메뉴 건너뛰기




Volumn 23, Issue 4, 2013, Pages 168-174

PolyQ disease: Misfiring of a developmental cell death program?

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; ATAXIN 1; ATAXIN 2; ATAXIN 3; ATAXIN 7; ATROPHIN 1; BIOLOGICAL MARKER; CACNA1A PROTEIN; HUNTINGTIN; POLYGLUTAMINE; TATA BINDING PROTEIN; UNCLASSIFIED DRUG; PEPTIDE;

EID: 84883541737     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.11.003     Document Type: Review
Times cited : (43)

References (97)
  • 1
    • 0027480960 scopus 로고
    • The Huntington's Disease Collaborative Research Group, A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72, 971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in Xlinked spinal and bulbar muscular atrophy
    • La Spada, A.R. et al. (1991) Androgen receptor gene mutations in Xlinked spinal and bulbar muscular atrophy. Nature 352, 77-79
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1
  • 3
    • 77958472984 scopus 로고    scopus 로고
    • Consensus and controversies in best practices for molecular genetic testing of spinocerebellar ataxias
    • Sequeiros, J. et al. (2010) Consensus and controversies in best practices for molecular genetic testing of spinocerebellar ataxias. Eur. J. Hum. Genet. 18, 1188-1195
    • (2010) Eur. J. Hum. Genet. , vol.18 , pp. 1188-1195
    • Sequeiros, J.1
  • 4
    • 78649566546 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 17 associated with an expansion of 42 glutamine residues in TATA-box binding protein gene
    • Nolte, D. et al. (2010) Spinocerebellar ataxia type 17 associated with an expansion of 42 glutamine residues in TATA-box binding protein gene. J. Neurol. Neurosurg. Psychiatry 81, 1396-1399
    • (2010) J. Neurol. Neurosurg. Psychiatry , vol.81 , pp. 1396-1399
    • Nolte, D.1
  • 5
    • 12944270425 scopus 로고    scopus 로고
    • Identification of a novel 45 repeat unstable allele associated with a disease phenotype at the MJD1/SCA3 locus
    • Padiath, Q.S. et al. (2005) Identification of a novel 45 repeat unstable allele associated with a disease phenotype at the MJD1/SCA3 locus. Am. J. Med. Genet. B: Neuropsychiatr. Genet. 133, 124-126
    • (2005) Am. J. Med. Genet. B: Neuropsychiatr. Genet. , vol.133 , pp. 124-126
    • Padiath, Q.S.1
  • 7
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H.Y. and Orr, H.T. (2000) Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23, 217-247
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 8
    • 79955660764 scopus 로고    scopus 로고
    • An antisense CAG repeat transcript at JPH3 locus mediates expanded polyglutamine protein toxicity in Huntington's disease-like 2 mice
    • Wilburn, B. et al. (2011) An antisense CAG repeat transcript at JPH3 locus mediates expanded polyglutamine protein toxicity in Huntington's disease-like 2 mice. Neuron 70, 427-440
    • (2011) Neuron , vol.70 , pp. 427-440
    • Wilburn, B.1
  • 9
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr, H.T. and Zoghbi, H.Y. (2007) Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30, 575-621
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 10
    • 84863230093 scopus 로고    scopus 로고
    • Control of nonapoptotic developmental cell death in Caenorhabditis elegans by a polyglutamine-repeat protein
    • Blum, E.S. et al. (2012) Control of nonapoptotic developmental cell death in Caenorhabditis elegans by a polyglutamine-repeat protein. Science 335, 970-973
    • (2012) Science , vol.335 , pp. 970-973
    • Blum, E.S.1
  • 11
    • 0018725140 scopus 로고
    • The postembryonic cell lineages of the hermaphrodite and male gonads in Caenorhabditis elegans
    • Kimble, J. and Hirsh, D. (1979) The postembryonic cell lineages of the hermaphrodite and male gonads in Caenorhabditis elegans. Dev. Biol. 70, 396-417
    • (1979) Dev. Biol. , vol.70 , pp. 396-417
    • Kimble, J.1    Hirsh, D.2
  • 12
    • 0018962395 scopus 로고
    • The Caenorhabditis elegans male: postembryonic development of nongonadal structures
    • Sulston, J.E. et al. (1980) The Caenorhabditis elegans male: postembryonic development of nongonadal structures. Dev. Biol. 78, 542-576
    • (1980) Dev. Biol. , vol.78 , pp. 542-576
