메뉴 건너뛰기




Volumn 2015, Issue , 2015, Pages

Targeting Histone Deacetylases: A Novel Approach in Parkinson's Disease

Author keywords

[No Author keywords available]

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; 6 ORTHOHYDROXYDOPAMINE; ALPHA SYNUCLEIN; ALPHA TUBULIN; GUANINE NUCLEOTIDE BINDING PROTEIN; HEAT SHOCK PROTEIN 90; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KU ANTIGEN; LIPOPOLYSACCHARIDE; NEUROTOXIN; NONHISTONE PROTEIN; PROTEIN P53; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; STAT1 PROTEIN; STAT3 PROTEIN; UNCLASSIFIED DRUG;

EID: 84930971150     PISSN: None     EISSN: 20420080     Source Type: Journal    
DOI: 10.1155/2015/303294     Document Type: Article
Times cited : (52)

References (91)
  • 2
    • 84885472234 scopus 로고    scopus 로고
    • Phosphodiesterases: Regulators of cyclic nucleotide signals and novel molecular target for movement disorders
    • S. Sharma, K. Kumar, R. Deshmukh, and P. L. Sharma, "Phosphodiesterases: regulators of cyclic nucleotide signals and novel molecular target for movement disorders, " European Journal of Pharmacology, vol. 714, no. 1-3, pp. 486-497, 2013.
    • (2013) European Journal of Pharmacology , vol.714 , Issue.1-3 , pp. 486-497
    • Sharma, S.1    Kumar, K.2    Deshmukh, R.3    Sharma, P.L.4
  • 3
    • 84920175879 scopus 로고    scopus 로고
    • Vinpocetine attenuates MPTPinduced motor deficit and biochemical abnormalities inWistar rats
    • S. Sharma and R. Deshmukh, "Vinpocetine attenuates MPTPinduced motor deficit and biochemical abnormalities inWistar rats, " Neuroscience C, vol. 286, pp. 393-403, 2014.
    • (2014) Neuroscience C , vol.286 , pp. 393-403
    • Sharma, S.1    Deshmukh, R.2
  • 4
    • 0037379324 scopus 로고    scopus 로고
    • Genetic and environmental factors in the cause of Parkinson's disease
    • T. T. Warner and A. H. V. Schapira, "Genetic and environmental factors in the cause of Parkinson's disease, " Annals of Neurology, vol. 53, no. 3, pp. S16-S25, 2003.
    • (2003) Annals of Neurology , vol.53 , Issue.3 , pp. S16-S25
    • Warner, T.T.1    Schapira, A.H.V.2
  • 5
    • 84870667053 scopus 로고    scopus 로고
    • Epigenetic histone acetylation and deacetylation mechanisms in experimental models of neurodegenerative disorders
    • Z. Konsoula and F. A. Barile, "Epigenetic histone acetylation and deacetylation mechanisms in experimental models of neurodegenerative disorders, " Journal of Pharmacological and Toxicological Methods, vol. 66, no. 3, pp. 215-220, 2012.
    • (2012) Journal of Pharmacological and Toxicological Methods , vol.66 , Issue.3 , pp. 215-220
    • Konsoula, Z.1    Barile, F.A.2
  • 6
    • 33748450288 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A novel therapeutic approach to huntington's disease (complex mechanism of neuronal death)
    • G. Sadri-Vakili and J.-H. J. Cha, "Histone deacetylase inhibitors: a novel therapeutic approach to huntington's disease (complex mechanism of neuronal death), " Current Alzheimer Research, vol. 3, no. 4, pp. 403-408, 2006.
    • (2006) Current Alzheimer Research , vol.3 , Issue.4 , pp. 403-408
    • Sadri-Vakili, G.1    Cha, J.-H.J.2
  • 7
    • 84883788666 scopus 로고    scopus 로고
    • Epigenetic targeting of histone deacetylase: Therapeutic potential in Parkinson's disease?
    • I. F. Harrison and D. T. Dexter, "Epigenetic targeting of histone deacetylase: Terapeutic potential in Parkinson's disease?" Pharmacology &Therapeutics, vol. 140, no. 1, pp. 34-52, 2013.
    • (2013) Pharmacology &Therapeutics , vol.140 , Issue.1 , pp. 34-52
    • Harrison, I.F.1    Dexter, D.T.2
  • 8
    • 84857674697 scopus 로고    scopus 로고
    • Long-term memory deficits in Huntington's disease are associated with reduced CBP histone acetylase activity
    • A. Giralt, M. Puigdellvol, O. Carretón et al., "Long-term memory deficits in Huntington's disease are associated with reduced CBP histone acetylase activity, " Human Molecular Genetics, vol. 21, no. 6, pp. 1203-1216, 2012.
    • (2012) Human Molecular Genetics , vol.21 , Issue.6 , pp. 1203-1216
    • Giralt, A.1    Puigdellvol, M.2    Carretón, O.3
  • 9
    • 84870378784 scopus 로고    scopus 로고
    • Selective histone deacetylase (HDAC) inhibition imparts beneficial effectsin Huntington's disease mice: Implications for the ubiquitinproteasomal and autophagy systems
    • H. Jia, R. J. Kast, J. S. Steffan, and E. A. Thomas, "Selective histone deacetylase (HDAC) inhibition imparts beneficial effectsin Huntington's disease mice: implications for the ubiquitinproteasomal and autophagy systems, " HumanMolecular Genetics, vol. 21, no. 24, pp. 5280-5293, 2012.
