메뉴 건너뛰기




Volumn 7, Issue 6, 2014, Pages 634-661

Involvement of HDAC1 and HDAC3 in the pathology of polyglutamine disorders: Therapeutic implications for selective HDAC1/HDAC3 inhibitors

Author keywords

Chromatin; HDAC1; HDAC3; Histone; Histone deacetylase (HDAC); Mechanism; Neurodegenerative; Polyglutamine; Selective; Subtype

Indexed keywords

ATAXIN 1; BRAIN DERIVED NEUROTROPHIC FACTOR; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE INHIBITOR; HUNTINGTIN; POLYGLUTAMINE; VALPROIC ACID;

EID: 84901505786     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph7060634     Document Type: Review
Times cited : (41)

References (146)
  • 1
    • 0042869974 scopus 로고    scopus 로고
    • Polyglutamine diseases: A transcription disorder?
    • Okazawa, H. Polyglutamine diseases: A transcription disorder? Cell Mol. Life Sci. 2003, 60, 1427-1439.
    • (2003) Cell Mol. Life Sci , vol.60 , pp. 1427-1439
    • Okazawa, H.1
  • 2
    • 84866139184 scopus 로고    scopus 로고
    • Polyglutamine (polyQ) disorders: The chromatin connection
    • Cohen-Carmon, D.; Meshorer, E. Polyglutamine (polyQ) disorders: The chromatin connection. Nucleus 2012, 3, 433-441.
    • (2012) Nucleus , vol.3 , pp. 433-441
    • Cohen-Carmon, D.1    Meshorer, E.2
  • 3
    • 33748928786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
    • Butler, R.; Bates, G.P. Histone deacetylase inhibitors as therapeutics for polyglutamine disorders. Nat. Rev. Neurosci. 2006, 7, 784-796.
    • (2006) Nat. Rev. Neurosci , vol.7 , pp. 784-796
    • Butler, R.1    Bates, G.P.2
  • 4
    • 67349227787 scopus 로고    scopus 로고
    • Isoform-specific histone deacetylase inhibitors: The next step?
    • Balasubramanian, S.; Verner, E.; Buggy, J.J. Isoform-specific histone deacetylase inhibitors: The next step? Cancer Lett. 2009, 280, 211-221.
    • (2009) Cancer Lett , vol.280 , pp. 211-221
    • Balasubramanian, S.1    Verner, E.2    Buggy, J.J.3
  • 5
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu, W.S.; Parmigiani, R.B.; Marks, P.A. Histone deacetylase inhibitors: Molecular mechanisms of action. Oncogene 2007, 26, 5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 7
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg, R.D.; Lorch, Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 1999, 98, 285-294.
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 8
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D.; Allis, C.D. The language of covalent histone modifications. Nature 2000, 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 9
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner, D.E.; Berger, S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 2000, 64, 435-459.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 10
    • 34249793251 scopus 로고    scopus 로고
    • Histone acetylation and methylation: Combinatorial players for transcriptional regulation
    • An, W. Histone acetylation and methylation: Combinatorial players for transcriptional regulation. Subcell Biochem. 2007, 41, 351-369.
    • (2007) Subcell Biochem , vol.41 , pp. 351-369
    • An, W.1
  • 11
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti, I.V.; Lee, Y.M.; Goodson, H.V. Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis. J. Mol. Biol. 2004, 338, 17-31.
    • (2004) J. Mol. Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 12
    • 0030812917 scopus 로고    scopus 로고
    • Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
    • Leipe, D.D.; Landsman, D. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res. 1997, 25, 3693-3697.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3693-3697
    • Leipe, D.D.1    Landsman, D.2
  • 13
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G.; Guarente, L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 2004, 73, 417-435.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 14
    • 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. 2002, 277, 25748-25755.
    • (2002) J. Biol. Chem , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 16
    • 34248656480 scopus 로고    scopus 로고
    • Histone deacetylases-An important class of cellular regulators with a variety of functions
    • Hildmann, C.; Riester, D.; Schwienhorst, A. Histone deacetylases-An important class of cellular regulators with a variety of functions. Appl. Microbiol. Biotechnol. 2007, 75, 487-497.
    • (2007) Appl. Microbiol. Biotechnol , vol.75 , pp. 487-497
    • Hildmann, C.1    Riester, D.2    Schwienhorst, A.3
  • 18
    • 84862875593 scopus 로고    scopus 로고
    • Multiple roles of class I HDACs in proliferation, differentiation, and development
    • Reichert, N.; Choukrallah, M.A.; Matthias, P. Multiple roles of class I HDACs in proliferation, differentiation, and development. Cell Mol. Life Sci. 2012, 69, 2173-2187.
    • (2012) Cell Mol. Life Sci , vol.69 , pp. 2173-2187
    • Reichert, N.1    Choukrallah, M.A.2    Matthias, P.3
  • 21
    • 84873376098 scopus 로고    scopus 로고
    • Evaluation of histone deacetylases as drug targets in Huntington's disease models. Study of HDACs in brain tissues from R6/2 and CAG140 knock-in HD mouse models and human patients and in a neuronal HD cell model
    • Quinti, L.; Chopra, V.; Rotili, D.; Valente, S.; Amore, A.; Franci, G.; Meade, S.; Valenza, M.; Altucci, L.; Maxwell, M.M.; et al. Evaluation of histone deacetylases as drug targets in Huntington's disease models. Study of HDACs in brain tissues from R6/2 and CAG140 knock-in HD mouse models and human patients and in a neuronal HD cell model. PLoS Curr. 2010, 1, 1-16.
