).
    • (2009) Clin. Cancer Res , vol.15 , Issue.12 , pp. 3918-3926
    • Piekarz, R.L.1    Bates, S.E.2
  • 58
    • 10744229917 scopus 로고    scopus 로고
    • N-hydroxy-3-phenyl-2-propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: Discovery of (2E)-N-hydroxy-3-[4- [[(2-hydroxyethyl) [2-(1H-indol-3-yl)ethyl]amino]methyl] phenyl]-2-propenamide (NVP-LAQ824)
    • Remiszewski SW, Sambucetti LC, Bair KW et al.: N-hydroxy-3-phenyl-2- propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: discovery of (2E)-N-hydroxy-3-[4-[[(2-hydroxyethyl) [2-(1H-indol-3-yl)ethyl]amino]methyl] phenyl]-2-propenamide (NVP-LAQ824). J. Med. Chem. 46(21), 4609-4624 (2003).
    • (2003) J. Med. Chem , vol.46 , Issue.21 , pp. 4609-4624
    • Remiszewski, S.W.1    Sambucetti, L.C.2    Bair, K.W.3
  • 59
    • 77954129865 scopus 로고    scopus 로고
    • In vitro and in vivo rationale for the triple combination of panobinostat (LBH589) and dexamethasone with either bortezomib or lenalidomide in multiple myeloma
    • Epub ahead of print
    • Ocio EM, Vilanova D, Atadja P et al.: In vitro and in vivo rationale for the triple combination of panobinostat (LBH589) and dexamethasone with either bortezomib or lenalidomide in multiple myeloma. Haematologica (2009) (Epub ahead of print).
    • (2009) Haematologica
    • Ocio, E.M.1    Vilanova, D.2    Atadja, P.3
  • 60
    • 38949146399 scopus 로고    scopus 로고
    • A Phase i pharmacokinetic and pharmacodynamic study of the histone deacetylase inhibitor belinostat in patients with advanced solid tumors
    • Steele NL, Plumb JA, Vidal L et al.: A Phase I pharmacokinetic and pharmacodynamic study of the histone deacetylase inhibitor belinostat in patients with advanced solid tumors. Clin. Cancer Res. 14(3), 804-810 (2008).
    • (2008) Clin. Cancer Res , vol.14 , Issue.3 , pp. 804-810
    • Steele, N.L.1    Plumb, J.A.2    Vidal, L.3
  • 61
    • 74049113834 scopus 로고    scopus 로고
    • A Phase II multiple dose clinical trial of histone deacetylase inhibitor ITF2357 in patients with relapsed or progressive multiple myeloma
    • Galli M, Salmoiraghi S, Golay J et al.: A Phase II multiple dose clinical trial of histone deacetylase inhibitor ITF2357 in patients with relapsed or progressive multiple myeloma. Ann. Hematol. 89(2), 185-190 (2010).
    • (2010) Ann. Hematol , vol.89 , Issue.2 , pp. 185-190
    • Galli, M.1    Salmoiraghi, S.2    Golay, J.3
  • 62
    • 42049118549 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Itoh Y, Suzuki T, Miyata N: Isoform-selective histone deacetylase inhibitors. Curr. Pharm. Des. 14(6), 529-544 (2008).
    • (2008) Curr. Pharm. des , vol.14 , Issue.6 , pp. 529-544
    • Itoh, Y.1    Suzuki, T.2    Miyata, N.3
  • 63
    • 77749309291 scopus 로고    scopus 로고
    • Romidepsin for the treatment of cutaneous T-cell lymphoma
    • Campas-Moya C: Romidepsin for the treatment of cutaneous T-cell lymphoma. Drugs Today (Barc.) 45(11), 787-795 (2009).
    • (2009) Drugs Today (Barc.) , vol.45 , Issue.11 , pp. 787-795
    • Campas-Moya, C.1
  • 64
    • 73949149251 scopus 로고    scopus 로고
    • Phase II multi-institutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma
    • Piekarz RL, Frye R, Turner M et al.: Phase II multi-institutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma. J. Clin. Oncol. 27(32), 5410-5417 (2009).
    • (2009) J. Clin. Oncol , vol.27 , Issue.32 , pp. 5410-5417
    • Piekarz, R.L.1    Frye, R.2    Turner, M.3
  • 65
    • 0033614993 scopus 로고    scopus 로고
    • Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives
    • Suzuki T, Ando T, Tsuchiya K et al.: Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives. J. Med. Chem. 42(15), 3001-3003 (1999).
    • (1999) J. Med. Chem , vol.42 , Issue.15 , pp. 3001-3003
    • Suzuki, T.1    Ando, T.2    Tsuchiya, K.3
  • 66
    • 3142689788 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells
    • Lucas DM, Davis ME, Parthun MR et al.: The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells. Leukemia 18(7), 1207-1214 (2004).
    • (2004) Leukemia , vol.18 , Issue.7 , pp. 1207-1214
    • Lucas, D.M.1    Davis, M.E.2    Parthun, M.R.3
  • 67
    • 13444306459 scopus 로고    scopus 로고
    • Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells
    • Nebbioso A, Clarke N, Voltz E et al.: Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells. Nat. Med. 11(1), 77-84 (2005).
    • (2005) Nat. Med , vol.11 , Issue.1 , pp. 77-84
    • Nebbioso, A.1    Clarke, N.2    Voltz, E.3
  • 68
    • 34547662889 scopus 로고    scopus 로고
    • Antitumor activity of the histone deacetylase inhibitor MS-275 in prostate cancer models
    • Qian DZ, Wei YF, Wang X, Kato Y, Cheng L, Pili R: Antitumor activity of the histone deacetylase inhibitor MS-275 in prostate cancer models. Prostate 67(11), 1182-1193 (2007).