    • (2012) HumanMolecular Genetics , vol.21 , Issue.24 , pp. 5280-5293
    • Jia, H.1    Kast, R.J.2    Steffan, J.S.3    Thomas, E.A.4
  • 11
    • 84937120504 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor, trichostatin A, improves learning and memory in high-fat diet-induced cognitive deficits in mice
    • S. Sharma, R. Taliyan, and S. Ramagiri, "Histone deacetylase inhibitor, trichostatin A, improves learning and memory in high-fat diet-induced cognitive deficits in mice, " Journal of Molecular Neuroscience, 2014.
    • (2014) Journal of Molecular Neuroscience
    • Sharma, S.1    Taliyan, R.2    Ramagiri, S.3
  • 12
    • 84937156332 scopus 로고    scopus 로고
    • Synergistic effects of GSK-3 and HDAC inhibitors in intracerebroventricular streptozotocininduced cognitive deficits in rats
    • S. Sharma and R. Taliyan, "Synergistic effects of GSK-3 and HDAC inhibitors in intracerebroventricular streptozotocininduced cognitive deficits in rats, " Naunyn-Schmiedeberg's Archives of Pharmacology, 2014.
    • (2014) Naunyn-Schmiedeberg's Archives of Pharmacology
    • Sharma, S.1    Taliyan, R.2
  • 13
    • 84884960688 scopus 로고    scopus 로고
    • Genomic targets, and histone acetylation and gene expression profiling of neural HDAC inhibition
    • J. P. Lopez-Atalaya, S. Ito, L. M. Valor, E. Benito, and A. Barco, "Genomic targets, and histone acetylation and gene expression profiling of neural HDAC inhibition, " Nucleic Acids Research, vol. 41, no. 17, pp. 8072-8084, 2013.
    • (2013) Nucleic Acids Research , vol.41 , Issue.17 , pp. 8072-8084
    • Lopez-Atalaya, J.P.1    Ito, S.2    Valor, L.M.3    Benito, E.4    Barco, A.5
  • 14
    • 84860257685 scopus 로고    scopus 로고
    • Roles of histone deacetylases in epigenetic regulation: Emerging paradigms from studies with inhibitors
    • article
    • G. P. Delcuve, D. H. Khan, and J. R. Davie, "Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors, " Clinical Epigenetics, vol. 4, no. 1, article 5, 2012.
    • (2012) Clinical Epigenetics , vol.4 , Issue.1
    • Delcuve, G.P.1    Khan, D.H.2    Davie, J.R.3
  • 15
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • E. Verdin, F. Dequiedt, and H. G. Kasler, "Class II histone deacetylases: versatile regulators, " Trends in Genetics, vol. 19, no. 5, pp. 286-293, 2003.
    • (2003) Trends in Genetics , vol.19 , Issue.5 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 16
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: From bacteria and yeast to mice and men
    • X. J. Yang and E. Seto, "The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men, " Nature Reviews Molecular Cell Biology, vol. 9, no. 3, pp. 206-218, 2008.
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 17
    • 26444439216 scopus 로고    scopus 로고
    • Prospects: Histone deacetylase inhibitors
    • M. Dokmanovic and P. A. Marks, "Prospects: histone deacetylase inhibitors, " Journal of Cellular Biochemistry, vol. 96, no. 2, pp. 293-304, 2005.
    • (2005) Journal of Cellular Biochemistry , vol.96 , Issue.2 , pp. 293-304
    • Dokmanovic, M.1    Marks, P.A.2
  • 18
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 byDBC1
    • W. Zhao, J.-P. Kruse, Y. Tang, S. Y. Jung, J. Qin, and W. Gu, "Negative regulation of the deacetylase SIRT1 byDBC1, " Nature, vol. 451, no. 7178, pp. 587-590, 2008.
    • (2008) Nature , vol.451 , Issue.7178 , pp. 587-590
    • Zhao, W.1    Kruse, J.-P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 19
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • M. A. Glozak, N. Sengupta, X. Zhang, and E. Seto, "Acetylation and deacetylation of non-histone proteins, " Gene, vol. 363, no. 1-2, pp. 15-23, 2005.
    • (2005) Gene , vol.363 , Issue.1-2 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 22
    • 52249090461 scopus 로고    scopus 로고
    • Differential expression of 12 histone deacetylase (HDAC) genes in astrocytomas and normal brain tissue: Class II and IV are hypoexpressed in glioblastomas
    • article
    • A. K. B. Lucio-Eterovic, M. A. A. Cortez, E. T. Valera et al., "Differential expression of 12 histone deacetylase (HDAC) genes in astrocytomas and normal brain tissue: class II and IV are hypoexpressed in glioblastomas, " BMC Cancer, vol. 8, article 243, 2008.
    • (2008) BMC Cancer , vol.8
    • Lucio-Eterovic, A.K.B.1    Cortez, M.A.A.2    Valera, E.T.3
  • 23
    • 80052239705 scopus 로고    scopus 로고
    • Expression of histone deacetylases in cellular compartments of the mouse brain and the effects of ischemia
    • S. Baltan, A. Bachleda, R. S. Morrison, and S. P. Murphy, "Expression of histone deacetylases in cellular compartments of the mouse brain and the effects of ischemia, " Translational Stroke Research, vol. 2, no. 3, pp. 411-423, 2011.
