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Volumn 3, Issue 4, 2006, Pages 403-408

Histone deacetylase inhibitors: A novel therapeutic approach to huntington's disease (complex mechanism of neuronal death)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE INHIBITOR; MESSENGER RNA; POLYGLUTAMINE;

EID: 33748450288     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720506778249407     Document Type: Review
Times cited : (61)

References (86)
  • 1
    • 0013218415 scopus 로고    scopus 로고
    • Bates G, Harper P, Jones L, editors New York: Oxford University Press
    • Bates G, Harper P, Jones L, editors. Huntington's Disease. 3rd ed. New York: Oxford University Press; (2002).
    • (2002) Huntington's Disease. 3rd Ed.
  • 2
    • 0024450903 scopus 로고
    • The functional anatomy of basal ganglia disorders
    • Albin RL, Young AB, Penney JB. The functional anatomy of basal ganglia disorders. Trends Neurosci. 12:366-375 (1989).
    • (1989) Trends Neurosci. , vol.12 , pp. 366-375
    • Albin, R.L.1    Young, A.B.2    Penney, J.B.3
  • 6
    • 0025885733 scopus 로고
    • Neuronal loss in layers V and VI of cerebral cortex in Huntington's disease
    • Hedreen JC, Peyser CE, Folstein SE, Ross CA. Neuronal loss in layers V and VI of cerebral cortex in Huntington's disease. Neurosci Lett 133:257-261 (1991).
    • (1991) Neurosci Lett , vol.133 , pp. 257-261
    • Hedreen, J.C.1    Peyser, C.E.2    Folstein, S.E.3    Ross, C.A.4
  • 8
    • 0023007832 scopus 로고
    • Neuropeptides in neurological disease
    • Beal MF, Martin JB. Neuropeptides in neurological disease. Ann Neurol 20(5):547-65 (1986).
    • (1986) Ann Neurol , vol.20 , Issue.5 , pp. 547-565
    • Beal, M.F.1    Martin, J.B.2
  • 10
    • 0025276132 scopus 로고
    • Striatal and nigral neuron subpopulations in rigid Huntington's disease: Implications for the functional anatomy of chorea and rigidity-akinesia
    • Albin RL, Reiner A, Anderson KD, Penney JB, Young AB. Striatal and nigral neuron subpopulations in rigid Huntington's disease: implications for the functional anatomy of chorea and rigidity-akinesia. Ann Neurol 27:357-365 (1990).
    • (1990) Ann Neurol , vol.27 , pp. 357-365
    • Albin, R.L.1    Reiner, A.2    Anderson, K.D.3    Penney, J.B.4    Young, A.B.5
  • 11
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is unstable in Huntington's disease chromosomes
    • Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is unstable in Huntington's disease chromosomes. Cell 72:971-983 (1993).
    • (1993) Cell , vol.72 , pp. 971-983
  • 13
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S, Liu JP, Chapman DL, Papaioannou VE, Efstratiadis A. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet 11:155-163 (1995).
    • (1995) Nat Genet , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 14
    • 0030613177 scopus 로고    scopus 로고
    • Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion
    • White JK, Auerbach W, Duyao MP, Vonsattel JP, Gusella JF, Joyner AL, et al. Huntingtin is required for neurogenesis and is not impaired by the Huntington's disease CAG expansion. Nat Genet 17(4):404-410 (1997).