    • (2007) Prostate , vol.67 , Issue.11 , pp. 1182-1193
    • Qian, D.Z.1    Wei, Y.F.2    Wang, X.3    Kato, Y.4    Cheng, L.5    Pili, R.6
  • 69
    • 42949154252 scopus 로고    scopus 로고
    • Phase i study of MGCD0103 given as a three-times-per-week oral dose in patients with advanced solid tumors
    • Siu LL, Pili R, Duran I et al.: Phase I study of MGCD0103 given as a three-times-per-week oral dose in patients with advanced solid tumors. J. Clin. Oncol. 26(12), 1940-1947 (2008).
    • (2008) J. Clin. Oncol , vol.26 , Issue.12 , pp. 1940-1947
    • Siu, L.L.1    Pili, R.2    Duran, I.3
  • 70
    • 51649110503 scopus 로고    scopus 로고
    • Phase 1 study of the oral isotype specifc histone deacetylase inhibitor MGCD0103 in leukemia
    • Garcia-Manero G, Assouline S, Cortes J et al.: Phase 1 study of the oral isotype specifc histone deacetylase inhibitor MGCD0103 in leukemia. Blood 112(4), 981-989 (2008).
    • (2008) Blood , vol.112 , Issue.4 , pp. 981-989
    • Garcia-Manero, G.1    Assouline, S.2    Cortes, J.3
  • 71
    • 70350448445 scopus 로고    scopus 로고
    • Phase II study of the histone deacetylase inhibitor MGCD0103 in patients with previously treated chronic lymphocytic leukaemia
    • Blum KA, Advani A, Fernandez L et al.: Phase II study of the histone deacetylase inhibitor MGCD0103 in patients with previously treated chronic lymphocytic leukaemia. Br. J. Haematol. 147(4), 507-514 (2009).
    • (2009) Br. J. Haematol , vol.147 , Issue.4 , pp. 507-514
    • Blum, K.A.1    Advani, A.2    Fernandez, L.3
  • 72
    • 55949088703 scopus 로고    scopus 로고
    • New pyrrole-based histone deacetylase inhibitors: Binding mode, enzyme-and cell-based investigations
    • Mai A, Valente S, Nebbioso A et al.: New pyrrole-based histone deacetylase inhibitors: binding mode, enzyme-and cell-based investigations. Int. J. Biochem. Cell Biol. 41(1), 235-247 (2009).
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , Issue.1 , pp. 235-247
    • Mai, A.1    Valente, S.2    Nebbioso, A.3
  • 74
    • 25144492801 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 2-, 3-, and 4-acylaminocinnamyl-N- hydroxyamides as novel synthetic HDAC inhibitors
    • Mai A, Massa S, Pezzi R, Valente S, Loidl P, Brosch G: Synthesis and biological evaluation of 2-, 3-, and 4-acylaminocinnamyl-N-hydroxyamides as novel synthetic HDAC inhibitors. Med. Chem. 1(3), 245-254 (2005).
    • (2005) Med. Chem , vol.1 , Issue.3 , pp. 245-254
    • Mai, A.1    Massa, S.2    Pezzi, R.3    Valente, S.4    Loidl, P.5    Brosch, G.6
  • 75
    • 37849010584 scopus 로고    scopus 로고
    • Nitric oxide modulates chromatin folding in human endothelial cells via protein phosphatase 2A activation and class II histone deacetylases nuclear shuttling
    • Illi B, Dello Russo C, Colussi C et al.: Nitric oxide modulates chromatin folding in human endothelial cells via protein phosphatase 2A activation and class II histone deacetylases nuclear shuttling. Circ. Res. 102(1), 51-58 (2008).
    • (2008) Circ. Res , vol.102 , Issue.1 , pp. 51-58
    • Illi, B.1    Dello Russo, C.2    Colussi, C.3
  • 76
    • 33746144518 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase class i but not class II is critical for the sensitization of leukemic cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis
    • Inoue S, Mai A, Dyer MJ, Cohen GM: Inhibition of histone deacetylase class I but not class II is critical for the sensitization of leukemic cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis. Cancer Res. 66(13), 6785-6792 (2006).
    • (2006) Cancer Res , vol.66 , Issue.13 , pp. 6785-6792
    • Inoue, S.1    Mai, A.2    Dyer, M.J.3    Cohen, G.M.4
  • 77
    • 20944435415 scopus 로고    scopus 로고
    • Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides
    • Mai A, Massa S, Pezzi R et al.: Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. J. Med. Chem. 48(9), 3344-3353 (2005).
    • (2005) J. Med. Chem. , vol.48 , Issue.9 , pp. 3344-3353
    • Mai, A.1    Massa, S.2    Pezzi, R.3
  • 78
    • 67650083046 scopus 로고    scopus 로고
    • Selective class II HDAC inhibitors impair myogenesis by modulating the stability and activity of HDAC-MEF2 complexes
    • Nebbioso A, Manzo F, Miceli M et al.: Selective class II HDAC inhibitors impair myogenesis by modulating the stability and activity of HDAC-MEF2 complexes. EMBO Rep. 10(7), 776-782 (2009).
