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Volumn 7, Issue 10, 2006, Pages 784-796

Histone deacetylase inhibitors as therapeutics for polyglutamine disorders

Author keywords

[No Author keywords available]

Indexed keywords

3 CARBOXYCINNAMIC ACID BISHYDROXAMIC ACID; 3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; ALIPHATIC CARBOXYLIC ACID; ARYLBUTYRIC ACID DERIVATIVE; BENZAMIDE; BUTYRIC ACID; CYCLOPEPTIDE; DEPSIPEPTIDE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; POLYGLUTAMINE; REPRESSOR PROTEIN; TRICHOSTATIN A; TUBACIN; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 33748928786     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn1989     Document Type: Review
Times cited : (190)

References (185)
  • 1
    • 0013218415 scopus 로고    scopus 로고
    • Bates, G. P., Harper, P. S. & Jones, A. L. (eds) (Oxford Univ. Press, Oxford)
    • Bates, G. P., Harper, P. S. & Jones, A. L. (eds) Huntington's Disease (Oxford Univ. Press, Oxford, 2002).
    • (2002) Huntington's Disease
  • 2
    • 0034640011 scopus 로고    scopus 로고
    • Fourteen and counting: Unraveling trinucleotide repeat diseases
    • Cummings, C. J. & Zoghbi, H. Y. Fourteen and counting: unraveling trinucleotide repeat diseases. Hum. Mol. Genet. 9, 909-916 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 909-916
    • Cummings, C.J.1    Zoghbi, H.Y.2
  • 3
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson, H. L. et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19, 333-344 (1997).
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1
  • 4
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S. W. et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548 (1997).
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1
  • 5
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M. et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993 (1997).
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 6
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker, J. L., Zareie, M. H., Fong, H., Sarikaya, M. & Muchowski, P. J. Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nature Struct. Mol. Biol. 11, 1215-1222 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 7
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R. & Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810 (2004).
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 8
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble detergentresistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells
    • Kazantsev, A., Preisinger, E., Dranovsky, A., Goldgaber, D. & Housman, D. Insoluble detergentresistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc. Natl Acad. Sci. USA 96, 11404-11409 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3    Goldgaber, D.4    Housman, D.5
  • 9
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • Perez, M. K. et al. Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J. Cell Biol. 143, 1457-1470 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1457-1470
    • Perez, M.K.1
  • 10
    • 0032568517 scopus 로고    scopus 로고
    • Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human Huntington disease gene
    • Cha, J.-H. J. et al. Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human Huntington disease gene. Proc. Natl Acad. Sci. USA 95, 6480-6485 (1998). The first study to show abnormal transcriptional regulation in HD.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6480-6485
    • Cha, J.-H.J.1
  • 11
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19, 1176-1179 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 12
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak, M. A., Sengupta, N., Zhang, X. & Seto, E. Acetylation and deacetylation of non-histone proteins. Gene 363, 15-23 (2005).
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 13
    • 0025244999 scopus 로고
    • Nucleosome linking number change controlled by acetylation of histones H3 and H4
    • Norton, V., Marvin, K., Yau, P. & Bradbury, E. Nucleosome linking number change controlled by acetylation of histones H3 and H4. J. Biol. Chem. 265, 19848-19852 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 19848-19852
    • Norton, V.1    Marvin, K.2    Yau, P.3    Bradbury, E.4
  • 14
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee, D. Y., Hayes, J. J., Pruss, D. & Wolffe, A. P. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 72, 73-84 (1993).
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 15
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T. R., Thorne, A. W., Crane-Robinson C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7, 1395-1402 (1988).
    • (1988) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 16
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S. E. et al. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc. Natl Acad. Sci. USA 93, 14503-14508 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1
  • 17
    • 0035866353 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors
    • Zhu, W. G., Lakshmanan, R. R., Beal, M. D. & Otterson, G. A. DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res. 61, 1327-1333 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 1327-1333
    • Zhu, W.G.1    Lakshmanan, R.R.2    Beal, M.D.3    Otterson, G.A.4
  • 18
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks, P. A., Richon, V. M. & Rifkind, R. A. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J. Natl Cancer Inst. 92, 1210-1216 (2000).
    • (2000) J. Natl Cancer Inst. , vol.92 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 19
    • 0042905956 scopus 로고    scopus 로고
    • Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: Defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines
    • Glaser, K. B. et al. Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines. Mol. Cancer Ther. 2, 151-163 (2003).
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 151-163
    • Glaser, K.B.1
  • 20
    • 0034662614 scopus 로고    scopus 로고
    • Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: Comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer
    • Mariadason, J. M., Corner, G. A. & Augenlicht, L. H. Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer. Cancer Res. 60, 4561-4572 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 4561-4572
    • Mariadason, J.M.1    Corner, G.A.2    Augenlicht, L.H.3
  • 21
    • 0038740851 scopus 로고    scopus 로고
    • Histone acetylation-mediated regulation of genes in leukaemic cells
    • Chambers, A. E. et al. Histone acetylation-mediated regulation of genes in leukaemic cells. Eur. J. Cancer 39, 1165-1175 (2003).
    • (2003) Eur. J. Cancer , vol.39 , pp. 1165-1175
    • Chambers, A.E.1
  • 22
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress, W. D. & Seto, E. Histone deacetylases, transcriptional control, and cancer. J. Cell. Physiol. 184, 1-16 (2000).
    • (2000) J. Cell. Physiol. , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 24
    • 0037133290 scopus 로고    scopus 로고
    • Polyglutamine disease: Acetyltransferases awry
    • Hughes, R. E. Polyglutamine disease: acetyltransferases awry. Curr. Biol. 12, R141-R143 (2002).
    • (2002) Curr. Biol. , vol.12
    • Hughes, R.E.1
  • 25
    • 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. 25, 2873-2884 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2873-2884
    • Yang, X.-J.1    Gregoire, S.2
  • 26
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • de Ruijter, A. J., van Gennip, A. H., Caron, H. N., Kemp, S. & van Kuilenburg, A. B. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. 370, 737-749 (2003). A comprehensive review of the different classes of HDAC.
