메뉴 건너뛰기




Volumn 9, Issue 3, 2009, Pages 257-271

Inhibition of histone deacetylases: A pharmacological approach to the treatment of non-cancer disorders

Author keywords

[No Author keywords available]

Indexed keywords

4 PHENYLBUTYRIC ACID; 6 (1,3 DIOXO 1H,3H BENZO[DE]ISOQUINOLIN 2 YL) N HYDROXYHEXANAMIDE; ALPHA INTERFERON; ANTIRETROVIRUS AGENT; APICIDIN; BELINOSTAT; BML 210; BUTYRIC ACID; CD28 ANTIGEN; CD40 LIGAND; DEPSIPEPTIDE; GAMMA GLOBIN; HEMOGLOBIN F; HISTONE DEACETYLASE; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE INHIBITOR; INTERLEUKIN 10; M 344; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; PLACEBO; ROMIDEPSIN; SK 7041; SURVIVAL MOTOR NEURON PROTEIN 2; TRANSMEMBRANE CONDUCTANCE REGULATOR; TRAPOXIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 65449160927     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802609788085241     Document Type: Review
Times cited : (69)

References (148)
  • 1
    • 0032702598 scopus 로고    scopus 로고
    • Role of covalent modifications of histones in regulating gene expression
    • Spencer, V.; Davie, J. R. Role of covalent modifications of histones in regulating gene expression. Gene 1999, 240, 1-12.
    • (1999) Gene , vol.240 , pp. 1-12
    • Spencer, V.1    Davie, J.R.2
  • 2
    • 20344392202 scopus 로고    scopus 로고
    • Epigenetics-an epicenter of gene regulation: Histones and histone-modifying enzymes
    • Biel, M., Wascholowski, V.; Giannis, A. Epigenetics-an epicenter of gene regulation: Histones and histone-modifying enzymes. Angew. Chem. Int. Ed. 2005, 44, 3186-3216.
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 3186-3216
    • Biel, M.1    Wascholowski, V.2    Giannis, A.3
  • 3
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 1997, 389, 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 4
    • 0034387004 scopus 로고    scopus 로고
    • 25 years after the nucleosome model: Chromatin modifications
    • Wu, J.; Grunstein, M. 25 years after the nucleosome model: chromatin modifications. Trends Biochem. Sci. 2000, 25, 619-623.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 619-623
    • Wu, J.1    Grunstein, M.2
  • 5
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J. E.; Peart, M. J., Johnstone, R.W. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Disc. 2006, 5, 769-784.
    • (2006) Nat. Rev. Drug Disc , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 6
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti, L.; Lee, Y.; Goodson, H. V. Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis. J. Mol. Biol. 2004, 17-31.
    • (2004) J. Mol. Biol , vol.17
    • Gregoretti, L.1    Lee, Y.2    Goodson, H.V.3
  • 7
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • van Lint, C.; Emiliani, S.; Verdin, E. The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr. 1996, 5, 245-253.
    • (1996) Gene Expr , vol.5 , pp. 245-253
    • van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 9
    • 33746328957 scopus 로고    scopus 로고
    • Signaling pathways in skeletal muscle remodeling
    • Bassel-Duby, R.; Olsen, E. N. Signaling pathways in skeletal muscle remodeling. Annu. Rev. Biochem. 2006, 75, 19-37.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 19-37
    • Bassel-Duby, R.1    Olsen, E.N.2
  • 10
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: From sequence to function, regulation, and clinical implication
    • Yang, X.-J.; Gregoire, S. Class II histone deacetylases: from sequence to function, regulation, and clinical implication. Mol. Cell Biol. 2005, 25, 2873-2884.
    • (2005) Mol. Cell Biol , vol.25 , pp. 2873-2884
    • Yang, X.-J.1    Gregoire, S.2
  • 11
    • 0017767153 scopus 로고
    • n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
    • Riggs, M. J.; Whittaker, R. G.; Neumann, J. R.; Ingram, V. M. n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 1977, 268, 462-464.
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.J.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 12
    • 0017898940 scopus 로고
    • Suppression of histone deacetylation in vivo and in vitro by sodium butyrate
    • Boffa, L. C.; Vidali, G.; Mann, R. S.; Allfrey, V. G. Suppression of histone deacetylation in vivo and in vitro by sodium butyrate. J. Biol. Chem. 1978, 253, 3364-3366.
    • (1978) J. Biol. Chem , vol.253 , pp. 3364-3366
    • Boffa, L.C.1    Vidali, G.2    Mann, R.S.3    Allfrey, V.G.4
  • 13
    • 0017291238 scopus 로고
    • Effect of sodium butyrate on mammalian cells in culture: A review
    • Prasad, K. N.; Sinha, P. K. Effect of sodium butyrate on mammalian cells in culture: a review. In Vitro 1976, 12, 125-132.
    • (1976) In Vitro , vol.12 , pp. 125-132
    • Prasad, K.N.1    Sinha, P.K.2
  • 14
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M.; Kijima, M.; Akita, M.; Beppu, T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 1990, 265, 17174-17179.
    • (1990) J. Biol. Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 16
    • 34547122494 scopus 로고    scopus 로고
    • HDAC inhibitors: Clinical update and mechanism-based potential
    • Glaser, K. B. HDAC inhibitors: Clinical update and mechanism-based potential. Biochem. Pharmacol. 2007, 74, 659-671.
    • (2007) Biochem. Pharmacol , vol.74 , pp. 659-671
    • Glaser, K.B.1
  • 17
    • 43049119236 scopus 로고    scopus 로고
    • The use of diversity profiling to characterize chemical modulators of the histone deacetylases
    • Blackwell, L.; Norris, J.; Suto, C. M.; Janzen, W. P. The use of diversity profiling to characterize chemical modulators of the histone deacetylases. Life Sci. 2008, 82, 1050-1058.
    • (2008) Life Sci , vol.82 , pp. 1050-1058
    • Blackwell, L.1    Norris, J.2    Suto, C.M.3    Janzen, W.P.4
  • 18
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P. A.; Breslow, R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol. 2007, 25, 84-90.
    • (2007) Nat. Biotechnol , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 19
    • 41149089267 scopus 로고    scopus 로고
    • Histone deacetylase Inhibitors: From bench to clinic
    • Paris, D.; Porcelloni, M.; Binaschi, M.; Fattori, D. Histone deacetylase Inhibitors: from bench to clinic. J. Med. Chem. 2008, 51, 1505-1529.
    • (2008) J. Med. Chem , vol.51 , pp. 1505-1529
    • Paris, D.1    Porcelloni, M.2    Binaschi, M.3    Fattori, D.4
  • 20
    • 33748509517 scopus 로고    scopus 로고
    • Recent advances in medicinal chemistry of histone deacetylase inhibitors
    • Weinmann, H.; Ottow, E. Recent advances in medicinal chemistry of histone deacetylase inhibitors. Ann. Rep. Med. Chem. 2004, 39, 185-196.
    • (2004) Ann. Rep. Med. Chem , vol.39 , pp. 185-196
    • Weinmann, H.1    Ottow, E.2
  • 21
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev, A. G.; Thompson, L. M. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat. Rev. Drug Discov. 2008, 7,854-868.
