메뉴 건너뛰기




Volumn 32, Issue 11, 2009, Pages 591-601

Multiple roles of HDAC inhibition in neurodegenerative conditions

Author keywords

[No Author keywords available]

Indexed keywords

4 PHENYLBUTYRIC ACID; AEOL 10150; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; LITHIUM; NICOTINAMIDE; RILUZOLE; ROMIDEPSIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 70350018325     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2009.06.002     Document Type: Review
Times cited : (554)

References (105)
  • 1
    • 16844362441 scopus 로고    scopus 로고
    • Histone deacetylation in epigenetics: an attractive target for anticancer therapy
    • Mai A., et al. Histone deacetylation in epigenetics: an attractive target for anticancer therapy. Med. Res. Rev. 25 (2005) 261-309
    • (2005) Med. Res. Rev. , vol.25 , pp. 261-309
    • Mai, A.1
  • 2
    • 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., et al. 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. 4 (2005) 41-50
    • (2005) Curr. Drug Targets CNS Neurol. Disord. , vol.4 , pp. 41-50
    • Langley, B.1
  • 3
    • 38649124003 scopus 로고    scopus 로고
    • Epigenetic targets of HDAC inhibition in neurodegenerative and psychiatric disorders
    • Abel T., and Zukin R.S. Epigenetic targets of HDAC inhibition in neurodegenerative and psychiatric disorders. Curr. Opin. Pharmacol. 8 (2008) 57-64
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 57-64
    • Abel, T.1    Zukin, R.S.2
  • 4
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev A.G., and Thompson L.M. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat. Rev. Drug Discov. 7 (2008) 854-868
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 5
    • 24144501159 scopus 로고    scopus 로고
    • DNA sequencing of CREBBP demonstrates mutations in 56% of patients with Rubinstein-Taybi syndrome (RSTS) and in another patient with incomplete RSTS
    • Bartsch O., et al. DNA sequencing of CREBBP demonstrates mutations in 56% of patients with Rubinstein-Taybi syndrome (RSTS) and in another patient with incomplete RSTS. Hum. Genet. 117 (2005) 485-493
    • (2005) Hum. Genet. , vol.117 , pp. 485-493
    • Bartsch, O.1
  • 6
    • 42049118549 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Itoh Y., et al. Isoform-selective histone deacetylase inhibitors. Curr. Pharm. Des. 14 (2008) 529-544
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 529-544
    • Itoh, Y.1
  • 7
    • 28644440158 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: discovery and development as anticancer agents
    • Marks P.A., and Dokmanovic M. Histone deacetylase inhibitors: discovery and development as anticancer agents. Expert. Opin. Investig. Drugs 14 (2005) 1497-1511
    • (2005) Expert. Opin. Investig. Drugs , vol.14 , pp. 1497-1511
    • Marks, P.A.1    Dokmanovic, M.2
  • 8
    • 33745920222 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: gathering pace
    • Carey N., and La Thangue N.B. Histone deacetylase inhibitors: gathering pace. Curr. Opin. Pharmacol. 6 (2006) 369-375
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 369-375
    • Carey, N.1    La Thangue, N.B.2
  • 9
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E., et al. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 (2005) 4623-4635
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1
  • 10
    • 33144484589 scopus 로고    scopus 로고
    • Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene
    • Voelter-Mahlknecht S., et al. Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene. Int. J. Mol. Med. 16 (2005) 589-598
    • (2005) Int. J. Mol. Med. , vol.16 , pp. 589-598
    • Voelter-Mahlknecht, S.1
  • 11
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C., et al. HDAC6 is a microtubule-associated deacetylase. Nature 417 (2002) 455-458
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1
  • 12
    • 0035965343 scopus 로고    scopus 로고
    • Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
    • Phiel C.J., et al. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 276 (2001) 36734-36741
    • (2001) J. Biol. Chem. , vol.276 , pp. 36734-36741
    • Phiel, C.J.1
  • 13
    • 18244383806 scopus 로고    scopus 로고
    • Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
    • Göttlicher M., et al. Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells. EMBO J. 20 (2001) 6969-6978
    • (2001) EMBO J. , vol.20 , pp. 6969-6978
    • Göttlicher, M.1
  • 14
    • 0842325787 scopus 로고    scopus 로고
    • Histone deacetylase is a target of valproic acid-mediated cellular differentiation