    • (2011) Translational Stroke Research , vol.2 , Issue.3 , pp. 411-423
    • Baltan, S.1    Bachleda, A.2    Morrison, R.S.3    Murphy, S.P.4
  • 25
    • 0034685766 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human class i histone deacetylase that functions as a transcription repressor
    • E. Hu, Z. Chen, T. Fredrickson et al., "Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor, " Journal of Biological Chemistry, vol. 275, no. 20, pp. 15254-15264, 2000.
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.20 , pp. 15254-15264
    • Hu, E.1    Chen, Z.2    Fredrickson, T.3
  • 27
    • 26844518082 scopus 로고    scopus 로고
    • Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death
    • T. A. Bolger and T.-P. Yao, "Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death, " Journal of Neuroscience, vol. 25, no. 41, pp. 9544-9553, 2005.
    • (2005) Journal of Neuroscience , vol.25 , Issue.41 , pp. 9544-9553
    • Bolger, T.A.1    Yao, T.-P.2
  • 28
    • 33645357786 scopus 로고    scopus 로고
    • Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action
    • N. M. Tsankova, O. Berton, W. Renthal, A. Kumar, R. L. Neve, and E. J. Nestler, "Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action, " Nature Neuroscience, vol. 9, no. 4, pp. 519-525, 2006.
    • (2006) Nature Neuroscience , vol.9 , Issue.4 , pp. 519-525
    • Tsankova, N.M.1    Berton, O.2    Renthal, W.3    Kumar, A.4    Neve, R.L.5    Nestler, E.J.6
  • 29
    • 66749119970 scopus 로고    scopus 로고
    • Genetic knock-down of HDAC7 does not ameliorate disease pathogenesis in the R6/2 mouse model of Huntington's disease
    • Article ID
    • C. L. Benn, R. Butler, L. Mariner et al., "Genetic knock-down of HDAC7 does not ameliorate disease pathogenesis in the R6/2 mouse model of Huntington's disease, " PLoS ONE, vol. 4, no. 6, Article ID e5747, 2009.
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Benn, C.L.1    Butler, R.2    Mariner, L.3
  • 30
    • 79955369578 scopus 로고    scopus 로고
    • Phenylbutyrate up-regulates the DJ-1 protein and protects neurons in cell culture and in animal models of Parkinson disease
    • W. Zhou, K. Bercury, J. Cummiskey, N. Luong, J. Lebin, and C. R. Freed, "Phenylbutyrate up-regulates the DJ-1 protein and protects neurons in cell culture and in animal models of Parkinson disease, " Journal of Biological Chemistry, vol. 286, no. 17, pp. 14941-14951, 2011.
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.17 , pp. 14941-14951
    • Zhou, W.1    Bercury, K.2    Cummiskey, J.3    Luong, N.4    Lebin, J.5    Freed, C.R.6
  • 31
    • 84899842005 scopus 로고    scopus 로고
    • HDAC9 is implicated in schizophrenia and expressed specifically in post-mitotic neurons but not in adult neural stem cells
    • B. Lang, T. M. Alrahbeni, D. S. Clair, D. H. Blackwood, C. D. McCaig, and S. Shen, "HDAC9 is implicated in schizophrenia and expressed specifically in post-mitotic neurons but not in adult neural stem cells, " American Journal of Stem Cells, vol. 1, no. 1, pp. 31-41, 2011.
    • (2011) American Journal of Stem Cells , vol.1 , Issue.1 , pp. 31-41
    • Lang, B.1    Alrahbeni, T.M.2    Clair, D.S.3    Blackwood, D.H.4    McCaig, C.D.5    Shen, S.6
  • 32
    • 33846930889 scopus 로고    scopus 로고
    • Microtubule deacetylases, SirT2 and HDAC6, in the nervous system
    • C. M. Southwood, M. Peppi, S. Dryden, M. A. Tainsky, and A. Gow, "Microtubule deacetylases, SirT2 and HDAC6, in the nervous system, " Neurochemical Research, vol. 32, no. 2, pp. 187-195, 2007.
    • (2007) Neurochemical Research , vol.32 , Issue.2 , pp. 187-195
    • Southwood, C.M.1    Peppi, M.2    Dryden, S.3    Tainsky, M.A.4    Gow, A.5
  • 33
    • 0037016696 scopus 로고    scopus 로고
    • Isolation and characterization ofmammalianHDAC10, a novel histone deacetylase
    • H. Y. Kao, C. H. Lee, A. Komarov, C. C. Han, and R. M. Evans, "Isolation and characterization ofmammalianHDAC10, a novel histone deacetylase, " The Journal of Biological Chemistry, vol. 277, no. 1, pp. 187-193, 2002.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 187-193
    • Kao, H.Y.1    Lee, C.H.2    Komarov, A.3    Han, C.C.4    Evans, R.M.5
  • 34
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • L. Gao, M. A. Cueto, F. Asselbergs, and P. Atadja, "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family, " Journal of Biological Chemistry, vol. 277, no. 28, pp. 25748-25755, 2002.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 35
    • 0347624644 scopus 로고    scopus 로고
    • Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
    • C. Rouaux, N. Jokic, C. Mbebi, S. Boutillier, J. P. Loeffler, and A. L. Boutillier, "Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration, " The EMBO Journal, vol. 22, no. 24, pp. 6537-6549, 2003.