    • (2009) EMBO Rep , vol.10 , Issue.7 , pp. 776-782
    • Nebbioso, A.1    Manzo, F.2    Miceli, M.3
  • 79
    • 57749101152 scopus 로고    scopus 로고
    • Specifc activity of class II histone deacetylases in human breast cancer cells
    • Duong V, Bret C, Altucci L et al.: Specifc activity of class II histone deacetylases in human breast cancer cells. Mol. Cancer Res. 6(12), 1908-1919 (2008).
    • (2008) Mol. Cancer Res , vol.6 , Issue.12 , pp. 1908-1919
    • Duong, V.1    Bret, C.2    Altucci, L.3
  • 80
    • 0033520944 scopus 로고    scopus 로고
    • Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specifc chromatin acetylation and antiproliferative effects
    • Sambucetti LC, Fischer DD, Zabludoff S et al.: Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specifc chromatin acetylation and antiproliferative effects. J. Biol. Chem. 274(49), 34940-34947 (1999).
    • (1999) J. Biol. Chem , vol.274 , Issue.49 , pp. 34940-34947
    • Sambucetti, L.C.1    Fischer, D.D.2    Zabludoff, S.3
  • 81
    • 13444274622 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway
    • Insinga A, Monestiroli S, Ronzoni S et al.: Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway. Nat. Med. 11(1), 71-76 (2005).
    • (2005) Nat. Med , vol.11 , Issue.1 , pp. 71-76
    • Insinga, A.1    Monestiroli, S.2    Ronzoni, S.3
  • 82
    • 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
    • Ruefi AA, Ausserlechner MJ, Bernhard D et al.: 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. USA 98(19), 10833-10838 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , Issue.19 , pp. 10833-10838
    • Ruefi, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3
  • 83
    • 0033604457 scopus 로고    scopus 로고
    • Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53
    • Vrana JA, Decker RH, Johnson CR et al.: Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53. Oncogene 18(50), 7016-7025 (1999).
    • (1999) Oncogene , vol.18 , Issue.50 , pp. 7016-7025
    • Vrana, J.A.1    Decker, R.H.2    Johnson, C.R.3
  • 84
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone RW, Licht JD: Histone deacetylase inhibitors in cancer therapy: is transcription the primary target? Cancer Cell 4(1), 13-18 (2003).
    • (2003) Cancer Cell , vol.4 , Issue.1 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 85
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • Rossig L, Li H, Fisslthaler B et al.: Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. Circ. Res. 91(9), 837-844 (2002).
    • (2002) Circ. Res , vol.91 , Issue.9 , pp. 837-844
    • Rossig, L.1    Li, H.2    Fisslthaler, B.3
  • 86
    • 31544464120 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with histone deacetylase inhibitors: The hydroxamic acid derivative LBH589
    • Qian DZ, Kato Y, Shabbeer S et al.: Targeting tumor angiogenesis with histone deacetylase inhibitors: the hydroxamic acid derivative LBH589. Clin. Cancer Res. 12(2), 634-642 (2006).
    • (2006) Clin. Cancer Res , vol.12 , Issue.2 , pp. 634-642
    • Qian, D.Z.1    Kato, Y.2    Shabbeer, S.3
  • 87
    • 28244502269 scopus 로고    scopus 로고
    • Cancer cells become susceptible to natural killer 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
    • Skov S, Pedersen MT, Andresen L, Straten PT, Woetmann A, Odum N: Cancer cells become susceptible to natural killer 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(23), 11136-11145 (2005).
    • (2005) Cancer Res , vol.65 , Issue.23 , pp. 11136-11145
    • Skov, S.1    Pedersen, M.T.2    Andresen, L.3    Straten, P.T.4    Woetmann, A.5    Odum, N.6
  • 88
    • 33845741562 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of g-H2AX foci and confnes HDAC4 to the cytoplasm in irradiated non-small cell lung cancer
    • Geng L, Cuneo KC, Fu A, Tu T, Atadja PW, Hallahan DE: Histone deacetylase (HDAC) inhibitor LBH589 increases duration of g-H2AX foci and confnes HDAC4 to the cytoplasm in irradiated non-small cell lung cancer. Cancer Res. 66(23), 11298-11304 (2006).
    • (2006) Cancer Res , vol.66 , Issue.23 , pp. 11298-11304
    • Geng, L.1    Cuneo, K.C.2    Fu, A.3    Tu, T.4    Atadja, P.W.5    Hallahan, D.E.6
  • 89
    • 34547122494 scopus 로고    scopus 로고
    • HDAC inhibitors: Clinical update and mechanism-based potential
    • Glaser KB: HDAC inhibitors: clinical update and mechanism-based potential. Biochem. Pharmacol. 74(5), 659-671 (2007).
    • (2007) Biochem. Pharmacol , vol.74 , Issue.5 , pp. 659-671
    • Glaser, K.B.1
  • 90
    • 67349285731 scopus 로고    scopus 로고
    • Enhancing the apoptotic and therapeutic effects of HDAC inhibitors
    • Frew AJ, Johnstone RW, Bolden JE: Enhancing the apoptotic and therapeutic effects of HDAC inhibitors. Cancer Lett. 280(2), 125-133 (2009).
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 125-133
    • Frew, A.J.1    Johnstone, R.W.2    Bolden, J.E.3
  • 91
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane AA, Chabner BA: Histone deacetylase inhibitors in cancer therapy. J. Clin. Oncol. 27(32), 5459-5468 (2009).
    • (2009) J. Clin. Oncol , vol.27 , Issue.32 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 92
    • 60749108001 scopus 로고    scopus 로고
    • Polymeric drugs for effcient tumor-targeted drug delivery based on EPR-effect
    • Maeda H, Bharate GY, Daruwalla J: Polymeric drugs for effcient tumor-targeted drug delivery based on EPR-effect. Eur. J. Pharm. Biopharm. 71(3), 409-419 (2009).