    • Sulston, J.E.1
  • 13
    • 33845794522 scopus 로고    scopus 로고
    • A morphologically conserved nonapoptotic program promotes linker cell death in Caenorhabditis elegans
    • Abraham, M.C. et al. (2007) A morphologically conserved nonapoptotic program promotes linker cell death in Caenorhabditis elegans. Dev. Cell 12, 73-86
    • (2007) Dev. Cell , vol.12 , pp. 73-86
    • Abraham, M.C.1
  • 14
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis, H.M. and Horvitz, H.R. (1986) Genetic control of programmed cell death in the nematode C. elegans. Cell 44, 817-829
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 15
    • 0017228158 scopus 로고
    • Ultrastructural differences during embryonic cell death in normal and peripherally deprived ciliary ganglia
    • Pilar, G. and Landmesser, L. (1976) Ultrastructural differences during embryonic cell death in normal and peripherally deprived ciliary ganglia. J. Cell Biol. 68, 339-356
    • (1976) J. Cell Biol. , vol.68 , pp. 339-356
    • Pilar, G.1    Landmesser, L.2
  • 17
    • 0035399637 scopus 로고    scopus 로고
    • Programmed cell death of developing mammalian neurons after genetic deletion of caspases
    • Oppenheim, R.W. et al. (2001) Programmed cell death of developing mammalian neurons after genetic deletion of caspases. J. Neurosci. 21, 4752-4760
    • (2001) J. Neurosci. , vol.21 , pp. 4752-4760
    • Oppenheim, R.W.1
  • 18
    • 0019425263 scopus 로고
    • Neuropathological changes of the nucleus accumbens in Huntington's chorea
    • Bots, G.T. and Bruyn, G.W. (1981) Neuropathological changes of the nucleus accumbens in Huntington's chorea. Acta Neuropathol. 55, 21-22
    • (1981) Acta Neuropathol , vol.55 , pp. 21-22
    • Bots, G.T.1    Bruyn, G.W.2
  • 19
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S.W. et al. (1997) Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1
  • 20
    • 0035900182 scopus 로고    scopus 로고
    • Neuronal nuclear alterations in dentatorubralpallidoluysian atrophy: ultrastructural and morphometric studies of the cerebellar granule cells
    • Takahashi, H. et al. (2001) Neuronal nuclear alterations in dentatorubralpallidoluysian atrophy: ultrastructural and morphometric studies of the cerebellar granule cells. Brain Res. 919, 12-19
    • (2001) Brain Res , vol.919 , pp. 12-19
    • Takahashi, H.1
  • 21
    • 0035888620 scopus 로고    scopus 로고
    • Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: proteins recruited in inclusions and activation of caspase-3
    • Zander, C. et al. (2001) Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: proteins recruited in inclusions and activation of caspase-3. Hum. Mol. Genet. 10, 2569-2579
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2569-2579
    • Zander, C.1
  • 22
    • 84861943506 scopus 로고    scopus 로고
    • The cell biology of disease: cell biology of spinocerebellar ataxia
    • Orr, H.T. (2012) The cell biology of disease: cell biology of spinocerebellar ataxia. J. Cell Biol. 197, 167-177
    • (2012) J. Cell Biol. , vol.197 , pp. 167-177
    • Orr, H.T.1
  • 23
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini, L. et al. (1996) Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87, 493-506
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1
  • 24
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model
    • Brignull, H.R. et al. (2006) Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model. J. Neurosci. 26, 7597-7606
    • (2006) J. Neurosci. , vol.26 , pp. 7597-7606
    • Brignull, H.R.1
  • 25
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson, G.R. et al. (1998) Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 21, 633-642
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.R.1
  • 26
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick, J.M. et al. (1998) Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 93, 939-949
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1
  • 27
    • 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. (1998) Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J. Biol. Chem. 273, 9158-9167
    • (1998) J. Biol. Chem. , vol.273 , pp. 9158-9167
