메뉴 건너뛰기




Volumn 6, Issue 10, 2005, Pages 756-765

Therapeutics development for triplet repeat expansion diseases

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO 2 OXABICYCLO[3.1.0]HEXANE 4,6 DICARBOXYLIC ACID; 5 AZA 2' DEOXYCYTIDINE; ALPHA TOCOPHEROL; ANTIOXIDANT; ARYLBUTYRIC ACID DERIVATIVE; BACLOFEN; BUTYRIC ACID; CARBAMAZEPINE; CISPLATIN; CREATINE; DEPSIPEPTIDE; DNA; HEMIN; HISTONE DEACETYLASE INHIBITOR; IDEBENONE; IMIPRAMINE; IRON CHELATING AGENT; MEMANTINE; METABOTROPIC RECEPTOR ANTAGONIST; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; NIFEDIPINE; PHENYLACETIC ACID; PHENYTOIN; PRASTERONE SULFATE; PYRIDOXAL ISONICOTINOYLHYDRAZONE; SELENIUM; SUBEROYL ANILIDE HYDROXAMIC ACID; TESTOSTERONE; TOCAINIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID;

EID: 25844506224     PISSN: 14710056     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrg1690     Document Type: Review
Times cited : (129)

References (134)
  • 1
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada, A. R., Wilson, E. M., Lubahn, D. B., Harding, A. E. & Fischbeck, K. H. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 352, 77-79 (1991).
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 2
    • 0034640011 scopus 로고    scopus 로고
    • Fourteen and counting: Unraveling trinucleotide repeat diseases
    • Cummings, C. J. & Zoghbi, H. Y. Fourteen and counting: unraveling trinucleotide repeat diseases. Hum. Mol. Genet. 9, 909-916 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 909-916
    • Cummings, C.J.1    Zoghbi, H.Y.2
  • 3
    • 9844222853 scopus 로고    scopus 로고
    • Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes
    • Campuzano, V. et al. Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. Hum. Mol. Genet. 6, 1771-1780 (1997).
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1771-1780
    • Campuzano, V.1
  • 4
    • 12244303650 scopus 로고    scopus 로고
    • Frataxin and frataxin deficiency in Friedreich's ataxia
    • Wilson, R. B. Frataxin and frataxin deficiency in Friedreich's ataxia. J. Neurol. Sci. 207, 103-105 (2003).
    • (2003) J. Neurol. Sci. , vol.207 , pp. 103-105
    • Wilson, R.B.1
  • 5
    • 0035470388 scopus 로고    scopus 로고
    • Molecular basis of Friedreich ataxia
    • Pandolfo, M. Molecular basis of Friedreich ataxia. Mov. Disord. 16, 815-821 (2001).
    • (2001) Mov. Disord. , vol.16 , pp. 815-821
    • Pandolfo, M.1
  • 6
    • 0028486222 scopus 로고
    • Idebenone. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic use in age-related cognitive disorders
    • Gillis, J. C., Benefield, P. & McTavish, D. Idebenone. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic use in age-related cognitive disorders. Drugs Aging 5, 133-152 (1994).
    • (1994) Drugs Aging , vol.5 , pp. 133-152
    • Gillis, J.C.1    Benefield, P.2    McTavish, D.3
  • 7
    • 0036252812 scopus 로고    scopus 로고
    • Molecular insights into Friedreich's ataxia and antioxidant-based therapies
    • Rotig, A., Sidi, D., Munnich, A. & Rustin, P. Molecular insights into Friedreich's ataxia and antioxidant-based therapies. Trends Mol. Med. 8, 221-224 (2002). This is a review of the consequences of frataxin loss and the rationale behind antioxidant therapy.
    • (2002) Trends Mol. Med. , vol.8 , pp. 221-224
    • Rotig, A.1    Sidi, D.2    Munnich, A.3    Rustin, P.4
  • 8
    • 0036694802 scopus 로고    scopus 로고
    • Friedreich's ataxia: Idebenone treatment in early stage patients
    • Artuch, R. et al. Friedreich's ataxia: idebenone treatment in early stage patients. Neuropediatrics 33, 190-193 (2002).
    • (2002) Neuropediatrics , vol.33 , pp. 190-193
    • Artuch, R.1
  • 9
    • 0031593616 scopus 로고    scopus 로고
    • Sustained efficacy and safety of idebenone in the treatment of Alzheimer's disease: Update on a 2-year double-blind multicentre study
    • Gutzmann, H. & Hadler, D. Sustained efficacy and safety of idebenone in the treatment of Alzheimer's disease: update on a 2-year double-blind multicentre study. J. Neural Transm. Suppl. 54, 301-310 (1998).
    • (1998) J. Neural Transm. Suppl. , vol.54 , pp. 301-310
    • Gutzmann, H.1    Hadler, D.2
  • 10
    • 0035895888 scopus 로고    scopus 로고
    • Selective targeting of a redox-active ubiquinone to mitochondria within cells: Antioxidant and antiapoptotic properties
    • Kelso, G. F. et al. Selective targeting of a redox-active ubiquinone to mitochondria within cells: antioxidant and antiapoptotic properties. J. Biol. Chem. 276, 4588-4596 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4588-4596
    • Kelso, G.F.1
  • 11
    • 0348136710 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect Friedreich ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants
    • Jauslin, M. L., Meier, T., Smith, R. A. & Murphy, M. P. Mitochondria-targeted antioxidants protect Friedreich ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants. FASEB J. 17, 1972-1974 (2003).
    • (2003) FASEB J. , vol.17 , pp. 1972-1974
    • Jauslin, M.L.1    Meier, T.2    Smith, R.A.3    Murphy, M.P.4
  • 12
    • 0030008268 scopus 로고    scopus 로고
    • Fenton chemistry: An introduction
    • Wardman, P. & Candeias, L. P. Fenton chemistry: an introduction. Radiat. Res. 145, 523-531 (1996).
    • (1996) Radiat. Res. , vol.145 , pp. 523-531
    • Wardman, P.1    Candeias, L.P.2
  • 13
    • 0018798539 scopus 로고
    • A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents
    • Ponka, P., Borova, J., Neuwirt, J., Fuchs, O. & Necas, E. A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents. Biochim. Biophys. Acta 586, 278-297 (1979).