    • (2009) Eur. J. Pharm. Biopharm , vol.71 , Issue.3 , pp. 409-419
    • Maeda, H.1    Bharate, G.Y.2    Daruwalla, J.3
  • 93
    • 10544250252 scopus 로고    scopus 로고
    • Apicidin: A novel antiprotozoal agent that inhibits parasite histone deacetylase
    • Darkin-Rattray SJ, Gurnett AM, Myers RW et al.: Apicidin: a novel antiprotozoal agent that inhibits parasite histone deacetylase. Proc. Natl Acad. Sci. USA 93(23), 13143-13147 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.23 , pp. 13143-13147
    • Darkin-Rattray, S.J.1    Gurnett, A.M.2    Myers, R.W.3
  • 94
    • 0034326799 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/Cip1 and gelsolin
    • Han JW, Ahn SH, Park SH et al.: Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/Cip1 and gelsolin. Cancer Res. 60(21), 6068-6074 (2000).
    • (2000) Cancer Res , vol.60 , Issue.21 , pp. 6068-6074
    • Han, J.W.1    Ahn, S.H.2    Park, S.H.3
  • 95
    • 0034649616 scopus 로고    scopus 로고
    • Synthesis of apicidin-derived quinolone derivatives: Parasite-selective histone deacetylase inhibitors and antiproliferative agents
    • Meinke PT, Colletti SL, Doss G et al.: Synthesis of apicidin-derived quinolone derivatives: parasite-selective histone deacetylase inhibitors and antiproliferative agents. J. Med. Chem. 43(25), 4919-4922 (2000).
    • (2000) J. Med. Chem , vol.43 , Issue.25 , pp. 4919-4922
    • Meinke, P.T.1    Colletti, S.L.2    Doss, G.3
  • 96
    • 0034192770 scopus 로고    scopus 로고
    • Anti-malarial effect of histone deacetylation inhibitors and mammalian tumour cytodifferentiating agents
    • Andrews KT, Walduck A, Kelso MJ, Fairlie DP, Saul A, Parsons PG: Anti-malarial effect of histone deacetylation inhibitors and mammalian tumour cytodifferentiating agents. Int. J. Parasitol. 30(6), 761-768 (2000).
    • (2000) Int. J. Parasitol , vol.30 , Issue.6 , pp. 761-768
    • Andrews, K.T.1    Walduck, A.2    Kelso, M.J.3    Fairlie, D.P.4    Saul, A.5    Parsons, P.G.6
  • 97
    • 42049106596 scopus 로고    scopus 로고
    • Potent antimalarial activity of histone deacetylase inhibitor analogues
    • Andrews KT, Tran TN, Lucke AJ et al.: Potent antimalarial activity of histone deacetylase inhibitor analogues. Antimicrob. Agents Chemother. 52(4), 1454-1461 (2008).
    • (2008) Antimicrob. Agents Chemother , vol.52 , Issue.4 , pp. 1454-1461
    • Andrews, K.T.1    Tran, T.N.2    Lucke, A.J.3
  • 98
    • 54049118868 scopus 로고    scopus 로고
    • Antimalarial activity of phenylthiazolyl-bearing hydroxamate-based histone deacetylase inhibitors
    • Dow GS, Chen Y, Andrews KT et al.: Antimalarial activity of phenylthiazolyl-bearing hydroxamate-based histone deacetylase inhibitors. Antimicrob. Agents Chemother. 52(10), 3467-3477 (2008).
    • (2008) Antimicrob. Agents Chemother , vol.52 , Issue.10 , pp. 3467-3477
    • Dow, G.S.1    Chen, Y.2    Andrews, K.T.3
  • 99
    • 45749103747 scopus 로고    scopus 로고
    • A series of potent and selective, triazolylphenyl-based histone deacetylases inhibitors with activity against pancreatic cancer cells and Plasmodium falciparum
    • Chen Y, Lopez-Sanchez M, Savoy DN, Billadeau DD, Dow GS, Kozikowski AP: A series of potent and selective, triazolylphenyl-based histone deacetylases inhibitors with activity against pancreatic cancer cells and Plasmodium falciparum. J. Med. Chem. 51(12), 3437-3448 (2008).
    • (2008) J. Med. Chem , vol.51 , Issue.12 , pp. 3437-3448
    • Chen, Y.1    Lopez-Sanchez, M.2    Savoy, D.N.3    Billadeau, D.D.4    Dow, G.S.5    Kozikowski, A.P.6
  • 102
    • 0034971016 scopus 로고    scopus 로고
    • A histone deacetylation inhibitor and mutant promote colony-type switching of the human pathogen Candida albicans
    • Klar AJ, Srikantha T, Soll DR: A histone deacetylation inhibitor and mutant promote colony-type switching of the human pathogen Candida albicans. Genetics 158(2), 919-924 (2001).
    • (2001) Genetics , vol.158 , Issue.2 , pp. 919-924
    • Klar, A.J.1    Srikantha, T.2    Soll, D.R.3
  • 103
    • 0036841830 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors enhance Candida albicans sensitivity to azoles and related antifungals: Correlation with reduction in CDR and ERG upregulation
    • Smith WL, Edlind TD: Histone deacetylase inhibitors enhance Candida albicans sensitivity to azoles and related antifungals: correlation with reduction in CDR and ERG upregulation. Antimicrob. Agents Chemother. 46(11), 3532-3539 (2002).
