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Volumn 14, Issue 9-10, 2009, Pages 453-464

Small molecule drug discovery for Huntington's Disease

Author keywords

[No Author keywords available]

Indexed keywords

HUNTINGTIN;

EID: 67349122746     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2009.02.006     Document Type: Review
Times cited : (38)

References (101)
  • 1
    • 39549109353 scopus 로고    scopus 로고
    • Huntington's disease: progress and potential in the field
    • Stack E.C., and Ferrante R.J. Huntington's disease: progress and potential in the field. Expert Opin. Investig. Drugs 16 (2007) 1933-1953
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 1933-1953
    • Stack, E.C.1    Ferrante, R.J.2
  • 2
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997) 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 3
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., et al. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421 (2003) 373-379
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1
  • 4
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M., et al. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004) 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1
  • 5
    • 0033373421 scopus 로고    scopus 로고
    • Bioenergetics in Huntington's disease
    • Grunewald T., and Beal M.F. Bioenergetics in Huntington's disease. Ann. N.Y. Acad. Sci. 893 (1999) 203-213
    • (1999) Ann. N.Y. Acad. Sci. , vol.893 , pp. 203-213
    • Grunewald, T.1    Beal, M.F.2
  • 6
    • 0029943742 scopus 로고    scopus 로고
    • Proton magnetic resonance spectroscopy in Huntington's disease: evidence in favour of the glutamate excitotoxic theory
    • Taylor-Robinson S.D., et al. Proton magnetic resonance spectroscopy in Huntington's disease: evidence in favour of the glutamate excitotoxic theory. Mov. Disord. 11 (1996) 167-173
    • (1996) Mov. Disord. , vol.11 , pp. 167-173
    • Taylor-Robinson, S.D.1
  • 7
    • 0034702030 scopus 로고    scopus 로고
    • Decreased expression of striatal signaling genes in a mouse model of Huntington's disease
    • Luthi-Carter R., et al. Decreased expression of striatal signaling genes in a mouse model of Huntington's disease. Hum. Mol. Genet. 9 (2000) 1259-1271
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1259-1271
    • Luthi-Carter, R.1
  • 8
    • 0037101838 scopus 로고    scopus 로고
    • Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease
    • Chan E.Y., et al. Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease. Hum. Mol. Genet. 11 (2002) 1939-1951
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1939-1951
    • Chan, E.Y.1
  • 9
    • 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., 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. 16 (2007) 1845-1861
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1845-1861
    • Kuhn, A.1
  • 10
    • 35348877164 scopus 로고    scopus 로고
    • Transcriptional signatures in Huntington's disease
    • Cha J.H. Transcriptional signatures in Huntington's disease. Prog. Neurobiol. 83 (2007) 228-248
    • (2007) Prog. Neurobiol. , vol.83 , pp. 228-248
    • Cha, J.H.1
  • 11
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah A.W., et al. Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296 (2002) 2238-2243
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1
  • 12
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • Li S.H., et al. Interaction of Huntington disease protein with transcriptional activator Sp1. Mol. Cell Biol. 22 (2002) 1277-1287
    • (2002) Mol. Cell Biol. , vol.22 , pp. 1277-1287
    • Li, S.H.1
  • 13
    • 12944263711 scopus 로고    scopus 로고
    • The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan J.S., et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 6763-6768
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6763-6768
    • Steffan, J.S.1
  • 14
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora Jr. F.C., et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291 (2001) 2423-2428
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora Jr., F.C.1
  • 15
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease
    • Wyttenbach A., et al. Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease. Hum. Mol. Genet. 10 (2001) 1829-1845