    • (1997) Nat Genet , vol.17 , Issue.4 , pp. 404-410
    • White, J.K.1    Auerbach, W.2    Duyao, M.P.3    Vonsattel, J.P.4    Gusella, J.F.5    Joyner, A.L.6
  • 16
    • 0035805504 scopus 로고    scopus 로고
    • Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing
    • Rigamonti D, Sipione S, Goffredo D, Zuccato C, Fossale E, Cattaneo E. Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing. J Biol Chem 276(18):14545-8 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.18 , pp. 14545-14548
    • Rigamonti, D.1    Sipione, S.2    Goffredo, D.3    Zuccato, C.4    Fossale, E.5    Cattaneo, E.6
  • 17
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of N-Methyl-D-aspartate receptors via post-synaptic density 95
    • Sun Y, Savanenin A, Reddy PH, Liu YF. Polyglutamine-expanded huntingtin promotes sensitization of N-Methyl-D-aspartate receptors via post-synaptic density 95. J Biol Chem 276(27):24713-24718 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.27 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3    Liu, Y.F.4
  • 18
    • 0036500862 scopus 로고    scopus 로고
    • Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: Relevance to Huntington's disease
    • Hoffner G, Kahlem P, Djian P. Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease. J Cell Sci 115(Pt 5):941-8 (2002).
    • (2002) J Cell Sci , vol.115 , Issue.5 PART , pp. 941-948
    • Hoffner, G.1    Kahlem, P.2    Djian, P.3
  • 19
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia M, Sapp E, Chase K, Schwarz C, Meloni A, Young C, et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14(5):1075-81 (1995).
    • (1995) Neuron , vol.14 , Issue.5 , pp. 1075-1081
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3    Schwarz, C.4    Meloni, A.5    Young, C.6
  • 20
    • 0028220405 scopus 로고
    • Trinucleotide repeats in neurological diseases: An hypothesis concerning the pathogenesis of Huntington's disease, Kennedy's disease, and spinocerebellar ataxia type I
    • Cha JJ, Dure LS, IV. Trinucleotide repeats in neurological diseases: an hypothesis concerning the pathogenesis of Huntington's disease, Kennedy's disease, and spinocerebellar ataxia type I. Life Sci. 54:1459-1464 (1994).
    • (1994) Life Sci , vol.54 , pp. 1459-1464
    • Cha, J.J.1    Dure IV, L.S.2
  • 21
    • 0029968460 scopus 로고    scopus 로고
    • Trinucleotide repeats in neurogenetic disorders
    • Paulson HL, Fischbeck KH. Trinucleotide repeats in neurogenetic disorders. Annu Rev Neurosci 19:79-107 (1996).
    • (1996) Annu Rev Neurosci , vol.19 , pp. 79-107
    • Paulson, H.L.1    Fischbeck, K.H.2
  • 22
    • 0002538312 scopus 로고    scopus 로고
    • Huntington's disease and other trinucleotide repeat disorders
    • Martin JB, editor. New York: Scientific American, Inc.
    • Young AB. Huntington's disease and other trinucleotide repeat disorders. In: Martin JB, editor. Scientific American Molecular Neurology. New York: Scientific American, Inc.; p. 35-54 (1998).
    • (1998) Scientific American Molecular Neurology , pp. 35-54
    • Young, A.B.1
  • 24
    • 0025363346 scopus 로고
    • Excitotoxic injury of the neostriatum: A model for Huntington's disease
    • DiFiglia M. Excitotoxic injury of the neostriatum: a model for Huntington's disease. Trends Neurosci 13(7):286-289 (1990).
    • (1990) Trends Neurosci , vol.13 , Issue.7 , pp. 286-289
    • DiFiglia, M.1
  • 26
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal MF. Mitochondrial dysfunction in neurodegenerative diseases. Biochim Biophys Acta Bio Energetics 1366(1-2):211-223 (1998).
    • (1998) Biochim Biophys Acta Bio Energetics , vol.1366 , Issue.1-2 , pp. 211-223
    • Beal, M.F.1
  • 27
    • 0033914747 scopus 로고    scopus 로고
    • Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropallidoluysian atrophy
    • Lodi R, Schapira AH, Manners D, Styles P, Wood NW, Taylor DJ, et al. Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropallidoluysian atrophy. Ann. Neurol 48(1):72-6 (2000).