    • (2002) Antimicrob. Agents Chemother , vol.46 , Issue.11 , pp. 3532-3539
    • Smith, W.L.1    Edlind, T.D.2
  • 104
    • 33846938126 scopus 로고    scopus 로고
    • Discovery of uracil-based histone deacetylase inhibitors able to reduce acquired antifungal resistance and trailing growth in Candida albicans
    • Mai A, Rotili D, Massa S et al.: Discovery of uracil-based histone deacetylase inhibitors able to reduce acquired antifungal resistance and trailing growth in Candida albicans. Bioorg. Med. Chem. Lett. 17(5), 1221-1225 (2007).
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , Issue.5 , pp. 1221-1225
    • Mai, A.1    Rotili, D.2    Massa, S.3
  • 105
    • 35448985401 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors may reduce pathogenicity and virulence in Candida albicans
    • Simonetti G, Passariello C, Rotili D, Mai A, Garaci E, Palamara AT: Histone deacetylase inhibitors may reduce pathogenicity and virulence in Candida albicans. FEMS Yeast Res. 7(8), 1371-1380 (2007).
    • (2007) FEMS Yeast Res , vol.7 , Issue.8 , pp. 1371-1380
    • Simonetti, G.1    Passariello, C.2    Rotili, D.3    Mai, A.4    Garaci, E.5    Palamara, A.T.6
  • 106
    • 71549146873 scopus 로고    scopus 로고
    • Activity of MGCD290, a Hos2 histone deacetylase inhibitor, in combination with azole antifungals against opportunistic fungal pathogens
    • Pfaller MA, Messer SA, Georgopapadakou N, Martell LA, Besterman JM, Diekema DJ: Activity of MGCD290, a Hos2 histone deacetylase inhibitor, in combination with azole antifungals against opportunistic fungal pathogens. J. Clin. Microbiol. 47(12), 3797-3804 (2009).
    • (2009) J. Clin. Microbiol , vol.47 , Issue.12 , pp. 3797-3804
    • Piatyszek, M.A..1    Messer, S.A.2    Georgopapadakou, N.3    Martell, L.A.4    Besterman, J.M.5    Diekema, D.J.6
  • 107
    • 4143089463 scopus 로고    scopus 로고
    • Administration of HDAC inhibitors to reactivate HIV-1 expression in latent cellular reservoirs: Implications for the development of therapeutic strategies
    • Demonte D, Quivy V, Colette Y, Van Lint C: Administration of HDAC inhibitors to reactivate HIV-1 expression in latent cellular reservoirs: implications for the development of therapeutic strategies. Biochem. Pharmacol. 68(6), 1231-1238 (2004).
    • (2004) Biochem. Pharmacol , vol.68 , Issue.6 , pp. 1231-1238
    • Demonte, D.1    Quivy, V.2    Colette, Y.3    Van Lint, C.4
  • 108
    • 33747162419 scopus 로고    scopus 로고
    • The regulation of HIV-1 transcription: Molecular targets for chemotherapeutic intervention
    • Stevens M, De Clercq E, Balzarini J: The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. Med. Res. Rev. 26(5), 595-625 (2006).
    • (2006) Med. Res. Rev , vol.26 , Issue.5 , pp. 595-625
    • Stevens, M.1    De Clercq, E.2    Balzarini, J.3
  • 109
    • 30444431914 scopus 로고    scopus 로고
    • NF-kB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation
    • Williams SA, Chen LF, Kwon H, Ruiz-Jarabo CM, Verdin E, Greene WC: NF-kB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation. EMBO J. 25(1), 139-149 (2006).
    • (2006) EMBO J , vol.25 , Issue.1 , pp. 139-149
    • Williams, S.A.1    Chen, L.F.2    Kwon, H.3    Ruiz-Jarabo, C.M.4    Verdin, E.5    Greene, W.C.6
  • 110
    • 35148858784 scopus 로고    scopus 로고
    • C-Myc and Sp1 contribute to proviral latency by recruiting histone deacetylase 1 to the human immunodefciency virus type 1 promoter
    • Jiang G, Espeseth A, Hazuda DJ, Margolis DM: c-Myc and Sp1 contribute to proviral latency by recruiting histone deacetylase 1 to the human immunodefciency virus type 1 promoter. J. Virol. 81(20), 10914-10923 (2007).
    • (2007) J. Virol , vol.81 , Issue.20 , pp. 10914-10923
    • Jiang, G.1    Espeseth, A.2    Hazuda, D.J.3    Margolis, D.M.4
  • 111
    • 23744500093 scopus 로고    scopus 로고
    • Depletion of latent HIV-1 infection in vivo: A proof-of-concept study
    • Lehrman G, Hogue IB, Palmer S et al.: Depletion of latent HIV-1 infection in vivo: a proof-of-concept study. Lancet 366(9485), 549-555 (2005).
    • (2005) Lancet , vol.366 , Issue.9485 , pp. 549-555
    • Lehrman, G.1    Hogue, I.B.2    Palmer, S.3
  • 112
    • 67649259174 scopus 로고    scopus 로고
    • 'Shock and kill' effects of class I-selective histone deacetylase inhibitors in combination with the glutathione synthesis inhibitor buthionine sulfoximine in cell line models for HIV-1 quiescence
    • Savarino A, Mai A, Norelli S et al.: 'Shock and kill' effects of class I-selective histone deacetylase inhibitors in combination with the glutathione synthesis inhibitor buthionine sulfoximine in cell line models for HIV-1 quiescence. Retrovirology 6, 52 (2009).