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1
  • 16
    • 34447302317 scopus 로고    scopus 로고
    • Modulation of nucleosome dynamics in Huntington's disease
    • Stack E.C., et al. Modulation of nucleosome dynamics in Huntington's disease. Hum. Mol. Genet. 16 (2007) 1164-1175
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1164-1175
    • Stack, E.C.1
  • 17
    • 34547807613 scopus 로고    scopus 로고
    • Global changes to the ubiquitin system in Huntington's disease
    • Bennett E.J., et al. Global changes to the ubiquitin system in Huntington's disease. Nature 448 (2007) 704-708
    • (2007) Nature , vol.448 , pp. 704-708
    • Bennett, E.J.1
  • 18
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B., et al. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11 (2002) 1107-1117
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1
  • 19
    • 0037417220 scopus 로고    scopus 로고
    • Apoptosis and caspases in neurodegenerative diseases
    • Friedlander R.M. Apoptosis and caspases in neurodegenerative diseases. N. Engl. J. Med. 348 (2003) 1365-1375
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1365-1375
    • Friedlander, R.M.1
  • 20
    • 20244378556 scopus 로고    scopus 로고
    • RNA interference improves motor and neuropathological abnormalities in a Huntington's disease mouse model
    • Harper S.Q., et al. RNA interference improves motor and neuropathological abnormalities in a Huntington's disease mouse model. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 5820-5825
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5820-5825
    • Harper, S.Q.1
  • 21
    • 0037154165 scopus 로고    scopus 로고
    • Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity
    • Khoshnan A., et al. Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1002-1007
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1002-1007
    • Khoshnan, A.1
  • 22
    • 43049140462 scopus 로고    scopus 로고
    • Tissue transglutaminase: a novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases
    • Wilhelmus M.M., et al. Tissue transglutaminase: a novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases. Eur. J. Pharmacol. 585 (2008) 464-472
    • (2008) Eur. J. Pharmacol. , vol.585 , pp. 464-472
    • Wilhelmus, M.M.1
  • 23
    • 27344447235 scopus 로고    scopus 로고
    • The therapeutic role of creatine in Huntington's disease
    • Ryu H., et al. The therapeutic role of creatine in Huntington's disease. Pharmacol. Ther. 108 (2005) 193-207
    • (2005) Pharmacol. Ther. , vol.108 , pp. 193-207
    • Ryu, H.1
  • 24
    • 0032555066 scopus 로고    scopus 로고
    • Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects
    • Matthews R.T., et al. Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 8892-8897
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 8892-8897
    • Matthews, R.T.1
  • 25
    • 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 4544234691 scopus 로고    scopus 로고
    • Neuroprotective effects of M826, a reversible caspase-3 inhibitor, in the rat malonate model of Huntington's disease
    • Toulmond S., et al. Neuroprotective effects of M826, a reversible caspase-3 inhibitor, in the rat malonate model of Huntington's disease. Br. J. Pharmacol. 141 (2004) 689-697
    • (2004) Br. J. Pharmacol. , vol.141 , pp. 689-697
    • Toulmond, S.1
  • 29
    • 51049090179 scopus 로고    scopus 로고
    • Drug discovery and development for Huntington's disease-an orphan indication with high medical need
    • Heitz F., et al. Drug discovery and development for Huntington's disease-an orphan indication with high medical need. IDrugs 11 (2008) 653-660
    • (2008) IDrugs , vol.11 , pp. 653-660
    • Heitz, F.1
  • 30
    • 41249101172 scopus 로고    scopus 로고
    • Neuroprotection for Huntington's disease: ready, set, slow
    • Hersch S.M., and Rosas H.D. Neuroprotection for Huntington's disease: ready, set, slow. Neurotherapeutics 5 (2008) 226-236
    • (2008) Neurotherapeutics , vol.5 , pp. 226-236
    • Hersch, S.M.1    Rosas, H.D.2
  • 31
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • Scherzinger E., et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90 (1997) 549-558
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1
  • 32
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy
    • Heiser V., et al. Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 6739-6744
