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Volumn 35, Issue 2, 2014, Pages 53-62

Drugging unconventional targets: Insights from Huntington's disease

Author keywords

antisense oligonucleotides; high throughput screening; neurodegenerative disorder; protein degradation; proteinopathies; RNA interference

Indexed keywords

ANTISENSE OLIGONUCLEOTIDES; HIGH-THROUGHPUT SCREENING; NEURODEGENERATIVE DISORDER; PROTEIN DEGRADATION; PROTEINOPATHIES; RNA INTERFERENCE;

EID: 84895072822     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2013.12.001     Document Type: Review
Times cited : (16)

References (107)
  • 1
    • 0021921176 scopus 로고
    • Senile plaque amyloid, paired helical filaments, and cerebrovascular amyloid in Alzheimer's disease are all deposits of the same protein
    • M. Kidd et al. Senile plaque amyloid, paired helical filaments, and cerebrovascular amyloid in Alzheimer's disease are all deposits of the same protein Lancet 1 1985 278
    • (1985) Lancet , vol.1 , pp. 278
    • Kidd, M.1
  • 2
    • 0030882856 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy bodies
    • M.G. Spillantini et al. Alpha-synuclein in Lewy bodies Nature 388 1997 839 840
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1
  • 3
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • J. Sreedharan et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis Science 319 2008 1668 1672
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1
  • 4
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes Cell 72 1993 971 983
    • (1993) Cell , vol.72 , pp. 971-983
  • 5
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • F.O. Walker Huntington's disease Lancet 369 2007 218 228
    • (2007) Lancet , vol.369 , pp. 218-228
    • Walker, F.O.1
  • 6
    • 84863833900 scopus 로고    scopus 로고
    • Network organization of the huntingtin proteomic interactome in mammalian brain
    • D.I. Shirasaki et al. Network organization of the huntingtin proteomic interactome in mammalian brain Neuron 75 2012 41 57
    • (2012) Neuron , vol.75 , pp. 41-57
    • Shirasaki, D.I.1
  • 7
    • 34249715853 scopus 로고    scopus 로고
    • Huntingtin interacting proteins are genetic modifiers of neurodegeneration
    • L.S. Kaltenbach et al. Huntingtin interacting proteins are genetic modifiers of neurodegeneration PLoS Genet. 3 2007 e82
    • (2007) PLoS Genet. , vol.3 , pp. 82
    • Kaltenbach, L.S.1
  • 8
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • P. Harjes, and E.E. Wanker The hunt for huntingtin function: interaction partners tell many different stories Trends Biochem. Sci. 28 2003 425 433
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 9
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • E. Cattaneo et al. Normal huntingtin function: an alternative approach to Huntington's disease Nat. Rev. Neurosci. 6 2005 919 930
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 919-930
    • Cattaneo, E.1
  • 10
    • 84855499458 scopus 로고    scopus 로고
    • Huntington's disease: Molecular basis of neurodegeneration
    • D.C. Rubinsztein, and J. Carmichael Huntington's disease: molecular basis of neurodegeneration Expert Rev. Mol. Med. 5 2003 1 21
    • (2003) Expert Rev. Mol. Med. , vol.5 , pp. 1-21
    • Rubinsztein, D.C.1    Carmichael, J.2
  • 11
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • M. Arrasate 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
  • 12
    • 84883204078 scopus 로고    scopus 로고
    • Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration
    • A.S. Tsvetkov et al. Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration Nat. Chem. Biol. 9 2013 586 592
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 586-592
    • Tsvetkov, A.S.1
  • 13
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • A. Yamamoto et al. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease Cell 101 2000 57 66