    • (2000) Ann Neurol , vol.48 , Issue.1 , pp. 72-76
    • Lodi, R.1    Schapira, A.H.2    Manners, D.3    Styles, P.4    Wood, N.W.5    Taylor, D.J.6
  • 29
    • 0027433553 scopus 로고
    • Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionaic acid
    • Beal MF, Brouillet E, Jenkins BG, Ferrante RJ, Kowall NW, Miller JM, et al. Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionaic acid. J Neurosci 13:4181-4192 (1993).
    • (1993) J Neurosci , vol.13 , pp. 4181-4192
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.G.3    Ferrante, R.J.4    Kowall, N.W.5    Miller, J.M.6
  • 31
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • Ona VO, Li M, Vonsattel JP, Andrews LJ, Khan SQ, Chung WM, et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease [see comments]. Nature 399(6733): 263-7 (1999).
    • (1999) Nature , vol.399 , Issue.6733 , pp. 263-267
    • Ona, V.O.1    Li, M.2    Vonsattel, J.P.3    Andrews, L.J.4    Khan, S.Q.5    Chung, W.M.6
  • 32
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington CL, Ellerby LM, Hackam AS, Margolis RL, Trifiro MA, Singaraja R, et al. Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J Biol Chem 273(15):9158-9167 (1998).
    • (1998) J Biol Chem , vol.273 , Issue.15 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3    Margolis, R.L.4    Trifiro, M.A.5    Singaraja, R.6
  • 33
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I, Xu CJ, Juo P, Kakizaka A, Blenis J, Yuan J. Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22(3):623-33 (1999).
    • (1999) Neuron , vol.22 , Issue.3 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 35
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA, DiFiglia M, Sharp AH, Ross CA, et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90(3):537-48 (1997).
    • (1997) Cell , vol.90 , Issue.3 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    DiFiglia, M.4    Sharp, A.H.5    Ross, C.A.6
  • 36
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions: A common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?
    • Ross CA. Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 19:1147-1150 (1997).
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 37
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castano JG, Aronin N, et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 20(19):7268-78 (2000).
    • (2000) J Neurosci , vol.20 , Issue.19 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6
  • 38
    • 0035364748 scopus 로고    scopus 로고
    • Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration
    • Petersen A, Larsen KE, Behr GG, Romero N, Przedborski S, Brundin P, et al. Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration. Hum Mol Genet 10(12):1243-54 (2001).
    • (2001) Hum Mol Genet , vol.10 , Issue.12 , pp. 1243-1254
    • Petersen, A.1    Larsen, K.E.2    Behr, G.G.3    Romero, N.4    Przedborski, S.5    Brundin, P.6
  • 39
    • 0032568517 scopus 로고    scopus 로고
    • Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human Huntington disease gene
    • Cha J-HJ, Kosinski CM, Kerner JA, Alsdorf SA, Mangiarini L, Davies SW, 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).
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6480-6485
    • Cha, J.-H.J.1    Kosinski, C.M.2    Kerner, J.A.3    Alsdorf, S.A.4    Mangiarini, L.5    Davies, S.W.6
  • 40
    • 0034283877 scopus 로고    scopus 로고
    • Transcriptional dysregulation in Huntington's disease
    • Cha J-HJ. 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
  • 42
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars KL, Rubinsztein DC. Transcriptional abnormalities in Huntington disease. Trends Genet 19(5):233-8 (2003).
    • (2003) Trends Genet , vol.19 , Issue.5 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 43
    • 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, Hanson SA, Strand AD, Bergstrom DA, Chun W, Peters NL, 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    Hanson, S.A.2    Strand, A.D.3    Bergstrom, D.A.4    Chun, W.5    Peters, N.L.6
  • 44
    • 0141828353 scopus 로고    scopus 로고
    • Mechanisms of transcriptional dysregulation in Huntington's disease
    • Luthi-Carter R, Cha J-HJ. Mechanisms of transcriptional dysregulation in Huntington's disease. Clin Neurosci Res 3:165-177 (2003).