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6739-6744
    • Heiser, V.1
  • 33
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • Tanaka M., et al. Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease. Nat. Med. 10 (2004) 148-154
    • (2004) Nat. Med. , vol.10 , pp. 148-154
    • Tanaka, M.1
  • 34
    • 18744369020 scopus 로고    scopus 로고
    • Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay
    • Heiser V., et al. Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl. 4 (2002) 16400-16406
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.SUPPL. 4 , pp. 16400-16406
    • Heiser, V.1
  • 35
    • 0033614947 scopus 로고    scopus 로고
    • Riluzole series. Synthesis and in vivo 'antiglutamate' activity of 6-substituted-2-benzothiazolamines and 3-substituted-2-imino-benzothiazolines
    • Jimonet P., et al. Riluzole series. Synthesis and in vivo 'antiglutamate' activity of 6-substituted-2-benzothiazolamines and 3-substituted-2-imino-benzothiazolines. J. Med. Chem. 42 (1999) 2828-2843
    • (1999) J. Med. Chem. , vol.42 , pp. 2828-2843
    • Jimonet, P.1
  • 36
    • 0035881211 scopus 로고    scopus 로고
    • A microtiter plate assay for polyglutamine aggregate extension
    • Berthelier V., et al. A microtiter plate assay for polyglutamine aggregate extension. Anal. Biochem. 295 (2001) 227-236
    • (2001) Anal. Biochem. , vol.295 , pp. 227-236
    • Berthelier, V.1
  • 37
    • 12944335007 scopus 로고    scopus 로고
    • Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation
    • Wang J., et al. Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation. BMC Neurosci. 6 (2005) 1
    • (2005) BMC Neurosci. , vol.6 , pp. 1
    • Wang, J.1
  • 38
    • 35348984636 scopus 로고    scopus 로고
    • Optimization of a polyglutamine aggregation inhibitor peptide (QBP1) using a thioflavin T fluorescence assay
    • Hamuro L., et al. Optimization of a polyglutamine aggregation inhibitor peptide (QBP1) using a thioflavin T fluorescence assay. Assay Drug Dev. Technol. 5 (2007) 629-636
    • (2007) Assay Drug Dev. Technol. , vol.5 , pp. 629-636
    • Hamuro, L.1
  • 39
    • 0034615932 scopus 로고    scopus 로고
    • Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening
    • Nagai Y., et al. Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J. Biol. Chem. 275 (2000) 10437-10442
    • (2000) J. Biol. Chem. , vol.275 , pp. 10437-10442
    • Nagai, Y.1
  • 40
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S., and Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 1589-1594
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 41
    • 20044390015 scopus 로고    scopus 로고
    • A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo
    • Zhang X., et al. A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 892-897
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 892-897
    • Zhang, X.1
  • 42
    • 0034988923 scopus 로고    scopus 로고
    • Gene transfer methods for CNS organotypic cultures: a comparison of three nonviral methods
    • Murphy R.C., and Messer A. Gene transfer methods for CNS organotypic cultures: a comparison of three nonviral methods. Mol. Ther. 3 (2001) 113-121
    • (2001) Mol. Ther. , vol.3 , pp. 113-121
    • Murphy, R.C.1    Messer, A.2
  • 43
    • 1242351323 scopus 로고    scopus 로고
    • A single-chain Fv intrabody provides functional protection against the effects of mutant protein in an organotypic slice culture model of Huntington's disease
    • Murphy R.C., and Messer A. A single-chain Fv intrabody provides functional protection against the effects of mutant protein in an organotypic slice culture model of Huntington's disease. Brain Res. Mol. Brain Res. 121 (2004) 141-145
    • (2004) Brain Res. Mol. Brain Res. , vol.121 , pp. 141-145
    • Murphy, R.C.1    Messer, A.2
  • 44
    • 41649114424 scopus 로고    scopus 로고
    • High throughput screening for neurodegeneration and complex disease phenotypes
    • Varma H., et al. High throughput screening for neurodegeneration and complex disease phenotypes. Comb. Chem. High Throughput Screen. 11 (2008) 238-248
    • (2008) Comb. Chem. High Throughput Screen. , vol.11 , pp. 238-248
    • Varma, H.1
  • 45
    • 0035668573 scopus 로고    scopus 로고
    • Inhibition of polyglutamine aggregation in R6/2 HD brain slices-complex dose-response profiles