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1
  • 14
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • S. Zeitlin et al. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue Nat. Genet. 11 1995 155 163
    • (1995) Nat. Genet. , vol.11 , pp. 155-163
    • Zeitlin, S.1
  • 15
    • 0029082383 scopus 로고
    • Inactivation of the mouse Huntington's disease gene homolog Hdh
    • M.P. Duyao et al. Inactivation of the mouse Huntington's disease gene homolog Hdh Science 269 1995 407 410
    • (1995) Science , vol.269 , pp. 407-410
    • Duyao, M.P.1
  • 16
    • 67349100160 scopus 로고    scopus 로고
    • Nonallele-specific silencing of mutant and wild-type huntingtin demonstrates therapeutic efficacy in Huntington's disease mice
    • R.L. Boudreau et al. Nonallele-specific silencing of mutant and wild-type huntingtin demonstrates therapeutic efficacy in Huntington's disease mice Mol. Ther. 17 2009 1053 1063
    • (2009) Mol. Ther. , vol.17 , pp. 1053-1063
    • Boudreau, R.L.1
  • 17
    • 84860192454 scopus 로고    scopus 로고
    • Six-month partial suppression of Huntingtin is well tolerated in the adult rhesus striatum
    • R. Grondin et al. Six-month partial suppression of Huntingtin is well tolerated in the adult rhesus striatum Brain 135 2012 1197 1209
    • (2012) Brain , vol.135 , pp. 1197-1209
    • Grondin, R.1
  • 18
    • 84877139837 scopus 로고    scopus 로고
    • A novel human embryonic stem cell-derived Huntington's disease neuronal model exhibits mutant huntingtin (mHTT) aggregates and soluble mHTT-dependent neurodegeneration
    • B. Lu, and J. Palacino A novel human embryonic stem cell-derived Huntington's disease neuronal model exhibits mutant huntingtin (mHTT) aggregates and soluble mHTT-dependent neurodegeneration FASEB J. 27 2013 1820 1829
    • (2013) FASEB J. , vol.27 , pp. 1820-1829
    • Lu, B.1    Palacino, J.2
  • 19
    • 20244378556 scopus 로고    scopus 로고
    • RNA interference improves motor and neuropathological abnormalities in a Huntington's disease mouse model
    • S.Q. Harper 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
  • 20
    • 25144464388 scopus 로고    scopus 로고
    • Intrastriatal rAAV-mediated delivery of anti-huntingtin shRNAs induces partial reversal of disease progression in R6/1 Huntington's disease transgenic mice
    • E. Rodriguez-Lebron et al. Intrastriatal rAAV-mediated delivery of anti-huntingtin shRNAs induces partial reversal of disease progression in R6/1 Huntington's disease transgenic mice Mol. Ther. 12 2005 618 633
    • (2005) Mol. Ther. , vol.12 , pp. 618-633
    • Rodriguez-Lebron, E.1
  • 21
    • 36749033738 scopus 로고    scopus 로고
    • Therapeutic silencing of mutant huntingtin with siRNA attenuates striatal and cortical neuropathology and behavioral deficits
    • M. DiFiglia et al. Therapeutic silencing of mutant huntingtin with siRNA attenuates striatal and cortical neuropathology and behavioral deficits Proc. Natl. Acad. Sci. U.S.A. 104 2007 17204 17209
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17204-17209
    • Difiglia, M.1
  • 22
    • 47549105506 scopus 로고    scopus 로고
    • Identification and allele-specific silencing of the mutant huntingtin allele in Huntington's disease patient-derived fibroblasts
    • P.H. van Bilsen et al. Identification and allele-specific silencing of the mutant huntingtin allele in Huntington's disease patient-derived fibroblasts Hum. Gene Ther. 19 2008 710 719
    • (2008) Hum. Gene Ther. , vol.19 , pp. 710-719
    • Van Bilsen, P.H.1
  • 23
    • 67349159137 scopus 로고    scopus 로고
    • Five siRNAs targeting three SNPs may provide therapy for three-quarters of Huntington's disease patients
    • E.L. Pfister et al. Five siRNAs targeting three SNPs may provide therapy for three-quarters of Huntington's disease patients Curr. Biol. 19 2009 774 778