    • (2009) Retrovirology , vol.6 , pp. 52
    • Savarino, A.1    Mai, A.2    Norelli, S.3
  • 113
    • 70449365376 scopus 로고    scopus 로고
    • Reactivation of DNA viruses in association with histone deacetylase inhibitor therapy: A case series report
    • Ritchie D, Piekarz RL, Blombery P et al.: Reactivation of DNA viruses in association with histone deacetylase inhibitor therapy: a case series report. Haematologica 94(11), 1618-1622 (2009).
    • (2009) Haematologica , vol.94 , Issue.11 , pp. 1618-1622
    • Ritchie, D.1    Piekarz, R.L.2    Blombery, P.3
  • 114
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan JS, Bodai L, Pallos J et al.: Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 413(6857), 739-743 (2001).
    • (2001) Nature , vol.413 , Issue.6857 , pp. 739-743
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3
  • 115
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specifc HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos J, Bodai L, Lukacsovich T et al.: Inhibition of specifc HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17(23), 3767-3775 (2008).
    • (2008) Hum. Mol. Genet , vol.17 , Issue.23 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3
  • 116
    • 33644830913 scopus 로고    scopus 로고
    • Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity
    • Bates EA, Victor M, Jones AK, Shi Y, Hart AC: Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity. J. Neurosci. 26(10), 2830-2838 (2006).
    • (2006) J. Neurosci , vol.26 , Issue.10 , pp. 2830-2838
    • Bates, E.A.1    Victor, M.2    Jones, A.K.3    Shi, Y.4    Hart, A.C.5
  • 117
    • 31944444233 scopus 로고    scopus 로고
    • The benzamide MS-275 is a potent, long-lasting brain region-selective inhibitor of histone deacetylases
    • Simonini MV, Camargo LM, Dong E et al.: The benzamide MS-275 is a potent, long-lasting brain region-selective inhibitor of histone deacetylases. Proc. Natl Acad. Sci. USA 103(5), 1587-1592 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.5 , pp. 1587-1592
    • Simonini, M.V.1    Camargo, L.M.2    Dong, E.3
  • 118
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante RJ, Kubilus JK, Lee J et al.: Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23(28), 9418-9427 (2003).
    • (2003) J. Neurosci , vol.23 , Issue.28 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3
  • 119
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor defcits in a mouse model of Huntington's disease
    • Hockly E, Richon VM, Woodman B et al.: Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor defcits in a mouse model of Huntington's disease. Proc. Natl Acad. Sci. USA 100(4), 2041-2046 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.4 , pp. 2041-2046
    • Hockly, E.1    Richon, V.M.2    Woodman, B.3
  • 120
    • 55749103407 scopus 로고    scopus 로고
    • The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice
    • Thomas EA, Coppola G, Desplats PA et al.: The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice. Proc. Natl Acad. Sci. USA 105(40), 15564-15569 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.40 , pp. 15564-15569
    • Thomas, E.A.1    Coppola, G.2    Desplats, P.A.3
  • 121
    • 67349232749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors that target tubulin
    • Schemies J, Sippl W, Jung M: Histone deacetylase inhibitors that target tubulin. Cancer Lett. 280(2), 222-232 (2009).
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 222-232
    • Schemies, J.1    Sippl, W.2    Jung, M.3
  • 122
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, Nie Z, Batlevi Y et al.: HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447(7146), 859-863 (2007).
    • (2007) Nature , vol.447 , Issue.7146 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3
  • 123
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain a-synuclein immunoreactivity
    • Irizarry MC, Growdon W, Gomez-Isla T et al.: Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain a-synuclein immunoreactivity. J. Neuropathol. Exp. Neurol. 57(4), 334-337 (1998).
    • (1998) J. Neuropathol. Exp. Neurol , vol.57 , Issue.4 , pp. 334-337
    • Irizarry, M.C.1    Growdon, W.2    Gomez-Isla, T.3
  • 124
    • 33749583553 scopus 로고    scopus 로고
    • A-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • Kontopoulos E, Parvin JD, Feany MB: a-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum. Mol. Genet. 15(20), 3012-3023 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , Issue.20 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 125
    • 33746065340 scopus 로고    scopus 로고
    • Endogenous a-synuclein is induced by valproic acid through histone deacetylase inhibition and participates in neuroprotection against glutamate-induced excitotoxicity
    • Leng Y, Chuang DM: Endogenous a-synuclein is induced by valproic acid through histone deacetylase inhibition and participates in neuroprotection against glutamate-induced excitotoxicity. J. Neurosci. 26(28), 7502-7512 (2006).
    • (2006) J. Neurosci , vol.26 , Issue.28 , pp. 7502-7512
    • Leng, Y.1    Chuang, D.M.2
  • 127
    • 58149089923 scopus 로고    scopus 로고
    • Pimelic diphenylamide 106 is a slow, tight-binding inhibitor of class i histone deacetylases
    • Chou CJ, Herman D, Gottesfeld JM: Pimelic diphenylamide 106 is a slow, tight-binding inhibitor of class I histone deacetylases. J. Biol. Chem. 283(51), 35402-35409 (2008).
    • (2008) J. Biol. Chem , vol.283 , Issue.51 , pp. 35402-35409
    • Chou, C.J.1    Herman, D.2    Gottesfeld, J.M.3
  • 128
    • 44349114629 scopus 로고    scopus 로고
    • HDAC inhibitors correct frataxin defciency in a Friedreich ataxia mouse model
    • Rai M, Soragni E, Jenssen K et al.: HDAC inhibitors correct frataxin defciency in a Friedreich ataxia mouse model. PLoS ONE 3(4), E1958 (2008).