    • (2003) The EMBO Journal , vol.22 , Issue.24 , pp. 6537-6549
    • Rouaux, C.1    Jokic, N.2    Mbebi, C.3    Boutillier, S.4    Loeffler, J.P.5    Boutillier, A.L.6
  • 36
    • 34447317536 scopus 로고    scopus 로고
    • Histones associated with downregulated genes are hypo-acetylated in Huntington's disease models
    • G. Sadri-Vakili, B. Bouzou, C. L. Benn et al., "Histones associated with downregulated genes are hypo-acetylated in Huntington's disease models, " Human Molecular Genetics, vol. 16, no. 11, pp. 1293-1306, 2007.
    • (2007) Human Molecular Genetics , vol.16 , Issue.11 , pp. 1293-1306
    • Sadri-Vakili, G.1    Bouzou, B.2    Benn, C.L.3
  • 37
    • 33749583553 scopus 로고    scopus 로고
    • Synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • E. Kontopoulos, J. D. Parvin, and M. B. Feany, "-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity, " Human Molecular Genetics, vol. 15, no. 20, pp. 3012-3023, 2006.
    • (2006) Human Molecular Genetics , vol.15 , Issue.20 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 38
  • 39
    • 0017767153 scopus 로고
    • N-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
    • M. G. Riggs, R. G. Whittaker, J. R. Neumann, and V. M. Ingram, "n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells, " Nature, vol. 268, no. 5619, pp. 462-464, 1977.
    • (1977) Nature , vol.268 , Issue.5619 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 40
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • M. Yoshida, M. Kijima, M. Akita, and T. Beppu, "Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A, " The Journal of Biological Chemistry, vol. 265, no. 28, pp. 17174-17179, 1990.
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.28 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 41
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • J. Taunton, C. A. Hassig, and S. L. Schreiber, "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p, " Science, vol. 272, no. 5260, pp. 408-411, 1996.
    • (1996) Science , vol.272 , Issue.5260 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 44
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (Sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • R. A. Frye, "Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (Sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity, " Biochemical and Biophysical Research Communications, vol. 260, no. 1, pp. 273-279, 1999.
    • (1999) Biochemical and Biophysical Research Communications , vol.260 , Issue.1 , pp. 273-279
    • Frye, R.A.1
  • 45
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class i and class II deacetylases promote SMRT-mediated repression
    • H.-Y. Kao, M. Downes, P. Ordentlich, and R. M. Evans, "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression, " Genes and Development, vol. 14, no. 1, pp. 55-66, 2000.
    • (2000) Genes and Development , vol.14 , Issue.1 , pp. 55-66
    • Kao, H.-Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 47
    • 0034725990 scopus 로고    scopus 로고
    • Cloning and characterization of human histone deacetylase 8
    • I. Van Den Wyngaert, W. De Vries, A. Kremer et al., "Cloning and characterization of human histone deacetylase 8, " FEBS Letters, vol. 478, no. 1-2, pp. 77-83, 2000.
    • (2000) FEBS Letters , vol.478 , Issue.1-2 , pp. 77-83
    • Wyngaert Den I.Van1    De Vries, W.2    Kremer, A.3
  • 49
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • A. R. Guardiola and T. P. Yao, "Molecular cloning and characterization of a novel histone deacetylase HDAC10, " The Journal of Biological Chemistry, vol. 277, no. 5, pp. 3350-3356, 2002.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 50
    • 0036493156 scopus 로고    scopus 로고
    • Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain
    • J. J. Tong, J. Liu, N. R. Bertos, and X.-J. Yang, "Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain, "Nucleic Acids Research, vol. 30, no. 5, pp. 1114-1123, 2002.
    • (2002) Nucleic Acids Research , vol.30 , Issue.5 , pp. 1114-1123
    • Tong, J.J.1    Liu, J.2    Bertos, N.R.3    Yang, X.-J.4
  • 51
    • 18544387930 scopus 로고    scopus 로고
    • Isolation and characterization of a novel class II histone deacetylase, HDAC10
    • D. D. Fischer, R. Cai, U. Bhatia et al., "Isolation and characterization of a novel class II histone deacetylase, HDAC10, " The Journal of Biological Chemistry, vol. 277, no. 8, pp. 6656-6666, 2002.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6656-6666
    • Fischer, D.D.1    Cai, R.2    Bhatia, U.3
  • 52
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • P. A. Marks and R. Breslow, "Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug, " Nature Biotechnology, vol. 25, no. 1, pp. 84-90, 2007.
    • (2007) Nature Biotechnology , vol.25 , Issue.1 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 53
    • 79952262759 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors in recent clinical trials for cancer therapy
    • J. M. Wagner, B. Hackanson, M. Lübbert, andM. Jung, "Histone deacetylase (HDAC) inhibitors in recent clinical trials for cancer therapy, " Clinical Epigenetics, vol. 1, no. 3-4, pp. 117-136, 2010.