    • (2003) Clin Neurosci Res , vol.3 , pp. 165-177
    • Luthi-Carter, R.1    Cha, J.-H.J.2
  • 45
    • 23444458415 scopus 로고
    • Transcriptional activation modulated by homopolymeric glutamine and proline stretches
    • Gerber HP, Seipel K, Georgiev O, Höfferer M, Hug M, Rusconi S, et al. Transcriptional activation modulated by homopolymeric glutamine and proline stretches. Science 263:808-811 (1994).
    • (1994) Science , vol.263 , pp. 808-811
    • Gerber, H.P.1    Seipel, K.2    Georgiev, O.3    Höfferer, M.4    Hug, M.5    Rusconi, S.6
  • 46
    • 0029983147 scopus 로고    scopus 로고
    • Trinucleotide repeats and long homopeptides in genes and proteins associated with nervous system disease and development
    • Karlin S, Burge C. Trinucleotide repeats and long homopeptides in genes and proteins associated with nervous system disease and development. Proc Natl Acad Sci USA 93:1560-1565 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1560-1565
    • Karlin, S.1    Burge, C.2
  • 47
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora FC Jr, Sasaki M, Peters MF, Huang H, Cooper JK, Yamada M, et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291(5512):2423-8 (2001).
    • (2001) Science , vol.291 , Issue.5512 , pp. 2423-2428
    • Nucifora Jr., F.C.1    Sasaki, M.2    Peters, M.F.3    Huang, H.4    Cooper, J.K.5    Yamada, M.6
  • 48
    • 0032450856 scopus 로고    scopus 로고
    • Amyloid formation by mutant huntingtin: Threshold, progressivity and recruitment of normal polyglutamine proteins
    • Huang CC, Faber PW, Persichetti F, Mittal V, Vonsattel JP, MacDonald ME, et al. Amyloid formation by mutant huntingtin: Threshold, progressivity and recruitment of normal polyglutamine proteins. Somat. Cell Mol Genet 24(4):217-233 (1998).
    • (1998) Somat Cell Mol Genet , vol.24 , Issue.4 , pp. 217-233
    • Huang, C.C.1    Faber, P.W.2    Persichetti, F.3    Mittal, V.4    Vonsattel, J.P.5    MacDonald, M.E.6
  • 49
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah AW, Jeong H, Griffin A, Kim YM, Standaert DG, Hersch SM, et al . Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296(5576):2238-43 (2002).
    • (2002) Science , vol.296 , Issue.5576 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3    Kim, Y.M.4    Standaert, D.G.5    Hersch, S.M.6
  • 50
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan JS, Bodai L, Pallos J, Poelman M, McCampbell A, Apostol BL, et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 413(6857): 739-43 (2001).
    • (2001) Nature , vol.413 , Issue.6857 , pp. 739-743
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3    Poelman, M.4    McCampbell, A.5    Apostol, B.L.6
  • 51
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante RJ, Kubilus JK, Lee J, Ryu H, Beesen A, Zucker B, et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J Neurosci 23(28):9418-27 (2003).
    • (2003) J Neurosci , vol.23 , Issue.28 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3    Ryu, H.4    Beesen, A.5    Zucker, B.6
  • 52
    • 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, Richon VM, Woodman B, Smith DL, Zhou X, Rosa 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).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2041-2046
    • Hockly, E.1    Richon, V.M.2    Woodman, B.3    Smith, D.L.4    Zhou, X.5    Rosa, E.6
  • 53
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
    • Gardian G, Browne SE, Choi DK, Klivenyi P, Gregorio J, Kubilus JK, et al. Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease. J Biol Chem 280(1):556-63 (2005).
    • (2005) J Biol Chem , vol.280 , Issue.1 , pp. 556-563
    • Gardian, G.1    Browne, S.E.2    Choi, D.K.3    Klivenyi, P.4    Gregorio, J.5    Kubilus, J.K.6
  • 54
    • 0030612119 scopus 로고    scopus 로고
    • Dopamine D1 and D2 receptor gene expression in the striatum in Huntington's disease
    • Augood SJ, Faull RLM, Emson PC. Dopamine D1 and D2 receptor gene expression in the striatum in Huntington's disease. Ann Neurol 42:215-221 (1997).