    • Gurvich N., et al. Histone deacetylase is a target of valproic acid-mediated cellular differentiation. Cancer Res. 64 (2004) 1079-1086
    • (2004) Cancer Res. , vol.64 , pp. 1079-1086
    • Gurvich, N.1
  • 15
    • 33748928786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
    • Butler R., and Bates G.P. Histone deacetylase inhibitors as therapeutics for polyglutamine disorders. Nat. Rev. Neurosci. 7 (2006) 784-796
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 784-796
    • Butler, R.1    Bates, G.P.2
  • 16
    • 37849019672 scopus 로고    scopus 로고
    • Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors
    • Khan N., et al. Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors. Biochem. J. 409 (2008) 581-589
    • (2008) Biochem. J. , vol.409 , pp. 581-589
    • Khan, N.1
  • 17
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty S.J., et al. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4389-4394
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1
  • 18
    • 20944435415 scopus 로고    scopus 로고
    • Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides
    • Mai A., et al. Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. J. Med. Chem. 48 (2005) 3344-3353
    • (2005) J. Med. Chem. , vol.48 , pp. 3344-3353
    • Mai, A.1
  • 19
    • 35548936745 scopus 로고    scopus 로고
    • Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins)
    • Trapp J., et al. Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins). Chem. Med. Chem. 2 (2007) 1419-1431
    • (2007) Chem. Med. Chem. , vol.2 , pp. 1419-1431
    • Trapp, J.1
  • 20
    • 58149267462 scopus 로고    scopus 로고
    • Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau
    • Green K.N., et al. Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau. J. Neurosci. 28 (2008) 11500-11510
    • (2008) J. Neurosci. , vol.28 , pp. 11500-11510
    • Green, K.N.1
  • 21
    • 0347624644 scopus 로고    scopus 로고
    • Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
    • Rouaux C., et al. Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration. EMBO J. 22 (2003) 6537-6549
    • (2003) EMBO J. , vol.22 , pp. 6537-6549
    • Rouaux, C.1
  • 22
    • 0037386621 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent oxidative neuronal death independent of expanded polyglutamine repeats via an Sp1-dependent pathway
    • Ryu H., et al. Histone deacetylase inhibitors prevent oxidative neuronal death independent of expanded polyglutamine repeats via an Sp1-dependent pathway. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4281-4286
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4281-4286
    • Ryu, H.1
  • 23
    • 0038066627 scopus 로고    scopus 로고
    • Valproic acid, a mood stabilizer and anticonvulsant, protects rat cerebral cortical neurons from spontaneous cell death: a role of histone deacetylase inhibition
    • Jeong M.R., et al. Valproic acid, a mood stabilizer and anticonvulsant, protects rat cerebral cortical neurons from spontaneous cell death: a role of histone deacetylase inhibition. FEBS Lett. 542 (2003) 74-78
    • (2003) FEBS Lett. , vol.542 , pp. 74-78
    • Jeong, M.R.1
  • 24
    • 24944474714 scopus 로고    scopus 로고
    • Bim is a direct target of a neuronal E2F-dependent apoptotic pathway
    • Biswas S.C., et al. Bim is a direct target of a neuronal E2F-dependent apoptotic pathway. J. Neurosci. 25 (2005) 8349-8358
    • (2005) J. Neurosci. , vol.25 , pp. 8349-8358
    • Biswas, S.C.1
  • 25
    • 38149116286 scopus 로고    scopus 로고
    • Pulse inhibition of histone deacetylases induces complete resistance to oxidative death in cortical neurons without toxicity and reveals a role for cytoplasmic p21(waf1/cip1) in cell cycle-independent neuroprotection
    • Langley B., et al. Pulse inhibition of histone deacetylases induces complete resistance to oxidative death in cortical neurons without toxicity and reveals a role for cytoplasmic p21(waf1/cip1) in cell cycle-independent neuroprotection. J. Neurosci. 28 (2008) 163-176
    • (2008) J. Neurosci. , vol.28 , pp. 163-176
    • Langley, B.1
  • 26
    • 63849206749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent p53-dependent and p53-independent Bax-mediated neuronal apoptosis through two distinct mechanisms
    • Uo T., et al. Histone deacetylase inhibitors prevent p53-dependent and p53-independent Bax-mediated neuronal apoptosis through two distinct mechanisms. J. Neurosci. 29 (2009) 2824-2832
    • (2009) J. Neurosci. , vol.29 , pp. 2824-2832
    • Uo, T.1
  • 27
    • 13344260679 scopus 로고    scopus 로고
    • Lithium protection from glutamate excitotoxicity: therapeutic implications