    • (2003) Biochem. J. , vol.370 , pp. 737-749
    • De Ruijter, A.J.1    Van Gennip, A.H.2    Caron, H.N.3    Kemp, S.4    Van Kuilenburg, A.B.5
  • 27
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C. A. & Schreiber, S. L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411 (1996).
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 28
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin, M. S. et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401, 188-193 (1999).
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1
  • 29
    • 33746578975 scopus 로고    scopus 로고
    • Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src
    • Longworth, M. S. & Laimins, L. A. Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src. Oncogene 25, 4495-4500 (2006).
    • (2006) Oncogene , vol.25 , pp. 4495-4500
    • Longworth, M.S.1    Laimins, L.A.2
  • 30
    • 0032940072 scopus 로고    scopus 로고
    • Histone deacetylases: Transcriptional repression with SINers and NuRDs
    • Ayer, D. E. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9, 193-198 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 193-198
    • Ayer, D.E.1
  • 31
    • 0029991514 scopus 로고    scopus 로고
    • HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex
    • Carmen, A. A., Rundlett, S. E. & Grunstein, M. HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J. Biol. Chem. 271, 15837-15844 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 15837-15844
    • Carmen, A.A.1    Rundlett, S.E.2    Grunstein, M.3
  • 32
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang, E. Y. et al. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 14, 45-54 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 45-54
    • Huang, E.Y.1
  • 33
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao, H. Y., Downes, M., Ordentlich, P. & Evans, R. M. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev 14, 55-66 (2000).
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 34
    • 0036161439 scopus 로고    scopus 로고
    • Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR
    • Fischle, W. et al. Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 9, 45-57 (2002). An important study showing HDAC3-dependent activity of class II HDACs.
    • (2002) Mol. Cell , vol.9 , pp. 45-57
    • Fischle, W.1
  • 35
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Berny, D. et al. Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol. Cell. Biol. 21, 8035-8044 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1
  • 36
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • Zhang, Y. et al. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168-1179 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1168-1179
    • Zhang, Y.1
  • 37
    • 18544387930 scopus 로고    scopus 로고
    • Isolation and characterization of a novel class II histone deacetylase, HDAC10
    • Fischer, D. D. et al. Isolation and characterization of a novel class II histone deacetylase, HDAC10. J. Biol. Chem. 277, 6656-6666 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 6656-6666
    • Fischer, D.D.1
  • 38
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola, A. R. & Yao, T. P. Molecular cloning and characterization of a novel histone deacetylase HDAC10. J. Biol. Chem. 277, 3350-3356 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 39
    • 0037016696 scopus 로고    scopus 로고
    • Isolation and characterization of mammalian HDAC10, a novel histone deacetylase
    • Kao, H. Y., Lee, C. H., Komarov, A., Han, C. C. & Evans, R. M. Isolation and characterization of mammalian HDAC10, a novel histone deacetylase. J. Biol. Chem. 277, 187-193 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 187-193
    • Kao, H.Y.1    Lee, C.H.2    Komarov, A.3    Han, C.C.4    Evans, R.M.5
  • 40
    • 0036493156 scopus 로고    scopus 로고
    • Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain
    • Tong, J. J., Liu, J., Bertos, N. R. & Yang, X. J. Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain. Nucleic Acids Res. 30, 1114-1123 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1114-1123
    • Tong, J.J.1    Liu, J.2    Bertos, N.R.3    Yang, X.J.4
  • 41
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R. A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273, 793-798 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 42
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M. & Guarente, L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13, 2570-2580 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 43
    • 0037221445 scopus 로고    scopus 로고
    • +-dependent deacetylases
    • +-dependent deacetylases. Trends Biochem. Sci. 28, 41-48 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 41-48
    • Denu, J.M.1
  • 44
    • 0035951072 scopus 로고    scopus 로고
    • +-dependent deacetylation reactions
    • +-dependent deacetylation reactions. Biochemistry 40, 15456-15463 (2001).
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1
  • 45
    • 1842430616 scopus 로고    scopus 로고
    • +-dependent protein deacetylation and ADP-ribosyl enzyme intermediates
    • +-dependent protein deacetylation and ADP-ribosyl enzyme intermediates. Curr. Med. Chem. 11, 807-826 (2004).
    • (2004) Curr. Med. Chem. , vol.11 , pp. 807-826
    • Sauve, A.A.1    Schramm, V.L.2
  • 46
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M. & Sinclair, D. A. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 277, 45099-45107 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 47
    • 33644875954 scopus 로고    scopus 로고
    • Neuronal protection by sirtuins in Alzheimer's disease
    • Anekonda, T. S. & Reddy, P. H. Neuronal protection by sirtuins in Alzheimer's disease. J. Neurochem. 96, 305-313 (2006).
    • (2006) J. Neurochem. , vol.96 , pp. 305-313
    • Anekonda, T.S.1    Reddy, P.H.2
  • 48
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • Gao, L., Cueto, M. A., Asselbergs, F. & Atadja, P. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J. Biol. Chem. 277, 25748-25755 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 49
    • 0034885934 scopus 로고    scopus 로고
    • Class II histone deacetylases: Structure, function, and regulation
    • Bertos, N. R., Wang, A. H. & Yang, X. J. Class II histone deacetylases: structure, function, and regulation. Biochem. Cell Biol. 79, 243-252 (2001).
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 243-252
    • Bertos, N.R.1    Wang, A.H.2    Yang, X.J.3
  • 50
    • 13844252820 scopus 로고    scopus 로고
    • Regulation of histone deacetylase activities
    • Sengupta, N. & Seto, E. Regulation of histone deacetylase activities. J. Cell. Biochem. 93, 57-67 (2004).
    • (2004) J. Cell. Biochem. , vol.93 , pp. 57-67
    • Sengupta, N.1    Seto, E.2
  • 51
    • 0035724044 scopus 로고    scopus 로고
    • Identification of a signal-responsive nuclear export sequence in class II histone deacetylases
    • McKinsey, T. A., Zhang, C. L. & Olson, E. N. Identification of a signal-responsive nuclear export sequence in class II histone deacetylases. Mol. Cell. Biol. 21, 6312-6321 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6312-6321
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 53
    • 0034635987 scopus 로고    scopus 로고
    • Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases
    • Lu, J., McKinsey, T. A., Nicol, R. L. & Olson, E. N. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc. Natl Acad. Sci. USA 97, 4070-4075 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4070-4075
    • Lu, J.1    McKinsey, T.A.2    Nicol, R.L.3    Olson, E.N.4
  • 54
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska, E. A. et al. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 18, 5099-5107 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1
  • 55
    • 0033595764 scopus 로고    scopus 로고
    • Neuronal activity-dependent cell survival mediated by transcription factor MEF2
    • Mao, Z., Bonni, A., Xia, F., Nadal-Vicens, M. & Greenberg, M. E. Neuronal activity-dependent cell survival mediated by transcription factor MEF2. Science 286, 785-790 (1999).