    • (1997) Ann Neurol , vol.42 , pp. 215-221
    • Augood, S.J.1    Faull, R.L.M.2    Emson, P.C.3
  • 56
    • 33744532300 scopus 로고    scopus 로고
    • Neurochemistry of Huntington's disease
    • Bates GP, Harper PS, Jones AL, editors. London: Oxford Medical Publications
    • Yohrling GJ, Cha J-HJ. Neurochemistry of Huntington's disease. In: Bates GP, Harper PS, Jones AL, editors. Huntington's Disease. 3rd ed. London: Oxford Medical Publications; 2002. p. 276-308.
    • (2002) Huntington's Disease. 3rd Ed. , pp. 276-308
    • Yohrling, G.J.1    Cha, J.-H.J.2
  • 57
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini L, Sathasivam K, Seller M, Cozens B, Harper A, Hetherington C, et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87:493-506 (1996).
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5    Hetherington, C.6
  • 58
    • 0029895292 scopus 로고    scopus 로고
    • Striatal D1 and D2 dopamine receptor loss in asymptomatic mutation carriers of Huntington's disease
    • Weeks RA, Piccini P, Harding AE, Brooks DJ. Striatal D1 and D2 dopamine receptor loss in asymptomatic mutation carriers of Huntington's disease. Ann Neurol 40:49-54 (1996).
    • (1996) Ann Neurol , vol.40 , pp. 49-54
    • Weeks, R.A.1    Piccini, P.2    Harding, A.E.3    Brooks, D.J.4
  • 61
    • 10944265363 scopus 로고    scopus 로고
    • Mutant huntingtin affects the rate of transcription of striatum-specific isoforms of phosphodiesterase 10A
    • Hu H, McCaw EA, Hebb AL, Gomez GT, Denovan-Wright EM. Mutant huntingtin affects the rate of transcription of striatum-specific isoforms of phosphodiesterase 10A. Eur J Neurosci 20(12):3351-63 (2004).
    • (2004) Eur J Neurosci , vol.20 , Issue.12 , pp. 3351-3363
    • Hu, H.1    McCaw, E.A.2    Hebb, A.L.3    Gomez, G.T.4    Denovan-Wright, E.M.5
  • 62
    • 11244306357 scopus 로고    scopus 로고
    • Structure, expression and regulation of the cannabinoid receptor gene (CB1) in Huntington's disease transgenic mice
    • McCaw EA, Hu H, Gomez GT, Hebb AL, Kelly ME, Denovan-Wright EM. Structure, expression and regulation of the cannabinoid receptor gene (CB1) in Huntington's disease transgenic mice. Eur J Biochem 271(23-24):4909-20 (2004).
    • (2004) Eur J Biochem , vol.271 , Issue.23-24 , pp. 4909-4920
    • McCaw, E.A.1    Hu, H.2    Gomez, G.T.3    Hebb, A.L.4    Kelly, M.E.5    Denovan-Wright, E.M.6
  • 63
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling G, Becher MW, Sharp AH, Jinnah HA, Duan K, Kotzuk JA, et al . Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum Mol Genet 8(3):397-407 (1999).
    • (1999) Hum Mol Genet , vol.8 , Issue.3 , pp. 397-407
    • Schilling, G.1    Becher, M.W.2    Sharp, A.H.3    Jinnah, H.A.4    Duan, K.5    Kotzuk, J.A.6
  • 64
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 403(6765):41-5 (2000).
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 65
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 293:1074-1080 (2001).
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 68
    • 85044700833 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer
    • Davis PK, Brackmann RK. Chromatin remodeling and cancer. Cancer Biol Ther 2(1):22-9 (2003).