    • (2008) PLoS ONE , vol.3 , Issue.4
    • Rai, M.1    Soragni, E.2    Jenssen, K.3
  • 129
    • 70349163898 scopus 로고    scopus 로고
    • Chemical probes identify a role for histone deacetylase 3 in Friedreich's ataxia gene silencing
    • Xu C, Soragni E, Chou CJ et al.: Chemical probes identify a role for histone deacetylase 3 in Friedreich's ataxia gene silencing. Chem. Biol. 16(9), 980-989 (2009).
    • (2009) Chem. Biol , vol.16 , Issue.9 , pp. 980-989
    • Xu, C.1    Soragni, E.2    Chou, C.J.3
  • 130
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • Michan S, Sinclair D: Sirtuins in mammals: insights into their biological function. Biochem. J. 404(1), 1-13 (2007).
    • (2007) Biochem. J , vol.404 , Issue.1 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 131
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T, Deng CX, Mostoslavsky R: Recent progress in the biology and physiology of sirtuins. Nature 460(7255), 587-591 (2009).
    • (2009) Nature , vol.460 , Issue.7255 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 133
    • 33646550204 scopus 로고    scopus 로고
    • SIRT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis
    • Vaquero A, Scher MB, Lee DH et al.: SIRT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev. 20(10), 1256-1261 (2006).
    • (2006) Genes Dev , vol.20 , Issue.10 , pp. 1256-1261
    • Vaquero, A.1    Scher, M.B.2    Lee, D.H.3
  • 134
    • 3943054839 scopus 로고    scopus 로고
    • The SIR2 family of protein deacetylases
    • Blander G, Guarente L: The SIR2 family of protein deacetylases. Annu. Rev. Biochem. 73, 417-435 (2004).
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 135
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • Bereshchenko OR, Gu W, Dalla-Favera R: Acetylation inactivates the transcriptional repressor BCL6. Nat. Genet. 32(4), 606-613 (2002).
    • (2002) Nat. Genet , vol.32 , Issue.4 , pp. 606-613
    • Bereshchenko, O.R.1    Gu, W.2    Dalla-Favera, R.3
  • 136
    • 0035913903 scopus 로고    scopus 로고
    • HSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E et al.: hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107(2), 149-159 (2001).
    • (2001) Cell , vol.107 , Issue.2 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3
  • 137
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • Bradbury CA, Khanim FL, Hayden R et al.: Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 19(10), 1751-1759 (2005).
    • (2005) Leukemia , vol.19 , Issue.10 , pp. 1751-1759
    • Bradbury, C.A.1    Khanim, F.L.2    Hayden, R.3
  • 138
    • 13844315463 scopus 로고    scopus 로고
    • Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation
    • Kuzmichev A, Margueron R, Vaquero A et al.: Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation. Proc. Natl Acad. Sci. USA 102(6), 1859-1864 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.6 , pp. 1859-1864
    • Kuzmichev, A.1    Margueron, R.2    Vaquero, A.3
  • 139
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS et al.: Modulation of NF-kB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23(12), 2369-2380 (2004).
    • (2004) EMBO J , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3
  • 140
    • 0035914304 scopus 로고    scopus 로고
    • Identifcation of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL: Identifcation of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276(42), 38837-38843 (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.42 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 141
    • 30544445468 scopus 로고    scopus 로고
    • SIRT1 inhibitor, sirtinol, induces senescencelike growth arrest with attenuated Ras-MAPK signaling in human cancer cells
    • Ota H, Tokunaga E, Chang K et al.: SIRT1 inhibitor, sirtinol, induces senescencelike growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Oncogene 25(2), 176-185 (2006).
    • (2006) Oncogene , vol.25 , Issue.2 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3
  • 142
    • 28144438533 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (sirtuin) inhibitors
    • Mai A, Massa S, Lavu S et al.: Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (sirtuin) inhibitors. J. Med. Chem. 48(24), 7789-7795 (2005).
    • (2005) J. Med. Chem , vol.48 , Issue.24 , pp. 7789-7795
    • Mai, A.1    Massa, S.2    Lavu, S.3
  • 143
    • 60149091562 scopus 로고    scopus 로고
    • Salermide, a sirtuin inhibitor with a strong cancer-specifc proapoptotic effect
    • Lara E, Mai A, Calvanese V et al.: Salermide, a sirtuin inhibitor with a strong cancer-specifc proapoptotic effect. Oncogene 28(6), 781-791 (2009).
    • (2009) Oncogene , vol.28 , Issue.6 , pp. 781-791
    • Lara, E.1    Mai, A.2    Calvanese, V.3
  • 144
    • 29144501185 scopus 로고    scopus 로고
    • Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1
    • Napper AD, Hixon J, McDonagh T et al.: Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1. J. Med. Chem. 48(25), 8045-8054 (2005).
    • (2005) J. Med. Chem , vol.48 , Issue.25 , pp. 8045-8054
    • Napper, A.D.1    Hixon, J.2    McDonagh, T.3
  • 145
    • 33645221885 scopus 로고    scopus 로고
    • Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage
    • Solomon JM, Pasupuleti R, Xu L et al.: Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage. Mol. Cell. Biol. 26(1), 28-38 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , Issue.1 , pp. 28-38
    • Solomon, J.M.1    Pasupuleti, R.2    Xu, L.3
  • 146
    • 59649126261 scopus 로고    scopus 로고
    • Deacetylation of cortactin by SIRT1 promotes cell migration
    • Zhang Y, Zhang M, Dong H et al.: Deacetylation of cortactin by SIRT1 promotes cell migration. Oncogene 28(3), 445-460 (2009).