    • (1979) Biochim. Biophys. Acta , vol.586 , pp. 278-297
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4    Necas, E.5
  • 14
    • 0035978474 scopus 로고    scopus 로고
    • Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron
    • Richardson, D. R., Mouralian, C., Ponka, P. & Becker, E. Development of potential iron chelators for the treatment of Friedreich's ataxia: ligands that mobilize mitochondrial iron. Biochim. Biophys. Acta 1536, 133-140 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 133-140
    • Richardson, D.R.1    Mouralian, C.2    Ponka, P.3    Becker, E.4
  • 15
    • 0038448961 scopus 로고    scopus 로고
    • Upregulation of expression from the FRDA genomic locus for the therapy of Friedreich ataxia
    • Sarsero, J. P. et al. Upregulation of expression from the FRDA genomic locus for the therapy of Friedreich ataxia. J. Gene Med. 5, 72-81 (2003).
    • (2003) J. Gene Med. , vol.5 , pp. 72-81
    • Sarsero, J.P.1
  • 16
    • 0042318834 scopus 로고    scopus 로고
    • Cisplatin may induce frataxin expression
    • Ghazizadeh, M. Cisplatin may induce frataxin expression. J. Nippon Med. Sch. 70, 367-371 (2003).
    • (2003) J. Nippon Med. Sch. , vol.70 , pp. 367-371
    • Ghazizadeh, M.1
  • 17
    • 0025833298 scopus 로고
    • Absence of expression of the FMR-1 gene in fragile X syndrome
    • Pieretti, M. et al. Absence of expression of the FMR-1 gene in fragile X syndrome. Cell 66, 817-822 (1991).
    • (1991) Cell , vol.66 , pp. 817-822
    • Pieretti, M.1
  • 19
    • 0037805263 scopus 로고    scopus 로고
    • Modulation of methylation in the FMR1 promoter region after long term treatment with L-carnitine and acetyl-L-carnitine
    • Pascale, E. et al. Modulation of methylation in the FMR1 promoter region after long term treatment with L-carnitine and acetyl-L-carnitine. J. Med. Genet. 40, e76 (2003).
    • (2003) J. Med. Genet. , vol.40
    • Pascale, E.1
  • 20
    • 0032905253 scopus 로고    scopus 로고
    • Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells
    • Coffee, B., Zhang, F., Warren, S. T. & Reines, D. Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells. Nature Genet. 22, 98-101 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 98-101
    • Coffee, B.1    Zhang, F.2    Warren, S.T.3    Reines, D.4
  • 21
    • 0032741429 scopus 로고    scopus 로고
    • Synergistic effect of histone hyperacetylation and DNA demethylation in the reactivation of the FMR1 gene
    • Chiurazzi, P. et al. Synergistic effect of histone hyperacetylation and DNA demethylation in the reactivation of the FMR1 gene. Hum. Mol. Genet. 8, 2317-2323 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2317-2323
    • Chiurazzi, P.1
  • 22
    • 0035879180 scopus 로고    scopus 로고
    • Abnormal development of dendritic spines in FMR1 knock-out mice
    • Nimchinsky, E. A., Oberlander, A. M. & Svoboda, K. Abnormal development of dendritic spines in FMR1 knock-out mice. J. Neurosci. 21, 5139-5146 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 5139-5146
    • Nimchinsky, E.A.1    Oberlander, A.M.2    Svoboda, K.3
  • 23
    • 0037158482 scopus 로고    scopus 로고
    • Dendritic spine and dendritic field characteristics of layer V pyramidal neurons in the visual cortex of fragile-X knockout mice
    • Irwin, S. A. et al. Dendritic spine and dendritic field characteristics of layer V pyramidal neurons in the visual cortex of fragile-X knockout mice. Am. J. Med. Genet. 111, 140-146 (2002).
    • (2002) Am. J. Med. Genet. , vol.111 , pp. 140-146
    • Irwin, S.A.1
  • 24
    • 0037188502 scopus 로고    scopus 로고
    • Altered synaptic plasticity in a mouse model of fragile X mental retardation
    • Huber, K. M., Gallagher, S. M., Warren, S. T. & Bear, M. F. Altered synaptic plasticity in a mouse model of fragile X mental retardation. Proc. Natl Acad. Sci. USA 99, 7746-7750 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7746-7750
    • Huber, K.M.1    Gallagher, S.M.2    Warren, S.T.3    Bear, M.F.4
  • 25
    • 3042647610 scopus 로고    scopus 로고
    • The mGluR theory of fragile X mental retardation
    • Bear, M. F., Huber, K. M. & Warren, S. T. The mGluR theory of fragile X mental retardation. Trends Neurosci. 27, 370-377 (2004). The theory of excessive metabotropic receptor function in fragile X syndrome.
    • (2004) Trends Neurosci. , vol.27 , pp. 370-377
    • Bear, M.F.1    Huber, K.M.2    Warren, S.T.3
  • 26
    • 20044388322 scopus 로고    scopus 로고
    • Pharmacological rescue of synaptic plasticity, courtship behavior, and mushroom body defects in a Drosophila model of fragile X syndrome
    • McBride, S. M. et al. Pharmacological rescue of synaptic plasticity, courtship behavior, and mushroom body defects in a Drosophila model of fragile X syndrome. Neuron 45, 753-764 (2005).
    • (2005) Neuron , vol.45 , pp. 753-764
    • McBride, S.M.1
  • 27
    • 2942704134 scopus 로고    scopus 로고
    • Treatment in myotonia and periodic paralysis
    • Meola, G. & Sansone, V. Treatment in myotonia and periodic paralysis. Rev. Neurol. 160, S55-S69 (2004).
    • (2004) Rev. Neurol. , vol.160
    • Meola, G.1    Sansone, V.2
  • 28
    • 0026598119 scopus 로고
    • An unstable triplet repeat in a gene related to myotonic muscular dystrophy
    • Fu, Y. H. et al. An unstable triplet repeat in a gene related to myotonic muscular dystrophy. Science 255, 1256-1258 (1992).