    • (2003) Cancer Biol Ther , vol.2 , Issue.1 , pp. 22-29
    • Davis, P.K.1    Brackmann, R.K.2
  • 70
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks PA, Richon VM, Rifkind RA. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J Natl Cancer Inst 92(15):1210-6 (2000).
    • (2000) J Natl Cancer Inst , vol.92 , Issue.15 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 71
    • 0034905872 scopus 로고    scopus 로고
    • Inhibition of transformed cell growth and induction of cellular differentiation by pyroxamide, an inhibitor of histone deacetylase
    • Butler LM, Webb Y, Agus DB, Higgins B, Tolentino TR, Kutko MC, et al . Inhibition of transformed cell growth and induction of cellular differentiation by pyroxamide, an inhibitor of histone deacetylase. Clin Cancer Res (4):962-70 (2001).
    • (2001) Clin Cancer Res , Issue.4 , pp. 962-970
    • Butler, L.M.1    Webb, Y.2    Agus, D.B.3    Higgins, B.4    Tolentino, T.R.5    Kutko, M.C.6
  • 72
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhoff TW, Rifkind RA, Marks PA. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci USA 97(18):10014-9 (2000).
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 73
    • 0036176617 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer treatment
    • Vigushin DM, Coombes RC. Histone deacetylase inhibitors in cancer treatment. Anticancer Drugs 13(1):1-13 (2002).
    • (2002) Anticancer Drugs , vol.13 , Issue.1 , pp. 1-13
    • Vigushin, D.M.1    Coombes, R.C.2
  • 74
    • 0035031779 scopus 로고    scopus 로고
    • Polyglutamine and CBP: Fatal attraction?
    • McCampbell A, Fischbeck KH. Polyglutamine and CBP: fatal attraction? Nat Med 7(5):528-30 (2001).
    • (2001) Nat Med , vol.7 , Issue.5 , pp. 528-530
    • McCampbell, A.1    Fischbeck, K.H.2
  • 76
    • 0037961686 scopus 로고    scopus 로고
    • Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation
    • Igarashi S, Morita H, Bennett KM, Tanaka Y, Engelender S, Peters MF, et al. Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation. Neuroreport 14(4):565-8 (2003).
    • (2003) Neuroreport , vol.14 , Issue.4 , pp. 565-568
    • Igarashi, S.1    Morita, H.2    Bennett, K.M.3    Tanaka, Y.4    Engelender, S.5    Peters, M.F.6
  • 77
    • 4544323749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Understanding a new wave of anticancer agents
    • Villar-Garea A, Esteller M. Histone deacetylase inhibitors: understanding a new wave of anticancer agents. Int J Cancer 112(2):171-8 (2004).
    • (2004) Int J Cancer , vol.112 , Issue.2 , pp. 171-178
    • Villar-Garea, A.1    Esteller, M.2
  • 78
    • 0020262168 scopus 로고
    • beta-Adrenergic receptor induction in HeLa cells: Synergistic effect of 5-azacytidine and butyrate
    • Jahangeer S, Elliott RM, Henneberry RC. beta-Adrenergic receptor induction in HeLa cells: synergistic effect of 5-azacytidine and butyrate. Biochem Biophys Res Commun 108(4):1434-40 (1982).
    • (1982) Biochem Biophys Res Commun , vol.108 , Issue.4 , pp. 1434-1440
    • Jahangeer, S.1    Elliott, R.M.2    Henneberry, R.C.3
  • 80
    • 0038677606 scopus 로고    scopus 로고
    • Inhibition of Histone Deacetylase activity increases chromosomal instability by the aberrant regulation of mitotic check point activation
    • Shin HJ, Baek KH, Jeon AH, Kin SJ, Jang, KL, Sung YC, et al. Inhibition of Histone Deacetylase activity increases chromosomal instability by the aberrant regulation of mitotic check point activation. Oncogene 2003; 22(25): 3853-8.