    • (2010) PLoS Curr , vol.1 , pp. 1-16
    • Quinti, L.1    Chopra, V.2    Rotili, D.3    Valente, S.4    Amore, A.5    Franci, G.6    Meade, S.7    Valenza, M.8    Altucci, L.9    Maxwell, M.M.10
  • 22
    • 82155182012 scopus 로고    scopus 로고
    • SAHA decreases HDAC 2 and 4 levels in vivo and improves molecular phenotypes in the R6/2 mouse model of Huntington's disease
    • Mielcarek, M.; Benn, C.L.; Franklin, S.A.; Smith, D.L.; Woodman, B.; Marks, P.A.; Bates, G.P. SAHA decreases HDAC 2 and 4 levels in vivo and improves molecular phenotypes in the R6/2 mouse model of Huntington's disease. PLoS One 2011, 6, e27746.
    • (2011) PLoS One , vol.6
    • Mielcarek, M.1    Benn, C.L.2    Franklin, S.A.3    Smith, D.L.4    Woodman, B.5    Marks, P.A.6    Bates, G.P.7
  • 23
    • 84875228213 scopus 로고    scopus 로고
    • Histone deacetylase class II and acetylated core histone immunohistochemistry in human brains with Huntington's disease
    • Yeh, H.H.; Young, D.; Gelovani, J.G.; Robinson, A.; Davidson, Y.; Herholz, K.; Mann, D.M. Histone deacetylase class II and acetylated core histone immunohistochemistry in human brains with Huntington's disease. Brain Res. 2013, 1504, 16-24.
    • (2013) Brain Res , vol.1504 , pp. 16-24
    • Yeh, H.H.1    Young, D.2    Gelovani, J.G.3    Robinson, A.4    Davidson, Y.5    Herholz, K.6    Mann, D.M.7
  • 24
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J.P.; Godin, J.D.; Charrin, B.C.; Cordelieres, F.P.; King, S.J.; Humbert, S.; Saudou, F. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 2007, 27, 3571-3583.
    • (2007) J. Neurosci , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 26
    • 0037199944 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 2 by protein kinase CK2
    • Tsai, S.C.; Seto, E. Regulation of histone deacetylase 2 by protein kinase CK2. J. Biol. Chem. 2002, 277, 31826-31833.
    • (2002) J. Biol. Chem , vol.277 , pp. 31826-31833
    • Tsai, S.C.1    Seto, E.2
  • 27
    • 70349227061 scopus 로고    scopus 로고
    • Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation
    • Brunmeir, R.; Lagger, S.; Seiser, C. Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation. Int. J. Dev. Biol. 2009, 53, 275-289.
    • (2009) Int. J. Dev. Biol , vol.53 , pp. 275-289
    • Brunmeir, R.1    Lagger, S.2    Seiser, C.3
  • 31
    • 84862819579 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors targeting HDAC3 and HDAC1 ameliorate polyglutamine-elicited phenotypes in model systems of Huntington's disease
    • Jia, H.; Pallos, J.; Jacques, V.; Lau, A.; Tang, B.; Cooper, A.; Syed, A.; Purcell, J.; Chen, Y.; Sharma, S.; et al. Histone deacetylase (HDAC) inhibitors targeting HDAC3 and HDAC1 ameliorate polyglutamine-elicited phenotypes in model systems of Huntington's disease. Neurobiol. Dis. 2012, 46, 351-361.
    • (2012) Neurobiol. Dis , vol.46 , pp. 351-361
    • Jia, H.1    Pallos, J.2    Jacques, V.3    Lau, A.4    Tang, B.5    Cooper, A.6    Syed, A.7    Purcell, J.8    Chen, Y.9    Sharma, S.10
  • 33
    • 69849093083 scopus 로고    scopus 로고
    • Focal nature of neurological disorders necessitates isotype-selective histone deacetylase (HDAC) inhibitors
    • Thomas, E.A. Focal nature of neurological disorders necessitates isotype-selective histone deacetylase (HDAC) inhibitors. Mol. Neurobiol. 2009, 40, 33-45.
    • (2009) Mol. Neurobiol , vol.40 , pp. 33-45
    • Thomas, E.A.1
  • 36
    • 58049214866 scopus 로고    scopus 로고
    • A novel germ cell-specific protein, SHIP1, forms a complex with chromatin remodeling activity during spermatogenesis
    • Choi, E.; Han, C.; Park, I.; Lee, B.; Jin, S.; Choi, H.; Kim do, H.; Park, Z.Y.; Eddy, E.M.; Cho, C. A novel germ cell-specific protein, SHIP1, forms a complex with chromatin remodeling activity during spermatogenesis. J. Biol. Chem. 2008, 283, 35283-35294.
    • (2008) J. Biol. Chem , vol.283 , pp. 35283-35294
    • Choi, E.1    Han, C.2    Park, I.3    Lee, B.4    Jin, S.5    Choi, H.6    do Kim, H.7    Park, Z.Y.8    Eddy, E.M.9    Cho, C.10
  • 37
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang, W.M.; Yao, Y.L.; Sun, J.M.; Davie, J.R.; Seto, E. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem. 1997, 272, 28001-28007.
    • (1997) J. Biol. Chem , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 38
    • 0034717022 scopus 로고    scopus 로고
    • N-terminal region, C-terminal region, nuclear export signal, and deacetylation activity of histone deacetylase-3 are essential for the viability of the DT40 chicken B cell line
    • Takami, Y.; Nakayama, T. N-terminal region, C-terminal region, nuclear export signal, and deacetylation activity of histone deacetylase-3 are essential for the viability of the DT40 chicken B cell line. J. Biol. Chem. 2000, 275, 16191-16201.