    • (1992) Science , vol.255 , pp. 1256-1258
    • Fu, Y.H.1
  • 29
    • 0035896610 scopus 로고    scopus 로고
    • RNA CUG repeats sequester CUGBP1 and alter protein levels and activity of CUGBP1
    • Timchenko, N. A. et al. RNA CUG repeats sequester CUGBP1 and alter protein levels and activity of CUGBP1. J. Biol. Chem. 276, 7820-7826 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 7820-7826
    • Timchenko, N.A.1
  • 30
    • 0031940035 scopus 로고    scopus 로고
    • Ribozyme-mediated trans-splicing of a trinucleotide repeat
    • Phylactou, L. A., Darrah, C. & Wood, M. J. Ribozyme-mediated trans-splicing of a trinucleotide repeat. Nature Genet. 18, 378-381 (1998).
    • (1998) Nature Genet. , vol.18 , pp. 378-381
    • Phylactou, L.A.1    Darrah, C.2    Wood, M.J.3
  • 31
    • 19944428473 scopus 로고    scopus 로고
    • Some flavonoids and DHEA-S prevent the cis-effect of expanded CTG repeats in a stable PC12 cell transformant
    • Furuya, H. et al. Some flavonoids and DHEA-S prevent the cis-effect of expanded CTG repeats in a stable PC12 cell transformant. Biochem. Pharmacol. 69, 503-516 (2005).
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 503-516
    • Furuya, H.1
  • 33
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz, K. T. et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425, 191-196 (2003).
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1
  • 34
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • Parker, J. A. et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nature Genet. 37, 349-350 (2005). This paper describes HDAC (sirtuin family) activation as a means of suppressing polyglutamine toxicity.
    • (2005) Nature Genet. , vol.37 , pp. 349-350
    • Parker, J.A.1
  • 35
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • Reddy, P. H. et al. Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA. Nature Genet. 20, 198-202 (1998).
    • (1998) Nature Genet. , vol.20 , pp. 198-202
    • Reddy, P.H.1
  • 36
    • 0032907359 scopus 로고    scopus 로고
    • Transgenic mice harboring a full-length human mutant DRPLA gene exhibit age-dependent intergenerational and somatic instabilities of CAG repeats comparable with those in DRPLA patients
    • Sato, T. et al. Transgenic mice harboring a full-length human mutant DRPLA gene exhibit age-dependent intergenerational and somatic instabilities of CAG repeats comparable with those in DRPLA patients. Hum. Mol. Genet. 8, 99-106 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 99-106
    • Sato, T.1
  • 37
    • 18644379256 scopus 로고    scopus 로고
    • Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno, M. et al. Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron 35, 843-854 (2002). The authors describe the ligand-dependent toxicity of the mutant androgen receptor in Kennedy disease. This emphasizes the need to understand each polyglutamine disorder in the context of the disease protein's normal function.
    • (2002) Neuron , vol.35 , pp. 843-854
    • Katsuno, M.1
  • 38
    • 0742304252 scopus 로고    scopus 로고
    • Wild-type huntingtin plays a role in brain development and neuronal survival
    • Reiner, A., Dragatsis, I., Zeitlin, S. & Goldowitz, D. Wild-type huntingtin plays a role in brain development and neuronal survival. Mol. Neurobiol. 28, 259-276 (2003).
    • (2003) Mol. Neurobiol. , vol.28 , pp. 259-276
    • Reiner, A.1    Dragatsis, I.2    Zeitlin, S.3    Goldowitz, D.4
  • 39
    • 0037292586 scopus 로고    scopus 로고
    • Dysfunction of wild-type huntingtin in Huntington disease
    • Cattaneo, E. Dysfunction of wild-type huntingtin in Huntington disease. News Physiol. Sci. 18, 34-37 (2003).
    • (2003) News Physiol. Sci. , vol.18 , pp. 34-37
    • Cattaneo, E.1
  • 40
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C. J. et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nature Genet. 19, 148-154 (1998).
    • (1998) Nature Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1
  • 41
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai, Y., Koppenhafer, S. L., Shoesmith, S. J., Perez, M. K. & Paulson, H. L. Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8, 673-682 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 673-682
    • Chai, Y.1    Koppenhafer, S.L.2    Shoesmith, S.J.3    Perez, M.K.4    Paulson, H.L.5
  • 42
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani, P. & Benzer, S. Genetic suppression of polyglutamine toxicity in Drosophila. Science 287, 1837-1840 (2000).
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 43
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach, A. et al. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl Acad. Sci. USA 97, 2898-2903 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1
  • 44
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler, A. et al. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10, 1307-1315 (2001).
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1
  • 45
    • 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. USA 99, 16400-16406 (2002). This paper describes the application of high-throughput screening for polyglutamine disorders and shows that inhibitors of aggregation are therapeutic targets.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16400-16406
    • Heiser, V.1
  • 46
    • 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, 1017-1026 (2001).
    • (2001) Neurobiol. Dis. , vol.8 , pp. 1017-1026
    • Smith, D.L.1
  • 47
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neu rodegenerative disorders
    • Sanchez, I., Mahlke, C. & Yuan, J. Pivotal role of oligomerization in expanded polyglutamine neu rodegenerative disorders. Nature 421, 373-379 (2003).
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 48
    • 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. Nature Med. 10, 148-154 (2004). The authors discuss an approach to inhibiting protein aggregation using a saccharide-polyglutamine interaction. The safety profile of this chemical seems exceptionally favourable.
    • (2004) Nature Med. , vol.10 , pp. 148-154
    • Tanaka, M.1
  • 49
    • 0037154165 scopus 로고    scopus 로고
    • Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity
    • Khoshnan, A., Ko, J. & Patterson, P. H. Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity. Proc. Natl Acad. Sci. USA 99, 1002-1007 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1002-1007
    • Khoshnan, A.1    Ko, J.2    Patterson, P.H.3
  • 50
    • 18544379477 scopus 로고    scopus 로고
    • A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila
    • Kazantsev, A. et al. A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila. Nature Genet. 30, 367-376 (2002).