    • (2009) Oncogene , vol.28 , Issue.3 , pp. 445-460
    • Zhang, Y.1    Zhang, M.2    Dong, H.3
  • 147
    • 33646254136 scopus 로고    scopus 로고
    • Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes
    • Heltweg B, Gatbonton T, Schuler AD et al.: Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes. Cancer Res. 66(8), 4368-4377 (2006).
    • (2006) Cancer Res , vol.66 , Issue.8 , pp. 4368-4377
    • Heltweg, B.1    Gatbonton, T.2    Schuler, A.D.3
  • 148
    • 42949114938 scopus 로고    scopus 로고
    • Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator
    • Lain S, Hollick JJ, Campbell J et al.: Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator. Cancer Cell 13(5), 454-463 (2008).
    • (2008) Cancer Cell , vol.13 , Issue.5 , pp. 454-463
    • Lain, S.1    Hollick, J.J.2    Campbell, J.3
  • 149
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue a-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro TF, Kontopoulos E, Altmann SM et al.: Sirtuin 2 inhibitors rescue a-synuclein-mediated toxicity in models of Parkinson's disease. Science 317(5837), 516-519 (2007).
    • (2007) Science , vol.317 , Issue.5837 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3
  • 150
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by a-synuclein and synphilin-1 are cytoprotective
    • Tanaka M, Kim YM, Lee G, Junn E, Iwatsubo T, Mouradian MM: Aggresomes formed by a-synuclein and synphilin-1 are cytoprotective. J. Biol. Chem. 279(6), 4625-4631 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.6 , pp. 4625-4631
    • Tanaka, M.1    Kim, Y.M.2    Lee, G.3    Junn, E.4    Iwatsubo, T.5    Mouradian, M.M.6
  • 151
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A: Opposing activities protect against age-onset proteotoxicity. Science 313(5793), 1604-1610 (2006).
    • (2006) Science , vol.313 , Issue.5793 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 152
    • 34250848194 scopus 로고    scopus 로고
    • Mammalian Sir2-related protein (SIRT) 2-mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: A crucial role of tubulin deacetylation
    • Suzuki K, Koike T: Mammalian Sir2-related protein (SIRT) 2-mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: a crucial role of tubulin deacetylation. Neuroscience 147(3), 599-612 (2007).
    • (2007) Neuroscience , vol.147 , Issue.3 , pp. 599-612
    • Suzuki, K.1    Koike, T.2
  • 153
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert M, Spillantini MG: A century of Alzheimer's disease. Science 314(5800), 777-781 (2006).
    • (2006) Science , vol.314 , Issue.5800 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 154
    • 43749121572 scopus 로고    scopus 로고
    • Therapeutic role of sirtuins in neurodegenerative disease
    • Outeiro TF, Marques O, Kazantsev A: Therapeutic role of sirtuins in neurodegenerative disease. Biochim. Biophys. Acta 1782(6), 363-369 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1782 , Issue.6 , pp. 363-369
    • Outeiro, T.F.1    Marques, O.2    Kazantsev, A.3
  • 155
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • Kim D, Nguyen MD, Dobbin MM et al.: SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J. 26(13), 3169-3179 (2007).
    • (2007) EMBO J , vol.26 , Issue.13 , pp. 3169-3179
    • Kim, D.1    Nguyen, M.D.2    Dobbin, M.M.3
  • 156
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearance of Alzheimer's disease amyloid-b peptides
    • Marambaud P, Zhao H, Davies P: Resveratrol promotes clearance of Alzheimer's disease amyloid-b peptides. J. Biol. Chem. 280(45), 37377-37382 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.45 , pp. 37377-37382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 157
    • 41549136422 scopus 로고    scopus 로고
    • Paths of convergence: Sirtuins in aging and neurodegeneration
    • Gan L, Mucke L: Paths of convergence: sirtuins in aging and neurodegeneration. Neuron 58(1), 10-14 (2008).
    • (2008) Neuron , vol.58 , Issue.1 , pp. 10-14
    • Gan, L.1    Mucke, L.2
  • 158
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-b toxicity through inhibiting NF-kB signaling
    • Chen J, Zhou Y, Mueller-Steiner S et al.: SIRT1 protects against microglia-dependent amyloid-b toxicity through inhibiting NF-kB signaling. J. Biol. Chem. 280(48), 40364-40374 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.48 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3
  • 159
    • 44449141876 scopus 로고    scopus 로고
    • SIRT1 negatively regulates HDAC1-dependent transcriptional repression by the RBP1 family of proteins
    • Binda O, Nassif C, Branton PE: SIRT1 negatively regulates HDAC1-dependent transcriptional repression by the RBP1 family of proteins. Oncogene 27(24), 3384-3392 (2008).
    • (2008) Oncogene , vol.27 , Issue.24 , pp. 3384-3392
    • Binda, O.1    Nassif, C.2    Branton, P.E.3
  • 160
    • 71749105526 scopus 로고    scopus 로고
    • Trans-regulation of histone deacetylase activities through acetylation
    • Luo Y, Jian W, Stavreva D et al.: Trans-regulation of histone deacetylase activities through acetylation. J. Biol. Chem. 284(50), 34901-34910 (2009).
    • (2009) J. Biol. Chem , vol.284 , Issue.50 , pp. 34901-34910
    • Luo, Y.1    Jian, W.2    Stavreva, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.