    • (2009) Curr. Biol. , vol.19 , pp. 774-778
    • Pfister, E.L.1
  • 24
    • 57249086448 scopus 로고    scopus 로고
    • Allele-specific silencing of mutant Huntington's disease gene
    • Y. Zhang et al. Allele-specific silencing of mutant Huntington's disease gene J. Neurochem. 108 2009 82 90
    • (2009) J. Neurochem. , vol.108 , pp. 82-90
    • Zhang, Y.1
  • 25
    • 78649359013 scopus 로고    scopus 로고
    • Allele-selective inhibition of huntingtin expression by switching to an miRNA-like RNAi mechanism
    • J. Hu et al. Allele-selective inhibition of huntingtin expression by switching to an miRNA-like RNAi mechanism Chem. Biol. 17 2010 1183 1188
    • (2010) Chem. Biol. , vol.17 , pp. 1183-1188
    • Hu, J.1
  • 26
    • 78649379362 scopus 로고    scopus 로고
    • Allele-selective inhibition of mutant huntingtin expression with antisense oligonucleotides targeting the expanded CAG repeat
    • K.T. Gagnon et al. Allele-selective inhibition of mutant huntingtin expression with antisense oligonucleotides targeting the expanded CAG repeat Biochemistry 49 2010 10166 10178
    • (2010) Biochemistry , vol.49 , pp. 10166-10178
    • Gagnon, K.T.1
  • 27
    • 82955237522 scopus 로고    scopus 로고
    • Potent and selective antisense oligonucleotides targeting single-nucleotide polymorphisms in the Huntington disease gene/allele-specific silencing of mutant huntingtin
    • J.B. Carroll et al. Potent and selective antisense oligonucleotides targeting single-nucleotide polymorphisms in the Huntington disease gene/allele-specific silencing of mutant huntingtin Mol. Ther. 19 2011 2178 2185
    • (2011) Mol. Ther. , vol.19 , pp. 2178-2185
    • Carroll, J.B.1
  • 28
    • 84862663712 scopus 로고    scopus 로고
    • Sustained therapeutic reversal of Huntington's disease by transient repression of huntingtin synthesis
    • H.B. Kordasiewicz et al. Sustained therapeutic reversal of Huntington's disease by transient repression of huntingtin synthesis Neuron 74 2012 1031 1044
    • (2012) Neuron , vol.74 , pp. 1031-1044
    • Kordasiewicz, H.B.1
  • 29
    • 84865688581 scopus 로고    scopus 로고
    • Single-stranded RNAs use RNAi to potently and allele-selectively inhibit mutant huntingtin expression
    • D. Yu et al. Single-stranded RNAs use RNAi to potently and allele-selectively inhibit mutant huntingtin expression Cell 150 2012 895 908
    • (2012) Cell , vol.150 , pp. 895-908
    • Yu, D.1
  • 30
    • 65249131740 scopus 로고    scopus 로고
    • Sustained effects of nonallele-specific Huntingtin silencing
    • V. Drouet et al. Sustained effects of nonallele-specific Huntingtin silencing Ann. Neurol. 65 2009 276 285
    • (2009) Ann. Neurol. , vol.65 , pp. 276-285
    • Drouet, V.1
  • 31
    • 82955199935 scopus 로고    scopus 로고
    • Preclinical safety of RNAi-mediated HTT suppression in the rhesus macaque as a potential therapy for Huntington's disease
    • J.L. McBride et al. Preclinical safety of RNAi-mediated HTT suppression in the rhesus macaque as a potential therapy for Huntington's disease Mol. Ther. 19 2011 2152 2162
    • (2011) Mol. Ther. , vol.19 , pp. 2152-2162
    • McBride, J.L.1
  • 32
    • 27644596641 scopus 로고    scopus 로고
    • What is the role of protein aggregation in neurodegeneration?
    • C.A. Ross, and M.A. Poirier What is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6 2005 891 898
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 33
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: Relationship to neuropathology
    • C.A. Gutekunst et al. Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology J. Neurosci. 19 1999 2522 2534
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1
  • 34
    • 0033614770 scopus 로고    scopus 로고
    • Are there multiple pathways in the pathogenesis of Huntington's disease?