    • (2010) Clinical Epigenetics , vol.1 , Issue.3-4 , pp. 117-136
    • Wagner, J.M.1    Hackanson, B.2    Lübbert, M.3    Jung, M.4
  • 55
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
    • G. Gardian, S. E. Browne, D. K. Choi et al., "Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease, " The Journal of Biological Chemistry, vol. 280, no. 1, pp. 556-563, 2005.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 556-563
    • Gardian, G.1    Browne, S.E.2    Choi, D.K.3
  • 56
    • 84896038598 scopus 로고    scopus 로고
    • Histone decacetylase inhibitors preventmitochondrial fragmentation and elicit early neuroprotection against MPP+
    • M. Zhu, W.-W. Li, andC.-Z. Lu, "Histone decacetylase inhibitors preventmitochondrial fragmentation and elicit early neuroprotection against MPP+, " CNS Neuroscience & Therapeutics, vol. 20, no. 4, pp. 308-316, 2014.
    • (2014) CNS Neuroscience & Therapeutics , vol.20 , Issue.4 , pp. 308-316
    • Zhu, M.1    Li, W.-W.2    Lu, C.-Z.3
  • 57
    • 84879420897 scopus 로고    scopus 로고
    • Sodium butyrate improves locomotor impairment and earlymortality in a rotenone-induced Drosophila model of Parkinson's disease
    • R. St. Laurent, L. M. O'Brien, and S. T. Ahmad, "Sodium butyrate improves locomotor impairment and earlymortality in a rotenone-induced Drosophila model of Parkinson's disease, " Neuroscience, vol. 246, pp. 382-390, 2013.
    • (2013) Neuroscience , vol.246 , pp. 382-390
    • St. Laurent, R.1    O'brien, L.M.2    Ahmad, S.T.3
  • 58
    • 0020680904 scopus 로고
    • Chronic parkinsonism in humans due to a product of meperidineanalog synthesis
    • J. W. Langston, P. Ballard, J. W. Tetrud, and I. Irwin, "Chronic parkinsonism in humans due to a product of meperidineanalog synthesis, " Science, vol. 219, no. 4587, pp. 979-980, 1983.
    • (1983) Science , vol.219 , Issue.4587 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 59
    • 84856350760 scopus 로고    scopus 로고
    • Lithium and valproate prevent olfactory discrimination and short-term memory impairments in the intranasal 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) rat model of Parkinson's disease
    • A. A. Castro, K. Ghisoni, A. Latini, J. Quevedo, C. I. Tasca, and R. D. S. Prediger, "Lithium and valproate prevent olfactory discrimination and short-term memory impairments in the intranasal 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) rat model of Parkinson's disease, " Behavioural Brain Research, vol. 229, no. 1, pp. 208-215, 2012.
    • (2012) Behavioural Brain Research , vol.229 , Issue.1 , pp. 208-215
    • Castro, A.A.1    Ghisoni, K.2    Latini, A.3    Quevedo, J.4    Tasca, C.I.5    Prediger, R.D.S.6
  • 60
    • 33751120697 scopus 로고    scopus 로고
    • Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain
    • G. Faraco, T. Pancani, L. Formentini et al., "Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain, " Molecular Pharmacology, vol. 70, no. 6, pp. 1876-1884, 2006.
    • (2006) Molecular Pharmacology , vol.70 , Issue.6 , pp. 1876-1884
    • Faraco, G.1    Pancani, T.2    Formentini, L.3
  • 61
    • 62549133546 scopus 로고    scopus 로고
    • Neuroinflammation in Parkinson's disease: A target for neuroprotection
    • E. C. Hirsch and S. Hunot, "Neuroinflammation in Parkinson's disease: a target for neuroprotection" The Lancet Neurology, vol. 8, no. 4, pp. 382-397, 2009.
    • (2009) The Lancet Neurology , vol.8 , Issue.4 , pp. 382-397
    • Hirsch, E.C.1    Hunot, S.2
  • 62
    • 84870025323 scopus 로고    scopus 로고
    • Piracetam and vinpocetine ameliorate rotenone-induced Parkinsonism in rats
    • S. A. Zaitone, D. M. Abo-Elmatty, and S. M. Elshazly, "Piracetam and vinpocetine ameliorate rotenone-induced Parkinsonism in rats, " Indian Journal of Pharmacology, vol. 44, no. 6, pp. 774-779, 2012.
    • (2012) Indian Journal of Pharmacology , vol.44 , Issue.6 , pp. 774-779
    • Zaitone, S.A.1    Abo-Elmatty, D.M.2    Elshazly, S.M.3
  • 63
    • 70349681975 scopus 로고    scopus 로고
    • Glutathione-A review on its role and significance in Parkinson's disease
    • H. L. Martin and P. Teismann, "Glutathione-a review on its role and significance in Parkinson's disease, "TheFASEB Journal, vol. 23, no. 10, pp. 3263-3272, 2009.
    • (2009) TheFASEB Journal , vol.23 , Issue.10 , pp. 3263-3272
    • Martin, H.L.1    Teismann, P.2
  • 64
    • 84862487151 scopus 로고    scopus 로고
    • Sodium phenylbutyrate controls neuroinflammatory and antioxidant activities and protects dopaminergic neurons in mousemodels of Parkinson's disease
    • Article ID
    • A. Roy, A. Ghosh, A. Jana et al., "Sodium phenylbutyrate controls neuroinflammatory and antioxidant activities and protects dopaminergic neurons in mousemodels of Parkinson's disease, " PLoS ONE, vol. 7, no. 6, Article ID e38113, 2012.