    • (2002) Nature Genet. , vol.30 , pp. 367-376
    • Kazantsev, A.1
  • 51
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • Kahlem, P., Terre, C., Green, H. & Djian, P. Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system. Proc. Natl Acad. Sci. USA 93, 14580-14585 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14580-14585
    • Kahlem, P.1    Terre, C.2    Green, H.3    Djian, P.4
  • 52
    • 0033594894 scopus 로고    scopus 로고
    • Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei
    • Karpuj, M. V. et al. Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei. Proc. Natl Acad. Sci. USA 96, 7388-7393 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7388-7393
    • Karpuj, M.V.1
  • 53
    • 0037109665 scopus 로고    scopus 로고
    • Therapeutic effects of cystamine in a murine model of Huntington's disease
    • Dedeoglu, A. et al. Therapeutic effects of cystamine in a murine model of Huntington's disease. J. Neurosci. 22, 8942-8950 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 8942-8950
    • Dedeoglu, A.1
  • 54
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj, M. V. et al. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nature Med. 8, 143-149 (2002). This article provides an example of effective treatment after the development of disease manifestations. It also describes activity of the drug outside its pharmacological target.
    • (2002) Nature Med. , vol.8 , pp. 143-149
    • Karpuj, M.V.1
  • 55
    • 0037423204 scopus 로고    scopus 로고
    • Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders
    • Lesort, M., Lee, M., Tucholski, J. & Johnson, G. V. Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders. J. Biol. Chem. 278, 3825-3830 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 3825-3830
    • Lesort, M.1    Lee, M.2    Tucholski, J.3    Johnson, G.V.4
  • 56
    • 13244279859 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate-independent mechanisms
    • Bailey, C. D. & Johnson, G. V. Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate-independent mechanisms. J. Neurochem. 92, 83-92 (2005).
    • (2005) J. Neurochem. , vol.92 , pp. 83-92
    • Bailey, C.D.1    Johnson, G.V.2
  • 57
    • 0033953015 scopus 로고    scopus 로고
    • Caspases and neurodegeneration: On the cutting edge of new therapeutic approaches
    • Wellington, C. L. & Hayden, M. R. Caspases and neurodegeneration: on the cutting edge of new therapeutic approaches. Clin. Genet. 57, 1-10 (2000).
    • (2000) Clin. Genet. , vol.57 , pp. 1-10
    • Wellington, C.L.1    Hayden, M.R.2
  • 58
    • 9344227302 scopus 로고    scopus 로고
    • Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
    • Goldberg, Y. P. et al. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nature Genet. 13, 442-449 (1996).
    • (1996) Nature Genet. , vol.13 , pp. 442-449
    • Goldberg, Y.P.1
  • 59
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington, C. L. et al. Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J. Biol. Chem. 273, 9158-9167 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 9158-9167
    • Wellington, C.L.1
  • 60
    • 0034733607 scopus 로고    scopus 로고
    • Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells
    • Wellington, C. L. et al. Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells. J. Biol. Chem. 275, 19831-19838 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 19831-19838
    • Wellington, C.L.1
  • 61
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • Ona, V. O. et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature 399, 263-267 (1999).
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1
  • 62
    • 0033912716 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease
    • Chen, M. et al. Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease. Nature Med. 6, 797-801 (2000). The authors describe the amelioration of disease manifestations in an HD model with a drug that inhibits caspase.
    • (2000) Nature Med. , vol.6 , pp. 797-801
    • Chen, M.1
  • 63
    • 0041335559 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-independent and -dependent mitochondrial cell death pathways in models of Huntington's disease
    • Wang, X. et al. Minocycline inhibits caspase-independent and -dependent mitochondrial cell death pathways in models of Huntington's disease. Proc. Natl Acad. Sci. USA 100, 10483-10487 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10483-10487
    • Wang, X.1
  • 65
    • 0036677435 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease
    • Keene, C. D. et al. Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc. Natl Acad. Sci. USA 99, 10671-10676 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 10671-10676
    • Keene, C.D.1
  • 66
    • 0017167057 scopus 로고
    • Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea
    • Coyle, J. T. & Schwarcz, R. Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea. Nature 263, 244-246 (1976).
    • (1976) Nature , vol.263 , pp. 244-246
    • Coyle, J.T.1    Schwarcz, R.2
  • 67
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal, M. F. et al. Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 321, 168-171 (1986).
    • (1986) Nature , vol.321 , pp. 168-171
    • Beal, M.F.1
  • 68
    • 0035889535 scopus 로고    scopus 로고
    • NMDA receptor function in mouse models of Huntington disease
    • Cepeda, C. et al. NMDA receptor function in mouse models of Huntington disease. J. Neurosci. Res. 66, 525-539 (2001).
    • (2001) J. Neurosci. Res. , vol.66 , pp. 525-539
    • Cepeda, C.1
  • 69
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron, M. M. et al. Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 33, 849-860 (2002).
    • (2002) Neuron , vol.33 , pp. 849-860
    • Zeron, M.M.1
  • 70
    • 0035180327 scopus 로고    scopus 로고
    • Altered striatal amino acid neurotransmitter release monitored using microdialysis in R6/1 Huntington transgenic mice
    • Nicniocaill, B., Haraldsson, B., Hansson, O., O'Connor, W. T. & Brundin, P. Altered striatal amino acid neurotransmitter release monitored using microdialysis in R6/1 Huntington transgenic mice. Eur. J. Neurosci. 13, 206-210 (2001).
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 206-210
    • Nicniocaill, B.1    Haraldsson, B.2    Hansson, O.3    O'Connor, W.T.4    Brundin, P.5
  • 71
    • 0142184100 scopus 로고    scopus 로고
    • Huntington's disease: A synaptopathy?
    • Li, J. Y., Plomann, M. & Brundin, P. Huntington's disease: a synaptopathy? Trends Mol. Med. 9, 414-420 (2003).
    • (2003) Trends Mol. Med. , vol.9 , pp. 414-420
    • Li, J.Y.1    Plomann, M.2    Brundin, P.3
  • 72
    • 0033614761 scopus 로고    scopus 로고
    • Altered neurotransmitter receptor expression in transgenic mouse models of Huntington's disease
    • Cha, J. H. et al. Altered neurotransmitter receptor expression in transgenic mouse models of Huntington's disease. Phil. Trans. R. Soc. Lond. B 354, 981-989 (1999).
    • (1999) Phil. Trans. R. Soc. Lond. B , vol.354 , pp. 981-989
    • Cha, J.H.1
  • 73
    • 0038375825 scopus 로고    scopus 로고
    • A randomized trial of amantadine in Huntington disease
    • O'Suilleabhain, P. & Dewey, R. B. Jr. A randomized trial of amantadine in Huntington disease. Arch. Neurol. 60, 996-998 (2003).