    • N. Aronin et al. Are there multiple pathways in the pathogenesis of Huntington's disease? Phillos. Trans. R. Soc. Lond. B: Biol. Sci. 354 1999 995 1003
    • (1999) Phillos. Trans. R. Soc. Lond. B: Biol. Sci. , vol.354 , pp. 995-1003
    • Aronin, N.1
  • 35
    • 84887792874 scopus 로고    scopus 로고
    • Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress
    • J. Leitman et al. Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress Nat. Commun. 4 2013 2753
    • (2013) Nat. Commun. , vol.4 , pp. 2753
    • Leitman, J.1
  • 36
    • 77950682093 scopus 로고    scopus 로고
    • Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease
    • X. Li et al. Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease J. Neurosci. 30 2010 4552 4561
    • (2010) J. Neurosci. , vol.30 , pp. 4552-4561
    • Li, X.1
  • 37
    • 84859760185 scopus 로고    scopus 로고
    • Native mutant huntingtin in human brain: Evidence for prevalence of full-length monomer
    • E. Sapp et al. Native mutant huntingtin in human brain: evidence for prevalence of full-length monomer J. Biol. Chem. 287 2012 13487 13499
    • (2012) J. Biol. Chem. , vol.287 , pp. 13487-13499
    • Sapp, E.1
  • 38
    • 81355160169 scopus 로고    scopus 로고
    • Identifying polyglutamine protein species in situ that best predict neurodegeneration
    • J. Miller et al. Identifying polyglutamine protein species in situ that best predict neurodegeneration Nat. Chem. Biol. 7 2011 925 934
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 925-934
    • Miller, J.1
  • 39
    • 0033280667 scopus 로고    scopus 로고
    • Vacuolar import of proteins and organelles from the cytoplasm
    • D.J. Klionsky, and Y. Ohsumi Vacuolar import of proteins and organelles from the cytoplasm Annu. Rev. Cell Dev. Biol. 15 1999 1 32
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 1-32
    • Klionsky, D.J.1    Ohsumi, Y.2
  • 40
    • 33847705665 scopus 로고    scopus 로고
    • Role of ubiquitin- and Ubl-binding proteins in cell signaling
    • V. Kirkin, and I. Dikic Role of ubiquitin- and Ubl-binding proteins in cell signaling Curr. Opin. Cell Biol. 19 2007 199 205
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 199-205
    • Kirkin, V.1    Dikic, I.2
  • 41
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • B. Levine, and G. Kroemer Autophagy in the pathogenesis of disease Cell 132 2008 27 42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 42
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • M. Komatsu et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice Cell 131 2007 1149 1163
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1
  • 43
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • G. Bjorkoy et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death J. Cell Biol. 171 2005 603 614
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjorkoy, G.1
  • 44
    • 77950903972 scopus 로고    scopus 로고
    • The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy
    • M. Filimonenko et al. The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy Mol. Cell 38 2010 265 279
    • (2010) Mol. Cell , vol.38 , pp. 265-279
    • Filimonenko, M.1
  • 45
    • 80955177196 scopus 로고    scopus 로고
    • TFEB links autophagy to lysosomal biogenesis
    • C. Settembre et al. TFEB links autophagy to lysosomal biogenesis Science 332 2011 1429 1433
    • (2011) Science , vol.332 , pp. 1429-1433
    • Settembre, C.1
  • 46
    • 84863923855 scopus 로고    scopus 로고
    • PGC-1α rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function
    • T. Tsunemi et al. PGC-1α rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function Sci. Transl. Med. 4 2012 142ra197
    • (2012) Sci. Transl. Med. , vol.4
    • Tsunemi, T.1
  • 47
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • N.R. Jana et al. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes J. Biol. Chem. 280 2005 11635 11640
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1
  • 48
    • 77749319356 scopus 로고    scopus 로고
    • Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
    • P.O. Bauer et al. Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein Nat. Biotechnol. 28 2010 256 263
    • (2010) Nat. Biotechnol. , vol.28 , pp. 256-263
    • Bauer, P.O.1
  • 49
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • B. Ravikumar et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease Nat. Genet. 36 2004 585 595
    • (2004) Nat. Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1