    • (2008) Nat. Rev. Drug Discov , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 23
    • 65449178260 scopus 로고
    • The effect of amelioration of anemia by the synthesis of fetal hemoglobin in sickle cell anemia
    • Reed, L. J.; Bradley, T. B.; Ranney, H. M. The effect of amelioration of anemia by the synthesis of fetal hemoglobin in sickle cell anemia. Blood 1965, 25, 37-43.
    • (1965) Blood , vol.25 , pp. 37-43
    • Reed, L.J.1    Bradley, T.B.2    Ranney, H.M.3
  • 24
    • 0020961106 scopus 로고
    • Developmental genetics of the human hemoglobins
    • Wood, W. G.; Weatherall, D. J. Developmental genetics of the human hemoglobins. Biochem. J. 1983, 215, 1-9.
    • (1983) Biochem. J , vol.215 , pp. 1-9
    • Wood, W.G.1    Weatherall, D.J.2
  • 25
    • 0024334257 scopus 로고
    • Sodium butyrate enhances fetal globin gene expression in erythroid progenitors of patients with Hb SS and β-thalassemia
    • Perrine, S. P.; Faller, D. V.; Cohen, R.; Vichinsky, E. P.; Hurst, D.; Lubin, B. H.; Papayannopoulou, T. Sodium butyrate enhances fetal globin gene expression in erythroid progenitors of patients with Hb SS and β-thalassemia. Blood 1989, 74, 454-459.
    • (1989) Blood , vol.74 , pp. 454-459
    • Perrine, S.P.1    Faller, D.V.2    Cohen, R.3    Vichinsky, E.P.4    Hurst, D.5    Lubin, B.H.6    Papayannopoulou, T.7
  • 27
    • 0026710710 scopus 로고
    • Increased fetal hemoglobin in patients receiving sodium-4-phenylbutyrate
    • Dover, G. J.; Brusilow, S. W.; Samid, D. Increased fetal hemoglobin in patients receiving sodium-4-phenylbutyrate. N. Engl. J. Med. 1992, 327, 569-570.
    • (1992) N. Engl. J. Med , vol.327 , pp. 569-570
    • Dover, G.J.1    Brusilow, S.W.2    Samid, D.3
  • 28
    • 0028303870 scopus 로고
    • Induction of fetal hemoglobin production in subjects with sickle cell anemia by oral sodium phenylbutyrate
    • Dover, G.; Brusilow, S.; Charache, S. Induction of fetal hemoglobin production in subjects with sickle cell anemia by oral sodium phenylbutyrate. Blood 1994, 84, 339-343.
    • (1994) Blood , vol.84 , pp. 339-343
    • Dover, G.1    Brusilow, S.2    Charache, S.3
  • 30
    • 85088670369 scopus 로고
    • Increased fetal hemoglobin in patients receiving valproic acid for epilepsy
    • Collins, A. F.; Luban, N. L. C.; Dover, G. Increased fetal hemoglobin in patients receiving valproic acid for epilepsy. Blood 1994, 84, 1690-1691.
    • (1994) Blood , vol.84 , pp. 1690-1691
    • Collins, A.F.1    Luban, N.L.C.2    Dover, G.3
  • 31
    • 0030856601 scopus 로고    scopus 로고
    • Valproic acid augmentation of fetal hemoglobin in individuals with and without sickle cell disease
    • Selby, R.; Nisbet-Brown, E.; Basran, R. K.; Chang, L.; Olivieri, N. F. Valproic acid augmentation of fetal hemoglobin in individuals with and without sickle cell disease. Blood 1997, 90, 891-893.
    • (1997) Blood , vol.90 , pp. 891-893
    • Selby, R.1    Nisbet-Brown, E.2    Basran, R.K.3    Chang, L.4    Olivieri, N.F.5
  • 32
    • 0030923438 scopus 로고    scopus 로고
    • Induction of gamma-globin by histone deacetylase inhibitors
    • McCaffrey, P. G.; Newsome, D. A.; Fibach, E.; Yoshida, M.; Su, M. S.-S. Induction of gamma-globin by histone deacetylase inhibitors. Blood 1997, 90, 2075-2083.
    • (1997) Blood , vol.90 , pp. 2075-2083
    • McCaffrey, P.G.1    Newsome, D.A.2    Fibach, E.3    Yoshida, M.4    Su, M.S.-S.5
  • 33
    • 33845244613 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FK228 is a potent inducer of human fetal hemoglobin
    • Cao, H.; Stamatoyannopoulos, G. Histone deacetylase inhibitor FK228 is a potent inducer of human fetal hemoglobin. Am. J. Hematol. 2006, 81, 981-983.
    • (2006) Am. J. Hematol , vol.81 , pp. 981-983
    • Cao, H.1    Stamatoyannopoulos, G.2
  • 36
    • 35148884369 scopus 로고    scopus 로고
    • Mechanisms of human gamma-globin transcritpional induction by apicidin involves p38 signalling to chromatin
    • Wei, G. H.; Zhao, G. W.; Song, W.; Hao, D. L.; Lv, X.; Liu, D. P.; Liang, C. C. Mechanisms of human gamma-globin transcritpional induction by apicidin involves p38 signalling to chromatin. Biophs. Res. Commun. 2007, 363, 889-894.
    • (2007) Biophs. Res. Commun , vol.363 , pp. 889-894
    • Wei, G.H.1    Zhao, G.W.2    Song, W.3    Hao, D.L.4    Lv, X.5    Liu, D.P.6    Liang, C.C.7
  • 37
    • 33751293605 scopus 로고    scopus 로고
    • Mechanism for fetal hemoglobin induction by histone deacetylase inhibitors involves γ-globin activation by CREB1 and ATF-2
    • Sangeman, J.; Lee, M. S.; Yao, X.; Oteng, E.; Hsiao, C. H.; Li, W.; Zein, S.; Ofori-Acquah, S. F.; Pace, B. Mechanism for fetal hemoglobin induction by histone deacetylase inhibitors involves γ-globin activation by CREB1 and ATF-2. Blood 2006, 108, 3590-3599.
    • (2006) Blood , vol.108 , pp. 3590-3599
    • Sangeman, J.1    Lee, M.S.2    Yao, X.3    Oteng, E.4    Hsiao, C.H.5    Li, W.6    Zein, S.7    Ofori-Acquah, S.F.8    Pace, B.9
  • 38
    • 65449179407 scopus 로고    scopus 로고
    • Pulsed-dosing with sodium phenylbutryrate increases Hemglobin F in a patient with sickle cell anemia
    • Hines, P.; Dover, G. J.; Resar, L. M. Pulsed-dosing with sodium phenylbutryrate increases Hemglobin F in a patient with sickle cell anemia. Pediatr. Blood Cancer 2007.
    • (2007) Pediatr. Blood Cancer
    • Hines, P.1    Dover, G.J.2    Resar, L.M.3
  • 39
    • 29744453274 scopus 로고    scopus 로고
    • Pharmacological induction of fetal hemoglobin. Why haven't we been more successful in thalassemia?