    • Chuang D.-M. Lithium protection from glutamate excitotoxicity: therapeutic implications. Clin. Neurosci. Res. 4 (2004) 243-252
    • (2004) Clin. Neurosci. Res. , vol.4 , pp. 243-252
    • Chuang, D.-M.1
  • 28
    • 33746065340 scopus 로고    scopus 로고
    • Endogenous alpha-synuclein is induced by valproic acid through histone deacetylase inhibition and participates in neuroprotection against glutamate-induced excitotoxicity
    • Leng Y., and Chuang D.M. Endogenous alpha-synuclein is induced by valproic acid through histone deacetylase inhibition and participates in neuroprotection against glutamate-induced excitotoxicity. J. Neurosci. 26 (2006) 7502-7512
    • (2006) J. Neurosci. , vol.26 , pp. 7502-7512
    • Leng, Y.1    Chuang, D.M.2
  • 29
    • 5044240976 scopus 로고    scopus 로고
    • Valproic acid inhibits histone deacetylase activity and suppresses excitotoxicity-induced GAPDH nuclear accumulation and apoptotic death in neurons
    • Kanai H., et al. Valproic acid inhibits histone deacetylase activity and suppresses excitotoxicity-induced GAPDH nuclear accumulation and apoptotic death in neurons. Pharmacogenomics J. 4 (2004) 336-344
    • (2004) Pharmacogenomics J. , vol.4 , pp. 336-344
    • Kanai, H.1
  • 30
    • 13844318224 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases
    • Chuang D.M., et al. Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 269-290
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 269-290
    • Chuang, D.M.1
  • 31
    • 46649101876 scopus 로고    scopus 로고
    • Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis
    • Sen N., et al. Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis. Nat. Cell Biol. 10 (2008) 866-873
    • (2008) Nat. Cell Biol. , vol.10 , pp. 866-873
    • Sen, N.1
  • 32
    • 34848881102 scopus 로고    scopus 로고
    • Alpha-synuclein protects cerebellar granule neurons against 6-hydroxydopamine-induced death
    • Monti B., et al. Alpha-synuclein protects cerebellar granule neurons against 6-hydroxydopamine-induced death. J. Neurochem. 103 (2007) 518-530
    • (2007) J. Neurochem. , vol.103 , pp. 518-530
    • Monti, B.1
  • 33
    • 33749583553 scopus 로고    scopus 로고
    • Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • Kontopoulos E., et al. Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum. Mol. Genet. 15 (2006) 3012-3023
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 3012-3023
    • Kontopoulos, E.1
  • 34
    • 40449135649 scopus 로고    scopus 로고
    • Synergistic neuroprotective effects of lithium and valproic acid or other histone deacetylase inhibitors in neurons: roles of glycogen synthase kinase-3 inhibition
    • Leng Y., et al. Synergistic neuroprotective effects of lithium and valproic acid or other histone deacetylase inhibitors in neurons: roles of glycogen synthase kinase-3 inhibition. J. Neurosci. 28 (2008) 2576-2588
    • (2008) J. Neurosci. , vol.28 , pp. 2576-2588
    • Leng, Y.1
  • 35
    • 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., et al. The mood stabilizers lithium and valproate selectively activate the promoter IV of brain-derived neurotrophic factor in neurons. Mol. Psychiatry 14 (2009) 51-59
    • (2009) Mol. Psychiatry , vol.14 , pp. 51-59
    • Yasuda, S.1
  • 36
    • 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., et al. Valproate protects dopaminergic neurons in midbrain neuron/glia cultures by stimulating the release of neurotrophic factors from astrocytes. Mol. Psychiatry 11 (2006) 1116-1125
    • (2006) Mol. Psychiatry , vol.11 , pp. 1116-1125
    • Chen, P.S.1
  • 37
    • 55549129648 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors up-regulate astrocyte GDNF and BDNF gene transcription and protect dopaminergic neurons
    • Wu X., et al. Histone deacetylase inhibitors up-regulate astrocyte GDNF and BDNF gene transcription and protect dopaminergic neurons. Int. J. Neuropsychopharmacol. 11 (2008) 1123-1134
    • (2008) Int. J. Neuropsychopharmacol. , vol.11 , pp. 1123-1134
    • Wu, X.1
  • 38
    • 15544387446 scopus 로고    scopus 로고
    • Valproate pretreatment protects dopaminergic neurons from LPS-induced neurotoxicity in rat primary midbrain cultures: role of microglia
    • Peng G.S., et al. Valproate pretreatment protects dopaminergic neurons from LPS-induced neurotoxicity in rat primary midbrain cultures: role of microglia. Brain Res. Mol. Brain Res. 134 (2005) 162-169
    • (2005) Brain Res. Mol. Brain Res. , vol.134 , pp. 162-169
    • Peng, G.S.1
  • 39
    • 34748922275 scopus 로고    scopus 로고