    • (2012) PLoS ONE , vol.7 , Issue.6
    • Roy, A.1    Ghosh, A.2    Jana, A.3
  • 66
    • 51649088278 scopus 로고    scopus 로고
    • Enhancement of glutamate uptake in 1-methyl-4-phenylpyridinium-treated astrocytes by trichostatin A
    • J.-Y. Wu, F.-N. Niu, R. Huang, and Y. Xu, "Enhancement of glutamate uptake in 1-methyl-4-phenylpyridinium-treated astrocytes by trichostatin A, " NeuroReport, vol. 19, no. 12, pp. 1209-1212, 2008.
    • (2008) NeuroReport , vol.19 , Issue.12 , pp. 1209-1212
    • Wu, J.-Y.1    Niu, F.-N.2    Huang, R.3    Xu, Y.4
  • 67
    • 33845296450 scopus 로고    scopus 로고
    • Valproate protects dopaminergic neurons in midbrain neuron/glia cultures by stimulating the release of neurotrophic factors from astrocytes
    • P.-S. Chen, G.-S. Peng, G. Li et al., "Valproate protects dopaminergic neurons in midbrain neuron/glia cultures by stimulating the release of neurotrophic factors from astrocytes, " Molecular Psychiatry, vol. 11, no. 12, pp. 1116-1125, 2006.
    • (2006) Molecular Psychiatry , vol.11 , Issue.12 , pp. 1116-1125
    • Chen, P.-S.1    Peng, G.-S.2    Li, G.3
  • 68
    • 0034959811 scopus 로고    scopus 로고
    • Depletion of glial cell line-derived neurotrophic factor in substantia nigra neurons of Parkinson's disease brain
    • N. B. Chauhan, G. J. Siegel, and J. M. Lee, "Depletion of glial cell line-derived neurotrophic factor in substantia nigra neurons of Parkinson's disease brain, " Journal of Chemical Neuroanatomy, vol. 21, no. 4, pp. 277-288, 2001.
    • (2001) Journal of Chemical Neuroanatomy , vol.21 , Issue.4 , pp. 277-288
    • Chauhan, N.B.1    Siegel, G.J.2    Lee, J.M.3
  • 69
    • 0033762265 scopus 로고    scopus 로고
    • Reduced BDNF mRNA expression in the Parkinson's disease substantia nigra
    • D. W. Howells, M. J. Porritt, J. Y. F. Wong et al., "Reduced BDNF mRNA expression in the Parkinson's disease substantia nigra, " Experimental Neurology, vol. 166, no. 1, pp. 127-135, 2000.
    • (2000) Experimental Neurology , vol.166 , Issue.1 , pp. 127-135
    • Howells, D.W.1    Porritt, M.J.2    Wong, J.Y.F.3
  • 70
    • 55549129648 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors up-regulate astrocyte GDNF and BDNF gene transcription and protect dopaminergic neurons
    • X. Wu, P. S. Chen, S. Dallas et al., "Histone deacetylase inhibitors up-regulate astrocyte GDNF and BDNF gene transcription and protect dopaminergic neurons, " International Journal of Neuropsychopharmacology, vol. 11, no. 8, pp. 1123-1134, 2008.
    • (2008) International Journal of Neuropsychopharmacology , vol.11 , Issue.8 , pp. 1123-1134
    • Wu, X.1    Chen, P.S.2    Dallas, S.3
  • 71
    • 58049196879 scopus 로고    scopus 로고
    • Themood stabilizers lithiumand valproate selectively activate the promoter IV of brain-derived neurotrophic factor in neurons
    • S. Yasuda, M. H. Liang, Z. Marinova, A. Yahyavi, and D. M. Chuang, "Themood stabilizers lithiumand valproate selectively activate the promoter IV of brain-derived neurotrophic factor in neurons, "Molecular Psychiatry, vol. 14, no. 1, pp. 51-59, 2009.
    • (2009) Molecular Psychiatry , vol.14 , Issue.1 , pp. 51-59
    • Yasuda, S.1    Liang, M.H.2    Marinova, Z.3    Yahyavi, A.4    Chuang, D.M.5
  • 72
    • 77956414742 scopus 로고    scopus 로고
    • Protection of dopaminergic cells from MPP+-mediated toxicity by histone deacetylase inhibition
    • S. K. Kidd and J. S. Schneider, "Protection of dopaminergic cells from MPP+-mediated toxicity by histone deacetylase inhibition, " Brain Research, vol. 1354, pp. 172-178, 2010.
    • (2010) Brain Research , vol.1354 , pp. 172-178
    • Kidd, S.K.1    Schneider, J.S.2
  • 73
    • 80053105675 scopus 로고    scopus 로고
    • Protective effects of valproic acid on the nigrostriatal dopamine system in a 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridinemouse model of Parkinson's disease
    • S. K. Kidd and J. S. Schneider, "Protective effects of valproic acid on the nigrostriatal dopamine system in a 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridinemouse model of Parkinson's disease, " Neuroscience, vol. 194, pp. 189-194, 2011.