    • (2003) Arch. Neurol. , vol.60 , pp. 996-998
    • O'Suilleabhain, P.1    Dewey Jr., R.B.2
  • 74
    • 0036757043 scopus 로고    scopus 로고
    • Amantadine in Huntington's disease: Open-label video-blinded study
    • Lucetti, C. et al. Amantadine in Huntington's disease: open-label video-blinded study. Neurol. Sci. 23, S83-S84 (2002).
    • (2002) Neurol. Sci. , vol.23
    • Lucetti, C.1
  • 75
    • 0037056392 scopus 로고    scopus 로고
    • Huntington's disease: A randomized, controlled trial using the NMDA-antagonist amantadine
    • Verhagen Metman, L. et al. Huntington's disease: a randomized, controlled trial using the NMDA-antagonist amantadine. Neurology 59, 694-699 (2002).
    • (2002) Neurology , vol.59 , pp. 694-699
    • Verhagen Metman, L.1
  • 76
    • 0030753956 scopus 로고    scopus 로고
    • Cognitive, behavioral, and motor effects of the NMDA antagonist ketamine in Huntington's disease
    • Murman, D. L. et al. Cognitive, behavioral, and motor effects of the NMDA antagonist ketamine in Huntington's disease. Neurology 49, 153-161 (1997).
    • (1997) Neurology , vol.49 , pp. 153-161
    • Murman, D.L.1
  • 77
    • 0024556360 scopus 로고
    • A controlled clinical trial of baclofen as protective therapy in early Huntington's disease
    • Shoulson, I. et al. A controlled clinical trial of baclofen as protective therapy in early Huntington's disease. Ann. Neurol. 25, 252-259 (1989).
    • (1989) Ann. Neurol. , vol.25 , pp. 252-259
    • Shoulson, I.1
  • 78
    • 0033595502 scopus 로고    scopus 로고
    • Influence of lamotrigine on progression of early Huntington disease: A randomized clinical trial
    • Kremer, B. et al. Influence of lamotrigine on progression of early Huntington disease: a randomized clinical trial. Neurology 53, 1000-1011 (1999).
    • (1999) Neurology , vol.53 , pp. 1000-1011
    • Kremer, B.1
  • 79
    • 0034796483 scopus 로고    scopus 로고
    • Riluzole in Huntington's disease (HD): An open label study with one year follow up
    • Seppi, K. et al. Riluzole in Huntington's disease (HD): an open label study with one year follow up. J. Neurol. 248, 866-869 (2001).
    • (2001) J. Neurol. , vol.248 , pp. 866-869
    • Seppi, K.1
  • 80
    • 0344413576 scopus 로고    scopus 로고
    • Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington disease
    • Li, L. et al. Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington disease. Neurobiol. Aging 24, 1113-1121 (2003).
    • (2003) Neurobiol. Aging , vol.24 , pp. 1113-1121
    • Li, L.1
  • 81
    • 14844314896 scopus 로고    scopus 로고
    • Enhanced striatal NR2B-containing N-methyl-D-aspartate receptor-mediated synaptic currents in a mouse model of Huntington disease
    • Li, L., Murphy, T. H., Hayden, M. R. & Raymond, L. A. Enhanced striatal NR2B-containing N-methyl-D-aspartate receptor-mediated synaptic currents in a mouse model of Huntington disease. J. Neurophysiol. 92, 2738-2746 (2004).
    • (2004) J. Neurophysiol. , vol.92 , pp. 2738-2746
    • Li, L.1    Murphy, T.H.2    Hayden, M.R.3    Raymond, L.A.4
  • 82
    • 15444363304 scopus 로고    scopus 로고
    • NR2A and NR2B receptor gene variations modify age of onset in Huntington's disease
    • Arning, L. et al. NR2A and NR2B receptor gene variations modify age of onset in Huntington's disease. Neurogenetics 6, 25-28 (2005).
    • (2005) Neurogenetics , vol.6 , pp. 25-28
    • Arning, L.1
  • 83
    • 0031034905 scopus 로고    scopus 로고
    • Mechanism of memantine block of NMDA-activated channels in rat retinal ganglion cells: Uncompetitive antagonism
    • Chen, H. S. & Lipton, S. A. Mechanism of memantine block of NMDA-activated channels in rat retinal ganglion cells: uncompetitive antagonism. J. Physiol. 499, 27-46 (1997).
    • (1997) J. Physiol. , vol.499 , pp. 27-46
    • Chen, H.S.1    Lipton, S.A.2
  • 84
    • 4544335687 scopus 로고    scopus 로고
    • The N-methyl-D-aspartate antagonist memantine retards progression of Huntington's disease
    • Beister, A. et al. The N-methyl-D-aspartate antagonist memantine retards progression of Huntington's disease. J. Neural Transm. 68, S117-S122 (2004).
    • (2004) J. Neural Transm. , vol.68
    • Beister, A.1
  • 85
    • 0032836680 scopus 로고    scopus 로고
    • Group-I metabotropic glutamate receptors: Hypotheses to explain their dual role in neurotoxicity and neuroprotection
    • Nicoletti, F. et al. Group-I metabotropic glutamate receptors: hypotheses to explain their dual role in neurotoxicity and neuroprotection. Neuropharmacology 38, 1477-1484 (1999).
    • (1999) Neuropharmacology , vol.38 , pp. 1477-1484
    • Nicoletti, F.1
  • 86
    • 4043164771 scopus 로고    scopus 로고
    • The metabotropic glutamate receptor 5 antagonist MPEP and the mGluR2 agonist LY379268 modify disease progression in a transgenic mouse model of Huntington's disease
    • Schiefer, J. et al. The metabotropic glutamate receptor 5 antagonist MPEP and the mGluR2 agonist LY379268 modify disease progression in a transgenic mouse model of Huntington's disease. Brain Res. 1019, 246-254 (2004).