    • Valproic acid and other histone deacetylase inhibitors induce microglial apoptosis and attenuate lipopolysaccharide-induced dopaminergic neurotoxicity
    • Chen P.S., et al. Valproic acid and other histone deacetylase inhibitors induce microglial apoptosis and attenuate lipopolysaccharide-induced dopaminergic neurotoxicity. Neuroscience 149 (2007) 203-212
    • (2007) Neuroscience , vol.149 , pp. 203-212
    • Chen, P.S.1
  • 40
    • 1842455106 scopus 로고    scopus 로고
    • Regulation of microglial inflammatory response by sodium butyrate and short-chain fatty acids
    • Huuskonen J., et al. Regulation of microglial inflammatory response by sodium butyrate and short-chain fatty acids. Br J. Pharmacol. 141 (2004) 874-880
    • (2004) Br J. Pharmacol. , vol.141 , pp. 874-880
    • Huuskonen, J.1
  • 41
    • 3042651448 scopus 로고    scopus 로고
    • Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction
    • Ren M., et al. Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction. J. Neurochem. 89 (2004) 1358-1367
    • (2004) J. Neurochem. , vol.89 , pp. 1358-1367
    • Ren, M.1
  • 42
    • 34248530339 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: multiple mechanisms of action
    • Kim H.J., et al. Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: multiple mechanisms of action. J. Pharmacol. Exp. Ther. 321 (2007) 892-901
    • (2007) J. Pharmacol. Exp. Ther. , vol.321 , pp. 892-901
    • Kim, H.J.1
  • 43
    • 33751120697 scopus 로고    scopus 로고
    • Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain
    • Faraco G., et al. Pharmacological inhibition of histone deacetylases by suberoylanilide hydroxamic acid specifically alters gene expression and reduces ischemic injury in the mouse brain. Mol. Pharmacol. 70 (2006) 1876-1884
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1876-1884
    • Faraco, G.1
  • 44
    • 67651146826 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, sodium butyrate, stimulates cell proliferation in the ischemic brain: roles of BDNF-TrkB signaling
    • Kim H., et al. The histone deacetylase inhibitor, sodium butyrate, stimulates cell proliferation in the ischemic brain: roles of BDNF-TrkB signaling. J. Neurochem. 110 (2009) 1226-1240
    • (2009) J. Neurochem. , vol.110 , pp. 1226-1240
    • Kim, H.1
  • 45
    • 4844224132 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate protects against cerebral ischemic injury
    • Qi X., et al. Sodium 4-phenylbutyrate protects against cerebral ischemic injury. Mol. Pharmacol. 66 (2004) 899-908
    • (2004) Mol. Pharmacol. , vol.66 , pp. 899-908
    • Qi, X.1
  • 46
    • 37549004821 scopus 로고    scopus 로고
    • Anti-inflammatory effects of the 70 kDa heat shock protein in experimental stroke
    • Zheng Z., et al. Anti-inflammatory effects of the 70 kDa heat shock protein in experimental stroke. J. Cereb. Blood Flow Metab. 28 (2008) 53-63
    • (2008) J. Cereb. Blood Flow Metab. , vol.28 , pp. 53-63
    • Zheng, Z.1
  • 47
    • 33746398550 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation protects wild-type but not gelsolin-deficient neurons from oxygen/glucose deprivation
    • Meisel A., et al. Inhibition of histone deacetylation protects wild-type but not gelsolin-deficient neurons from oxygen/glucose deprivation. J. Neurochem. 98 (2006) 1019-1031
    • (2006) J. Neurochem. , vol.98 , pp. 1019-1031
    • Meisel, A.1
  • 48
    • 41149124866 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation protects wildtype but not gelsolin-deficient mice from ischemic brain injury
    • Yildirim F., et al. Inhibition of histone deacetylation protects wildtype but not gelsolin-deficient mice from ischemic brain injury. Exp. Neurol. 210 (2008) 531-542
    • (2008) Exp. Neurol. , vol.210 , pp. 531-542
    • Yildirim, F.1
  • 49
    • 34147199586 scopus 로고    scopus 로고
    • Valproic acid-mediated neuroprotection in intracerebral hemorrhage via histone deacetylase inhibition and transcriptional activation
    • Sinn D.I., et al. Valproic acid-mediated neuroprotection in intracerebral hemorrhage via histone deacetylase inhibition and transcriptional activation. Neurobiol. Dis. 26 (2007) 464-472
    • (2007) Neurobiol. Dis. , vol.26 , pp. 464-472
    • Sinn, D.I.1
  • 50
    • 54049090410 scopus 로고    scopus 로고
    • Histone deacetylase inhibition reduces myocardial ischemia-reperfusion injury in mice
    • Granger A., et al. Histone deacetylase inhibition reduces myocardial ischemia-reperfusion injury in mice. FASEB J. 22 (2008) 3549-3560
    • (2008) FASEB J. , vol.22 , pp. 3549-3560
    • Granger, A.1
  • 51
    • 33644783812 scopus 로고    scopus 로고