    • (2000) J. Biol. Chem , vol.275 , pp. 16191-16201
    • Takami, Y.1    Nakayama, T.2
  • 39
    • 41549156540 scopus 로고    scopus 로고
    • Deletion of histone deacetylase 3 reveals critical roles in S phase progression and DNA damage control
    • Bhaskara, S.; Chyla, B.J.; Amann, J.M.; Knutson, S.K.; Cortez, D.; Sun, Z.W.; Hiebert, S.W. Deletion of histone deacetylase 3 reveals critical roles in S phase progression and DNA damage control. Mol. Cell 2008, 30, 61-72.
    • (2008) Mol. Cell , vol.30 , pp. 61-72
    • Bhaskara, S.1    Chyla, B.J.2    Amann, J.M.3    Knutson, S.K.4    Cortez, D.5    Sun, Z.W.6    Hiebert, S.W.7
  • 41
    • 22344446199 scopus 로고    scopus 로고
    • Histone modifications affect timing of oligodendrocyte progenitor differentiation in the developing rat brain
    • Shen, S.; Li, J.; Casaccia-Bonnefil, P. Histone modifications affect timing of oligodendrocyte progenitor differentiation in the developing rat brain. J. Cell Biol. 2005, 169, 577-589.
    • (2005) J. Cell Biol , vol.169 , pp. 577-589
    • Shen, S.1    Li, J.2    Casaccia-Bonnefil, P.3
  • 45
    • 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.; Dequiedt, F.; Hendzel, M.J.; Guenther, M.G.; Lazar, M.A.; Voelter, W.; Verdin, E. Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 2002, 9,45-57.
    • (2002) Mol. Cell , vol.9 , pp. 45-57
    • Fischle, W.1    Dequiedt, F.2    Hendzel, M.J.3    Guenther, M.G.4    Lazar, M.A.5    Voelter, W.6    Verdin, E.7
  • 46
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang, E.Y.; Zhang, J.; Miska, E.A.; Guenther, M.G.; Kouzarides, T.; Lazar, M.A. Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 2000, 14, 45-54.
    • (2000) Genes Dev , vol.14 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 48
    • 84867431257 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC1) is a molecular switch between neuronal survival and death
    • Bardai, F.H.; Price, V.; Zaayman, M.; Wang, L.; D'Mello, S.R. Histone deacetylase (HDAC1) is a molecular switch between neuronal survival and death. J. Biol. Chem. 2012, 287, 35444-35453.
    • (2012) J. Biol. Chem , vol.287 , pp. 35444-35453
    • Bardai, F.H.1    Price, V.2    Zaayman, M.3    Wang, L.4    D'Mello, S.R.5
  • 49
    • 79551517312 scopus 로고    scopus 로고
    • Selective toxicity by HDAC3 in neurons: Regulation by Akt and GSK3beta
    • Bardai, F.H.; D'Mello, S.R. Selective toxicity by HDAC3 in neurons: Regulation by Akt and GSK3beta. J. Neurosci 2011, 31, 1746-1751.
    • (2011) J. Neurosci , vol.31 , pp. 1746-1751
    • Bardai, F.H.1    D'Mello, S.R.2
  • 50
    • 75549089982 scopus 로고    scopus 로고
    • HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage
    • Kim, J.Y.; Shen, S.; Dietz, K.; He, Y.; Howell, O.; Reynolds, R.; Casaccia, P. HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage. Nat. Neurosci. 2010, 13, 180-189.
    • (2010) Nat. Neurosci , vol.13 , pp. 180-189
    • Kim, J.Y.1    Shen, S.2    Dietz, K.3    He, Y.4    Howell, O.5    Reynolds, R.6    Casaccia, P.7
  • 54
    • 33744504676 scopus 로고    scopus 로고
    • Mechanisms of disease: Histone modifications in Huntington's disease
    • Sadri-Vakili, G.; Cha, J.H. Mechanisms of disease: Histone modifications in Huntington's disease. Nat. Clin. Pract. Neurol. 2006, 2, 330-338.
    • (2006) Nat. Clin. Pract. Neurol , vol.2 , pp. 330-338
    • Sadri-Vakili, G.1    Cha, J.H.2
  • 55
    • 84879137604 scopus 로고    scopus 로고
    • Genomic landscape of transcriptional and epigenetic dysregulation in early onset polyglutamine disease
    • Valor, L.M.; Guiretti, D.; Lopez-Atalaya, J.P.; Barco, A. Genomic landscape of transcriptional and epigenetic dysregulation in early onset polyglutamine disease. J. Neurosci. 2013, 33, 10471-10482.
    • (2013) J. Neurosci , vol.33 , pp. 10471-10482
    • Valor, L.M.1    Guiretti, D.2    Lopez-Atalaya, J.P.3    Barco, A.4
  • 57
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group
    • Huntington's Disease Research Group
    • Huntington's Disease Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 1993, 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 61
    • 34547839797 scopus 로고    scopus 로고
    • Mutant huntingtin's effects on striatal gene expression in mice recapitulate changes observed in human Huntington's disease brain and do not differ with mutant huntingtin length or wild-type huntingtin dosage
    • Kuhn, A.; Goldstein, D.R.; Hodges, A.; Strand, A.D.; Sengstag, T.; Kooperberg, C.; Becanovic, K.; Pouladi, M.A.; Sathasivam, K.; Cha, J.H.; et al. Mutant huntingtin's effects on striatal gene expression in mice recapitulate changes observed in human Huntington's disease brain and do not differ with mutant huntingtin length or wild-type huntingtin dosage. Hum. Mol. Genet. 2007, 16, 1845-1861.