    • Smith D.L., et al. Inhibition of polyglutamine aggregation in R6/2 HD brain slices-complex dose-response profiles. Neurobiol. Dis. 8 (2001) 1017-1026
    • (2001) Neurobiol. Dis. , vol.8 , pp. 1017-1026
    • Smith, D.L.1
  • 46
    • 0242657586 scopus 로고    scopus 로고
    • A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor
    • Pollitt S.K., et al. A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor. Neuron 40 (2003) 685-694
    • (2003) Neuron , vol.40 , pp. 685-694
    • Pollitt, S.K.1
  • 47
    • 50249147874 scopus 로고    scopus 로고
    • Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation
    • Shao J., et al. Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation. Mol. Cell Biol. 28 (2008) 5196-5208
    • (2008) Mol. Cell Biol. , vol.28 , pp. 5196-5208
    • Shao, J.1
  • 48
    • 33745239787 scopus 로고    scopus 로고
    • Biologically active molecules that reduce polyglutamine aggregation and toxicity
    • Desai U.A., et al. Biologically active molecules that reduce polyglutamine aggregation and toxicity. Hum. Mol. Genet. 15 (2006) 2114-2124
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2114-2124
    • Desai, U.A.1
  • 49
    • 37349007785 scopus 로고    scopus 로고
    • Time-lapse analysis of aggregate formation in an inducible PC12 cell model of Huntington's disease reveals time-dependent aggregate formation that transiently delays cell death
    • Gong B., et al. Time-lapse analysis of aggregate formation in an inducible PC12 cell model of Huntington's disease reveals time-dependent aggregate formation that transiently delays cell death. Brain Res. Bull. 75 (2008) 146-157
    • (2008) Brain Res. Bull. , vol.75 , pp. 146-157
    • Gong, B.1
  • 50
    • 42749089622 scopus 로고    scopus 로고
    • High throughput quantification of mutant huntingtin aggregates
    • Scotter E.L., et al. High throughput quantification of mutant huntingtin aggregates. J. Neurosci. Methods 171 (2008) 174-179
    • (2008) J. Neurosci. Methods , vol.171 , pp. 174-179
    • Scotter, E.L.1
  • 51
    • 38049139425 scopus 로고    scopus 로고
    • Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease
    • Weiss A., et al. Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease. J. Neurochem. 104 (2008) 846-858
    • (2008) J. Neurochem. , vol.104 , pp. 846-858
    • Weiss, A.1
  • 52
    • 39349094523 scopus 로고    scopus 로고
    • Small-molecule aggregates inhibit amyloid polymerization
    • Feng B.Y., et al. Small-molecule aggregates inhibit amyloid polymerization. Nat. Chem. Biol. 4 (2008) 197-199
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 197-199
    • Feng, B.Y.1
  • 53
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • Sarkar S., et al. Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat. Chem. Biol. 3 (2007) 331-338
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 331-338
    • Sarkar, S.1
  • 54
    • 0037947662 scopus 로고    scopus 로고
    • A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila
    • Apostol B.L., et al. A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5950-5955
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5950-5955
    • Apostol, B.L.1
  • 55
    • 34047170795 scopus 로고    scopus 로고
    • Discovery of a novel small-molecule targeting selective clearance of mutant huntingtin fragments
    • Coufal M., et al. Discovery of a novel small-molecule targeting selective clearance of mutant huntingtin fragments. J. Biomol. Screen. 12 (2007) 351-360
    • (2007) J. Biomol. Screen. , vol.12 , pp. 351-360
    • Coufal, M.1
  • 56
    • 21544450545 scopus 로고    scopus 로고
    • p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae B.I., et al. p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 47 (2005) 29-41
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1
  • 57
    • 40949135766 scopus 로고    scopus 로고
    • Mutant Huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor
    • Yamanaka T., et al. Mutant Huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor. EMBO J. 27 (2008) 827-839
    • (2008) EMBO J. , vol.27 , pp. 827-839
    • Yamanaka, T.1
  • 58
    • 44449177217 scopus 로고    scopus 로고
    • RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells
    • Doi H., et al. RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. J. Biol. Chem. 283 (2008) 6489-6500