  • 50
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies
    • S. Sarkar et al. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies Cell Death Differ. 16 2009 46 56
    • (2009) Cell Death Differ. , vol.16 , pp. 46-56
    • Sarkar, S.1
  • 51
    • 0038364056 scopus 로고    scopus 로고
    • Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy
    • B. Ravikumar et al. Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy Hum. Mol. Genet. 12 2003 985 994
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 985-994
    • Ravikumar, B.1
  • 52
    • 53749104349 scopus 로고    scopus 로고
    • Akt inhibition promotes autophagy and sensitizes PTEN-null tumors to lysosomotropic agents
    • M. Degtyarev et al. Akt inhibition promotes autophagy and sensitizes PTEN-null tumors to lysosomotropic agents J. Cell Biol. 183 2008 101 116
    • (2008) J. Cell Biol. , vol.183 , pp. 101-116
    • Degtyarev, M.1
  • 53
    • 65949086045 scopus 로고    scopus 로고
    • Atg5 regulates phenethyl isothiocyanate-induced autophagic and apoptotic cell death in human prostate cancer cells
    • A. Bommareddy et al. Atg5 regulates phenethyl isothiocyanate-induced autophagic and apoptotic cell death in human prostate cancer cells Cancer Res. 69 2009 3704 3712
    • (2009) Cancer Res. , vol.69 , pp. 3704-3712
    • Bommareddy, A.1
  • 54
    • 57349180534 scopus 로고    scopus 로고
    • Antioxidants in central nervous system diseases: Preclinical promise and translational challenges
    • C.D. Kamat et al. Antioxidants in central nervous system diseases: preclinical promise and translational challenges J. Alzheimers Dis. 15 2008 473 493
    • (2008) J. Alzheimers Dis. , vol.15 , pp. 473-493
    • Kamat, C.D.1
  • 55
    • 77955383021 scopus 로고    scopus 로고
    • Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease
    • B.R. Underwood et al. Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease Hum. Mol. Genet. 19 2010 3413 3429
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3413-3429
    • Underwood, B.R.1
  • 56
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • S. Sarkar et al. Lithium induces autophagy by inhibiting inositol monophosphatase J. Cell Biol. 170 2005 1101 1111
    • (2005) J. Cell Biol. , vol.170 , pp. 1101-1111
    • Sarkar, S.1
  • 57
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • S. Sarkar et al. A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin Hum. Mol. Genet. 17 2008 170 178
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 170-178
    • Sarkar, S.1
  • 58
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • A. Williams 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
  • 59
    • 77953486943 scopus 로고    scopus 로고
    • Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington's disease
    • C. Rose et al. Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington's disease Hum. Mol. Genet. 19 2010 2144 2153
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2144-2153
    • Rose, C.1
  • 60
    • 0027495705 scopus 로고
    • Dependence of hepatocytic autophagy on intracellularly sequestered calcium
    • P.B. Gordon et al. Dependence of hepatocytic autophagy on intracellularly sequestered calcium J. Biol. Chem. 268 1993 26107 26112
    • (1993) J. Biol. Chem. , vol.268 , pp. 26107-26112
    • Gordon, P.B.1
  • 61
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein
    • S. Sarkar et al. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein J. Biol. Chem. 282 2007 5641 5652
    • (2007) J. Biol. Chem. , vol.282 , pp. 5641-5652
    • Sarkar, S.1
  • 62
    • 37649024076 scopus 로고    scopus 로고
    • Small molecule regulators of autophagy identified by an image-based high-throughput screen
    • L. Zhang et al. Small molecule regulators of autophagy identified by an image-based high-throughput screen Proc. Natl. Acad. Sci. U.S.A. 104 2007 19023 19028
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19023-19028
    • Zhang, L.1
  • 63
    • 84860681788 scopus 로고    scopus 로고
    • Autophagy and polyglutamine diseases
    • M. Jimenez-Sanchez et al. Autophagy and polyglutamine diseases Prog. Neurobiol. 97 2012 67 82
    • (2012) Prog. Neurobiol. , vol.97 , pp. 67-82
    • Jimenez-Sanchez, M.1
  • 64
    • 56749170677 scopus 로고    scopus 로고
    • Autophagic cell death: The story of a misnomer
    • G. Kroemer, and B. Levine Autophagic cell death: the story of a misnomer Nat. Rev. Mol. Cell Biol. 9 2008 1004 1010