    • (2007) Hum. Mol. Genet , vol.16 , pp. 1845-1861
    • Kuhn, A.1    Goldstein, D.R.2    Hodges, A.3    Strand, A.D.4    Sengstag, T.5    Kooperberg, C.6    Becanovic, K.7    Pouladi, M.A.8    Sathasivam, K.9    Cha, J.H.10
  • 63
    • 84880422675 scopus 로고    scopus 로고
    • Disassociation of histone deacetylase-3 from normal huntingtin underlies mutant huntingtin neurotoxicity
    • Bardai, F.H.; Verma, P.; Smith, C.; Rawat, V.; Wang, L.; D'Mello, S.R. Disassociation of histone deacetylase-3 from normal huntingtin underlies mutant huntingtin neurotoxicity. J. Neurosci. 2013, 33, 11833-11838.
    • (2013) J. Neurosci , vol.33 , pp. 11833-11838
    • Bardai, F.H.1    Verma, P.2    Smith, C.3    Rawat, V.4    Wang, L.5    D'Mello, S.R.6
  • 64
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar, B.; Vacher, C.; Berger, Z.; Davies, J.E.; Luo, S.; Oroz, L.G.; Scaravilli, F.; Easton, D.F.; Duden, R.; O'Kane, C.J.; et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat. Genet. 2004, 36, 585-595.
    • (2004) Nat. Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6    Scaravilli, F.7    Easton, D.F.8    Duden, R.9    O'Kane, C.J.10
  • 65
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto, A.; Cremona, M.L.; Rothman, J.E. Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J. Cell Biol. 2006, 172, 719-731.
    • (2006) J. Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 68
    • 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. 2006, 26, 2830-2838.
    • (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
  • 69
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos, J.; Bodai, L.; Lukacsovich, T.; Purcell, J.M.; Steffan, J.S.; Thompson, L.M.; Marsh, J.L. Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 2008, 17, 3767-3775.
    • (2008) Hum. Mol. Genet , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6    Marsh, J.L.7
  • 70
    • 84856710176 scopus 로고    scopus 로고
    • Genetic knock-down of HDAC3 does not modify disease-related phenotypes in a mouse model of Huntington's disease
    • Moumne, L.; Campbell, K.; Howland, D.; Ouyang, Y.; Bates, G.P. Genetic knock-down of HDAC3 does not modify disease-related phenotypes in a mouse model of Huntington's disease. PLoS One 2012, 7, e31080.
    • (2012) PLoS One , vol.7
    • Moumne, L.1    Campbell, K.2    Howland, D.3    Ouyang, Y.4    Bates, G.P.5
  • 71
    • 65849288724 scopus 로고    scopus 로고
    • Spinocerebellar ataxias caused by polyglutamine expansions: A review of therapeutic strategies
    • Underwood, B.R.; Rubinsztein, D.C. Spinocerebellar ataxias caused by polyglutamine expansions: A review of therapeutic strategies. Cerebellum 2008, 7, 215-221.
    • (2008) Cerebellum , vol.7 , pp. 215-221
    • Underwood, B.R.1    Rubinsztein, D.C.2
  • 75
    • 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.; Kao, H.Y.; Mitzutani, A.; Banayo, E.; Rajan, H.; McKeown, M.; Evans, R.M. 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 2004, 101, 4047-4052.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4047-4052
    • Tsai, C.C.1    Kao, H.Y.2    Mitzutani, A.3    Banayo, E.4    Rajan, H.5    McKeown, M.6    Evans, R.M.7
  • 76
    • 65849514220 scopus 로고    scopus 로고
    • SCA3: Neurological features, pathogenesis and animal models
    • Riess, O.; Rub, U.; Pastore, A.; Bauer, P.; Schols, L. SCA3: Neurological features, pathogenesis and animal models. Cerebellum 2008, 7, 125-137.
    • (2008) Cerebellum , vol.7 , pp. 125-137
    • Riess, O.1    Rub, U.2    Pastore, A.3    Bauer, P.4    Schols, L.5
  • 77
    • 33750962224 scopus 로고    scopus 로고
    • Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation
    • Evert, B.O.; Araujo, J.; Vieira-Saecker, A.M.; de Vos, R.A.; Harendza, S.; Klockgether, T.; Wullner, U. Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation. J. Neurosci. 2006, 26, 11474-11486.
    • (2006) J. Neurosci , vol.26 , pp. 11474-11486
    • Evert, B.O.1    Araujo, J.2    Vieira-Saecker, A.M.3    de Vos, R.A.4    Harendza, S.5    Klockgether, T.6    Wullner, U.7
  • 78
    • 78650613146 scopus 로고    scopus 로고
    • HDAC inhibitor sodium butyrate reverses transcriptional downregulation and ameliorates ataxic symptoms in a transgenic mouse model of SCA3
    • Chou, A.H.; Chen, S.Y.; Yeh, T.H.; Weng, Y.H.; Wang, H.L. HDAC inhibitor sodium butyrate reverses transcriptional downregulation and ameliorates ataxic symptoms in a transgenic mouse model of SCA3. Neurobiol. Dis. 2011, 41, 481-488.
    • (2011) Neurobiol. Dis , vol.41 , pp. 481-488
    • Chou, A.H.1    Chen, S.Y.2    Yeh, T.H.3    Weng, Y.H.4    Wang, H.L.5
  • 79
    • 84886126273 scopus 로고    scopus 로고
    • Histone deacetylase-3 interacts with ataxin-7 and is altered in a spinocerebellar ataxia type 7 mouse model
    • Duncan, C.E.; An, M.C.; Papanikolaou, T.; Rugani, C.; Vitelli, C.; Ellerby, L.M. Histone deacetylase-3 interacts with ataxin-7 and is altered in a spinocerebellar ataxia type 7 mouse model. Mol. Neurodegener 2013, 8, 42-56.