    • (1999) Science , vol.286 , pp. 785-790
    • Mao, Z.1    Bonni, A.2    Xia, F.3    Nadal-Vicens, M.4    Greenberg, M.E.5
  • 56
    • 0037195903 scopus 로고    scopus 로고
    • RNA Interference reveals a requirement for myocyte enhancer factor 2A in activity-dependent neuronal survival
    • Gaudilliere, B., Shi, Y. & Bonni, A. RNA Interference reveals a requirement for myocyte enhancer factor 2A in activity-dependent neuronal survival. J. Biol. Chem. 277, 46442-46446 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46442-46446
    • Gaudilliere, B.1    Shi, Y.2    Bonni, A.3
  • 57
    • 0035881078 scopus 로고    scopus 로고
    • Differential localization of HDAC4 orchestrates muscle differentiation
    • Miska, E. A. et al. Differential localization of HDAC4 orchestrates muscle differentiation. Nucleic Acids Res. 29, 3439-3447 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3439-3447
    • Miska, E.A.1
  • 58
    • 0035861739 scopus 로고    scopus 로고
    • Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7
    • Kao, H. Y. et al. Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7. J. Biol. Chem. 276, 47496-47507 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 47496-47507
    • Kao, H.Y.1
  • 59
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • Grozinger, C. M. & Schreiber, S. L. Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl Acad. Sci. USA 97, 7835-7840 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 60
    • 26844518082 scopus 로고    scopus 로고
    • Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death
    • Bolger, T. A. & Yao, T. P. Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death. J. Neurosci. 25, 9544-9553 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 9544-9553
    • Bolger, T.A.1    Yao, T.P.2
  • 61
    • 0037379709 scopus 로고    scopus 로고
    • Neuronal activity-dependent nucleocytoplasmic shuttling of HDAC4 and HDAC5
    • Chawla, S., Vanhoutte, P., Arnold, F. J., Huang, C. L. & Bading, H. Neuronal activity-dependent nucleocytoplasmic shuttling of HDAC4 and HDAC5. J. Neurochem. 85, 151-159 (2003).
    • (2003) J. Neurochem. , vol.85 , pp. 151-159
    • Chawla, S.1    Vanhoutte, P.2    Arnold, F.J.3    Huang, C.L.4    Bading, H.5
  • 62
    • 0037117712 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent proteins in R6/2 Huntington's disease mice
    • 2+/calmodulin-dependent proteins in R6/2 Huntington's disease mice. Neuroreport 13, 707-711 (2002).
    • (2002) Neuroreport , vol.13 , pp. 707-711
    • Deckel, A.W.1    Elder, R.2    Fuhrer, G.3
  • 63
    • 0141642242 scopus 로고    scopus 로고
    • Histone deacetylase activity is retained in primary neurons expressing mutant huntingtin protein
    • Hoshino, M. et al. Histone deacetylase activity is retained in primary neurons expressing mutant huntingtin protein. J. Neurochem. 87, 257-267 (2003).
    • (2003) J. Neurochem. , vol.87 , pp. 257-267
    • Hoshino, M.1
  • 64
    • 0346094379 scopus 로고    scopus 로고
    • Predominant expression of Sir2α, an NAD-dependent histone deacetylase, in the embryonic mouse heart and brain
    • Sakamoto, J., Miura, T., Shimamoto, K. & Horio, Y. Predominant expression of Sir2α, an NAD-dependent histone deacetylase, in the embryonic mouse heart and brain. FEBS Lett. 556, 281-286 (2004).
    • (2004) FEBS Lett. , vol.556 , pp. 281-286
    • Sakamoto, J.1    Miura, T.2    Shimamoto, K.3    Horio, Y.4
  • 65
    • 24744467838 scopus 로고    scopus 로고
    • Transcriptional regulation of neuronal genes and its effect on neural functions: NAD-dependent histone deacetylase SIRT1 (Sir2α)
    • Hisahara, S., Chiba, S., Matsumoto, H. & Horio, Y. Transcriptional regulation of neuronal genes and its effect on neural functions: NAD-dependent histone deacetylase SIRT1 (Sir2α). J. Pharmacol. Sci. 98, 200-204 (2005).
    • (2005) J. Pharmacol. Sci. , vol.98 , pp. 200-204
    • Hisahara, S.1    Chiba, S.2    Matsumoto, H.3    Horio, Y.4
  • 66
    • 0034283877 scopus 로고    scopus 로고
    • Transcriptional dysregulation in Huntington's disease
    • Cha, J.-H. J. Transcriptional dysregulation in Huntington's disease. Trends Neurosci. 23, 387-392 (2000).
    • (2000) Trends Neurosci. , vol.23 , pp. 387-392
    • Cha, J.-H.J.1
  • 67
    • 0037101835 scopus 로고    scopus 로고
    • Dysregulation of gene expression in the R6/2 model of polyglutamine disease: Parallel changes in muscle and brain
    • Luthi-Carter, R. et al. Dysregulation of gene expression in the R6/2 model of polyglutamine disease: parallel changes in muscle and brain. Hum. Mol. Genet. 11, 1911-1926 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1911-1926
    • Luthi-Carter, R.1
  • 68
    • 0037101837 scopus 로고    scopus 로고
    • Polyglutamine and transcription: Gene expression changes shared by DRPLA and Huntington's disease mouse models reveal contextindependent effects
    • Luthi-Carter, R. et al. Polyglutamine and transcription: gene expression changes shared by DRPLA and Huntington's disease mouse models reveal contextindependent effects. Hum. Mol. Genet. 11, 1927-1937 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1927-1937
    • Luthi-Carter, R.1
  • 69
    • 33644783812 scopus 로고    scopus 로고
    • Regional and cellular gene expression changes in human Huntington's disease brain
    • Hodges, A. et al. Regional and cellular gene expression changes in human Huntington's disease brain. Hum. Mol. Genet. 15, 965-977 (2006). The above three papers contain important microarray expression profile information about HD and DRPLA.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 965-977
    • Hodges, A.1
  • 70
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan, J. S. et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc. Natl Acad. Sci. USA 97, 6763-6768 (2000). The first paper to implicate aberrant interactions between CBP and HTT in transcriptional repression in HD.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6763-6768
    • Steffan, J.S.1
  • 71
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora, F. C. Jr et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291, 2423-2428 (2001). Highlights the implications of CBP in the pathogenic mechanism of polyglutamine repeat disease.