    • (2008) J. Biol. Chem. , vol.283 , pp. 6489-6500
    • Doi, H.1
  • 59
    • 0742287915 scopus 로고    scopus 로고
    • CRE-mediated transcription is increased in Huntington's disease transgenic mice
    • Obrietan K., and Hoyt K.R. CRE-mediated transcription is increased in Huntington's disease transgenic mice. J. Neurosci. 24 (2004) 791-796
    • (2004) J. Neurosci. , vol.24 , pp. 791-796
    • Obrietan, K.1    Hoyt, K.R.2
  • 60
    • 33745200299 scopus 로고    scopus 로고
    • Sp1 is up-regulated in cellular and transgenic models of Huntington disease, and its reduction is neuroprotective
    • Qiu Z., et al. Sp1 is up-regulated in cellular and transgenic models of Huntington disease, and its reduction is neuroprotective. J. Biol. Chem. 281 (2006) 16672-16680
    • (2006) J. Biol. Chem. , vol.281 , pp. 16672-16680
    • Qiu, Z.1
  • 61
    • 1042289730 scopus 로고    scopus 로고
    • Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis
    • Sugars K.L., et al. Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis. J. Biol. Chem. 279 (2004) 4988-4999
    • (2004) J. Biol. Chem. , vol.279 , pp. 4988-4999
    • Sugars, K.L.1
  • 62
    • 54849422301 scopus 로고    scopus 로고
    • Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner
    • Benn C.L., et al. Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J. Neurosci. 28 (2008) 10720-10733
    • (2008) J. Neurosci. , vol.28 , pp. 10720-10733
    • Benn, C.L.1
  • 63
    • 35348880250 scopus 로고    scopus 로고
    • Drug targeting of dysregulated transcription in Huntington's disease
    • Kazantsev A.G., and Hersch S.M. Drug targeting of dysregulated transcription in Huntington's disease. Prog. Neurobiol. 83 (2007) 249-259
    • (2007) Prog. Neurobiol. , vol.83 , pp. 249-259
    • Kazantsev, A.G.1    Hersch, S.M.2
  • 64
    • 27744443276 scopus 로고    scopus 로고
    • Progressive and selective striatal degeneration in primary neuronal cultures using lentiviral vector coding for a mutant huntingtin fragment
    • Zala D., et al. Progressive and selective striatal degeneration in primary neuronal cultures using lentiviral vector coding for a mutant huntingtin fragment. Neurobiol. Dis. 20 (2005) 785-798
    • (2005) Neurobiol. Dis. , vol.20 , pp. 785-798
    • Zala, D.1
  • 65
    • 1242353099 scopus 로고    scopus 로고
    • A screen for drugs that protect against the cytotoxicity of polyglutamine-expanded androgen receptor
    • Piccioni F., et al. A screen for drugs that protect against the cytotoxicity of polyglutamine-expanded androgen receptor. Hum. Mol. Genet. 13 (2004) 437-446
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 437-446
    • Piccioni, F.1
  • 66
    • 3242723420 scopus 로고    scopus 로고
    • A cell-based screen for drugs to treat Huntington's disease
    • Aiken C.T., et al. A cell-based screen for drugs to treat Huntington's disease. Neurobiol. Dis. 16 (2004) 546-555
    • (2004) Neurobiol. Dis. , vol.16 , pp. 546-555
    • Aiken, C.T.1
  • 67
    • 26944458863 scopus 로고    scopus 로고
    • Compounds blocking mutant huntingtin toxicity identified using a Huntington's disease neuronal cell model
    • Wang W., et al. Compounds blocking mutant huntingtin toxicity identified using a Huntington's disease neuronal cell model. Neurobiol. Dis. 20 (2005) 500-508
    • (2005) Neurobiol. Dis. , vol.20 , pp. 500-508
    • Wang, W.1
  • 68
    • 33846351654 scopus 로고    scopus 로고
    • Selective inhibitors of death in mutant huntingtin cells
    • Varma H., et al. Selective inhibitors of death in mutant huntingtin cells. Nat. Chem. Biol. 3 (2007) 99-100
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 99-100
    • Varma, H.1
  • 69
    • 0034657112 scopus 로고    scopus 로고
    • Wild-type huntingtin protects from apoptosis upstream of caspase-3
    • Rigamonti D., et al. Wild-type huntingtin protects from apoptosis upstream of caspase-3. J. Neurosci. 20 (2000) 3705-3713
    • (2000) J. Neurosci. , vol.20 , pp. 3705-3713
    • Rigamonti, D.1
  • 70
    • 45549084270 scopus 로고    scopus 로고
    • Neuronal transfection using particle-mediated gene transfer
    • Chapter 3, Unit 3.15
    • Lo D.C. Neuronal transfection using particle-mediated gene transfer. Curr. Protoc. Neurosci. (2001) Chapter 3, Unit 3.15
    • (2001) Curr. Protoc. Neurosci.