    • Fathallah, H.; Sutton, M.; Atweh, G. F. Pharmacological induction of fetal hemoglobin. Why haven't we been more successful in thalassemia?. Ann. N. Y. Acad. Sci. 2005, 1054, 228-237.
    • (2005) Ann. N. Y. Acad. Sci , vol.1054 , pp. 228-237
    • Fathallah, H.1    Sutton, M.2    Atweh, G.F.3
  • 40
    • 0030809817 scopus 로고    scopus 로고
    • In vitro pharamcologic restoration of CFTR-mediated chloride transport with sodium phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR
    • Rubenstein, R. C.; Zeitlin, P. L. In vitro pharamcologic restoration of CFTR-mediated chloride transport with sodium phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR. J. Clin. Invest. 1997, 100, 2457-2465.
    • (1997) J. Clin. Invest , vol.100 , pp. 2457-2465
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 41
    • 0034099743 scopus 로고    scopus 로고
    • Sodium-4-phenylbutyrate downregulates Hsc70: Implications for intracellular trafficking of Delta F508CFTR
    • Rubenstein, R. C.; Zeitlin, P. L. Sodium-4-phenylbutyrate downregulates Hsc70: implications for intracellular trafficking of Delta F508CFTR. Am. J. Physiol. Cell Physiol. 2000, 278, C259-C267.
    • (2000) Am. J. Physiol. Cell Physiol , vol.278
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 42
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of sodium phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrotic patients: Evidence of restoration of nasal epithelial CFTR function
    • Rubenstein, R. C.; Zeitlin, P. L. A pilot clinical trial of sodium phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrotic patients: evidence of restoration of nasal epithelial CFTR function. Am. J. Resp. Crit. Care Med. 1998, 157, 484-490.
    • (1998) Am. J. Resp. Crit. Care Med , vol.157 , pp. 484-490
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 43
    • 1442331948 scopus 로고    scopus 로고
    • Gene expression profile analysis of 4-phenylbutyrate treatment of IB3-1 bronchial epithelial cell line demonstrates a major influence on heat-shock proteins
    • Wright, J. M.; Zeitlin, P. L.; Cebotaru, L.; Guggino, S. E.; Guggino, W. B. Gene expression profile analysis of 4-phenylbutyrate treatment of IB3-1 bronchial epithelial cell line demonstrates a major influence on heat-shock proteins. Physiol. Genomics. 2004, 16, 204-211.
    • (2004) Physiol. Genomics , vol.16 , pp. 204-211
    • Wright, J.M.1    Zeitlin, P.L.2    Cebotaru, L.3    Guggino, S.E.4    Guggino, W.B.5
  • 44
    • 46749108883 scopus 로고    scopus 로고
    • Chemical rescue of deltaF508-CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells
    • Singh, O. V.; Pollard, H. B.; Zeitlin, P. Chemical rescue of deltaF508-CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells. Mol. Cell Proteomics 2008, 7, 1099-1110.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 1099-1110
    • Singh, O.V.1    Pollard, H.B.2    Zeitlin, P.3
  • 45
    • 0033583306 scopus 로고    scopus 로고
    • Transcriptional repression of the cystic fibrosis transmembrane conductance regulator gene, mediated by CCAAT displacement protein/cut homolog, is associated with histone deacetylation
    • Li, S.; Moy, L.; Pittman, N.; Shue, G.; Aufiero, B.; Neufeld, E. J.; LeLeiko, N. S.; Walsh, M. J. Transcriptional repression of the cystic fibrosis transmembrane conductance regulator gene, mediated by CCAAT displacement protein/cut homolog, is associated with histone deacetylation. J. Biol. Chem. 1999, 274, 7803-7815.
    • (1999) J. Biol. Chem , vol.274 , pp. 7803-7815
    • Li, S.1    Moy, L.2    Pittman, N.3    Shue, G.4    Aufiero, B.5    Neufeld, E.J.6    LeLeiko, N.S.7    Walsh, M.J.8
  • 46
    • 37549046411 scopus 로고    scopus 로고
    • The epigenetic signature of CFTR expression is co-ordinated via chromatin acetylation through a complex intronic element
    • Paul, T.; Li, S.; Khurana, S.; Leliko, N. S.; Walsh, M. J. The epigenetic signature of CFTR expression is co-ordinated via chromatin acetylation through a complex intronic element. Biochem. J. 2007, 408, 317-326.
    • (2007) Biochem. J , vol.408 , pp. 317-326
    • Paul, T.1    Li, S.2    Khurana, S.3    Leliko, N.S.4    Walsh, M.J.5
  • 48
    • 0034059821 scopus 로고    scopus 로고
    • Pharmacological induction of peroxisomes in peroxisome biogenesis disorders
    • Wei, H.; Kemp, S.; McGuinness, M. C.; Moser, A. B.; Smith, K. D. Pharmacological induction of peroxisomes in peroxisome biogenesis disorders. Ann. Neurol. 2000, 47, 286-296.
    • (2000) Ann. Neurol , vol.47 , pp. 286-296
    • Wei, H.1    Kemp, S.2    McGuinness, M.C.3    Moser, A.B.4    Smith, K.D.5
  • 50
    • 0034798513 scopus 로고    scopus 로고
    • Evaluation of pharmacological induction of fatty acid oxidation in X-linked adrenoleukodystrophy
    • McGuiness, M. C.; Zhang, H.-P.; Smith, K. D. Evaluation of pharmacological induction of fatty acid oxidation in X-linked adrenoleukodystrophy. Mol. Gen. Met. 2001, 74, 256-263.
    • (2001) Mol. Gen. Met , vol.74 , pp. 256-263
    • McGuiness, M.C.1    Zhang, H.-P.2    Smith, K.D.3
  • 51
    • 0037188532 scopus 로고    scopus 로고
    • Stage-specific modualtion of skeletal muscle myogenesis by inhibitors of nuclear deacetylases
    • Iezzi, S.; Cossu, G.; Nervi, C.; Sartorelli, V.; Puri, P. L. Stage-specific modualtion of skeletal muscle myogenesis by inhibitors of nuclear deacetylases. Proc. Nat. Acad. Sci. 2002, 99, 7757-7762.
    • (2002) Proc. Nat. Acad. Sci , vol.99 , pp. 7757-7762
    • Iezzi, S.1    Cossu, G.2    Nervi, C.3    Sartorelli, V.4    Puri, P.L.5
  • 52
    • 2342627231 scopus 로고    scopus 로고
    • Deacetylase inhibitors increase muscle cell size by promoting myoblast recruitment and fusion through induction of follistatin
    • Iezzi, S.; Di Padova, M.; Serra, C.; Caretti, G.; Simone, C.; Maklan, E.; Minetti, G.; Zhao, P.; Hoffman, E. P.; Puri, P. L. Deacetylase inhibitors increase muscle cell size by promoting myoblast recruitment and fusion through induction of follistatin. Dev. Cell 2004, 6, 673-684.