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 1004-1010
    • Kroemer, G.1    Levine, B.2
  • 65
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • N.F. Bence et al. Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1
  • 66
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • P. Venkatraman et al. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins Mol. Cell 14 2004 95 104
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1
  • 67
    • 67650258745 scopus 로고    scopus 로고
    • Enhanced degradation of mutant huntingtin by rho kinase inhibition is mediated through activation of proteasome and macroautophagy
    • P.O. Bauer, and N. Nukina Enhanced degradation of mutant huntingtin by rho kinase inhibition is mediated through activation of proteasome and macroautophagy Autophagy 5 2009 747 748
    • (2009) Autophagy , vol.5 , pp. 747-748
    • Bauer, P.O.1    Nukina, N.2
  • 68
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • L.M. Thompson et al. IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome J. Cell Biol. 187 2009 1083 1099
    • (2009) J. Cell Biol. , vol.187 , pp. 1083-1099
    • Thompson, L.M.1
  • 69
    • 84884567375 scopus 로고    scopus 로고
    • Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes
    • K. Juenemann et al. Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes J. Biol. Chem. 288 2013 27068 27084
    • (2013) J. Biol. Chem. , vol.288 , pp. 27068-27084
    • Juenemann, K.1
  • 70
    • 84876917897 scopus 로고    scopus 로고
    • Identification of NUB1 as a suppressor of mutant Huntington toxicity via enhanced protein clearance
    • B. Lu et al. Identification of NUB1 as a suppressor of mutant Huntington toxicity via enhanced protein clearance Nat. Neurosci. 16 2013 562 570
    • (2013) Nat. Neurosci. , vol.16 , pp. 562-570
    • Lu, B.1
  • 71
    • 0035824559 scopus 로고    scopus 로고
    • Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1
    • T. Kamitani et al. Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1 J. Biol. Chem. 276 2001 46655 46660
    • (2001) J. Biol. Chem. , vol.276 , pp. 46655-46660
    • Kamitani, T.1
  • 72
    • 0035827621 scopus 로고    scopus 로고
    • NUB1, a NEDD8-interacting protein, is induced by interferon and down-regulates the NEDD8 expression
    • K. Kito et al. NUB1, a NEDD8-interacting protein, is induced by interferon and down-regulates the NEDD8 expression J. Biol. Chem. 276 2001 20603 20609
    • (2001) J. Biol. Chem. , vol.276 , pp. 20603-20609
    • Kito, K.1
  • 73
    • 0041856380 scopus 로고    scopus 로고
    • Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L
    • T. Tanaka et al. Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L J. Biol. Chem. 278 2003 32905 32913
    • (2003) J. Biol. Chem. , vol.278 , pp. 32905-32913
    • Tanaka, T.1
  • 74
    • 1942533448 scopus 로고    scopus 로고
    • NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation
    • M.S. Hipp et al. NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation J. Biol. Chem. 279 2004 16503 16510
    • (2004) J. Biol. Chem. , vol.279 , pp. 16503-16510
    • Hipp, M.S.1
  • 75
    • 84876934388 scopus 로고    scopus 로고
    • NUB1 snubs huntingtin toxicity
    • R. Aron et al. NUB1 snubs huntingtin toxicity Nat. Neurosci. 16 2013 523 525
    • (2013) Nat. Neurosci. , vol.16 , pp. 523-525
    • Aron, R.1
  • 76
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • L. Pintard et al. Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family EMBO J. 23 2004 1681 1687
    • (2004) EMBO J. , vol.23 , pp. 1681-1687
    • Pintard, L.1
  • 77
    • 74049138620 scopus 로고    scopus 로고
    • The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis
    • S. Maerki et al. The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis J. Cell Biol. 187 2009 791 800
    • (2009) J. Cell Biol. , vol.187 , pp. 791-800
    • Maerki, S.1
  • 78
    • 34249305132 scopus 로고    scopus 로고
    • A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells
    • I. Sumara et al. A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells Dev. Cell 12 2007 887 900
    • (2007) Dev. Cell , vol.12 , pp. 887-900
    • Sumara, I.1
  • 79
    • 0027521002 scopus 로고
    • Interferon β-1b is effective in relapsing-remitting multiple sclerosis. II. MRI analysis results of a multicenter, randomized, double-blind, placebo-controlled trial. UBC MS/MRI Study Group and the IFNB Multiple Sclerosis Study Group