    • (2013) Mol. Neurodegener , vol.8 , pp. 42-56
    • Duncan, C.E.1    An, M.C.2    Papanikolaou, T.3    Rugani, C.4    Vitelli, C.5    Ellerby, L.M.6
  • 80
    • 84883788666 scopus 로고    scopus 로고
    • Epigenetic targeting of histone deacetylase: Therapeutic potential in Parkinson's disease?
    • Harrison, I.F.; Dexter, D.T. Epigenetic targeting of histone deacetylase: therapeutic potential in Parkinson's disease? Pharmacol. Ther. 2013, 140, 34-52.
    • (2013) Pharmacol. Ther. , vol.140 , pp. 34-52
    • Harrison, I.F.1    Dexter, D.T.2
  • 81
    • 84883155892 scopus 로고    scopus 로고
    • Development and therapeutic implications of selective histone deacetylase 6 inhibitors
    • Kalin, J.H.; Bergman, J.A. Development and therapeutic implications of selective histone deacetylase 6 inhibitors. J. Med. Chem 2013, 56, 6297-6313.
    • (2013) J. Med. Chem , vol.56 , pp. 6297-6313
    • Kalin, J.H.1    Bergman, J.A.2
  • 82
    • 84863408932 scopus 로고    scopus 로고
    • Selective histone deacetylase inhibitors
    • Pan, H.; Cao, J.; Xu, W. Selective histone deacetylase inhibitors. Anticancer Agents Med. Chem. 2012, 12, 247-270.
    • (2012) Anticancer Agents Med. Chem. , vol.12 , pp. 247-270
    • Pan, H.1    Cao, J.2    Xu, W.3
  • 84
    • 84865662814 scopus 로고    scopus 로고
    • Rationale for the development of 2-aminobenzamide histone deacetylase inhibitors as therapeutics for Friedreich ataxia
    • Soragni, E.; Xu, C.; Plasterer, H.L.; Jacques, V.; Rusche, J.R.; Gottesfeld, J.M. Rationale for the development of 2-aminobenzamide histone deacetylase inhibitors as therapeutics for Friedreich ataxia. J. Child. Neurol. 2012, 27, 1164-1173.
    • (2012) J. Child. Neurol. , vol.27 , pp. 1164-1173
    • Soragni, E.1    Xu, C.2    Plasterer, H.L.3    Jacques, V.4    Rusche, J.R.5    Gottesfeld, J.M.6
  • 86
    • 74549200467 scopus 로고    scopus 로고
    • Is there a future for histone deacetylase inhibitors in the pharmacotherapy of psychiatric disorders?
    • Grayson, D.R.; Kundakovic, M.; Sharma, R.P. Is there a future for histone deacetylase inhibitors in the pharmacotherapy of psychiatric disorders? Mol. Pharmacol. 2010, 77, 126-135.
    • (2010) Mol. Pharmacol. , vol.77 , pp. 126-135
    • Grayson, D.R.1    Kundakovic, M.2    Sharma, R.P.3
  • 87
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev, A.G.; Thompson, L.M. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat. Rev. Drug Discov. 2008, 7, 854-868.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 90
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante, R.J.; Kubilus, J.K.; Lee, J.; Ryu, H.; Beesen, A.; Zucker, B.; Smith, K.; Kowall, N.W.; Ratan, R.R.; Luthi-Carter, R.; et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 2003, 23, 9418-9427.
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3    Ryu, H.4    Beesen, A.5    Zucker, B.6    Smith, K.7    Kowall, N.W.8    Ratan, R.R.9    Luthi-Carter, R.10
  • 96
    • 0842325787 scopus 로고    scopus 로고
    • Histone deacetylase is a target of valproic acid-mediated cellular differentiation
    • Gurvich, N.; Tsygankova, O.M.; Meinkoth, J.L.; Klein, P.S. Histone deacetylase is a target of valproic acid-mediated cellular differentiation. Cancer Res. 2004, 64, 1079-1086.
    • (2004) Cancer Res. , vol.64 , pp. 1079-1086
    • Gurvich, N.1    Tsygankova, O.M.2    Meinkoth, J.L.3    Klein, P.S.4
  • 97
    • 70349195820 scopus 로고    scopus 로고
    • Valproate ameliorates the survival and the motor performance in a transgenic mouse model of Huntington's disease
    • Zadori, D.; Geisz, A.; Vamos, E.; Vecsei, L.; Klivenyi, P. Valproate ameliorates the survival and the motor performance in a transgenic mouse model of Huntington's disease. Pharmacol. Biochem. Behav. 2009, 94, 148-153.
    • (2009) Pharmacol. Biochem. Behav. , vol.94 , pp. 148-153
    • Zadori, D.1    Geisz, A.2    Vamos, E.3    Vecsei, L.4    Klivenyi, P.5
  • 98
    • 80054772539 scopus 로고    scopus 로고
    • Combined treatment with the mood stabilizers lithium and valproate produces multiple beneficial effects in transgenic mouse models of Huntington's disease
    • Chiu, C.T.; Liu, G.; Leeds, P.; Chuang, D.M. Combined treatment with the mood stabilizers lithium and valproate produces multiple beneficial effects in transgenic mouse models of Huntington's disease. Neuropsychopharmacology 2011, 36, 2406-2421.