    • (2004) Dev. Cell , vol.6 , pp. 673-684
    • Iezzi, S.1    Di Padova, M.2    Serra, C.3    Caretti, G.4    Simone, C.5    Maklan, E.6    Minetti, G.7    Zhao, P.8    Hoffman, E.P.9    Puri, P.L.10
  • 54
    • 65449182964 scopus 로고    scopus 로고
    • Panozzo, C.; Frugier, T.; Cifuentes-Diaz, C.; Melki, J. Spinal muscular atrophy. In: The Metabolic & Molecular Bases of Inherited Disease, IV. 8th ed 2001, Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Childs, B., Kinzler, K.W., Vogelstein, B. Eds., McGraw-Hill: New York, 5833-5843.
    • Panozzo, C.; Frugier, T.; Cifuentes-Diaz, C.; Melki, J. Spinal muscular atrophy. In: The Metabolic & Molecular Bases of Inherited Disease, Vol. IV. 8th ed 2001, Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Childs, B., Kinzler, K.W., Vogelstein, B. Eds., McGraw-Hill: New York, 5833-5843.
  • 57
    • 65449117076 scopus 로고    scopus 로고
    • Valproic acid increases the SMN2 protein level: A well-known drug as a potential therapy for spinal muscular atrophy
    • Brichta, L.; Hofmann, E.; Hahnen, E.; Siebzernrubl, F. A.; Raschke, H.; Blumcke, I.; Eyupoglu, I. Y.; Wirth, B. Valproic acid increases the SMN2 protein level: a well-known drug as a potential therapy for spinal muscular atrophy. Ann. Neurol. 2003, 59, 970-975.
    • (2003) Ann. Neurol , vol.59 , pp. 970-975
    • Brichta, L.1    Hofmann, E.2    Hahnen, E.3    Siebzernrubl, F.A.4    Raschke, H.5    Blumcke, I.6    Eyupoglu, I.Y.7    Wirth, B.8
  • 58
    • 33744803707 scopus 로고    scopus 로고
    • In vivo activation of SMN in spinal muscular atrophy carriers and patients treated with valproate
    • Brichta, L.; Holker, I.; Haug, K.; Klockgetter, T.; Wirth, B. In vivo activation of SMN in spinal muscular atrophy carriers and patients treated with valproate. Ann. Neurol. 2006, 59, 970-975.
    • (2006) Ann. Neurol , vol.59 , pp. 970-975
    • Brichta, L.1    Holker, I.2    Haug, K.3    Klockgetter, T.4    Wirth, B.5
  • 60
    • 0043092414 scopus 로고    scopus 로고
    • The Hammersmith functional motor scale for children with spinal muscular atrophy: A scale to test ability and monitor progress in children with limited ambulation
    • Main, M.; Kairon, H.; Mercuri, E.; Muntoni, F. The Hammersmith functional motor scale for children with spinal muscular atrophy: a scale to test ability and monitor progress in children with limited ambulation. Eur. J. Paediatr. Neurol. 2003, 7, 155-159.
    • (2003) Eur. J. Paediatr. Neurol , vol.7 , pp. 155-159
    • Main, M.1    Kairon, H.2    Mercuri, E.3    Muntoni, F.4
  • 63
    • 33745686137 scopus 로고    scopus 로고
    • The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/ protein levels in spinal muscular atrophy cells
    • Riessland, M.; Brichta, L.; Hahnen, E.; Wirth, B. The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/ protein levels in spinal muscular atrophy cells. Hum. Genet. 2006, 120, 101-110.
    • (2006) Hum. Genet , vol.120 , pp. 101-110
    • Riessland, M.1    Brichta, L.2    Hahnen, E.3    Wirth, B.4
  • 67
    • 34548301409 scopus 로고    scopus 로고
    • Histone deacetylases: Focus on the nervous system
    • Morrison, R. E.; Majdzadeh, N.; D'Mello, S. R. Histone deacetylases: Focus on the nervous system. Cell Mol. Life Sci. 2007, 64, 2258-2269.
    • (2007) Cell Mol. Life Sci , vol.64 , pp. 2258-2269
    • Morrison, R.E.1    Majdzadeh, N.2    D'Mello, S.R.3
  • 68
    • 47249095889 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Therapeutic agents and research tools for deciphering motor neuron diseases
    • Echaniz-Laguna, A.; Bousiges, O.; Loeffler, J.-P.; Boutllier, A.-L. Histone deacetylase inhibitors: Therapeutic agents and research tools for deciphering motor neuron diseases. Curr. Med. Chem. 2008, 15, 1263-1273.
    • (2008) Curr. Med. Chem , vol.15 , pp. 1263-1273
    • Echaniz-Laguna, A.1    Bousiges, O.2    Loeffler, J.-P.3    Boutllier, A.-L.4
  • 69
    • 0011876588 scopus 로고    scopus 로고
    • Huntington disease
    • 8th ed. Scriver, C.R, Beaudet, A.L, Sly, W.S, Valle, D, Childs, B, Kinzler, K.W, Vogelstein, B. Eds, McGraw-Hill: New York
    • Hayden, M. R.; Kremer, B. Huntington disease. In: The Metabolic & Molecular Bases of Inherited Disease, Vol. IV. 8th ed. Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Childs, B., Kinzler, K.W., Vogelstein, B. Eds.; 2001, McGraw-Hill: New York, 5677-5701.
    • (2001) The Metabolic & Molecular Bases of Inherited Disease , vol.4 , pp. 5677-5701
    • Hayden, M.R.1    Kremer, B.2
  • 72
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante, R. J.; Kubilus, J. K.; Lee, J.; Ryu, H.; Beesen, A.; Zucker, B.; Smith, K.; Kowall, N. W.; Ratan, R. R.; Luthi-Carter, R. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 2003, 23, 9418-9427.
    • (2003) J. Neurosci , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3    Ryu, H.4    Beesen, A.5    Zucker, B.6    Smith, K.7    Kowall, N.W.8    Ratan, R.R.9    Luthi-Carter, R.10
  • 75
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J. P.; Godin, J. D.; Charrin, B. C.; Cordelières, F. P.; King, S. J.; Humbert, S.; Saudou, F. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 2007, 27, 3571-3583.
    • (2007) J. Neurosci , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelières, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 77
    • 30044442933 scopus 로고    scopus 로고
    • Class II histone deacetylases confer signal responsiveness to the ankyrin-repeat proteins ANKRA2 and RFXANK
    • McKinsey, T. A.; Kuwahara, K.; Bezprozvannaya, S.; Olson, E. N. Class II histone deacetylases confer signal responsiveness to the ankyrin-repeat proteins ANKRA2 and RFXANK. Mol. Biol. Cell 2006, 17, 438-447.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 438-447
    • McKinsey, T.A.1    Kuwahara, K.2    Bezprozvannaya, S.3    Olson, E.N.4
  • 78
    • 0034635987 scopus 로고    scopus 로고
    • Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases
    • Lu, J.; McKinsey, T. A.; Olson, E. N. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc. Nat. Acad. Sci. 2000, 97, 4070-4075.