    • Lo, D.C.1
  • 71
    • 33745888419 scopus 로고    scopus 로고
    • Cardiac glycosides provide neuroprotection against ischemic stroke: discovery by a brain slice-based compound screening platform
    • Wang J.K., et al. Cardiac glycosides provide neuroprotection against ischemic stroke: discovery by a brain slice-based compound screening platform. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 10461-10466
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10461-10466
    • Wang, J.K.1
  • 72
    • 0033524413 scopus 로고    scopus 로고
    • Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron
    • Faber P.W., et al. Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 179-184
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 179-184
    • Faber, P.W.1
  • 73
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson G.R., et al. Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 21 (1998) 633-642
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.R.1
  • 74
    • 0141891216 scopus 로고    scopus 로고
    • Fly models of Huntington's disease
    • 12 Spec No
    • Marsh J.L., et al. Fly models of Huntington's disease. Hum. Mol. Genet. 2 (2003) R187-R193 12 Spec No
    • (2003) Hum. Mol. Genet. , vol.2
    • Marsh, J.L.1
  • 75
    • 27144558034 scopus 로고    scopus 로고
    • CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo
    • Miller V.M., et al. CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo. J. Neurosci. 25 (2005) 9152-9161
    • (2005) J. Neurosci. , vol.25 , pp. 9152-9161
    • Miller, V.M.1
  • 76
    • 35548950179 scopus 로고    scopus 로고
    • Identification of potential therapeutic drugs for huntington's disease using Caenorhabditis elegans
    • Voisine C., et al. Identification of potential therapeutic drugs for huntington's disease using Caenorhabditis elegans. PLOS ONE 2 (2007) e504
    • (2007) PLOS ONE , vol.2
    • Voisine, C.1
  • 77
    • 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
  • 78
    • 12444292683 scopus 로고    scopus 로고
    • Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila
    • Nagai Y., et al. Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila. Hum. Mol. Genet. 12 (2003) 1253-1259
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1253-1259
    • Nagai, Y.1
  • 79
    • 49549101116 scopus 로고    scopus 로고
    • Zebrafish as a new animal model for movement disorders
    • Flinn L., et al. Zebrafish as a new animal model for movement disorders. J. Neurochem. 106 (2008) 1991-1997
    • (2008) J. Neurochem. , vol.106 , pp. 1991-1997
    • Flinn, L.1
  • 80
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • Williams A., et al. Novel targets for Huntington's disease in an mTOR-independent autophagy pathway. Nat. Chem. Biol. 4 (2008) 295-305
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 295-305
    • Williams, A.1
  • 81
    • 0017167057 scopus 로고
    • Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea
    • Coyle J.T., and Schwarcz R. Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea. Nature 263 (1976) 244-246
    • (1976) Nature , vol.263 , pp. 244-246
    • Coyle, J.T.1    Schwarcz, R.2
  • 82
    • 0027730251 scopus 로고
    • Intrastriatal injections of quinolinic acid or kainic acid: differential patterns of cell survival and the effects of data analysis on outcome
    • Roberts R.C., et al. Intrastriatal injections of quinolinic acid or kainic acid: differential patterns of cell survival and the effects of data analysis on outcome. Exp. Neurol. 124 (1993) 274-282
    • (1993) Exp. Neurol. , vol.124 , pp. 274-282
    • Roberts, R.C.1
  • 83
    • 0027433553 scopus 로고
    • Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid
    • Beal M.F., et al. Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid. J. Neurosci. 13 (1993) 4181-4192
    • (1993) J. Neurosci. , vol.13 , pp. 4181-4192
    • Beal, M.F.1
  • 84
    • 29144468251 scopus 로고    scopus 로고
    • 3-Nitropropionic acid: a mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease
    • Brouillet E., et al. 3-Nitropropionic acid: a mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease. J. Neurochem. 95 (2005) 1521-1540
    • (2005) J. Neurochem. , vol.95 , pp. 1521-1540
    • Brouillet, E.1
  • 85
    • 2342598416 scopus 로고    scopus 로고
    • Experimental therapeutics in transgenic mouse models of Huntington's disease
    • Beal M.F., and Ferrante R.J. Experimental therapeutics in transgenic mouse models of Huntington's disease. Nat. Rev. Neurosci. 5 (2004) 373-384
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 373-384
    • Beal, M.F.1    Ferrante, R.J.2
  • 86
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini L., et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87 (1996) 493-506
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1
  • 87
    • 0034643362 scopus 로고    scopus 로고
    • Delaying the onset of Huntington's in mice