    • Regional and cellular gene expression changes in human Huntington's disease brain
    • Hodges A., et al. Regional and cellular gene expression changes in human Huntington's disease brain. Hum. Mol. Genet. 15 (2006) 965-977
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 965-977
    • Hodges, A.1
  • 52
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars K.L., and Rubinsztein D.C. Transcriptional abnormalities in Huntington disease. Trends Genet. 19 (2003) 233-238
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 53
    • 39049159734 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: possible implications for neurodegenerative disorders
    • Hahnen E., et al. Histone deacetylase inhibitors: possible implications for neurodegenerative disorders. Expert Opin. Investig. Drugs 17 (2008) 169-184
    • (2008) Expert Opin. Investig. Drugs , vol.17 , pp. 169-184
    • Hahnen, E.1
  • 54
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan J.S., et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 413 (2001) 739-743
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1
  • 55
    • 33644830913 scopus 로고    scopus 로고
    • Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity
    • Bates E.A., et al. Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity. J. Neurosci. 26 (2006) 2830-2838
    • (2006) J. Neurosci. , vol.26 , pp. 2830-2838
    • Bates, E.A.1
  • 56
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos J., et al. Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17 (2008) 3767-3775
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3767-3775
    • Pallos, J.1
  • 57
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong H., et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 137 (2009) 60-72
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1
  • 58
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease
    • Hockly E., et al. Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 2041-2046
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2041-2046
    • Hockly, E.1
  • 59
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante R.J., et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23 (2003) 9418-9427
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 60
    • 34447317536 scopus 로고    scopus 로고
    • Histones associated with downregulated genes are hypo-acetylated in Huntington's disease models
    • Sadri-Vakili G., et al. Histones associated with downregulated genes are hypo-acetylated in Huntington's disease models. Hum. Mol. Genet. 16 (2007) 1293-1306
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1293-1306
    • Sadri-Vakili, G.1
  • 61
    • 55749103407 scopus 로고    scopus 로고
    • The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice
    • Thomas E.A., et al. The HDAC inhibitor 4b ameliorates the disease phenotype and transcriptional abnormalities in Huntington's disease transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 15564-15569
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15564-15569
    • Thomas, E.A.1
  • 62
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
    • Gardian G., et al. Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease. J. Biol. Chem. 280 (2005) 556-563
    • (2005) J. Biol. Chem. , vol.280 , pp. 556-563
    • Gardian, G.1
  • 63
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease
    • Zuccato C., et al. Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science 293 (2001) 493-498
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1
  • 64
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay D.G., et al. Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 13 (2004) 1389-1405
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1
  • 65
    • 33846611068 scopus 로고    scopus 로고
    • The induction levels of heat shock protein 70 differentiate the vulnerabilities to mutant huntingtin among neuronal subtypes
    • Tagawa K., et al. The induction levels of heat shock protein 70 differentiate the vulnerabilities to mutant huntingtin among neuronal subtypes. J. Neurosci. 27 (2007) 868-880
    • (2007) J. Neurosci. , vol.27 , pp. 868-880
    • Tagawa, K.1
  • 66
    • 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., et al. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27 (2007) 3571-3583
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1
  • 67
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A., et al. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J. Biol. Chem. 280 (2005) 40282-40292
    • (2005) J. Biol. Chem. , vol.280 , pp. 40282-40292