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora Jr., F.C.1
  • 72
    • 0034285017 scopus 로고    scopus 로고
    • CREB-binding protein sequestration by expanded polyglutamine
    • McCampbell, A. et al. CREB-binding protein sequestration by expanded polyglutamine. Hum. Mol. Genet. 9, 2197-2202 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2197-2202
    • McCampbell, A.1
  • 73
    • 0035031779 scopus 로고    scopus 로고
    • Polyglutamine and CBP: Fatal attraction?
    • McCampbell, A. & Fischbeck, K. H. Polyglutamine and CBP: fatal attraction? Nature Med. 7, 528-530 (2001).
    • (2001) Nature Med. , vol.7 , pp. 528-530
    • McCampbell, A.1    Fischbeck, K.H.2
  • 74
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah, A. W. et al. Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296, 2238-2243 (2002).
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1
  • 75
    • 12244300919 scopus 로고    scopus 로고
    • Insoluble TATA-binding protein accumulation in Huntington's disease cortex
    • van Roon-Mom, W. M. et al. Insoluble TATA-binding protein accumulation in Huntington's disease cortex. Brain Res. Mol. Brain Res. 109, 1-10 (2002).
    • (2002) Brain Res. Mol. Brain Res. , vol.109 , pp. 1-10
    • Van Roon-Mom, W.M.1
  • 76
    • 0037961686 scopus 로고    scopus 로고
    • Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation
    • Igarashi, S. et al. Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation. Neuroreport 14, 565-568 (2003).
    • (2003) Neuroreport , vol.14 , pp. 565-568
    • Igarashi, S.1
  • 77
    • 18444371744 scopus 로고    scopus 로고
    • Ultrastructure of nuclear aggregates formed by expressing an expanded polyglutamine
    • Hazeki, N. et al. Ultrastructure of nuclear aggregates formed by expressing an expanded polyglutamine. Biochem. Biophys. Res. Commun. 294, 429-440 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 429-440
    • Hazeki, N.1
  • 78
  • 79
    • 0029796093 scopus 로고    scopus 로고
    • Identification of potential target genes for the neuronrestrictive silencer factor
    • Schoenherr, C. J., Paquette, A. J. & Anderson, D. J. Identification of potential target genes for the neuronrestrictive silencer factor. Proc. Natl Acad. Sci. USA 93, 9881-9886 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9881-9886
    • Schoenherr, C.J.1    Paquette, A.J.2    Anderson, D.J.3
  • 80
    • 0031694917 scopus 로고    scopus 로고
    • NRSF/REST is required in vivo for repression of multiple neuronal target genes during embryogenesis
    • Chen, Z.-F., Paquette, A. J. & Anderson, D. J. NRSF/REST is required in vivo for repression of multiple neuronal target genes during embryogenesis. Nature Genet. 20, 136-142 (1998).
    • (1998) Nature Genet. , vol.20 , pp. 136-142
    • Chen, Z.-F.1    Paquette, A.J.2    Anderson, D.J.3
  • 81
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in huntington's disease
    • Zuccato, C. et al. Loss of huntingtin-mediated BDNF gene transcription in huntington's disease. Science 293, 493-498 (2001).
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1
  • 83
    • 33644830913 scopus 로고    scopus 로고
    • Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity
    • Bates, E. A., Victor, M., Jones, A. K., Shi, Y. & Hart, A. C. Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity. J. Neurosci. 26, 2830-2838 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 2830-2838
    • Bates, E.A.1    Victor, M.2    Jones, A.K.3    Shi, Y.4    Hart, A.C.5
  • 84
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert, C. et al. HDAC6 is a microtubule-associated deacetylase. Nature 417, 455-458 (2002).
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1
  • 85
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali, P. et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 280, 26729-26734 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 26729-26734
    • Bali, P.1
  • 86
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs, J. J. et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol. Cell 18, 601-607 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1
  • 87
    • 0037108963 scopus 로고    scopus 로고
    • Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes
    • Hook, S. S., Orian, A., Cowley, S. M. & Eisenman, R. N. Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc. Natl Acad. Sci. USA 99, 13425-13430 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13425-13430
    • Hook, S.S.1    Orian, A.2    Cowley, S.M.3    Eisenman, R.N.4
  • 88
    • 20844435806 scopus 로고    scopus 로고
    • Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma
    • Hideshima, T. et al. Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma. Proc. Natl Acad. Sci. USA 102, 8567-8572 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8567-8572
    • Hideshima, T.1
  • 89
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata, A., Riley, B. E., Johnston, J. A. & Kopito, R. R. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J. Biol. Chem. 280, 40282-40292 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 90
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi, Y. et al. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727-738 (2003).
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1
  • 91
    • 25444484672 scopus 로고    scopus 로고
    • Small molecule regulation of Sir2 protein deacetylases
    • Grubisha, O., Smith, B. C. & Denu, J. M. Small molecule regulation of Sir2 protein deacetylases. FEBS J. 272, 4607-4616 (2005).
    • (2005) FEBS J. , vol.272 , pp. 4607-4616
    • Grubisha, O.1    Smith, B.C.2    Denu, J.M.3
  • 92
    • 5744248243 scopus 로고    scopus 로고
    • Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases
    • Ghosh, S. & Feany, M. B. Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases. Hum. Mol. Genet. 13, 2011-2018 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2011-2018
    • Ghosh, S.1    Feany, M.B.2
  • 93
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • Parker, J. A. et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nature Genet. 37, 349-350 (2005).