    • D.W. Paty, and D.K. Li Interferon β-1b is effective in relapsing-remitting multiple sclerosis. II. MRI analysis results of a multicenter, randomized, double-blind, placebo-controlled trial. UBC MS/MRI Study Group and the IFNB Multiple Sclerosis Study Group Neurology 43 1993 662 667
    • (1993) Neurology , vol.43 , pp. 662-667
    • Paty, D.W.1    Li, D.K.2
  • 80
    • 84878820326 scopus 로고    scopus 로고
    • Interferon β induces clearance of mutant ataxin 7 and improves locomotion in SCA7 knock-in mice
    • A. Chort et al. Interferon β induces clearance of mutant ataxin 7 and improves locomotion in SCA7 knock-in mice Brain 136 2013 1732 1745
    • (2013) Brain , vol.136 , pp. 1732-1745
    • Chort, A.1
  • 81
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease
    • M. Martinez-Vicente et al. Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease Nat. Neurosci. 13 2010 567 576
    • (2010) Nat. Neurosci. , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1
  • 82
    • 84859983420 scopus 로고    scopus 로고
    • Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease
    • M.S. Hipp et al. Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease J. Cell Biol. 196 2012 573 587
    • (2012) J. Cell Biol. , vol.196 , pp. 573-587
    • Hipp, M.S.1
  • 83
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice
    • X. Gu et al. Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice Neuron 64 2009 828 840
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1
  • 84
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • H. Jeong et al. Acetylation targets mutant huntingtin to autophagosomes for degradation Cell 137 2009 60 72
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1
  • 85
    • 78349301194 scopus 로고    scopus 로고
    • Antibody therapy in neurodegenerative disease
    • A.L. Southwell, and P.H. Patterson Antibody therapy in neurodegenerative disease Rev. Neurosci. 21 2010 273 287
    • (2010) Rev. Neurosci. , vol.21 , pp. 273-287
    • Southwell, A.L.1    Patterson, P.H.2
  • 86
    • 84855478434 scopus 로고    scopus 로고
    • A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (Hsp90) client protein
    • B. Baldo et al. A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (Hsp90) client protein J. Biol. Chem. 287 2012 1406 1414
    • (2012) J. Biol. Chem. , vol.287 , pp. 1406-1414
    • Baldo, B.1
  • 87
    • 77955870526 scopus 로고    scopus 로고
    • A genome-wide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila
    • S. Zhang et al. A genome-wide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila Genetics 184 2010 1165 1179
    • (2010) Genetics , vol.184 , pp. 1165-1179
    • Zhang, S.1
  • 88
    • 77955500335 scopus 로고    scopus 로고
    • Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease
    • J.P. Miller et al. Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease Neuron 67 2010 199 212
    • (2010) Neuron , vol.67 , pp. 199-212
    • Miller, J.P.1
  • 89
    • 70349675573 scopus 로고    scopus 로고
    • RNAi screening in Drosophila cells identifies new modifiers of mutant huntingtin aggregation
    • J. Doumanis et al. RNAi screening in Drosophila cells identifies new modifiers of mutant huntingtin aggregation PLoS ONE 4 2009 e7275
    • (2009) PLoS ONE , vol.4 , pp. 7275
    • Doumanis, J.1
  • 90
    • 84864628471 scopus 로고    scopus 로고
    • Induced pluripotent stem cells from patients with Huntington's disease show CAG-repeat-expansion-associated phenotypes
    • H.D. The, and iPSC
    • H.D. The, and iPSC. Consortium Induced pluripotent stem cells from patients with Huntington's disease show CAG-repeat-expansion-associated phenotypes Cell Stem Cell 11 2012 264 278
    • (2012) Cell Stem Cell , vol.11 , pp. 264-278
  • 91
    • 79551655290 scopus 로고    scopus 로고
    • Huntington's disease: Can mice lead the way to treatment?
    • Z.R. Crook, and D. Housman Huntington's disease: can mice lead the way to treatment? Neuron 69 2011 423 435
    • (2011) Neuron , vol.69 , pp. 423-435
    • Crook, Z.R.1    Housman, D.2
  • 93
    • 45149105779 scopus 로고    scopus 로고
    • Towards a transgenic model of Huntington's disease in a non-human primate
    • S.H. Yang 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
  • 94
    • 77957732707 scopus 로고    scopus 로고
    • Expression of Huntington's disease protein results in apoptotic neurons in the brains of cloned transgenic pigs
    • D. Yang et al. Expression of Huntington's disease protein results in apoptotic neurons in the brains of cloned transgenic pigs Hum. Mol. Genet. 19 2010 3983 3994