    • Iwata, A.1
  • 68
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey U.B., et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447 (2007) 859-863
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1
  • 69
    • 20144385858 scopus 로고    scopus 로고
    • Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice
    • Ryu H., et al. Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice. J. Neurochem. 93 (2005) 1087-1098
    • (2005) J. Neurochem. , vol.93 , pp. 1087-1098
    • Ryu, H.1
  • 70
    • 62549133620 scopus 로고    scopus 로고
    • Combined riluzole and sodium phenylbutyrate therapy in transgenic amyotrophic lateral sclerosis mice
    • Del Signore S.J., et al. Combined riluzole and sodium phenylbutyrate therapy in transgenic amyotrophic lateral sclerosis mice. Amyotroph. Lateral Scler. 10 (2009) 85-94
    • (2009) Amyotroph. Lateral Scler. , vol.10 , pp. 85-94
    • Del Signore, S.J.1
  • 71
    • 33645076252 scopus 로고    scopus 로고
    • Additive neuroprotective effects of a histone deacetylase inhibitor and a catalytic antioxidant in a transgenic mouse model of amyotrophic lateral sclerosis
    • Petri S., et al. Additive neuroprotective effects of a histone deacetylase inhibitor and a catalytic antioxidant in a transgenic mouse model of amyotrophic lateral sclerosis. Neurobiol. Dis. 22 (2006) 40-49
    • (2006) Neurobiol. Dis. , vol.22 , pp. 40-49
    • Petri, S.1
  • 72
    • 34548157024 scopus 로고    scopus 로고
    • Microarray analysis of the cellular pathways involved in the adaptation to and progression of motor neuron injury in the SOD1 G93A mouse model of familial ALS
    • Ferraiuolo L., et al. Microarray analysis of the cellular pathways involved in the adaptation to and progression of motor neuron injury in the SOD1 G93A mouse model of familial ALS. J. Neurosci. 27 (2007) 9201-9219
    • (2007) J. Neurosci. , vol.27 , pp. 9201-9219
    • Ferraiuolo, L.1
  • 73
    • 10844284615 scopus 로고    scopus 로고
    • Benefit of valproic acid in suppressing disease progression of ALS model mice
    • Sugai F., et al. Benefit of valproic acid in suppressing disease progression of ALS model mice. Eur. J. Neurosci. 20 (2004) 3179-3183
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 3179-3183
    • Sugai, F.1
  • 74
    • 34250612194 scopus 로고    scopus 로고
    • Sodium valproate exerts neuroprotective effects in vivo through CREB-binding protein-dependent mechanisms but does not improve survival in an amyotrophic lateral sclerosis mouse model
    • Rouaux C., et al. Sodium valproate exerts neuroprotective effects in vivo through CREB-binding protein-dependent mechanisms but does not improve survival in an amyotrophic lateral sclerosis mouse model. J. Neurosci. 27 (2007) 5535-5545
    • (2007) J. Neurosci. , vol.27 , pp. 5535-5545
    • Rouaux, C.1
  • 75
    • 49249136687 scopus 로고    scopus 로고
    • Combined lithium and valproate treatment delays disease onset, reduces neurological deficits and prolongs survival in an amyotrophic lateral sclerosis mouse model
    • Feng H.L., et al. Combined lithium and valproate treatment delays disease onset, reduces neurological deficits and prolongs survival in an amyotrophic lateral sclerosis mouse model. Neuroscience 155 (2008) 567-572
    • (2008) Neuroscience , vol.155 , pp. 567-572
    • Feng, H.L.1
  • 76
    • 62549133175 scopus 로고    scopus 로고
    • Phase 2 study of sodium phenylbutyrate in ALS
    • Cudkowicz M.E., et al. Phase 2 study of sodium phenylbutyrate in ALS. Amyotroph. Lateral Scler. 10 (2009) 99-106
    • (2009) Amyotroph. Lateral Scler. , vol.10 , pp. 99-106
    • Cudkowicz, M.E.1
  • 77
    • 0035859952 scopus 로고    scopus 로고
    • Treatment of spinal muscular atrophy by sodium butyrate
    • Chang J.G., et al. Treatment of spinal muscular atrophy by sodium butyrate. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 9808-9813
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9808-9813
    • Chang, J.G.1
  • 78
    • 10744229981 scopus 로고    scopus 로고
    • Phenylbutyrate increases SMN expression in vitro: relevance for treatment of spinal muscular atrophy
    • Andreassi C., et al. Phenylbutyrate increases SMN expression in vitro: relevance for treatment of spinal muscular atrophy. Eur. J. Hum. Genet. 12 (2004) 59-65
    • (2004) Eur. J. Hum. Genet. , vol.12 , pp. 59-65
    • Andreassi, C.1
  • 79
    • 0242290062 scopus 로고    scopus 로고
    • Valproic acid increases SMN levels in spinal muscular atrophy patient cells
    • Sumner C.J., et al. Valproic acid increases SMN levels in spinal muscular atrophy patient cells. Ann. Neurol. 54 (2003) 647-654