    • (2005) Nature Genet. , vol.37 , pp. 349-350
    • Parker, J.A.1
  • 94
    • 16844385222 scopus 로고    scopus 로고
    • Sirtuins for healthy neurons
    • Sinclair, D. Sirtuins for healthy neurons. Nature Genet. 37, 339-340 (2005).
    • (2005) Nature Genet. , vol.37 , pp. 339-340
    • Sinclair, D.1
  • 95
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. p53, the cellular gatekeeper for growth and division. Cell 88, 323-331 (1997).
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 96
    • 0030809127 scopus 로고    scopus 로고
    • A role for the tumour suppressor gene p53 in regulating neuronal apoptosis
    • Hughes, P. E., Alexi, T. & Schreiber, S. S. A role for the tumour suppressor gene p53 in regulating neuronal apoptosis. Neuroreport 8, v-xii (1997).
    • (1997) Neuroreport , vol.8
    • Hughes, P.E.1    Alexi, T.2    Schreiber, S.S.3
  • 97
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W. & Roeder, R. G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606 (1997).
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 98
    • 0037112901 scopus 로고    scopus 로고
    • MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation
    • Ito, A. et al. MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. EMBO J. 21, 6236-6245 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6236-6245
    • Ito, A.1
  • 99
    • 33144464295 scopus 로고    scopus 로고
    • Regulation of the p53 transcriptional activity
    • Gang Liu, X. C. Regulation of the p53 transcriptional activity. J. Cell. Biochem. 97, 448-458 (2006).
    • (2006) J. Cell. Biochem. , vol.97 , pp. 448-458
    • Gang Liu, X.C.1
  • 100
    • 1442330508 scopus 로고    scopus 로고
    • Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo
    • Luo, J. et al. Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo. Proc. Natl Acad. Sci. USA 101, 2259-2264 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2259-2264
    • Luo, J.1
  • 101
    • 21544450545 scopus 로고    scopus 로고
    • p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae, B. I. et al. p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 47, 29-41 (2005).
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1
  • 102
    • 22244437618 scopus 로고    scopus 로고
    • The binding of the ubiquitous transcription factor Sp1 at the locus control region represses the expression of β-like globin genes
    • Feng, D. & Kan, Y. W. The binding of the ubiquitous transcription factor Sp1 at the locus control region represses the expression of β-like globin genes. Proc. Natl Acad. Sci. USA 102, 9896-9900 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9896-9900
    • Feng, D.1    Kan, Y.W.2
  • 103
    • 0033215387 scopus 로고    scopus 로고
    • Transcriptional repression by wildtype p53 utilizes histone deacetylases, mediated by interaction with mSin3a
    • Murphy, M. et al. Transcriptional repression by wildtype p53 utilizes histone deacetylases, mediated by interaction with mSin3a. Genes Dev. 13, 2490-2501 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2490-2501
    • Murphy, M.1
  • 104
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo, J., Su, F., Chen, D., Shiloh, A. & Gu, W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408, 377-381 (2000).
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 105
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan, L. J. et al. Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 275, 20436-20443 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1
  • 106
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B. & Toft, D. O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228, 111-133 (2003).
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 107
    • 0034777916 scopus 로고    scopus 로고
    • Destabilization of steroid receptors by heat shock protein 90-binding drugs: A ligand-independent approach to hormonal therapy of breast cancer
    • Bagatell, R. et al. Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer. Clin. Cancer Res. 7, 2076-2084 (2001).
    • (2001) Clin. Cancer Res. , vol.7 , pp. 2076-2084
    • Bagatell, R.1
  • 108
    • 0036098002 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition by 17-allylamino-17- Demethoxygeldanamycin: A novel therapeutic approach for treating hormone-refractory prostate cancer
    • Neckers, L. Heat shock protein 90 inhibition by 17-allylamino-17- demethoxygeldanamycin: a novel therapeutic approach for treating hormone-refractory prostate cancer. Clin. Cancer Res. 8, 962-966 (2002).
    • (2002) Clin. Cancer Res. , vol.8 , pp. 962-966
    • Neckers, L.1
  • 109
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
    • Waza, M. et al. 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nature Med. 11, 1088-1095 (2005).
    • (2005) Nature Med. , vol.11 , pp. 1088-1095
    • Waza, M.1
  • 110
    • 27744479712 scopus 로고    scopus 로고
    • Modulating molecular chaperone Hsp90 functions through reversible acetylation
    • Aoyagi, S. & Archer, T. K. Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol. 15, 565-567 (2005).
    • (2005) Trends Cell Biol. , vol.15 , pp. 565-567
    • Aoyagi, S.1    Archer, T.K.2
  • 111
    • 33644696512 scopus 로고    scopus 로고
    • Chemical ablation of androgen receptor in prostate cancer cells by the histone deacetylase inhibitor LAQ824
    • Chen, L. et al. Chemical ablation of androgen receptor in prostate cancer cells by the histone deacetylase inhibitor LAQ824. Mol. Cancer Ther. 4, 1311-1319 (2005).
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1311-1319
    • Chen, L.1
  • 112
    • 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. 89, 1358-1367 (2004).
    • (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
  • 113
    • 15044356553 scopus 로고    scopus 로고
    • Lifespan extension and elevated hsp gene expression in Drosophila caused by histone deacetylase inhibitors
    • Zhao, Y. et al. Lifespan extension and elevated hsp gene expression in Drosophila caused by histone deacetylase inhibitors. J. Exp. Biol. 208, 697-705 (2005).
    • (2005) J. Exp. Biol. , vol.208 , pp. 697-705
    • Zhao, Y.1
  • 114
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay, D. G. et al. Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 13, 1389-1405 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1
  • 115
    • 33847684865 scopus 로고    scopus 로고
    • The HdhQ150/Q150 knock-in mouse model of HD and the R6/2 exon 1 model develop comparable and widespread molecular phenotypes
    • in the press
    • Woodman, B. et al. The HdhQ150/Q150 knock-in mouse model of HD and the R6/2 exon 1 model develop comparable and widespread molecular phenotypes. Brain Res. Bull. (in the press).
    • Brain Res. Bull.