    • (2011) Neuropsychopharmacology , vol.36 , pp. 2406-2421
    • Chiu, C.T.1    Liu, G.2    Leeds, P.3    Chuang, D.M.4
  • 99
    • 84873874848 scopus 로고    scopus 로고
    • Sodium valproate alleviates neurodegeneration in SCA3/MJD via suppressing apoptosis and rescuing the hypoacetylation levels of histone H3 and H4
    • Yi, J.; Zhang, L.; Tang, B.; Han, W.; Zhou, Y.; Chen, Z.; Jia, D.; Jiang, H. Sodium valproate alleviates neurodegeneration in SCA3/MJD via suppressing apoptosis and rescuing the hypoacetylation levels of histone H3 and H4. PLoS ONE 2013, 8, e54792.
    • (2013) PLoS ONE , vol.8
    • Yi, J.1    Zhang, L.2    Tang, B.3    Han, W.4    Zhou, Y.5    Chen, Z.6    Jia, D.7    Jiang, H.8
  • 102
    • 33645216173 scopus 로고    scopus 로고
    • Dose-dependent improvement of myoclonic hyperkinesia due to Valproic acid in eight Huntington's Disease patients: A case series
    • Saft, C.; Lauter, T.; Kraus, P.H.; Przuntek, H.; Andrich, J.E. Dose-dependent improvement of myoclonic hyperkinesia due to Valproic acid in eight Huntington's Disease patients: A case series. BMC Neurol. 2006, 6, 11-17.
    • (2006) BMC Neurol. , vol.6 , pp. 11-17
    • Saft, C.1    Lauter, T.2    Kraus, P.H.3    Przuntek, H.4    Andrich, J.E.5
  • 103
    • 0034727062 scopus 로고    scopus 로고
    • Improvement of Huntington's disease with olanzapine and valproate
    • Grove, V.E., Jr.; Quintanilla, J.; DeVaney, G.T. Improvement of Huntington's disease with olanzapine and valproate. N. Engl. J. Med. 2000, 343, 973-974.
    • (2000) N. Engl. J. Med. , vol.343 , pp. 973-974
    • Grove Jr., V.E.1    Quintanilla, J.2    DeVaney, G.T.3
  • 106
    • 58149089923 scopus 로고    scopus 로고
    • Pimelic diphenylamide 106 is a slow, tight-binding inhibitor of class I histone deacetylases
    • Chou, C.J.; Herman, D.M.; Gottesfeld, J.M. Pimelic diphenylamide 106 is a slow, tight-binding inhibitor of class I histone deacetylases. J. Biol. Chem. 2008, 283, 35402-35409.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35402-35409
    • Chou, C.J.1    Herman, D.M.2    Gottesfeld, J.M.3
  • 107
    • 70349163898 scopus 로고    scopus 로고
    • Chemical probes identify a role for histone deacetylase 3 in Friedreich's ataxia gene silencing
    • Xu, C.; Soragni, E.; Chou, C.J.; Herman, D.; Plasterer, H.L.; Rusche, J.R.; Gottesfeld, J.M. Chemical probes identify a role for histone deacetylase 3 in Friedreich's ataxia gene silencing. Chem. Biol. 2009, 16, 980-989.
    • (2009) Chem. Biol. , vol.16 , pp. 980-989
    • Xu, C.1    Soragni, E.2    Chou, C.J.3    Herman, D.4    Plasterer, H.L.5    Rusche, J.R.6    Gottesfeld, J.M.7
  • 108
    • 84874144398 scopus 로고    scopus 로고
    • Effects of the Pimelic Diphenylamide Histone Deacetylase Inhibitor HDACi 4b on the R6/2 and N171-82Q Mouse Models of Huntington's Disease
    • Chen, J.Y.; Wang, E.; Galvan, L.; Huynh, M.; Joshi, P.; Cepeda, C.; Levine, M.S. Effects of the Pimelic Diphenylamide Histone Deacetylase Inhibitor HDACi 4b on the R6/2 and N171-82Q Mouse Models of Huntington's Disease. PLoS Curr. 2013, 5-12.
    • (2013) PLoS Curr , pp. 5-12
    • Chen, J.Y.1    Wang, E.2    Galvan, L.3    Huynh, M.4    Joshi, P.5    Cepeda, C.6    Levine, M.S.7
  • 109
    • 84866015138 scopus 로고    scopus 로고
    • Oral administration of the pimelic diphenylamide HDAC inhibitor HDACi 4b is unsuitable for chronic inhibition of HDAC activity in the CNS in vivo
    • Beconi, M.; Aziz, O.; Matthews, K.; Moumne, L.; O'Connell, C.; Yates, D.; Clifton, S.; Pett, H.; Vann, J.; Crowley, L.; et al. Oral administration of the pimelic diphenylamide HDAC inhibitor HDACi 4b is unsuitable for chronic inhibition of HDAC activity in the CNS in vivo. PLoS ONE 2012, 7, e44498.
    • (2012) PLoS ONE , vol.7
    • Beconi, M.1    Aziz, O.2    Matthews, K.3    Moumne, L.4    O'Connell, C.5    Yates, D.6    Clifton, S.7    Pett, H.8    Vann, J.9    Crowley, L.10
  • 110
    • 84870378784 scopus 로고    scopus 로고
    • Selective histone deacetylase (HDAC) inhibition imparts beneficial effects in Huntington's disease mice: Implications for the ubiquitin-proteasomal and autophagy systems
    • Jia, H.; Kast, R.J.; Steffan, J.S.; Thomas, E.A. Selective histone deacetylase (HDAC) inhibition imparts beneficial effects in Huntington's disease mice: Implications for the ubiquitin-proteasomal and autophagy systems. Hum. Mol. Genet. 2012, 21, 5280-5293.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 5280-5293
    • Jia, H.1    Kast, R.J.2    Steffan, J.S.3    Thomas, E.A.4
  • 114
    • 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 2005, 363, 15-23.