    • Wellington, C.L.1
  • 28
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • Landles, C. et al. (2010) Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J. Biol. Chem. 285, 8808-8823
    • (2010) J. Biol. Chem. , vol.285 , pp. 8808-8823
    • Landles, C.1
  • 29
    • 84860879196 scopus 로고    scopus 로고
    • Identification of novel potentially toxic oligomers formed in vitro from mammalian-derived expanded huntingtin exon-1 protein
    • Nucifora, L.G. et al. (2012) Identification of novel potentially toxic oligomers formed in vitro from mammalian-derived expanded huntingtin exon-1 protein. J. Biol. Chem. 287, 16017-16028
    • (2012) J. Biol. Chem. , vol.287 , pp. 16017-16028
    • Nucifora, L.G.1
  • 30
    • 77951988103 scopus 로고    scopus 로고
    • Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • Legleiter, J. et al. (2010) Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. J. Biol. Chem. 285, 14777-14790
    • (2010) J. Biol. Chem. , vol.285 , pp. 14777-14790
    • Legleiter, J.1
  • 31
    • 84855921378 scopus 로고    scopus 로고
    • Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin
    • Waldron-Roby, E. et al. (2012) Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin. J. Neurosci. 32, 183-193
    • (2012) J. Neurosci. , vol.32 , pp. 183-193
    • Waldron-Roby, E.1
  • 32
    • 79959802847 scopus 로고    scopus 로고
    • Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivative
    • Tebbenkamp, A.T.N. et al. (2011) Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivative. Hum. Mol. Genet. 20, 2770-2782
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2770-2782
    • Tebbenkamp, A.T.N.1
  • 33
    • 80052644148 scopus 로고    scopus 로고
    • Modulation of mutant huntingtin Nterminal cleavage and its effect on aggregation and cell death
    • Juenemann, K. et al. (2011) Modulation of mutant huntingtin Nterminal cleavage and its effect on aggregation and cell death. Neurotox. Res. 20, 120-133
    • (2011) Neurotox. Res. , vol.20 , pp. 120-133
    • Juenemann, K.1
  • 34
    • 77955500335 scopus 로고    scopus 로고
    • Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease
    • Miller, J.P. et al. (2010) Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease. Neuron 67, 199-212
    • (2010) Neuron , vol.67 , pp. 199-212
    • Miller, J.P.1
  • 35
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham, R.K. et al. (2006) Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125, 1179-1191
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1
  • 36
    • 84861630493 scopus 로고    scopus 로고
    • Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment
    • Gafni, J. et al. (2012) Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment. J. Neurosci. 32, 7454-7465
    • (2012) J. Neurosci. , vol.32 , pp. 7454-7465
    • Gafni, J.1
  • 37
    • 0033605746 scopus 로고    scopus 로고
    • Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity
    • Ellerby, L.M. et al. (1999) Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity. J. Biol. Chem. 274, 8730-8736
    • (1999) J. Biol. Chem. , vol.274 , pp. 8730-8736
    • Ellerby, L.M.1
  • 38
    • 78449292904 scopus 로고    scopus 로고
    • Proteolytic processing regulates pathological accumulation in dentatorubral-pallidoluysian atrophy
    • Suzuki, Y. et al. (2010) Proteolytic processing regulates pathological accumulation in dentatorubral-pallidoluysian atrophy. FEBS J. 277, 4873-4887
    • (2010) FEBS J , vol.277 , pp. 4873-4887
    • Suzuki, Y.1
  • 39
    • 20844462057 scopus 로고    scopus 로고
    • A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration
    • Goti, D. et al. (2004) A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration. J. Neurosci. 24, 10266-10279
    • (2004) J. Neurosci. , vol.24 , pp. 10266-10279
    • Goti, D.1
  • 40
    • 34548329581 scopus 로고    scopus 로고
    • A mutant ataxin-3 fragment results from processing at a site N-terminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice
    • Colomer Gould, V.F. et al. (2007) A mutant ataxin-3 fragment results from processing at a site N-terminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice. Neurobiol. Dis. 27, 362-369