    • Woodman, B.1
  • 116
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li, F., Macfarlan, T., Pittman, R. N. & Chakravarti, D. Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J. Biol. Chem. 277, 45004-45012 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45004-45012
    • Li, F.1    Macfarlan, T.2    Pittman, R.N.3    Chakravarti, D.4
  • 117
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel, J. R. & Zoghbi, H. Y. Diseases of unstable repeat expansion: mechanisms and common principles. Nature Rev. Genet. 6, 743-755 (2005).
    • (2005) Nature Rev. Genet. , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 118
    • 1642447764 scopus 로고    scopus 로고
    • Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors
    • Tsai, C. C. et al. Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors. Proc. Natl Acad. Sci. USA 101, 4047-4052 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4047-4052
    • Tsai, C.C.1
  • 119
    • 0030716768 scopus 로고    scopus 로고
    • The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
    • Matilla, A. et al. The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Nature 389, 974-978 (1997).
    • (1997) Nature , vol.389 , pp. 974-978
    • Matilla, A.1
  • 120
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
    • Seo, S. et al. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein. Cell 104, 119-130 (2001).
    • (2001) Cell , vol.104 , pp. 119-130
    • Seo, S.1
  • 121
    • 0037726598 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
    • Chen, H. K. et al. Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell 113, 457-468 (2003).
    • (2003) Cell , vol.113 , pp. 457-468
    • Chen, H.K.1
  • 122
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett, B., Li, F. & Pittman, R. N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet. 12, 3195-3205 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 123
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • Burnett, B. G. & Pittman, R. N. The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Proc. Natl Acad. Sci. USA 102, 4330-4335 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 124
    • 20844444637 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration
    • Palhan, V. B. et al. Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration. Proc. Natl Acad. Sci. USA 102, 8472-8477 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8472-8477
    • Palhan, V.B.1
  • 125
    • 20844441094 scopus 로고    scopus 로고
    • Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity
    • McMahon, S. J., Pray-Grant, M. G., Schieltz, D., Yates, J. R. & Grant, P. A. Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity. Proc. Natl Acad. Sci. USA 102, 8478-8482 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8478-8482
    • McMahon, S.J.1    Pray-Grant, M.G.2    Schieltz, D.3    Yates, J.R.4    Grant, P.A.5
  • 126
    • 0037015044 scopus 로고    scopus 로고
    • SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription
    • Sterner, D. E., Belotserkovskaya, R. & Berger, S. L. SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription. Proc. Natl Acad. Sci. USA 99, 11622-11627 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11622-11627
    • Sterner, D.E.1    Belotserkovskaya, R.2    Berger, S.L.3
  • 127
    • 18744374136 scopus 로고    scopus 로고
    • The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway
    • Pray-Grant, M. G. et al. The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway. Mol. Cell. Biol. 22, 8774-8786 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8774-8786
    • Pray-Grant, M.G.1
  • 128
    • 33144469085 scopus 로고    scopus 로고
    • Glutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction
    • Helmlinger, D. et al. Glutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction. PLoS Biol. 4, e67 (2006).
    • (2006) PLoS Biol. , vol.4
    • Helmlinger, D.1
  • 129
    • 0009744392 scopus 로고    scopus 로고
    • Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA
    • Schilling, G. et al. Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA. Neuron 24, 275-286 (1999).
    • (1999) Neuron , vol.24 , pp. 275-286
    • Schilling, G.1
  • 130
    • 0034605071 scopus 로고    scopus 로고
    • Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription
    • Wood, J. D. et al. Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription. J. Cell Biol. 150, 939-948 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 939-948
    • Wood, J.D.1
  • 131
    • 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. et al. Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO. Mol. Cell. Biol. 18, 7185-7191 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7185-7191
    • Gelmetti, V.1
  • 132
    • 0031724804 scopus 로고    scopus 로고
    • ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors
    • Lutterbach, B. et al. ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors. Mol. Cell. Biol. 18, 7176-7184 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7176-7184
    • Lutterbach, B.1
  • 133
    • 0032169858 scopus 로고    scopus 로고
    • ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex
    • Wang, J., Hoshino, T., Redner, R. L., Kajigaya, S. & Liu, J. M. ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex. Proc. Natl Acad. Sci. USA 95, 10860-10865 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10860-10865
    • Wang, J.1    Hoshino, T.2    Redner, R.L.3    Kajigaya, S.4    Liu, J.M.5
  • 134
    • 33744965475 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates histone hypoacetylation and neurodegenerative phenotypes in a mouse model for DRPLA
    • Ying, M. et al. Sodium butyrate ameliorates histone hypoacetylation and neurodegenerative phenotypes in a mouse model for DRPLA. J. Biol. Chem. 281, 12580-12586 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 12580-12586
    • Ying, M.1
  • 135
    • 33644771241 scopus 로고    scopus 로고
    • Histone deacetylase-associating Atrophin proteins are nuclear receptor corepressors
    • Wang, L., Rajan, H., Pitman, J. L., McKeown, M. & Tsai, C.-C. Histone deacetylase-associating Atrophin proteins are nuclear receptor corepressors. Genes Dev. 20, 525-530 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 525-530
    • Wang, L.1    Rajan, H.2    Pitman, J.L.3    McKeown, M.4    Tsai, C.-C.5
  • 136
    • 0035909999 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors reduce polyglutamine toxicity
    • McCampbell, A. et al. Histone deacetylase inhibitors reduce polyglutamine toxicity. Proc. Natl Acad. Sci. USA 98, 15179-15184 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15179-15184
    • McCampbell, A.1
  • 137
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan, J. S. et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 413, 739-743 (2001). The first study in Drosophila to show HDAC inhibitors as a beneficial therapy for polyglutamine repeat disease.
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1
  • 138
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease
    • Hockly, E. et al. Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc. Natl Acad. Sci. USA 100, 2041-2046 (2003). The first published study of the use of an HDAC inhibitor as a therapeutic agent in a mouse model of HD.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2041-2046
    • Hockly, E.1
  • 139
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante, R. J. et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23, 9418-9427 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 140
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
    • Gardian, G. et al. Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease. J. Biol. Chem. 280, 556-563 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 556-563
    • Gardian, G.1
  • 141
    • 13844309711 scopus 로고    scopus 로고
    • Clinical development of histone deacetylase inhibitors as anticancer agents
    • Drummond, D. C. et al. Clinical development of histone deacetylase inhibitors as anticancer agents. Annu. Rev. Pharmacol. Toxicol. 45, 495-528 (2005).