    • (2003) Oncogene , vol.22 , Issue.25 , pp. 3853-3858
    • Shin, H.J.1    Baek, K.H.2    Jeon, A.H.3    Kin, S.J.4    Jang, K.L.5    Sung, Y.C.6
  • 81
    • 0028303870 scopus 로고
    • Induction of fetal hemoglobin production in subjects with sickle cell anemia by oral sodium phenylbutyrate
    • Dover GJ, Brusilow S, Charache S. Induction of fetal hemoglobin production in subjects with sickle cell anemia by oral sodium phenylbutyrate. Blood 84(1):339-43 (1994).
    • (1994) Blood , vol.84 , Issue.1 , pp. 339-343
    • Dover, G.J.1    Brusilow, S.2    Charache, S.3
  • 82
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrosis patients: Partial restoration of nasal epithelial CFTR function
    • Rubenstein RC, Zeitlin PL. A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrosis patients: partial restoration of nasal epithelial CFTR function. Am J Respir Crit Care Med 157(2):484-90 (1998).
    • (1998) Am J Respir Crit Care Med , vol.157 , Issue.2 , pp. 484-490
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 83
    • 0032709471 scopus 로고    scopus 로고
    • Hydroxyurea and sodium phenylbutyrate therapy in thalassemia intermedia
    • Hoppe C, Vichinsky E, Lewis B, Foote D, Styles L. Hydroxyurea and sodium phenylbutyrate therapy in thalassemia intermedia. Am J Hematol 62(4):221-7 (1999).
    • (1999) Am J Hematol , vol.62 , Issue.4 , pp. 221-227
    • Hoppe, C.1    Vichinsky, E.2    Lewis, B.3    Foote, D.4    Styles, L.5
  • 84
    • 0034796871 scopus 로고    scopus 로고
    • A Phase I clinical and pharmacological evaluation of sodium phenylbutyrate on an 120-h infusion schedule
    • Carducci MA, Gilbert J, Bowling MK, Noe D, Eisenberger MA, Sinibaldi V, et al. A Phase I clinical and pharmacological evaluation of sodium phenylbutyrate on an 120-h infusion schedule. Clin Cancer Res 7(10):3047-55 (2001).
    • (2001) Clin Cancer Res , vol.7 , Issue.10 , pp. 3047-3055
    • Carducci, M.A.1    Gilbert, J.2    Bowling, M.K.3    Noe, D.4    Eisenberger, M.A.5    Sinibaldi, V.6
  • 85
    • 0034885248 scopus 로고    scopus 로고
    • A phase I dose escalation and bioavailability study of oral sodium phenylbutyrate in patients with refractory solid tumor malignancies
    • Gilbert J, Baker SD, Bowling MK, Grochow L, Figg WD, Zabelina Y, et al. A phase I dose escalation and bioavailability study of oral sodium phenylbutyrate in patients with refractory solid tumor malignancies. Clin Cancer Res 7(8):2292-300 (2001).
    • (2001) Clin Cancer Res , vol.7 , Issue.8 , pp. 2292-2300
    • Gilbert, J.1    Baker, S.D.2    Bowling, M.K.3    Grochow, L.4    Figg, W.D.5    Zabelina, Y.6
  • 86
    • 12444321545 scopus 로고    scopus 로고
    • Phase I clinical trial of histone deacetylase inhibitor: Suberoylanilide hydroxamic acid administered intravenously
    • Kelly WK, Richon VM, O'Connor O, Curley T, MacGregor-Curtelli B, Tong W, et al. Phase I clinical trial of histone deacetylase inhibitor: suberoylanilide hydroxamic acid administered intravenously. Clin Cancer Res 9(10 Pt 1):3578-88 (2003).
    • (2003) Clin Cancer Res , vol.9 , Issue.10 PART 1 , pp. 3578-3588
    • Kelly, W.K.1    Richon, V.M.2    O'Connor, O.3    Curley, T.4    MacGregor-Curtelli, B.5    Tong, W.6


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