    • (2003) Ann. Neurol. , vol.54 , pp. 647-654
    • Sumner, C.J.1
  • 80
    • 0141506887 scopus 로고    scopus 로고
    • Valproic acid increases the SMN2 protein level: a well-known drug as a potential therapy for spinal muscular atrophy
    • Brichta L., et al. Valproic acid increases the SMN2 protein level: a well-known drug as a potential therapy for spinal muscular atrophy. Hum. Mol. Genet. 12 (2003) 2481-2489
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2481-2489
    • Brichta, L.1
  • 81
    • 33745079980 scopus 로고    scopus 로고
    • In vitro and ex vivo evaluation of second-generation histone deacetylase inhibitors for the treatment of spinal muscular atrophy
    • Hahnen E., et al. In vitro and ex vivo evaluation of second-generation histone deacetylase inhibitors for the treatment of spinal muscular atrophy. J. Neurochem. 98 (2006) 193-202
    • (2006) J. Neurochem. , vol.98 , pp. 193-202
    • Hahnen, E.1
  • 82
    • 33745686137 scopus 로고    scopus 로고
    • The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/protein levels in spinal muscular atrophy cells
    • Riessland M., et al. The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/protein levels in spinal muscular atrophy cells. Hum. Genet. 120 (2006) 101-110
    • (2006) Hum. Genet. , vol.120 , pp. 101-110
    • Riessland, M.1
  • 83
    • 58049206781 scopus 로고    scopus 로고
    • Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition
    • Hauke J., et al. Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition. Hum. Mol. Genet. 18 (2009) 304-317
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 304-317
    • Hauke, J.1
  • 84
    • 33847358736 scopus 로고    scopus 로고
    • Trichostatin A increases SMN expression and survival in a mouse model of spinal muscular atrophy
    • Avila A.M., et al. Trichostatin A increases SMN expression and survival in a mouse model of spinal muscular atrophy. J. Clin. Invest. 117 (2007) 659-671
    • (2007) J. Clin. Invest. , vol.117 , pp. 659-671
    • Avila, A.M.1
  • 85
    • 18144400082 scopus 로고    scopus 로고
    • The role of histone acetylation in SMN gene expression
    • Kernochan L.E., et al. The role of histone acetylation in SMN gene expression. Hum. Mol. Genet. 14 (2005) 1171-1182
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1171-1182
    • Kernochan, L.E.1
  • 86
    • 33750001213 scopus 로고    scopus 로고
    • Establishing a standardized therapeutic testing protocol for spinal muscular atrophy
    • Tsai L.K., et al. Establishing a standardized therapeutic testing protocol for spinal muscular atrophy. Neurobiol. Dis. 24 (2006) 286-295
    • (2006) Neurobiol. Dis. , vol.24 , pp. 286-295
    • Tsai, L.K.1
  • 87
    • 54249110856 scopus 로고    scopus 로고
    • Multiple therapeutic effects of valproic acid in spinal muscular atrophy model mice
    • Tsai L.K., et al. Multiple therapeutic effects of valproic acid in spinal muscular atrophy model mice. J. Mol. Med. 86 (2008) 1243-1254
    • (2008) J. Mol. Med. , vol.86 , pp. 1243-1254
    • Tsai, L.K.1
  • 88
    • 49349107825 scopus 로고    scopus 로고
    • Restoring Bcl-x(L) levels benefits a mouse model of spinal muscular atrophy
    • Tsai L.K., et al. Restoring Bcl-x(L) levels benefits a mouse model of spinal muscular atrophy. Neurobiol. Dis. 31 (2008) 361-367
    • (2008) Neurobiol. Dis. , vol.31 , pp. 361-367
    • Tsai, L.K.1
  • 89
    • 9144269242 scopus 로고    scopus 로고
    • Pilot trial of phenylbutyrate in spinal muscular atrophy
    • Mercuri E., et al. Pilot trial of phenylbutyrate in spinal muscular atrophy. Neuromuscul. Disord. 14 (2004) 130-135
    • (2004) Neuromuscul. Disord. , vol.14 , pp. 130-135
    • Mercuri, E.1
  • 90
    • 13544258982 scopus 로고    scopus 로고
    • Phenylbutyrate increases SMN gene expression in spinal muscular atrophy patients
    • Brahe C., et al. Phenylbutyrate increases SMN gene expression in spinal muscular atrophy patients. Eur. J. Hum. Genet. 13 (2005) 256-259
    • (2005) Eur. J. Hum. Genet. , vol.13 , pp. 256-259
    • Brahe, C.1
  • 91
    • 33744803707 scopus 로고    scopus 로고
    • In vivo activation of SMN in spinal muscular atrophy carriers and patients treated with valproate
    • Brichta L., et al. In vivo activation of SMN in spinal muscular atrophy carriers and patients treated with valproate. Ann. Neurol. 59 (2006) 970-975
    • (2006) Ann. Neurol. , vol.59 , pp. 970-975
    • Brichta, L.1
  • 92
    • 33747083488 scopus 로고    scopus 로고
    • Valproate may improve strength and function in patients with type III/IV spinal muscle atrophy