    • (2007) Neurobiol. Dis. , vol.27 , pp. 362-369
    • Colomer Gould, V.F.1
  • 41
    • 70450191208 scopus 로고    scopus 로고
    • Preventing Ataxin-3 protein cleavage mitigates degeneration in a Drosophila model of SCA3
    • Jung, J. et al. (2009) Preventing Ataxin-3 protein cleavage mitigates degeneration in a Drosophila model of SCA3. Hum. Mol. Genet. 18, 4843-4852
    • (2009) Hum. Mol. Genet , vol.18 , pp. 4843-4852
    • Jung, J.1
  • 42
    • 35648964788 scopus 로고    scopus 로고
    • Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation
    • Young, J.E. et al. (2007) Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation. J. Biol. Chem. 282, 30150-30160
    • (2007) J. Biol. Chem. , vol.282 , pp. 30150-30160
    • Young, J.E.1
  • 43
    • 0032898311 scopus 로고    scopus 로고
    • Kennedy's disease: caspase cleavage of the androgen receptor is a crucial event in cytotoxicity
    • Ellerby, L.M. et al. (1999) Kennedy's disease: caspase cleavage of the androgen receptor is a crucial event in cytotoxicity. J. Neurochem. 72, 185-195
    • (1999) J. Neurochem. , vol.72 , pp. 185-195
    • Ellerby, L.M.1
  • 44
    • 25444516516 scopus 로고    scopus 로고
    • Frequent occurrence of protein isoforms with or without a single amino acid residue by subtle alternative splicing: the case of Gln in DRPLA affects subcellular localization of the products
    • Tadokoro, K. et al. (2005) Frequent occurrence of protein isoforms with or without a single amino acid residue by subtle alternative splicing: the case of Gln in DRPLA affects subcellular localization of the products. J. Hum. Genet. 50, 382-394
    • (2005) J. Hum. Genet. , vol.50 , pp. 382-394
    • Tadokoro, K.1
  • 45
    • 54249142192 scopus 로고    scopus 로고
    • Cell-type-specific alternative splicing in spinocerebellar ataxia type 6
    • Tsunemi, T. et al. (2008) Cell-type-specific alternative splicing in spinocerebellar ataxia type 6. Neurosci. Lett. 447, 78-81
    • (2008) Neurosci. Lett. , vol.447 , pp. 78-81
    • Tsunemi, T.1
  • 46
    • 78149430698 scopus 로고    scopus 로고
    • Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties
    • PLoS ONE
    • Harris, G.M. et al. (2010) Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties. PLoS ONE 5, e13695
    • (2010) , vol.5
    • Harris, G.M.1
  • 47
    • 77954656232 scopus 로고    scopus 로고
    • Increased transcript diversity: novel splicing variants of Machado-Joseph disease gene (ATXN3)
    • Bettencourt, C. et al. (2010) Increased transcript diversity: novel splicing variants of Machado-Joseph disease gene (ATXN3). Neurogenetics 11, 193-202
    • (2010) Neurogenetics , vol.11 , pp. 193-202
    • Bettencourt, C.1
  • 48
    • 51349107479 scopus 로고    scopus 로고
    • Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure
    • Parry, D.A.D. et al. (2008) Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J. Struct. Biol. 163, 258-269
    • (2008) J. Struct. Biol. , vol.163 , pp. 258-269
    • Parry, D.A.D.1
  • 49
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • Takahashi, T. et al. (2007) Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum. Mol. Genet. 17, 345-356
    • (2007) Hum. Mol. Genet. , vol.17 , pp. 345-356
    • Takahashi, T.1
  • 50
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M. et al. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1
  • 51
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases
    • Perutz, M.F. et al. (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. U.S.A. 91, 5355-5358
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5355-5358
    • Perutz, M.F.1
  • 52
    • 37549011420 scopus 로고    scopus 로고
    • In-cell aggregation of a polyglutaminecontaining chimera is a multistep process initiated by the flanking sequence
    • Ignatova, Z. et al. (2007) In-cell aggregation of a polyglutaminecontaining chimera is a multistep process initiated by the flanking sequence. J. Biol. Chem. 282, 36736-36743
    • (2007) J. Biol. Chem. , vol.282 , pp. 36736-36743
    • Ignatova, Z.1
  • 53
    • 0035976971 scopus 로고    scopus 로고
    • Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