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 115
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F.; Sampat, R.M.; Kopito, R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 116
    • 43449129732 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Huntington's disease
    • Finkbeiner, S.; Mitra, S. The ubiquitin-proteasome pathway in Huntington's disease. Sci. World J. 2008, 8, 421-433.
    • (2008) Sci. World J. , vol.8 , pp. 421-433
    • Finkbeiner, S.1    Mitra, S.2
  • 120
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang, J.; Wang, C.E.; Orr, A.; Tydlacka, S.; Li, S.H.; Li, X.J. Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J. Cell. Biol. 2008, 180, 1177-1189.
    • (2008) J. Cell. Biol. , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3    Tydlacka, S.4    Li, S.H.5    Li, X.J.6
  • 121
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana, N.R.; Dikshit, P.; Goswami, A.; Kotliarova, S.; Murata, S.; Tanaka, K.; Nukina, N. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J. Biol. Chem. 2005, 280, 11635-11640.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 123
    • 33845898194 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases
    • De Pril, R.; Fischer, D.F.; Roos, R.A.; van Leeuwen, F.W. Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases. Mol. Cell. Neurosci. 2007, 34, 10-19.
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 10-19
    • De Pril, R.1    Fischer, D.F.2    Roos, R.A.3    van Leeuwen, F.W.4
  • 124
    • 20844438031 scopus 로고    scopus 로고
    • Remodeling chromatin and stress resistance in the central nervous system: Histone deacetylase inhibitors as novel and broadly effective neuroprotective agents
    • Langley, B.; Gensert, J.M.; Beal, M.F.; Ratan, R.R. Remodeling chromatin and stress resistance in the central nervous system: histone deacetylase inhibitors as novel and broadly effective neuroprotective agents. Curr Drug Targets CNS Neurol Disord 2005, 4, 41-50.
    • (2005) Curr Drug Targets CNS Neurol Disord , vol.4 , pp. 41-50
    • Langley, B.1    Gensert, J.M.2    Beal, M.F.3    Ratan, R.R.4
  • 126
    • 84881480358 scopus 로고    scopus 로고
    • Effect of HDAC inhibitors on neuroprotection and neurite outgrowth in primary rat cortical neurons following ischemic insult
    • Hasan, M.R.; Kim, J.H.; Kim, Y.J.; Kwon, K.J.; Shin, C.Y.; Kim, H.Y.; Han, S.H.; Choi, D.H.; Lee, J. Effect of HDAC inhibitors on neuroprotection and neurite outgrowth in primary rat cortical neurons following ischemic insult. Neurochem. Res. 2013, 38, 1921-1934.
    • (2013) Neurochem. Res. , vol.38 , pp. 1921-1934
    • Hasan, M.R.1    Kim, J.H.2    Kim, Y.J.3    Kwon, K.J.4    Shin, C.Y.5    Kim, H.Y.6    Han, S.H.7    Choi, D.H.8    Lee, J.9
  • 127
    • 33845296450 scopus 로고    scopus 로고
    • Valproate protects dopaminergic neurons in midbrain neuron/glia cultures by stimulating the release of neurotrophic factors from astrocytes
    • Chen, P.S.; Peng, G.S.; Li, G.; Yang, S.; Wu, X.; Wang, C.C.; Wilson, B.; Lu, R.B.; Gean, P.W.; Chuang, D.M.; et al. Valproate protects dopaminergic neurons in midbrain neuron/glia cultures by stimulating the release of neurotrophic factors from astrocytes. Mol. Psychiatry 2006, 11, 1116-1125.
    • (2006) Mol. Psychiatry , vol.11 , pp. 1116-1125
    • Chen, P.S.1    Peng, G.S.2    Li, G.3    Yang, S.4    Wu, X.5    Wang, C.C.6    Wilson, B.7    Lu, R.B.8    Gean, P.W.9    Chuang, D.M.10
  • 128
    • 84867197730 scopus 로고    scopus 로고
    • Valproate promotes survival of retinal ganglion cells in a rat model of optic nerve crush
    • Zhang, Z.Z.; Gong, Y.Y.; Shi, Y.H.; Zhang, W.; Qin, X.H.; Wu, X.W. Valproate promotes survival of retinal ganglion cells in a rat model of optic nerve crush. Neuroscience 2012, 224, 282-293.
    • (2012) Neuroscience , vol.224 , pp. 282-293
    • Zhang, Z.Z.1    Gong, Y.Y.2    Shi, Y.H.3    Zhang, W.4    Qin, X.H.5    Wu, X.W.6
  • 129
    • 67650360880 scopus 로고    scopus 로고
    • Valproic acid induces up-or down-regulation of gene expression responsible for the neuronal excitation and inhibition in rat cortical neurons through its epigenetic actions
    • Fukuchi, M.; Nii, T.; Ishimaru, N.; Minamino, A.; Hara, D.; Takasaki, I.; Tabuchi, A.; Tsuda, M. Valproic acid induces up-or down-regulation of gene expression responsible for the neuronal excitation and inhibition in rat cortical neurons through its epigenetic actions. Neurosci. Res. 2009, 65, 35-43.
    • (2009) Neurosci. Res. , vol.65 , pp. 35-43
    • Fukuchi, M.1    Nii, T.2    Ishimaru, N.3    Minamino, A.4    Hara, D.5    Takasaki, I.6    Tabuchi, A.7    Tsuda, M.8
  • 130
    • 58049196879 scopus 로고    scopus 로고
    • The mood stabilizers lithium and valproate selectively activate the promoter IV of brain-derived neurotrophic factor in neurons
    • Yasuda, S.; Liang, M.H.; Marinova, Z.; Yahyavi, A.; Chuang, D.M. The mood stabilizers lithium and valproate selectively activate the promoter IV of brain-derived neurotrophic factor in neurons. Mol. Psychiatry 2009, 14, 51-59.