    • (2000) Proc. Nat. Acad. Sci , vol.97 , pp. 4070-4075
    • Lu, J.1    McKinsey, T.A.2    Olson, E.N.3
  • 79
    • 0037470133 scopus 로고    scopus 로고
    • The transcriptional co-activators CREB-binding protein (CBP) and p300 play a critical role in cardiac hypertrophy that is dependent on their histone acetyltransferase activity
    • Gusterson, R. J.; Jazrawi, E.; Adcock, I. M.; Latchman, D. S. The transcriptional co-activators CREB-binding protein (CBP) and p300 play a critical role in cardiac hypertrophy that is dependent on their histone acetyltransferase activity. J. Biol. Chem. 2003, 278, 6838-6847.
    • (2003) J. Biol. Chem , vol.278 , pp. 6838-6847
    • Gusterson, R.J.1    Jazrawi, E.2    Adcock, I.M.3    Latchman, D.S.4
  • 81
    • 85047694248 scopus 로고    scopus 로고
    • Cardiac hypertrophy and histone deacetylase-dependent transcritiptional repression mediated by the atypical homeodomain protein Hop
    • Kook, H.; Lepore, J. J.; Gitler, A. D.; Lu, M. M.; Yung, W. W.-M.; Mackay, J.; Zhou, R.; Ferrari, V.; Gruber, P.; Epstein, J. A. Cardiac hypertrophy and histone deacetylase-dependent transcritiptional repression mediated by the atypical homeodomain protein Hop. J. Clin. Invest. 2003, 112, 863-871.
    • (2003) J. Clin. Invest , vol.112 , pp. 863-871
    • Kook, H.1    Lepore, J.J.2    Gitler, A.D.3    Lu, M.M.4    Yung, W.W.-M.5    Mackay, J.6    Zhou, R.7    Ferrari, V.8    Gruber, P.9    Epstein, J.A.10
  • 82
    • 33745173485 scopus 로고    scopus 로고
    • Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy
    • Kong, Y.; Tannous, P.; Lu, G.; Berenji, K.; Rothermel, B. A.; Olson, E. N.; Hill, J. A. Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy. Circulation 2006, 113, 2579-2588.
    • (2006) Circulation , vol.113 , pp. 2579-2588
    • Kong, Y.1    Tannous, P.2    Lu, G.3    Berenji, K.4    Rothermel, B.A.5    Olson, E.N.6    Hill, J.A.7
  • 83
    • 33644861578 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation blocks cardiac hypertrophy induced by angiotensin II infusion and aortic banding
    • Kee, H. J.; Sohn, I. S.; Nam, K. I.; Park, J. E.; Qian, Y. R.; Yin, Z.; Ahn, Y.; Jeong, M. H.; Bang, Y. J.; Kim, N. Inhibition of histone deacetylation blocks cardiac hypertrophy induced by angiotensin II infusion and aortic banding. Circulation 2006, 113, 51-59.
    • (2006) Circulation , vol.113 , pp. 51-59
    • Kee, H.J.1    Sohn, I.S.2    Nam, K.I.3    Park, J.E.4    Qian, Y.R.5    Yin, Z.6    Ahn, Y.7    Jeong, M.H.8    Bang, Y.J.9    Kim, N.10
  • 84
    • 3042651448 scopus 로고    scopus 로고
    • Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: Potential roles of histone deacetylase inhibition and heat shock protein induction
    • Ren, M.; Leng, Y.; Jeong, M.; Leeds, P. R.; Chuang, D. M. Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction. J. Neurochem. 2004, 89, 1358-1367.
    • (2004) J. Neurochem , vol.89 , pp. 1358-1367
    • Ren, M.1    Leng, Y.2    Jeong, M.3    Leeds, P.R.4    Chuang, D.M.5
  • 85
    • 33751120697 scopus 로고    scopus 로고
    • Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain
    • Faraco, G.; Pancani, T.; Formentini, L.; Mascagni, P.; Fossati, G.; Leoni, F.; Moroni, F.; Chiarugi, A. Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain. Mol. Pharmacol. 2006, 70, 1876-1884.
    • (2006) Mol. Pharmacol , vol.70 , pp. 1876-1884
    • Faraco, G.1    Pancani, T.2    Formentini, L.3    Mascagni, P.4    Fossati, G.5    Leoni, F.6    Moroni, F.7    Chiarugi, A.8
  • 87
    • 33645001027 scopus 로고    scopus 로고
    • Cardiac histones are substrates of histone deacetylase activity in hemorrhagic shock and resuscitation
    • Lin, T.; Alam, H. B.; Chen, H.; Britten-Webb, J.; Rhee, P.; Kirkpatrick, J.; Koustova, E. Cardiac histones are substrates of histone deacetylase activity in hemorrhagic shock and resuscitation. Surgery 2006, 139, 365-376.
    • (2006) Surgery , vol.139 , pp. 365-376
    • Lin, T.1    Alam, H.B.2    Chen, H.3    Britten-Webb, J.4    Rhee, P.5    Kirkpatrick, J.6    Koustova, E.7
  • 88
    • 35548942629 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury
    • Zhao, T. C.; Cheng, G.; Zhang, L. X.; Tseng, Y. T.; Padbury, J. F. Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury. Cardiovasc. Res. 2007, 76, 473-481.
    • (2007) Cardiovasc. Res , vol.76 , pp. 473-481
    • Zhao, T.C.1    Cheng, G.2    Zhang, L.X.3    Tseng, Y.T.4    Padbury, J.F.5
  • 89
    • 34147199586 scopus 로고    scopus 로고
    • Valproic acid-mediated neuroprotection in intracerebral hemorrhage via histone deacetylase inhibition and transcriptional activation
    • Sinn, D. I.; Kim, S. J.; Chu, K.; Jung, K. H.; Lee, S. T.; Song, E. C.; Kim, J. M.; Park, D. K.; Kun Lee, S.; Kim, M. Valproic acid-mediated neuroprotection in intracerebral hemorrhage via histone deacetylase inhibition and transcriptional activation. Neurobiol. Dis. 2007, 26, 464-472.
    • (2007) Neurobiol. Dis , vol.26 , pp. 464-472
    • Sinn, D.I.1    Kim, S.J.2    Chu, K.3    Jung, K.H.4    Lee, S.T.5    Song, E.C.6    Kim, J.M.7    Park, D.K.8    Kun Lee, S.9    Kim, M.10
  • 90
    • 34248530339 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: Multiple mechanisms of action
    • Kim, H. J.; Rowe, M.; Ren, M.; Hong, J. S.; Chen, P. S.; Chuang, D. M. Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: multiple mechanisms of action. J. Pharmacol. Exp. Ther. 2007, 321, 892-901.
    • (2007) J. Pharmacol. Exp. Ther , vol.321 , pp. 892-901
    • Kim, H.J.1    Rowe, M.2    Ren, M.3    Hong, J.S.4    Chen, P.S.5    Chuang, D.M.6
  • 91
    • 0035957015 scopus 로고    scopus 로고
    • Trichostatin A reverses skewed expression of CD 154, interleukin, and interferon- gene and protein expression in lupus T cells
    • Mishra, N.; Brown, D. R.; Olorenshaw, I. M.; Kammer, G. M. Trichostatin A reverses skewed expression of CD 154, interleukin, and interferon- gene and protein expression in lupus T cells. Proc. Nat. Acad. Sci. 2001, 98, 2628-2633.