    • (2004) Brain Res. , vol.1019 , pp. 246-254
    • Schiefer, J.1
  • 87
    • 0036522987 scopus 로고    scopus 로고
    • 2A receptor reduces, through a presynaptic mechanism, quinolinic acid-induced excitotoxicity: Possible relevance to neuroprotective interventions in neurodegenerative diseases of the striatum
    • 2A receptor reduces, through a presynaptic mechanism, quinolinic acid-induced excitotoxicity: possible relevance to neuroprotective interventions in neurodegenerative diseases of the striatum. J. Neurosci. 22, 1967-1975 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 1967-1975
    • Popoli, P.1
  • 88
    • 0038201773 scopus 로고    scopus 로고
    • Effects of cannabinoids in the rat model of Huntington's disease generated by an intrastriatal injection of malonate
    • Lastres-Becker, I. et al. Effects of cannabinoids in the rat model of Huntington's disease generated by an intrastriatal injection of malonate. Neuroreport 14, 813-816 (2003).
    • (2003) Neuroreport , vol.14 , pp. 813-816
    • Lastres-Becker, I.1
  • 89
    • 0028900665 scopus 로고
    • Systemic 3-nitropropionic acid: Behavioral deficits and striatal damage in adult rats
    • Borlongan, C. V. et al. Systemic 3-nitropropionic acid: behavioral deficits and striatal damage in adult rats. Brain Res. Bull. 36, 549-556 (1995).
    • (1995) Brain Res. Bull. , vol.36 , pp. 549-556
    • Borlongan, C.V.1
  • 90
    • 0029875381 scopus 로고    scopus 로고
    • Mitochondrial defect in Huntington's disease caudate nucleus
    • Gu, M. et al. Mitochondrial defect in Huntington's disease caudate nucleus. Ann. Neurol. 39, 385-389 (1996).
    • (1996) Ann. Neurol. , vol.39 , pp. 385-389
    • Gu, M.1
  • 91
    • 0030919567 scopus 로고    scopus 로고
    • Oxidative damage and metabolic dysfunction in Huntington's disease: Selective vulnerability of the basal ganglia
    • Browne, S. E. et al. Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia. Ann. Neurol. 41, 646-653 (1997).
    • (1997) Ann. Neurol. , vol.41 , pp. 646-653
    • Browne, S.E.1
  • 92
    • 2342598416 scopus 로고    scopus 로고
    • Experimental therapeutics in transgenic mouse models of Huntington's disease
    • Beal, M. F. & Ferrante, R. J. Experimental therapeutics in transgenic mouse models of Huntington's disease. Nature Rev. Neurosci. 5, 373-384 (2004). A review of the pathogenesis of HD in the context of mouse models and the efficacy of therapeutic agents tested in these models.
    • (2004) Nature Rev. Neurosci. , vol.5 , pp. 373-384
    • Beal, M.F.1    Ferrante, R.J.2
  • 93
    • 0038115294 scopus 로고    scopus 로고
    • Creatinetherapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice
    • Dedeoglu, A. et al. Creatinetherapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice. J. Neurochem. 85, 1359-1367 (2003).
    • (2003) J. Neurochem. , vol.85 , pp. 1359-1367
    • Dedeoglu, A.1
  • 94
    • 0141959170 scopus 로고    scopus 로고
    • Creatine supplementation in Huntington's disease: A placebo-controlled pilot trial
    • Verbessem, P. et al. Creatine supplementation in Huntington's disease: a placebo-controlled pilot trial. Neurology 61, 925-930 (2003).
    • (2003) Neurology , vol.61 , pp. 925-930
    • Verbessem, P.1
  • 95
    • 85009226418 scopus 로고    scopus 로고
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • Huntington Study Group. A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology 57, 397-404 (2001).
    • (2001) Neurology , vol.57 , pp. 397-404
  • 96
    • 9544255791 scopus 로고    scopus 로고
    • A controlled trial of idebenone in Huntington's disease
    • Ranen, N. G. et al. A controlled trial of idebenone in Huntington's disease. Mov. Disord. 11, 549-554 (1996).
    • (1996) Mov. Disord. , vol.11 , pp. 549-554
    • Ranen, N.G.1
  • 97
    • 0042869974 scopus 로고    scopus 로고
    • Polyglutamine diseases: A transcription disorder?
    • Okazawa, H. Polyglutamine diseases: a transcription disorder? Cell. Mol. Life Sci. 60, 1427-1439 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1427-1439
    • Okazawa, H.1
  • 98
    • 0034285017 scopus 로고    scopus 로고
    • CREB-binding protein sequestration by expanded polyglutamine
    • McCampbell, A. et al. CREB-binding protein sequestration by expanded polyglutamine. Hum. Mol. Genet. 9, 2197-2202 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2197-2202
    • McCampbell, A.1
  • 99
    • 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, 2238-2243 (2002).
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1
  • 100
    • 0038722748 scopus 로고    scopus 로고
    • Aberrant histone acetylation, altered transcription, and retinal degeneration in a Drosophila model of polyglutamine disease are rescued by CREB-binding protein
    • Taylor, J. P. et al. Aberrant histone acetylation, altered transcription, and retinal degeneration in a Drosophila model of polyglutamine disease are rescued by CREB-binding protein. Genes Dev. 17, 1463-1468 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1463-1468
    • Taylor, J.P.1
  • 101
    • 0042528729 scopus 로고    scopus 로고
    • Heterochromatin and epigenetic control of gene expression
    • Grewal, S. I. & Moazed, D. Heterochromatin and epigenetic control of gene expression. Science 301, 798-802 (2003).
    • (2003) Science , vol.301 , pp. 798-802
    • Grewal, S.I.1    Moazed, D.2
  • 102
    • 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, 739-743 (2001). This is a description of reduced acetyltransferase activity and histone acetylation in polyglutamine disease, and how this can be overcome by HDAC inhibitors with consequent amelioration of toxicity.
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1
  • 103
    • 0037961686 scopus 로고    scopus 로고
    • Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation
    • Igarashi, S. et al. Inducible PC12 cell model of Huntington's disease shows toxicity and decreased histone acetylation. Neuroreport 14, 565-568 (2003).
    • (2003) Neuroreport , vol.14 , pp. 565-568
    • Igarashi, S.1
  • 104
    • 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. USA 100, 2041-2046 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2041-2046
    • Hockly, E.1
  • 105
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neu rodegenerative phenotype in Huntington's disease mice
    • Ferrante, R. J. et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neu rodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23, 9418-9427 (2003). This article discusses the beneficial effects of HDAC inhibitors in an HD mouse model.