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3983-3994
    • Yang, D.1
  • 95
    • 84868093925 scopus 로고    scopus 로고
    • Mouse models of polyglutamine diseases in therapeutic approaches: Review and data table. Part II
    • P.M. Switonski et al. Mouse models of polyglutamine diseases in therapeutic approaches: review and data table. Part II Mol. Neurobiol. 46 2012 430 466
    • (2012) Mol. Neurobiol. , vol.46 , pp. 430-466
    • Switonski, P.M.1
  • 97
    • 0041691176 scopus 로고    scopus 로고
    • Time course of early motor and neuropathological anomalies in a knock-in mouse model of Huntington's disease with 140 CAG repeats
    • L.B. Menalled et al. Time course of early motor and neuropathological anomalies in a knock-in mouse model of Huntington's disease with 140 CAG repeats J. Comp. Neurol. 465 2003 11 26
    • (2003) J. Comp. Neurol. , vol.465 , pp. 11-26
    • Menalled, L.B.1
  • 98
    • 38349171781 scopus 로고    scopus 로고
    • Comparative analysis of genetic modifiers in Drosophila points to common and distinct mechanisms of pathogenesis among polyglutamine diseases
    • J. Branco et al. Comparative analysis of genetic modifiers in Drosophila points to common and distinct mechanisms of pathogenesis among polyglutamine diseases Hum. Mol. Genet. 17 2008 376 390
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 376-390
    • Branco, J.1
  • 99
    • 33749633639 scopus 로고    scopus 로고
    • Modeling polyglutamine pathogenesis in C. Elegans
    • H.R. Brignull et al. Modeling polyglutamine pathogenesis in C. elegans Methods Enzymol. 412 2006 256 282
    • (2006) Methods Enzymol. , vol.412 , pp. 256-282
    • Brignull, H.R.1
  • 100
    • 84879414055 scopus 로고    scopus 로고
    • RAS-MAPK-MSK1 pathway modulates ataxin 1 protein levels and toxicity in SCA1
    • J. Park et al. RAS-MAPK-MSK1 pathway modulates ataxin 1 protein levels and toxicity in SCA1 Nature 498 2013 325 331
    • (2013) Nature , vol.498 , pp. 325-331
    • Park, J.1
  • 101
    • 84870686106 scopus 로고    scopus 로고
    • A genome-scale RNA-interference screen identifies RRAS signaling as a pathologic feature of Huntington's disease
    • J.P. Miller et al. A genome-scale RNA-interference screen identifies RRAS signaling as a pathologic feature of Huntington's disease PLoS Genet. 8 2012 e1003042
    • (2012) PLoS Genet. , vol.8 , pp. 1003042
    • Miller, J.P.1
  • 102
    • 84887560529 scopus 로고    scopus 로고
    • Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington's disease
    • M.R. Sarantos et al. Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington's disease J. Huntingtons Dis. 1 2012 195 210
    • (2012) J. Huntingtons Dis. , vol.1 , pp. 195-210
    • Sarantos, M.R.1
  • 103
    • 84885020652 scopus 로고    scopus 로고
    • Glutathione peroxidase activity is neuroprotective in models of Huntington's disease
    • R.P. Mason et al. Glutathione peroxidase activity is neuroprotective in models of Huntington's disease Nat. Genet. 45 2013 1249 1254
    • (2013) Nat. Genet. , vol.45 , pp. 1249-1254
    • Mason, R.P.1
  • 104
    • 70349103737 scopus 로고    scopus 로고
    • Single-step detection of mutant huntingtin in animal and human tissues: A bioassay for Huntington's disease
    • A. Weiss et al. Single-step detection of mutant huntingtin in animal and human tissues: a bioassay for Huntington's disease Anal. Biochem. 395 2009 8 15
    • (2009) Anal. Biochem. , vol.395 , pp. 8-15
    • Weiss, A.1
  • 105
    • 20044390015 scopus 로고    scopus 로고
    • A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo
    • X. Zhang 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
  • 106
    • 84859179041 scopus 로고    scopus 로고
    • A pathogenic mechanism in Huntington's disease involves small CAG-repeated RNAs with neurotoxic activity
    • M. Banez-Coronel et al. A pathogenic mechanism in Huntington's disease involves small CAG-repeated RNAs with neurotoxic activity PLoS Genet. 8 2012 e1002481
    • (2012) PLoS Genet. , vol.8 , pp. 1002481
    • Banez-Coronel, M.1
  • 107
    • 84864631163 scopus 로고    scopus 로고
    • Genetic correction of Huntington's disease phenotypes in induced pluripotent stem cells
    • M.C. An et al. Genetic correction of Huntington's disease phenotypes in induced pluripotent stem cells Cell Stem Cell 11 2012 253 263
    • (2012) Cell Stem Cell , vol.11 , pp. 253-263
    • An, M.C.1


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