    • Weihl C.C., et al. Valproate may improve strength and function in patients with type III/IV spinal muscle atrophy. Neurology 67 (2006) 500-501
    • (2006) Neurology , vol.67 , pp. 500-501
    • Weihl, C.C.1
  • 93
    • 36248958610 scopus 로고    scopus 로고
    • Valproic acid treatment in six patients with spinal muscular atrophy
    • Tsai L.K., et al. Valproic acid treatment in six patients with spinal muscular atrophy. Eur. J. Neurol. 14 (2007) e8-9
    • (2007) Eur. J. Neurol. , vol.14
    • Tsai, L.K.1
  • 94
    • 12344291203 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate against MPTP neurotoxicity
    • Gardian G., et al. Neuroprotective effects of phenylbutyrate against MPTP neurotoxicity. Neuromolecular Med. 5 (2004) 235-241
    • (2004) Neuromolecular Med. , vol.5 , pp. 235-241
    • Gardian, G.1
  • 95
    • 0036581222 scopus 로고    scopus 로고
    • The GDNF family: signalling, biological functions and therapeutic value
    • Airaksinen M.S., and Saarma M. The GDNF family: signalling, biological functions and therapeutic value. Nat. Rev. Neurosci. 3 (2002) 383-394
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 383-394
    • Airaksinen, M.S.1    Saarma, M.2
  • 96
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro T.F., et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317 (2007) 516-519
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1
  • 97
    • 2642552331 scopus 로고    scopus 로고
    • Lithium, a common drug for bipolar disorder treatment, regulates amyloid-beta precursor protein processing
    • Su Y., et al. Lithium, a common drug for bipolar disorder treatment, regulates amyloid-beta precursor protein processing. Biochemistry 43 (2004) 6899-6908
    • (2004) Biochemistry , vol.43 , pp. 6899-6908
    • Su, Y.1
  • 98
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • Fischer A., et al. Recovery of learning and memory is associated with chromatin remodelling. Nature 447 (2007) 178-182
    • (2007) Nature , vol.447 , pp. 178-182
    • Fischer, A.1
  • 99
    • 57049177826 scopus 로고    scopus 로고
    • Deregulation of HDAC1 by p25/Cdk5 in neurotoxicity
    • Kim D., et al. Deregulation of HDAC1 by p25/Cdk5 in neurotoxicity. Neuron 60 (2008) 803-817
    • (2008) Neuron , vol.60 , pp. 803-817
    • Kim, D.1
  • 100
    • 65549123471 scopus 로고    scopus 로고
    • HDAC2 negatively regulates memory formation and synaptic plasticity
    • Guan J.S., et al. HDAC2 negatively regulates memory formation and synaptic plasticity. Nature 459 (2009) 55-60
    • (2009) Nature , vol.459 , pp. 55-60
    • Guan, J.S.1
  • 101
    • 47549109984 scopus 로고    scopus 로고
    • Beyond transcription factors: the role of chromatin modifying enzymes in regulating transcription required for memory
    • Barrett R.M., and Wood M.A. Beyond transcription factors: the role of chromatin modifying enzymes in regulating transcription required for memory. Learn. Mem. 15 (2008) 460-467
    • (2008) Learn. Mem. , vol.15 , pp. 460-467
    • Barrett, R.M.1    Wood, M.A.2
  • 102
    • 67349220155 scopus 로고    scopus 로고
    • Phenylbutyrate ameliorates cognitive deficit and reduces tau pathology in an Alzheimer's disease mouse model
    • Ricobaraza A., et al. Phenylbutyrate ameliorates cognitive deficit and reduces tau pathology in an Alzheimer's disease mouse model. Neuropsychopharmacology 34 (2009) 1721-1732
    • (2009) Neuropsychopharmacology , vol.34 , pp. 1721-1732
    • Ricobaraza, A.1
  • 103
    • 58149314221 scopus 로고    scopus 로고
    • Valproic acid inhibits Abeta production, neuritic plaque formation, and behavioral deficits in Alzheimer's disease mouse models
    • Qing H., et al. Valproic acid inhibits Abeta production, neuritic plaque formation, and behavioral deficits in Alzheimer's disease mouse models. J. Exp. Med. 205 (2008) 2781-2789
    • (2008) J. Exp. Med. , vol.205 , pp. 2781-2789
    • Qing, H.1
  • 104
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • Kim D., et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J. 26 (2007) 3169-3179
    • (2007) EMBO J. , vol.26 , pp. 3169-3179
    • Kim, D.1
  • 105
    • 37249071337 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer treatment: a review of the clinical toxicity and the modulation of gene expression in cancer cell
    • Bruserud O., et al. Histone deacetylase inhibitors in cancer treatment: a review of the clinical toxicity and the modulation of gene expression in cancer cell. Curr. Pharm. Biotechnol. 8 (2007) 388-400
    • (2007) Curr. Pharm. Biotechnol. , vol.8 , pp. 388-400
    • Bruserud, O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.