    • (2009) Mol. Psychiatry , vol.14 , pp. 51-59
    • Yasuda, S.1    Liang, M.H.2    Marinova, Z.3    Yahyavi, A.4    Chuang, D.M.5
  • 131
    • 0033534468 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor expression in vivo is under the control of neuron-restrictive silencer element
    • Timmusk, T.; Palm, K.; Lendahl, U.; Metsis, M. Brain-derived neurotrophic factor expression in vivo is under the control of neuron-restrictive silencer element. J. Biol. Chem. 1999, 274, 1078-1084.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1078-1084
    • Timmusk, T.1    Palm, K.2    Lendahl, U.3    Metsis, M.4
  • 132
    • 34447325642 scopus 로고    scopus 로고
    • Defective cholesterol traffic and neuronal differentiation in neural stem cells of Niemann-Pick type C disease improved by valproic acid, a histone deacetylase inhibitor
    • Kim, S.J.; Lee, B.H.; Lee, Y.S.; Kang, K.S. Defective cholesterol traffic and neuronal differentiation in neural stem cells of Niemann-Pick type C disease improved by valproic acid, a histone deacetylase inhibitor. Biochem. Biophys. Res. Commun. 2007, 360, 593-599.
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 593-599
    • Kim, S.J.1    Lee, B.H.2    Lee, Y.S.3    Kang, K.S.4
  • 133
    • 84896740535 scopus 로고    scopus 로고
    • p53 in neurodegenerative diseases and brain cancers
    • Checler, F.; da Costa, C.A. p53 in neurodegenerative diseases and brain cancers. Pharmacol. Ther. 2013, 142, 99-113.
    • (2013) Pharmacol. Ther. , vol.142 , pp. 99-113
    • Checler, F.1    da Costa, C.A.2
  • 134
    • 0033215387 scopus 로고    scopus 로고
    • Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a
    • Murphy, M.; Ahn, J.; Walker, K.K.; Hoffman, W.H.; Evans, R.M.; Levine, A.J.; George, D.L. Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a. Genes Dev. 1999, 13, 2490-2501.
    • (1999) Genes Dev. , vol.13 , pp. 2490-2501
    • Murphy, M.1    Ahn, J.2    Walker, K.K.3    Hoffman, W.H.4    Evans, R.M.5    Levine, A.J.6    George, D.L.7
  • 135
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan, L.J.; Shia, W.J.; Chen, M.H.; Yang, W.M.; Seto, E.; Lin, Y.S.; Wu, C.W. Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 2000, 275, 20436-20443.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1    Shia, W.J.2    Chen, M.H.3    Yang, W.M.4    Seto, E.5    Lin, Y.S.6    Wu, C.W.7
  • 136
    • 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 2000, 408, 377-381.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 139
    • 77953810971 scopus 로고    scopus 로고
    • MS-275, an histone deacetylase inhibitor, reduces the inflammatory reaction in rat experimental autoimmune neuritis
    • Zhang, Z.Y.; Zhang, Z.; Schluesener, H.J. MS-275, an histone deacetylase inhibitor, reduces the inflammatory reaction in rat experimental autoimmune neuritis. Neuroscience 2010, 169, 370-377.
    • (2010) Neuroscience , vol.169 , pp. 370-377
    • Zhang, Z.Y.1    Zhang, Z.2    Schluesener, H.J.3
  • 140
    • 84863395477 scopus 로고    scopus 로고
    • Histone deacetylases are dysregulated in rheumatoid arthritis and a novel histone deacetylase 3-selective inhibitor reduces interleukin-6 production by peripheral blood mononuclear cells from rheumatoid arthritis patients
    • Gillespie, J.; Savic, S.; Wong, C.; Hempshall, A.; Inman, M.; Emery, P.; Grigg, R.; McDermott, M.F. Histone deacetylases are dysregulated in rheumatoid arthritis and a novel histone deacetylase 3-selective inhibitor reduces interleukin-6 production by peripheral blood mononuclear cells from rheumatoid arthritis patients. Arthr. Rheum 2012, 64, 418-422.
    • (2012) Arthr. Rheum , vol.64 , pp. 418-422
    • Gillespie, J.1    Savic, S.2    Wong, C.3    Hempshall, A.4    Inman, M.5    Emery, P.6    Grigg, R.7    McDermott, M.F.8
  • 143
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • Chen, L.; Fischle, W.; Verdin, E.; Greene, W.C. Duration of nuclear NF-kappaB action regulated by reversible acetylation. Science 2001, 293, 1653-1657.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 144
    • 84899856633 scopus 로고    scopus 로고
    • Histone deacetylase isoforms regulate innate immune responses by deacetylating mitogen-activated protein kinase phosphatase-1
    • Jeong, Y.; Du, R.; Zhu, X.; Yin, S.; Wang, J.; Cui, H.; Cao, W.; Lowenstein, C.J. Histone deacetylase isoforms regulate innate immune responses by deacetylating mitogen-activated protein kinase phosphatase-1. J. Leukoc Biol. 2013, 95, 651-659.
    • (2013) J. Leukoc Biol. , vol.95 , pp. 651-659
    • Jeong, Y.1    Du, R.2    Zhu, X.3    Yin, S.4    Wang, J.5    Cui, H.6    Cao, W.7    Lowenstein, C.J.8
  • 145
    • 33749055328 scopus 로고    scopus 로고
    • NF-kappaB functions in the nervous system: From development to disease
    • Memet, S. NF-kappaB functions in the nervous system: from development to disease. Biochem. Pharmacol. 2006, 72, 1180-1195.
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1180-1195
    • Memet, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.