    • (2001) Proc. Nat. Acad. Sci , vol.98 , pp. 2628-2633
    • Mishra, N.1    Brown, D.R.2    Olorenshaw, I.M.3    Kammer, G.M.4
  • 93
    • 0037330279 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors modulate renal disease in the MRL-1pr/1pr mouse
    • Mishra, N.; Reilly, C. M.; Brown, D. R.; Ruiz, P.; Gilkeson, G. S. Histone deacetylase inhibitors modulate renal disease in the MRL-1pr/1pr mouse. J. Clin. Invest. 2003, 111, 539-552.
    • (2003) J. Clin. Invest , vol.111 , pp. 539-552
    • Mishra, N.1    Reilly, C.M.2    Brown, D.R.3    Ruiz, P.4    Gilkeson, G.S.5
  • 94
    • 29144491494 scopus 로고    scopus 로고
    • Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition
    • Garcia, B. A.; Busby, S. A.; Shabanowitz, J.; Hunt, D. F.; Mishra, N. Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition.. J. Proteome Res. 2005, 4, 2032-2042.
    • (2005) J. Proteome Res , vol.4 , pp. 2032-2042
    • Garcia, B.A.1    Busby, S.A.2    Shabanowitz, J.3    Hunt, D.F.4    Mishra, N.5
  • 95
    • 0037356314 scopus 로고    scopus 로고
    • Reservoirs, sanctuaries and residual disease: The hiding spots of HIV-1
    • Pomerantz, R. J. Reservoirs, sanctuaries and residual disease: the hiding spots of HIV-1. HIV Clin. Trials 2003, 4, 137-143.
    • (2003) HIV Clin. Trials , vol.4 , pp. 137-143
    • Pomerantz, R.J.1
  • 97
    • 30444431914 scopus 로고    scopus 로고
    • NF-kappaB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation
    • Williams, S. A.; Chen, L. F.; Kwon, H.; Ruiz-Jarabo, C. M.; Verdin, E.; Greene, W. C. NF-kappaB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation. EMBO J. 2007, 25, 139-149.
    • (2007) EMBO J , vol.25 , 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
  • 100
    • 0037465638 scopus 로고    scopus 로고
    • Anti-parasitic activity of depudecin on Neospora caninum via the inhibition of histone deacetylase
    • Kwon, H. J.; Kim, J. H.; Kim, M.; Lee, J. K.; Hwang, W. S.; Kim, D. Y. Anti-parasitic activity of depudecin on Neospora caninum via the inhibition of histone deacetylase. Vet. Parasitol. 2003, 112, 269-276.
    • (2003) Vet. Parasitol , vol.112 , pp. 269-276
    • Kwon, H.J.1    Kim, J.H.2    Kim, M.3    Lee, J.K.4    Hwang, W.S.5    Kim, D.Y.6
  • 101
    • 10544250252 scopus 로고    scopus 로고
    • Darkin-Rattray, S. J.; Gurnett, A. M.; Myers, R. W.; Dulski, P. M.; Crumley, T. M.; Allocco, J. J.; Cannova, C.; Meinke, P. T.; Colletti, S. L.; Bednarek, M. A. Apicidin: a novel anti-protozoal agent that inhibits parasite histone deactylase. Proc. Nat. Acad. Sci. 1996, 93, 13143-13147.
    • Darkin-Rattray, S. J.; Gurnett, A. M.; Myers, R. W.; Dulski, P. M.; Crumley, T. M.; Allocco, J. J.; Cannova, C.; Meinke, P. T.; Colletti, S. L.; Bednarek, M. A. Apicidin: a novel anti-protozoal agent that inhibits parasite histone deactylase. Proc. Nat. Acad. Sci. 1996, 93, 13143-13147.
  • 103
    • 0034192770 scopus 로고    scopus 로고
    • Anti-malarial effect of histone deacetylation inhibitors and mammalian tumor cytodifferentiating agents
    • Andrews, K. T.; Walduck, A.; Kelso, M. J.; Fairlie, D. P.; Saul, A.; Parson, P. G. Anti-malarial effect of histone deacetylation inhibitors and mammalian tumor cytodifferentiating agents. Int. J. Paristol. 2000, 30, 761-768.
    • (2000) Int. J. Paristol , vol.30 , pp. 761-768
    • Andrews, K.T.1    Walduck, A.2    Kelso, M.J.3    Fairlie, D.P.4    Saul, A.5    Parson, P.G.6
  • 106
    • 13244252362 scopus 로고    scopus 로고
    • Trichostatin A attenuates airway inflammation in mouse asthma model
    • Choi, J. H.; Kang, M. S.; Kwon, H. J.; Oh, G. T.; Kim, D. Y. Trichostatin A attenuates airway inflammation in mouse asthma model. Clin. Exp. Allergy 2005, 35, 89-96.
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 89-96
    • Choi, J.H.1    Kang, M.S.2    Kwon, H.J.3    Oh, G.T.4    Kim, D.Y.5
  • 107
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT)Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency
    • Burrows, J. A. J.; Willis, L.; Perlmutter, D. H. Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT)Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc. Nat. Acad. Sci. 2000, 97, 1796-1801.
    • (2000) Proc. Nat. Acad. Sci , vol.97 , pp. 1796-1801
    • Burrows, J.A.J.1    Willis, L.2    Perlmutter, D.H.3
  • 108
    • 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.; Brosch, G.; Simonetti, G.; Passariello, C.; Palamara, A. T. Discovery of uracil-based histone deacetylase inhibitors able to reduce acquired antifungal resistance and trailing growth in Candida albicans. Bioorg. Med. Chem. Lett. 2007, 17, 1221-1225.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 1221-1225
    • Mai, A.1    Rotili, D.2    Massa, S.3    Brosch, G.4    Simonetti, G.5    Passariello, C.6    Palamara, A.T.7
  • 112
    • 34447325642 scopus 로고    scopus 로고
    • Defective cholesterol traffic and neuronal differentiation in neural stem cells of Niemann-Pick type C disease improved by valproic acid, a histone deacetylase inhibitor
    • Kim, S.-J.; Lee, B.-H.; Lee, Y.-S.; Kang, K.-S. Defective cholesterol traffic and neuronal differentiation in neural stem cells of Niemann-Pick type C disease improved by valproic acid, a histone deacetylase inhibitor. Biochem. Biophys. Res. Commun. 2007, 360, 593-599.
    • (2007) Biochem. Biophys. Res. Commun , vol.360 , pp. 593-599
    • Kim, S.-J.1    Lee, B.-H.2    Lee, Y.-S.3    Kang, K.-S.4
  • 113
    • 1642415712 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor for suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect
    • Reddy, P.; Maeda, Y.; Hotary, K.; Liu, C.; Reznikov, L. L.; Dinarello, C. A.; Ferrara, L. M. Histone deacetylase inhibitor for suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect. Proc. Nat. Acad. Sci. 2004, 101, 3921-3926.
    • (2004) Proc. Nat. Acad. Sci , 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, L.M.7
  • 116
    • 34548556060 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors preferentially augment transient transgene expression in human dermal fibroblasts
    • Yasukawa, K.; Sawamura, D.; Goto, M.; Nakamura, H.; Shimizu, H. Histone deacetylase inhibitors preferentially augment transient transgene expression in human dermal fibroblasts. Br. J. Dermatol. 2007, 157, 662-669.