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 106
    • 3042576479 scopus 로고    scopus 로고
    • Valproic acid: An old drug newly discovered as inhibitor of histone deacetylases
    • Gottlicher, M. Valproic acid: an old drug newly discovered as inhibitor of histone deacetylases. Ann. Hematol. 83 (Suppl. 1), 91-92 (2004).
    • (2004) Ann. Hematol. , vol.83 , Issue.1 SUPPL. , pp. 91-92
    • Gottlicher, M.1
  • 107
    • 0035714841 scopus 로고    scopus 로고
    • Long-term treatment with sodium phenylbutyrate in ornithine transcar bamylase-deficient patients
    • Burlina, A. B., Ogier, H., Korall, H. & Trefz, F. K. Long-term treatment with sodium phenylbutyrate in ornithine transcar bamylase-deficient patients. Mol. Genet. Metab. 72, 351-355 (2001).
    • (2001) Mol. Genet. Metab. , vol.72 , pp. 351-355
    • Burlina, A.B.1    Ogier, H.2    Korall, H.3    Trefz, F.K.4
  • 108
    • 0036906832 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: From target to clinical trials
    • Kelly, W. K., O'Connor, O. A. & Marks, P. A. Histone deacetylase inhibitors: from target to clinical trials. Expert Opin. Investig. Drugs 11, 1695-1713 (2002).
    • (2002) Expert Opin. Investig. Drugs , vol.11 , pp. 1695-1713
    • Kelly, W.K.1    O'Connor, O.A.2    Marks, P.A.3
  • 109
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet, A. et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303, 2011-2015 (2004).
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1
  • 110
    • 0028130227 scopus 로고
    • Implants of polymer-encapsulated human NGF-secreting cells in the nonhuman primate: Rescue and sprouting of degenerating cholinergic basal forebrain neurons
    • Emerich, D. F. et al. Implants of polymer-encapsulated human NGF-secreting cells in the nonhuman primate: rescue and sprouting of degenerating cholinergic basal forebrain neurons. J. Comp. Neurol. 349, 148-164 (1994).
    • (1994) J. Comp. Neurol. , vol.349 , pp. 148-164
    • Emerich, D.F.1
  • 111
    • 0029761786 scopus 로고    scopus 로고
    • Implants of encapsulated human CNTF-producing fibroblasts prevent behavioral deficits and striatal degeneration in a rodent model of Huntington's disease
    • Emerich, D. F. et al. Implants of encapsulated human CNTF-producing fibroblasts prevent behavioral deficits and striatal degeneration in a rodent model of Huntington's disease. J. Neurosci. 16, 5168-5181 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 5168-5181
    • Emerich, D.F.1
  • 112
    • 0033544840 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor-mediated protection of striatal neurons in an excitotoxic rat model of Huntington's disease, as demonstrated by adenoviral gene transfer
    • Bemelmans, A. P. et al. Brain-derived neurotrophic factor-mediated protection of striatal neurons in an excitotoxic rat model of Huntington's disease, as demonstrated by adenoviral gene transfer. Hum. Gene Ther. 10, 2987-2997 (1999).
    • (1999) Hum. Gene Ther. , vol.10 , pp. 2987-2997
    • Bemelmans, A.P.1
  • 113
    • 0033789409 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4/5 prevent the death of striatal projection neurons in a rodent model of Huntington's disease
    • Perez-Navarro, E., Canudas, A. M., Akerund, P., Alberch, J. & Arenas, E. Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4/5 prevent the death of striatal projection neurons in a rodent model of Huntington's disease. J. Neurochem. 75, 2190-2199 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 2190-2199
    • Perez-Navarro, E.1    Canudas, A.M.2    Akerund, P.3    Alberch, J.4    Arenas, E.5
  • 114
    • 0037762555 scopus 로고    scopus 로고
    • Structural and functional neuroprotection in a rat model of Huntington's disease by viral gene transfer of GDNF
    • McBride, J. L. et al. Structural and functional neuroprotection in a rat model of Huntington's disease by viral gene transfer of GDNF. Exp. Neurol. 181, 213-223 (2003).
    • (2003) Exp. Neurol. , vol.181 , pp. 213-223
    • McBride, J.L.1
  • 115
    • 2442702838 scopus 로고    scopus 로고
    • AAV-mediated gene delivery of BDNF or GDNF is neuroprotective in a model of Huntington disease
    • Kells, A. P. et al. AAV-mediated gene delivery of BDNF or GDNF is neuroprotective in a model of Huntington disease. Mol. Ther. 9, 682-688 (2004).
    • (2004) Mol. Ther. , vol.9 , pp. 682-688
    • Kells, A.P.1
  • 116
    • 4444350918 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor regulates the onset and severity of motor dysfunction associated with enkephalinergic neuronal degeneration in Huntington's disease
    • Canals, J. M. et al. Brain-derived neurotrophic factor regulates the onset and severity of motor dysfunction associated with enkephalinergic neuronal degeneration in Huntington's disease. J. Neurosci. 24, 7727-7739 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 7727-7739
    • Canals, J.M.1
  • 117
    • 10644241634 scopus 로고    scopus 로고
    • Increased GABAergic function in mouse models of Huntington's disease: Reversal by BDNF
    • Cepeda, C. et al. Increased GABAergic function in mouse models of Huntington's disease: reversal by BDNF. J. Neurosci. Res. 78, 855-867 (2004).
    • (2004) J. Neurosci. Res. , vol.78 , pp. 855-867
    • Cepeda, C.1
  • 118
    • 16244373680 scopus 로고    scopus 로고
    • Lentiviral gene delivery of GDNF into the striatum of R6/2 Huntington mice fails to attenuate behavioral and neuropathological changes
    • Popovic, N., Maingay, M., Kirik, D. & Brundin, P. Lentiviral gene delivery of GDNF into the striatum of R6/2 Huntington mice fails to attenuate behavioral and neuropathological changes. Exp. Neurol. 193, 65-74 (2005).
    • (2005) Exp. Neurol. , vol.193 , pp. 65-74
    • Popovic, N.1    Maingay, M.2    Kirik, D.3    Brundin, P.4
  • 119
    • 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, 493-498 (2001).