    • (2011) Neuroscience , vol.194 , pp. 189-194
    • Kidd, S.K.1    Schneider, J.S.2
  • 74
    • 83755224359 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, protects dopaminergic neurons from neurotoxin-induced damage
    • S. H. Chen, H. M. Wu, B. Ossola et al., "Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, protects dopaminergic neurons from neurotoxin-induced damage, " British Journal of Pharmacology, vol. 165, no. 2, pp. 494-505, 2012.
    • (2012) British Journal of Pharmacology , vol.165 , Issue.2 , pp. 494-505
    • Chen, S.H.1    Wu, H.M.2    Ossola, B.3
  • 75
    • 2542596183 scopus 로고    scopus 로고
    • Parkinson's disease
    • A. Samii, J. G. Nutt, and B. R. Ransom, "Parkinson's disease, " The Lancet, vol. 363, no. 9423, pp. 1783-1793, 2004.
    • (2004) The Lancet , vol.363 , Issue.9423 , pp. 1783-1793
    • Samii, A.1    Nutt, J.G.2    Ransom, B.R.3
  • 76
    • 84873718850 scopus 로고    scopus 로고
    • RGFP109, a histone deacetylase inhibitor attenuates l-DOPA-induced dyskinesia in the MPTP-lesioned marmoset: A proof-of-concept study
    • T. H. Johnston, P. Huot, S. Damude et al., "RGFP109, a histone deacetylase inhibitor attenuates l-DOPA-induced dyskinesia in the MPTP-lesioned marmoset: a proof-of-concept study, " Parkinsonism and Related Disorders, vol. 19, no. 2, pp. 260-264, 2013.
    • (2013) Parkinsonism and Related Disorders , vol.19 , Issue.2 , pp. 260-264
    • Johnston, T.H.1    Huot, P.2    Damude, S.3
  • 77
    • 34848881102 scopus 로고    scopus 로고
    • Alpha-synuclein protects cerebellar granule neurons against 6-hydroxydopamine-induced death
    • B. Monti, E. Polazzi, L. Batti, C. Crochemore, M. Virgili, and A. Contestabile, "Alpha-synuclein protects cerebellar granule neurons against 6-hydroxydopamine-induced death, " Journal of Neurochemistry, vol. 103, no. 2, pp. 518-530, 2007.
    • (2007) Journal of Neurochemistry , vol.103 , Issue.2 , pp. 518-530
    • Monti, B.1    Polazzi, E.2    Batti, L.3    Crochemore, C.4    Virgili, M.5    Contestabile, A.6
  • 78
    • 84876409566 scopus 로고    scopus 로고
    • Valproic acid neuroprotection in 6-OHDA lesioned rat, a model for Parkinson's Disease
    • B. Monti, D. Mercatelli, and A. Contestabile, "Valproic acid neuroprotection in 6-OHDA lesioned rat, a model for Parkinson's Disease, " HOAJ Biology, vol. 1, no. 1, pp. 1-4, 2012.
    • (2012) HOAJ Biology , vol.1 , Issue.1 , pp. 1-4
    • Monti, B.1    Mercatelli, D.2    Contestabile, A.3
  • 79
    • 84862785786 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, sodium butyrate, alleviates cognitive deficits in pre-motor stage PD
    • P. Rane, J. Shields, M. Heffernan, Y. Guo, S. Akbarian, and J. A. King, "The histone deacetylase inhibitor, sodium butyrate, alleviates cognitive deficits in pre-motor stage PD, " Neuropharmacology, vol. 62, no. 7, pp. 2409-2412, 2012.
    • (2012) Neuropharmacology , vol.62 , Issue.7 , pp. 2409-2412
    • Rane, P.1    Shields, J.2    Heffernan, M.3    Guo, Y.4    Akbarian, S.5    King, J.A.6
  • 80
    • 33745612296 scopus 로고    scopus 로고
    • Intersecting pathways to neurodegeneration in Parkinson's disease: Effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system
    • R. Betarbet, R. M. Canet-Aviles, T. B. Sherer et al., "Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system, " Neurobiology of Disease, vol. 22, no. 2, pp. 404-420, 2006.
    • (2006) Neurobiology of Disease , vol.22 , Issue.2 , pp. 404-420
    • Betarbet, R.1    Canet-Aviles, R.M.2    Sherer, T.B.3
  • 81
    • 77449091519 scopus 로고    scopus 로고
    • Valproic acid is neuroprotective in the rotenone rat model of Parkinson's disease: Involvement of-synuclein
    • B. Monti, V. Gatta, F. Piretti, S. S. Raffaelli, M. Virgili, and A. Contestabile, "Valproic acid is neuroprotective in the rotenone rat model of Parkinson's disease: involvement of-synuclein, " Neurotoxicity Research, vol. 17, no. 2, pp. 130-141, 2010.
    • (2010) Neurotoxicity Research , vol.17 , Issue.2 , pp. 130-141
    • Monti, B.1    Gatta, V.2    Piretti, F.3    Raffaelli, S.S.4    Virgili, M.5    Contestabile, A.6
  • 82
    • 0036884573 scopus 로고    scopus 로고
    • Prostaglandin A1 inhibits rotenone-induced apoptosis in SH-SY5Y cells
    • X. Wang, Z.-H. Qin, Y. Leng et al., "Prostaglandin A1 inhibits rotenone-induced apoptosis in SH-SY5Y cells, " Journal of Neurochemistry, vol. 83, no. 5, pp. 1094-1102, 2002.