    • (2007) Br. J. Dermatol , vol.157 , pp. 662-669
    • Yasukawa, K.1    Sawamura, D.2    Goto, M.3    Nakamura, H.4    Shimizu, H.5
  • 117
    • 3042566927 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor Trichostatin A modulates CD4+ T cell responses
    • Moreira, J. M.; Scheipers, P.; Sørensen, P. The histone deacetylase inhibitor Trichostatin A modulates CD4+ T cell responses. BMC Cancer 2003, 3, 30.
    • (2003) BMC Cancer , vol.3 , pp. 30
    • Moreira, J.M.1    Scheipers, P.2    Sørensen, P.3
  • 119
    • 0346873023 scopus 로고    scopus 로고
    • A therapeutic strategy uses histone deacetylase inhibitors to modulate the expression of genes involved in the pathogenesis of rheumatoid arthritis
    • Chung, Y. L.; Lee, M. Y.; Wang, A. J.; Yao, L. F. A therapeutic strategy uses histone deacetylase inhibitors to modulate the expression of genes involved in the pathogenesis of rheumatoid arthritis. Mol. Therap. 2003, 8, 707-717.
    • (2003) Mol. Therap , vol.8 , pp. 707-717
    • Chung, Y.L.1    Lee, M.Y.2    Wang, A.J.3    Yao, L.F.4
  • 121
    • 35648972756 scopus 로고    scopus 로고
    • Suppression of IL-1beta COX-2 expression by trichostatin A (TSA) in human endometrial stromal cells
    • Wu, Y.; Guo, S. W. Suppression of IL-1beta COX-2 expression by trichostatin A (TSA) in human endometrial stromal cells. Eur. J. Obstet. Gynecol. Reprod. 2007, 135, 88-93.
    • (2007) Eur. J. Obstet. Gynecol. Reprod , vol.135 , pp. 88-93
    • Wu, Y.1    Guo, S.W.2
  • 122
    • 48149084783 scopus 로고    scopus 로고
    • Moynihan, A.; Hehir, M.; Sharkey, A. Histone deacetylase inhibitors and a functional potent inhibitory effect on human uterine contractility. Am. J. Obstet. & Gynecol. 2008, 199, 167.e1-167.e7.
    • Moynihan, A.; Hehir, M.; Sharkey, A. Histone deacetylase inhibitors and a functional potent inhibitory effect on human uterine contractility. Am. J. Obstet. & Gynecol. 2008, 199, 167.e1-167.e7.
  • 123
    • 45049085648 scopus 로고    scopus 로고
    • Trichostatin A improves insulin stimulated glucose utilization and insulin signaling transduction through the repression of HDAC2
    • Sun, C.; Zhou, J. Trichostatin A improves insulin stimulated glucose utilization and insulin signaling transduction through the repression of HDAC2. Biochem. Pharmacol. 2008, 76, 120-127.
    • (2008) Biochem. Pharmacol , vol.76 , pp. 120-127
    • Sun, C.1    Zhou, J.2
  • 124
    • 0030923438 scopus 로고    scopus 로고
    • Induction of γ-globin by histone deacetylase inhibitors
    • McCaffrey, P. G.; Newsome, D. A.; Fibach, E.; Yoshida, M.; Su, M. S.-S. Induction of γ-globin by histone deacetylase inhibitors. Blood 1997, 90, 2075-2083.
    • (1997) Blood , vol.90 , pp. 2075-2083
    • McCaffrey, P.G.1    Newsome, D.A.2    Fibach, E.3    Yoshida, M.4    Su, M.S.-S.5
  • 125
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of sodium phenylbutyrate (Buphenyl) in delta F508-homozygous cystic fibrotic patients: Evidence of restoration of nasal epithelial CFTR function
    • Rubenstein, R. C.; Zeitlin, P. L. A pilot clinical trial of sodium phenylbutyrate (Buphenyl) in delta F508-homozygous cystic fibrotic patients: evidence of restoration of nasal epithelial CFTR function. Am. J. Resp. Crit. Care 1998, 157, 484-490.
    • (1998) Am. J. Resp. Crit. Care , vol.157 , pp. 484-490
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 126
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-call lymphoma
    • Mann, B. S.; Johnson, J. R.; Cohen, M. H.; Justice, R.; Pazdur, R. FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-call lymphoma. Oncologist 2007, 12, 1247-1252.
    • (2007) Oncologist , vol.12 , pp. 1247-1252
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 127
    • 0015793816 scopus 로고
    • Biochemical formation and pharmacological, and toxicological, and pathological properties of hydroxylamines and hydroxamic acids
    • Weisburger, J. H.; Weisburger, E. K. Biochemical formation and pharmacological, and toxicological, and pathological properties of hydroxylamines and hydroxamic acids. Pharmacol. Rev. 1973, 25, 1-66.
    • (1973) Pharmacol. Rev , vol.25 , pp. 1-66
    • Weisburger, J.H.1    Weisburger, E.K.2
  • 128
    • 0037361991 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): A therapeutic role for inhibitors of MMPs?
    • Belvisi, M. G.; Bottomley, K. M. The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): a therapeutic role for inhibitors of MMPs? Inflamm. Res. 2003, 52, 95-100.
    • (2003) Inflamm. Res , vol.52 , pp. 95-100
    • Belvisi, M.G.1    Bottomley, K.M.2
  • 129
    • 33847239896 scopus 로고    scopus 로고
    • Assessment of developmental toxicity of vorinostat, histone deacetylase inhibitor, in Sprague-Dawley rats and Dutch Belted rabbits
    • Wise, L. D.; Turner, K. J.; Kerr, J. S. Assessment of developmental toxicity of vorinostat, histone deacetylase inhibitor, in Sprague-Dawley rats and Dutch Belted rabbits. Birth Defects Res. B Dev. Reprod. Toxicol. 2007, 80, 57-68.
    • (2007) Birth Defects Res. B Dev. Reprod. Toxicol , vol.80 , pp. 57-68
    • Wise, L.D.1    Turner, K.J.2    Kerr, J.S.3
  • 130
    • 39849097353 scopus 로고    scopus 로고
    • Assessment of female and male fertility in Sprague-Dawley rats administered vorinostat, a histone deacetylase inhinbitor
    • Wise, L. D.; Spence, S.; Sidutti, L. P.; Kerr, J. S. Assessment of female and male fertility in Sprague-Dawley rats administered vorinostat, a histone deacetylase inhinbitor. Birth Defects Res. B. Dev. Reprod Toxicol. 2008, 83, 19-26.
    • (2008) Birth Defects Res. B. Dev. Reprod Toxicol , vol.83 , pp. 19-26
    • Wise, L.D.1    Spence, S.2    Sidutti, L.P.3    Kerr, J.S.4
  • 131
    • 33847779059 scopus 로고    scopus 로고
    • Site-specific acetylation of p53 directs selective transcription complex assembly
    • Roy, S.; Tenniswood, M. Site-specific acetylation of p53 directs selective transcription complex assembly. J. Biol. Chem. 2007, 282, 4765-4771.