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 495-528
    • Drummond, D.C.1
  • 143
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of smallmolecule inhibitors
    • Grozinger, C. M. & Schreiber, S. L. Deacetylase enzymes: biological functions and the use of smallmolecule inhibitors. Chem. Biol. 9, 3-16 (2002).
    • (2002) Chem. Biol. , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 144
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zincdependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
    • Vannini, A. et al. Crystal structure of a eukaryotic zincdependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc. Natl Acad. Sci. USA 101, 15064-15069 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15064-15069
    • Vannini, A.1
  • 145
    • 2942733520 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Minamiyama, M. et al. Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Hum. Mol. Genet. 13, 1183-1192 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1183-1192
    • Minamiyama, M.1
  • 146
    • 23344448837 scopus 로고    scopus 로고
    • Genome-wide expression profiling of human blood reveals biomarkers for Huntington's disease
    • Borovecki, F. et al. Genome-wide expression profiling of human blood reveals biomarkers for Huntington's disease. Proc. Natl Acad. Sci. USA 102, 11023-11028 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11023-11028
    • Borovecki, F.1
  • 147
    • 14844341251 scopus 로고    scopus 로고
    • Identification of combinatorial drug regimens for treatment of Huntington's disease using Drosophila
    • Agrawal, N. et al. Identification of combinatorial drug regimens for treatment of Huntington's disease using Drosophila. Proc. Natl Acad. Sci. USA 102, 3777-3781 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3777-3781
    • Agrawal, N.1
  • 148
    • 0000220374 scopus 로고
    • Infantile muscular atrophy
    • Byers, R. K. & Banker, B. Q. Infantile muscular atrophy. Arch. Neurol. 5, 140-164 (1961).
    • (1961) Arch. Neurol. , vol.5 , pp. 140-164
    • Byers, R.K.1    Banker, B.Q.2
  • 149
    • 0025260440 scopus 로고
    • Genetic mapping of chronic childhood-onset spinal muscular atrophy to chromosome 5q11.2-13.3
    • Brzustowicz, L. M. et al. Genetic mapping of chronic childhood-onset spinal muscular atrophy to chromosome 5q11.2-13.3. Nature 344, 540-541 (1990).
    • (1990) Nature , vol.344 , pp. 540-541
    • Brzustowicz, L.M.1
  • 150
    • 0025319713 scopus 로고
    • Gene for chronic proximal spinal muscular atrophies maps to chromosome 5q
    • Melki, J. et al. Gene for chronic proximal spinal muscular atrophies maps to chromosome 5q. Nature 344, 767-768 (1990).
    • (1990) Nature , vol.344 , pp. 767-768
    • Melki, J.1
  • 151
    • 0025330316 scopus 로고
    • Genetic homogeneity between acute and chronic forms of spinal muscular atrophy
    • Gilliam, T. C. et al. Genetic homogeneity between acute and chronic forms of spinal muscular atrophy. Nature 345, 823-825 (1990).
    • (1990) Nature , vol.345 , pp. 823-825
    • Gilliam, T.C.1
  • 152
    • 0030981541 scopus 로고    scopus 로고
    • Correlation between severity and SMN protein level in spinal muscular atrophy
    • Lefebvre, S. et al. Correlation between severity and SMN protein level in spinal muscular atrophy. Nature Genet. 16, 265-269 (1997).
    • (1997) Nature Genet. , vol.16 , pp. 265-269
    • Lefebvre, S.1
  • 154
    • 0035859952 scopus 로고    scopus 로고
    • Treatment of spinal muscular atrophy by sodium butyrate
    • Chang, J. G. et al. Treatment of spinal muscular atrophy by sodium butyrate. Proc. Natl Acad. Sci. USA 98, 9808-9813 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9808-9813
    • Chang, J.G.1
  • 155
    • 0242290062 scopus 로고    scopus 로고
    • Valproic acid increases SMN levels in spinal muscular atrophy patient cells
    • Sumner, C. J. et al. Valproic acid increases SMN levels in spinal muscular atrophy patient cells. Ann. Neurol. 54, 647-654 (2003).
    • (2003) Ann. Neurol. , vol.54 , pp. 647-654
    • Sumner, C.J.1
  • 156
    • 0141506887 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. et al. Valproic acid increases the SMN2 protein level: a well-known drug as a potential therapy for spinal muscular atrophy. Hum. Mol. Genet. 12, 2481-2489 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2481-2489
    • Brichta, L.1
  • 157
    • 10744229981 scopus 로고    scopus 로고
    • Phenylbutyrate increases SMN expression in vitro: Relevance for treatment of spinal muscular atrophy
    • Andreassi, C. et al. Phenylbutyrate increases SMN expression in vitro: relevance for treatment of spinal muscular atrophy. Eur. J. Hum. Genet. 12, 59-65 (2004).
    • (2004) Eur. J. Hum. Genet. , vol.12 , pp. 59-65
    • Andreassi, C.1
  • 158
    • 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. 1-10 (2006).
    • (2006) Hum. Genet. , pp. 1-10
    • Riessland, M.1    Brichta, L.2    Hahnen, E.3    Wirth, B.4
  • 159
    • 18144400082 scopus 로고    scopus 로고
    • The role of histone acetylation in SMN gene expression
    • Kernochan, L. E. et al. The role of histone acetylation in SMN gene expression. Hum. Mol. Genet. 14, 1171-1182 (2005).