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1
  • 120
    • 12144286872 scopus 로고    scopus 로고
    • Androgen receptor YAC transgenic mice recapitulate SBMA motor neuronopathy and implicate VEGF164 in the motor neuron degeneration
    • Sopher, B. L. et al. Androgen receptor YAC transgenic mice recapitulate SBMA motor neuronopathy and implicate VEGF164 in the motor neuron degeneration. Neuron 41, 687-699 (2004).
    • (2004) Neuron , vol.41 , pp. 687-699
    • Sopher, B.L.1
  • 121
    • 5644295321 scopus 로고    scopus 로고
    • Neuroprotective gene therapy for Huntington's disease, using polymer-encapsulated cells engineered to secrete human ciliary neurotrophic factor: Results of a phase I study
    • Bloch, J. et al. Neuroprotective gene therapy for Huntington's disease, using polymer-encapsulated cells engineered to secrete human ciliary neurotrophic factor: results of a phase I study. Hum. Gene Ther. 15, 968-975 (2004).
    • (2004) Hum. Gene Ther. , vol.15 , pp. 968-975
    • Bloch, J.1
  • 122
    • 0032211289 scopus 로고    scopus 로고
    • Striatal transplantation in a transgenic mouse model of Huntington's disease
    • Dunnett, S. B. et al. Striatal transplantation in a transgenic mouse model of Huntington's disease. Exp. Neurol. 154, 31-40 (1998).
    • (1998) Exp. Neurol. , vol.154 , pp. 31-40
    • Dunnett, S.B.1
  • 123
    • 0035503912 scopus 로고    scopus 로고
    • Anterior cingulate cortical transplantation in transgenic Huntington's disease mice
    • van Dellen, A., Deacon, R., York, D., Blakemore, C. & Hannan, A. J. Anterior cingulate cortical transplantation in transgenic Huntington's disease mice. Brain Res. Bull. 56, 313-318 (2001).
    • (2001) Brain Res. Bull. , vol.56 , pp. 313-318
    • Van Dellen, A.1    Deacon, R.2    York, D.3    Blakemore, C.4    Hannan, A.J.5
  • 124
    • 12944288307 scopus 로고    scopus 로고
    • Transplanted fetal striatum in Huntington's disease: Phenotypic development and lack of pathology
    • Freeman, T. B. et al. Transplanted fetal striatum in Huntington's disease: phenotypic development and lack of pathology. Proc. Natl Acad. Sci. USA 97, 13877-13882 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13877-13882
    • Freeman, T.B.1
  • 125
    • 0034627143 scopus 로고    scopus 로고
    • Motor and cognitive improvements in patients with Huntington's disease after neural transplantation
    • Bachoud-Levi, A. C. et al. Motor and cognitive improvements in patients with Huntington's disease after neural transplantation. Lancet 356, 1975-1979 (2000).
    • (2000) Lancet , vol.356 , pp. 1975-1979
    • Bachoud-Levi, A.C.1
  • 126
    • 9144221004 scopus 로고    scopus 로고
    • Striatal neural grafting improves cortical metabolism in Huntington's disease patients
    • Gaura, V. et al. Striatal neural grafting improves cortical metabolism in Huntington's disease patients. Brain 127, 65-72 (2004).
    • (2004) Brain , vol.127 , pp. 65-72
    • Gaura, V.1
  • 127
    • 3042721905 scopus 로고    scopus 로고
    • Human neural stem cell transplants improve motor function in a rat model of Huntington's disease
    • McBride, J. L. et al. Human neural stem cell transplants improve motor function in a rat model of Huntington's disease. J. Comp. Neurol. 475, 211-219 (2004).
    • (2004) J. Comp. Neurol. , vol.475 , pp. 211-219
    • McBride, J.L.1
  • 128
    • 0042527172 scopus 로고    scopus 로고
    • Autologous adult bone marrow stem cell transplantation in an animal model of huntington's disease: Behavioral and morphological outcomes
    • Lescaudron, L., Unni, D. & Dunbar, G. L. Autologous adult bone marrow stem cell transplantation in an animal model of huntington's disease: behavioral and morphological outcomes. Int. J. Neurosci. 113, 945-956 (2003).
    • (2003) Int. J. Neurosci. , vol.113 , pp. 945-956
    • Lescaudron, L.1    Unni, D.2    Dunbar, G.L.3
  • 129
    • 0034795158 scopus 로고    scopus 로고
    • Human umbilical cord blood cells ameliorate Huntington's disease in transgenic mice
    • Ende, N. & Chen, R. Human umbilical cord blood cells ameliorate Huntington's disease in transgenic mice. J. Med. 32, 231-240 (2001).
    • (2001) J. Med. , vol.32 , pp. 231-240
    • Ende, N.1    Chen, R.2
  • 130
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto, A., Lucas, J. J. & Hen, R. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 101, 57-66 (2000). The authors show that blockade of expression of the mutant protein leads to a disappearance of inclusions and a reversal of the behavioural phenotype. This indicates that continuous expression of the mutant protein is necessary for the disease.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 131
    • 0037081772 scopus 로고    scopus 로고
    • Rescue of polyglutamine-mediated cytotoxicity by double-stranded RNA-mediated RNA interference
    • Caplen, N. J. et al. Rescue of polyglutamine-mediated cytotoxicity by double-stranded RNA-mediated RNA interference. Hum. Mol. Genet. 11, 175-184 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 175-184
    • Caplen, N.J.1
  • 132
    • 4043057946 scopus 로고    scopus 로고
    • RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia
    • Xia, H. et al. RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia. Nature Med. 10, 816-820 (2004). A discussion of in vivo use of RNAi as a potential therapy for dominant neurodegenerative disorders.
    • (2004) Nature Med. , vol.10 , pp. 816-820
    • Xia, H.1
  • 133
    • 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. USA 102, 5820-5825 (2005). This paper shows that RNAi can accomplish disease allele-specific silencing in vivo.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5820-5825
    • Harper, S.Q.1
  • 134
    • 0037461309 scopus 로고    scopus 로고
    • Neuroprotective agents for clinical trials in Parkinson's disease: A systematic assessment
    • Ravina, B. M. et al. Neuroprotective agents for clinical trials in Parkinson's disease: a systematic assessment. Neurology 60, 1234-1240 (2003).
    • (2003) Neurology , vol.60 , pp. 1234-1240
    • Ravina, B.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.