    • (2007) J. Biol. Chem , vol.282 , pp. 4765-4771
    • Roy, S.1    Tenniswood, M.2
  • 132
    • 51049115570 scopus 로고    scopus 로고
    • Array-based analysis of the effects of trichostatin A and CG-1521 on cell cycle and cell death in LNCaP prostate cancer cells
    • Roy, S.; Jeffrey, R.; Tenniswood, M. Array-based analysis of the effects of trichostatin A and CG-1521 on cell cycle and cell death in LNCaP prostate cancer cells. Mol. Cancer Ther. 2009, 7, 1931-1939.
    • (2009) Mol. Cancer Ther , vol.7 , pp. 1931-1939
    • Roy, S.1    Jeffrey, R.2    Tenniswood, M.3
  • 133
    • 37249075061 scopus 로고    scopus 로고
    • Gene profile analysis of osteoblast genes differentially regulated by histone deacetylase inhibitors
    • Schroeder, T. M.; Nair, A. K.; Staggs, R.; Lamblin, A.-F.; Westendorf, J. J. Gene profile analysis of osteoblast genes differentially regulated by histone deacetylase inhibitors. BMC Genomics 2007, 8, 362.
    • (2007) BMC Genomics , vol.8 , pp. 362
    • Schroeder, T.M.1    Nair, A.K.2    Staggs, R.3    Lamblin, A.-F.4    Westendorf, J.J.5
  • 134
    • 0034086168 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells
    • Qui, L.; Burgess, A.; Fairlie, D. P.; Leonard, H.; Parsons, P. G.; Gabrielli, B. G. Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells. Mol. Biol. Cell 2000, 11, 2069-2083.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2069-2083
    • Qui, L.1    Burgess, A.2    Fairlie, D.P.3    Leonard, H.4    Parsons, P.G.5    Gabrielli, B.G.6
  • 136
    • 0036301281 scopus 로고    scopus 로고
    • Goldspiel B; Fojo AT; Balcerzak SP; SE., B. Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms
    • Sandor, V.; Baake, S.; Robey, R.; Kang, M. H.; Blagosklonny, M. V.; Bender, J.; Brooks, R.; Piekarz, R. L.; Tucker, E.; Figg, W. D.; Chan KK; Goldspiel B; Fojo AT; Balcerzak SP; SE., B. Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms.. Clin. Caner Res. 2002, 8, 718-728.
    • (2002) Clin. Caner Res , vol.8 , pp. 718-728
    • Sandor, V.1    Baake, S.2    Robey, R.3    Kang, M.H.4    Blagosklonny, M.V.5    Bender, J.6    Brooks, R.7    Piekarz, R.L.8    Tucker, E.9    Figg, W.D.10    Chan, K.K.11
  • 137
    • 33847355584 scopus 로고    scopus 로고
    • Molife R; Fong P; Scurr M; Judson I; Kaye S; J., d. B. HDAC inhibitors and cardiac safety. Clin. Cancer Res. 2007, 13, 1068.
    • Molife R; Fong P; Scurr M; Judson I; Kaye S; J., d. B. HDAC inhibitors and cardiac safety. Clin. Cancer Res. 2007, 13, 1068.
  • 138
    • 33746035691 scopus 로고    scopus 로고
    • Cardiotoxicity of histone deacetylase inhibitor depsipeptide in patients with metastatic neuroendocrine tumors
    • Shah, M. H.; Binkley, P.; Chan, K.; Xiao, J.; Arbogast, D.; Collamore, M.; Farra, Y.; Young, D.; Grever, M. Cardiotoxicity of histone deacetylase inhibitor depsipeptide in patients with metastatic neuroendocrine tumors. Clin. Cancer Res. 2006, 12, 3997-4003.
    • (2006) Clin. Cancer Res , vol.12 , pp. 3997-4003
    • Shah, M.H.1    Binkley, P.2    Chan, K.3    Xiao, J.4    Arbogast, D.5    Collamore, M.6    Farra, Y.7    Young, D.8    Grever, M.9
  • 140
    • 52449112167 scopus 로고    scopus 로고
    • Residues in the 11Å Channel of Histone Deacetylase 1 Promote Catalytic Activity: Implications for Designing Isoform-Selective HDAC inhibitors
    • Weerasinghe, S. V. W.; Estiu, G.; Wiest, O.; Pflum, M. K. Residues in the 11Å Channel of Histone Deacetylase 1 Promote Catalytic Activity: Implications for Designing Isoform-Selective HDAC inhibitors. J. Med. Chem. 2008, 51, 5543-5551.
    • (2008) J. Med. Chem , vol.51 , pp. 5543-5551
    • Weerasinghe, S.V.W.1    Estiu, G.2    Wiest, O.3    Pflum, M.K.4
  • 141
    • 49349104503 scopus 로고    scopus 로고
    • A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia
    • Gimsing, P.; Hansen, M.; Knudsen, L. M.; Knoblauch, P.; Christensen, I. J.; Ooi, C. E.; Buhl-Jensen, P. A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia. Eur. J. Haematol. 2008, 81, 170-176.
    • (2008) Eur. J. Haematol , vol.81 , pp. 170-176
    • Gimsing, P.1    Hansen, M.2    Knudsen, L.M.3    Knoblauch, P.4    Christensen, I.J.5    Ooi, C.E.6    Buhl-Jensen, P.7
  • 145
    • 45749142120 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Bieliauskas, A. V.; Pflum, M. K. Isoform-selective histone deacetylase inhibitors. Chem. Soc. Rev. 2008, 37, 1402-1413.
    • (2008) Chem. Soc. Rev , vol.37 , pp. 1402-1413
    • Bieliauskas, A.V.1    Pflum, M.K.2
  • 147
    • 27444435580 scopus 로고    scopus 로고
    • Toward selective histone deacetylase inhibitor design. Homology modeling, docking studies and molecular dynamic simulations of human class I histone deacetylases
    • Wang, D.-F.; Helquist, P.; Wiech, N.; Wiest, O. Toward selective histone deacetylase inhibitor design. Homology modeling, docking studies and molecular dynamic simulations of human class I histone deacetylases. J. Med. Chem. 2005, 48, 6936-6947.
    • (2005) J. Med. Chem , vol.48 , pp. 6936-6947
    • Wang, D.-F.1    Helquist, P.2    Wiech, N.3    Wiest, O.4
  • 148
    • 2942545807 scopus 로고    scopus 로고
    • On the Function of the 14 A Long Internal Cavity of Histone Deacetylase-Like Protein: Implications for the Design of Histone Deacetylase Inhibitors
    • Wang, D.-F.; Wiest, O.; Helquist, P.; Lan-Hargest, H.-Y.; Wiech, N. On the Function of the 14 A Long Internal Cavity of Histone Deacetylase-Like Protein: Implications for the Design of Histone Deacetylase Inhibitors. J. Med. Chem. 2004, 47, 3409-3417.
    • (2004) J. Med. Chem , vol.47 , pp. 3409-3417
    • Wang, D.-F.1    Wiest, O.2    Helquist, P.3    Lan-Hargest, H.-Y.4    Wiech, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.