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1171-1182
    • Kernochan, L.E.1
  • 160
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • Jung, M. et al. Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J. Med. Chem. 42, 4669-4679 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 4669-4679
    • Jung, M.1
  • 161
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin a and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai, R. et al. Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc. Natl Acad. Sci. USA 98, 87-92 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 87-92
    • Furumai, R.1
  • 162
    • 0034001908 scopus 로고    scopus 로고
    • Transcriptional repression by neuronrestrictive silencer factor is mediated via the Sin3-histone deacetylase complex
    • Roopra, A. et al. Transcriptional repression by neuronrestrictive silencer factor is mediated via the Sin3-histone deacetylase complex. Mol. Cell. Biol. 20, 2147-2157 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2147-2157
    • Roopra, A.1
  • 163
    • 0032145527 scopus 로고    scopus 로고
    • A histone deacetylase corepressor complex regulates the Notch signal transduction pathway
    • Kao, H. Y. et al. A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev. 12, 2269-2277 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2269-2277
    • Kao, H.Y.1
  • 164
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
    • Zhang, Y. et al. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. Genes Dev. 13, 1924-1935 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1924-1935
    • Zhang, Y.1
  • 165
    • 0034817075 scopus 로고    scopus 로고
    • ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain
    • Amann, J. M. et al. ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol. Cell. Biol. 21, 6470-6483 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6470-6483
    • Amann, J.M.1
  • 166
    • 0034691131 scopus 로고    scopus 로고
    • The histone deacetylase-3 complex contains nuclear receptor corepressors
    • Wen, Y. D. et al. The histone deacetylase-3 complex contains nuclear receptor corepressors. Proc. Natl Acad. Sci. USA 97, 7202-7207 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7202-7207
    • Wen, Y.D.1
  • 167
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3
    • Li, J. et al. Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. EMBO J. 19, 4342-4350 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4342-4350
    • Li, J.1
  • 168
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger, C. M., Hassig, C. A. & Schreiber, S. L. Three proteins define a class of human histone deacetylases related to yeast Hda1p. PNAS 96, 4868-4873 (1999).
    • (1999) PNAS , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 169
    • 20444487771 scopus 로고    scopus 로고
    • Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility
    • Waltregny, D. et al. Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility. FASEB J. 19, 966-998 (2005).
    • (2005) FASEB J. , vol.19 , pp. 966-998
    • Waltregny, D.1
  • 170
    • 0034685893 scopus 로고    scopus 로고
    • MHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity
    • Lemercier, C. et al. mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity. J. Biol. Chem. 275, 15594-15599 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 15594-15599
    • Lemercier, C.1
  • 171
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington's Disease Collaborative Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72, 971-983 (1993).
    • (1993) Cell , vol.72 , pp. 971-983
  • 172
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • Spada, A. R. L., Wilson, E. M., Lubahn, D. B., Harding, A. E. & Fischbeck, K. H. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 352, 77-79 (1991).
    • (1991) Nature , vol.352 , pp. 77-79
    • Spada, A.R.L.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 173
    • 0028216760 scopus 로고
    • Unstable expansion of CAG repeat in hereditary dentatorubral- pallidoluysian atrophy (DRPLA)
    • Koide, R. et al. Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA). Nature Genet. 6, 9-13 (1994).
    • (1994) Nature Genet. , vol.6 , pp. 9-13
    • Koide, R.1
  • 174
    • 0028335386 scopus 로고
    • Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p
    • Nagafuchi, S. et al. Dentatorubral and pallidoluysian atrophy expansion of an unstable CAG trinucleotide on chromosome 12p. Nature Genet. 6, 14-18 (1994).
    • (1994) Nature Genet. , vol.6 , pp. 14-18
    • Nagafuchi, S.1
  • 175
    • 0027164698 scopus 로고
    • Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
    • Orr, H. T. et al. Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1. Nature Genet. 4, 221-226 (1993).
    • (1993) Nature Genet. , vol.4 , pp. 221-226
    • Orr, H.T.1
  • 176
    • 0027716371 scopus 로고
    • Presymptomatic analysis of spinocerebellar ataxia type 1 (SCA1) via the expansion of the SCA1 CAG-repeat in a large pedigree displaying anticipation and parental male bias
    • Matilla, T. et al. Presymptomatic analysis of spinocerebellar ataxia type 1 (SCA1) via the expansion of the SCA1 CAG-repeat in a large pedigree displaying anticipation and parental male bias. Hum. Mol. Genet. 2, 2123-2128 (1993).
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 2123-2128
    • Matilla, T.1
  • 177
    • 0030294345 scopus 로고    scopus 로고
    • Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats
    • Imbert, G. et al. Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats. Nature Genet. 14, 285-291 (1996).
    • (1996) Nature Genet. , vol.14 , pp. 285-291
    • Imbert, G.1
  • 178
    • 0030292368 scopus 로고    scopus 로고
    • Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT
    • Sanpei, K. et al. Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT. Nature Genet. 14, 277-284 (1996).
    • (1996) Nature Genet. , vol.14 , pp. 277-284
    • Sanpei, K.1
  • 179
    • 0030292488 scopus 로고    scopus 로고
    • Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2
    • Pulst, S.-M. et al. Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2. Nature Genet. 14, 269-276 (1996).
    • (1996) Nature Genet. , vol.14 , pp. 269-276
    • Pulst, S.-M.1
  • 180
    • 0028143527 scopus 로고
    • CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. 8
    • Kawaguchi, Y. et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. 8, Nature Genet. 221-228 (1994).
    • (1994) Nature Genet. , pp. 221-228
    • Kawaguchi, Y.1
  • 181
    • 0031012399 scopus 로고    scopus 로고
    • 1A-voltage-dependent calcium channel
    • 1A- voltage-dependent calcium channel. Nature Genet. 15, 62-69 (1997).
    • (1997) Nature Genet. , vol.15 , pp. 62-69
    • Zhuchenko, O.1
  • 182
    • 16944364511 scopus 로고    scopus 로고
    • Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion
    • David, G. et al. Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion. Nature Genet. 17, 65-70 (1997).
    • (1997) Nature Genet. , vol.17 , pp. 65-70
    • David, G.1
  • 183
    • 16144363213 scopus 로고    scopus 로고
    • An expanded CAG repeat sequence in spinocerebellar ataxia type 7
    • Lindblad, K. et al. An expanded CAG repeat sequence in spinocerebellar ataxia type 7. Genome Res. 6, 965-971 (1996).
    • (1996) Genome Res. , vol.6 , pp. 965-971
    • Lindblad, K.1
  • 184
    • 0032885515 scopus 로고    scopus 로고
    • A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: A new polyglutamine disease?
    • Koide, R. et al. A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease? Hum. Mol. Genet. 8, 2047-2053 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2047-2053
    • Koide, R.1
  • 185
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation
    • Schaffar, G. et al. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol. Cell 15, 95-105 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 95-105
    • Schaffar, G.1


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