    • (2002) Journal of Neurochemistry , vol.83 , Issue.5 , pp. 1094-1102
    • Wang, X.1    Qin, Z.-H.2    Leng, Y.3
  • 83
    • 28844480953 scopus 로고    scopus 로고
    • Valproic acidmediated Hsp70 induction and anti-apoptotic neuroprotection in SH-SY5Y cells
    • T. Pan, X. Li, W. Xie, J. Jankovic, and W. Le, "Valproic acidmediated Hsp70 induction and anti-apoptotic neuroprotection in SH-SY5Y cells, " FEBS Letters, vol. 579, no. 30, pp. 6716-6720, 2005.
    • (2005) FEBS Letters , vol.579 , Issue.30 , pp. 6716-6720
    • Pan, T.1    Li, X.2    Xie, W.3    Jankovic, J.4    Le, W.5
  • 84
    • 34249814605 scopus 로고    scopus 로고
    • Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone
    • M. Inden, Y. Kitamura, H. Takeuchi et al., "Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone, " Journal of Neurochemistry, vol. 101, no. 6, pp. 1491-1504, 2007.
    • (2007) Journal of Neurochemistry , vol.101 , Issue.6 , pp. 1491-1504
    • Inden, M.1    Kitamura, Y.2    Takeuchi, H.3
  • 85
    • 58149512092 scopus 로고    scopus 로고
    • Low dose rotenone treatment causes selective transcriptional activation of cell death related pathways in dopaminergic neurons in vivo
    • B. H. Meurers, C. Zhu, P. O. Fernagut et al., "Low dose rotenone treatment causes selective transcriptional activation of cell death related pathways in dopaminergic neurons in vivo, " Neurobiology of Disease, vol. 33, no. 2, pp. 182-192, 2009.
    • (2009) Neurobiology of Disease , vol.33 , Issue.2 , pp. 182-192
    • Meurers, B.H.1    Zhu, C.2    Fernagut, P.O.3
  • 86
    • 15544387446 scopus 로고    scopus 로고
    • Valproate pretreatment protects dopaminergic neurons from LPS-induced neurotoxicity in rat primary midbrain cultures: Role of microglia
    • G. S. Peng, G. Li, N. S. Tzeng et al., "Valproate pretreatment protects dopaminergic neurons from LPS-induced neurotoxicity in rat primary midbrain cultures: role of microglia, " Molecular Brain Research, vol. 134, no. 1, pp. 162-169, 2005.
    • (2005) Molecular Brain Research , vol.134 , Issue.1 , pp. 162-169
    • Peng, G.S.1    Li, G.2    Tzeng, N.S.3
  • 87
    • 34748922275 scopus 로고    scopus 로고
    • Valproic acid and other histone deacetylase inhibitors induce microglial apoptosis and attenuate lipopolysaccharide-induced dopaminergic neurotoxicity
    • P. S. Chen, C.-C. Wang, C. D. Bortner et al., "Valproic acid and other histone deacetylase inhibitors induce microglial apoptosis and attenuate lipopolysaccharide-induced dopaminergic neurotoxicity, " Neuroscience, vol. 149, no. 1, pp. 203-212, 2007.
    • (2007) Neuroscience , vol.149 , Issue.1 , pp. 203-212
    • Chen, P.S.1    Wang, C.-C.2    Bortner, C.D.3
  • 88
    • 78649663993 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress the expression of inflammatory and innate immune response genes in human microglia and astrocytes
    • H.-S. Suh, S. Choi, P. Khattar, N. Choi, and S. C. Lee, "Histone deacetylase inhibitors suppress the expression of inflammatory and innate immune response genes in human microglia and astrocytes, " Journal of Neuroimmune Pharmacology, vol. 5, no. 4, pp. 521-532, 2010.
    • (2010) Journal of Neuroimmune Pharmacology , vol.5 , Issue.4 , pp. 521-532
    • Suh, H.-S.1    Choi, S.2    Khattar, P.3    Choi, N.4    Lee, S.C.5
  • 89
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue-synuclein-mediated toxicity in models of Parkinson's disease
    • T. F. Outeiro, E. Kontopoulos, S. M. Altmann et al., "Sirtuin 2 inhibitors rescue-synuclein-mediated toxicity in models of Parkinson's disease, " Science, vol. 317, no. 5837, pp. 516-519, 2007.
    • (2007) Science , vol.317 , Issue.5837 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3
  • 90
    • 0018675782 scopus 로고
    • Treatment of Parkinson's disease with sodium valproate: Clinical, pharmacological, and biochemical observations
    • J. Nutt, A. Williams, C. Plotkin, N. Eng, M. Ziegler, and D. B. Calne, "Treatment of Parkinson's disease with sodium valproate: clinical, pharmacological, and biochemical observations, " Canadian Journal of Neurological Sciences, vol. 6, no. 3, pp. 337-343, 1979.
    • (1979) Canadian Journal of Neurological Sciences , vol.6 , Issue.3 , pp. 337-343
    • Nutt, J.1    Williams, A.2    Plotkin, C.3    Eng, N.4    Ziegler, M.5    Calne, D.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.