    • Van Dellen A., et al. Delaying the onset of Huntington's in mice. Nature 404 (2000) 721-722
    • (2000) Nature , vol.404 , pp. 721-722
    • Van Dellen, A.1
  • 88
    • 33947286031 scopus 로고    scopus 로고
    • Phenotypic abnormalities in the YAC128 mouse model of Huntington disease are penetrant on multiple genetic backgrounds and modulated by strain
    • Van Raamsdonk J.M., et al. Phenotypic abnormalities in the YAC128 mouse model of Huntington disease are penetrant on multiple genetic backgrounds and modulated by strain. Neurobiol. Dis. 26 (2007) 189-200
    • (2007) Neurobiol. Dis. , vol.26 , pp. 189-200
    • Van Raamsdonk, J.M.1
  • 89
    • 11144358364 scopus 로고    scopus 로고
    • Environmental, pharmacological, and genetic modulation of the HD phenotype in transgenic mice
    • Schilling G., et al. Environmental, pharmacological, and genetic modulation of the HD phenotype in transgenic mice. Exp. Neurol. 187 (2004) 137-149
    • (2004) Exp. Neurol. , vol.187 , pp. 137-149
    • Schilling, G.1
  • 90
    • 33745593763 scopus 로고    scopus 로고
    • Genetic background modifies nuclear mutant huntingtin accumulation and HD CAG repeat instability in Huntington's disease knock-in mice
    • Lloret A., et al. Genetic background modifies nuclear mutant huntingtin accumulation and HD CAG repeat instability in Huntington's disease knock-in mice. Hum. Mol. Genet. 15 (2006) 2015-2024
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2015-2024
    • Lloret, A.1
  • 91
    • 0036152343 scopus 로고    scopus 로고
    • Environmental enrichment slows disease progression in R6/2 Huntington's disease mice
    • Hockly E., et al. Environmental enrichment slows disease progression in R6/2 Huntington's disease mice. Ann. Neurol. 51 (2002) 235-242
    • (2002) Ann. Neurol. , vol.51 , pp. 235-242
    • Hockly, E.1
  • 92
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling G., et al. Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8 (1999) 397-407
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1
  • 93
    • 0037444426 scopus 로고    scopus 로고
    • Transgenic rat model of Huntington's disease
    • von Horsten S., et al. Transgenic rat model of Huntington's disease. Hum. Mol. Genet. 12 (2003) 617-624
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 617-624
    • von Horsten, S.1
  • 94
    • 0033136692 scopus 로고    scopus 로고
    • A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration
    • Hodgson J.G., et al. A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 23 (1999) 181-192
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1
  • 95
    • 46749157501 scopus 로고    scopus 로고
    • Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice
    • Gray M., et al. Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice. J. Neurosci. 28 (2008) 6182-6195
    • (2008) J. Neurosci. , vol.28 , pp. 6182-6195
    • Gray, M.1
  • 96
    • 0037107191 scopus 로고    scopus 로고
    • Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice
    • Menalled L.B., et al. Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice. J. Neurosci. 22 (2002) 8266-8276
    • (2002) J. Neurosci. , vol.22 , pp. 8266-8276
    • Menalled, L.B.1
  • 97
    • 0034163497 scopus 로고    scopus 로고
    • Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice
    • Wheeler V.C., et al. Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice. Hum. Mol. Genet. 9 (2000) 503-513
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 503-513
    • Wheeler, V.C.1
  • 98
    • 0035862896 scopus 로고    scopus 로고
    • Neurological abnormalities in a knock-in mouse model of Huntington's disease
    • Lin C.H., et al. Neurological abnormalities in a knock-in mouse model of Huntington's disease. Hum. Mol. Genet. 10 (2001) 137-144
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 137-144
    • Lin, C.H.1
  • 99
    • 45149105779 scopus 로고    scopus 로고
    • Towards a transgenic model of Huntington's disease in a non-human primate
    • Yang S.H., et al. Towards a transgenic model of Huntington's disease in a non-human primate. Nature 453 (2008) 921-924
    • (2008) Nature , vol.453 , pp. 921-924
    • Yang, S.H.1
  • 100
    • 35748983210 scopus 로고    scopus 로고
    • Target deconvolution strategies in drug discovery
    • Terstappen G.C., et al. Target deconvolution strategies in drug discovery. Nat. Rev. Drug Discov. 6 (2007) 891-903
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 891-903
    • Terstappen, G.C.1
  • 101
    • 41649115887 scopus 로고    scopus 로고
    • Discovery of novel targets with high throughput RNA interference screening
    • Kassner P.D. Discovery of novel targets with high throughput RNA interference screening. Comb. Chem. High Throughput Screen. 11 (2008) 175-184
    • (2008) Comb. Chem. High Throughput Screen. , vol.11 , pp. 175-184
    • Kassner, P.D.1


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