    • Tanaka, M. et al. (2001) Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J. Biol. Chem. 276, 45470-45475
    • (2001) J. Biol. Chem. , vol.276 , pp. 45470-45475
    • Tanaka, M.1
  • 54
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • Thakur, A.K. et al. (2009) Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat. Struct. Mol. Biol. 16, 380-389
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 380-389
    • Thakur, A.K.1
  • 55
    • 78650441363 scopus 로고    scopus 로고
    • Essential role of coiled coils for aggregation and activity of Q/N-Rich prions and PolyQ proteins
    • Fiumara, F. et al. (2010) Essential role of coiled coils for aggregation and activity of Q/N-Rich prions and PolyQ proteins. Cell 143, 1121-1135
    • (2010) Cell , vol.143 , pp. 1121-1135
    • Fiumara, F.1
  • 56
    • 78049430399 scopus 로고    scopus 로고
    • Polyglutamine diseases: where does toxicity come from? What is toxicity? Where are we going? J
    • Takahashi, T. et al. (2010) Polyglutamine diseases: where does toxicity come from? What is toxicity? Where are we going? J. Mol. Cell Biol. 2, 180-191
    • (2010) Mol. Cell Biol. , vol.2 , pp. 180-191
    • Takahashi, T.1
  • 57
    • 33646831610 scopus 로고    scopus 로고
    • CA150 expression delays striatal cell death in overexpression and knock-in conditions for mutant huntingtin neurotoxicity
    • Arango, M. et al. (2006) CA150 expression delays striatal cell death in overexpression and knock-in conditions for mutant huntingtin neurotoxicity. J. Neurosci. 26, 4649-4659
    • (2006) J. Neurosci. , vol.26 , pp. 4649-4659
    • Arango, M.1
  • 58
    • 80052358032 scopus 로고    scopus 로고
    • Aggregation kinetics of interrupted polyglutamine peptides
    • Walters, R.H. and Murphy, R.M. (2011) Aggregation kinetics of interrupted polyglutamine peptides. J. Mol. Biol. 412, 505-519
    • (2011) J. Mol. Biol. , vol.412 , pp. 505-519
    • Walters, R.H.1    Murphy, R.M.2
  • 59
    • 0037406093 scopus 로고    scopus 로고
    • Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: a molecular approach
    • Sen, S. et al. (2003) Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: a molecular approach. Protein Sci. 12, 953-962
    • (2003) Protein Sci , vol.12 , pp. 953-962
    • Sen, S.1
  • 60
    • 70349194529 scopus 로고    scopus 로고
    • The impact of ataxin-1-like histidine insertions on polyglutamine aggregation
    • Jayaraman, M. et al. (2009) The impact of ataxin-1-like histidine insertions on polyglutamine aggregation. Protein Eng. Des. Sel. 22, 469-478
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 469-478
    • Jayaraman, M.1
  • 61
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M. et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-133
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1
  • 62
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis, G.S. et al. (2009) Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet. 18, R156-R162
    • (2009) Hum. Mol. Genet. , vol.18
    • Pesiridis, G.S.1
  • 63
    • 77956155794 scopus 로고    scopus 로고
    • Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43
    • Fuentealba, R.A. et al. (2010) Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43. J. Biol. Chem. 285, 26304-26314
    • (2010) J. Biol. Chem. , vol.285 , pp. 26304-26314
    • Fuentealba, R.A.1
  • 64
    • 0034695569 scopus 로고    scopus 로고
    • Molecular basis of a yeast prion species barrier
    • Santoso, A. et al. (2000) Molecular basis of a yeast prion species barrier. Cell 100, 277-288
    • (2000) Cell , vol.100 , pp. 277-288
    • Santoso, A.1
  • 65
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: an epigenetic modifier of protein function in yeast
    • Sondheimer, N. and Lindquist, S. (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell 5, 163-172
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 66
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/ asparagine-rich regions: implications for their conserved function and the prediction of novel prions
    • Michelitsch, M.D. and Weissman, J.S. (2000) A census of glutamine/ asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. U.S.A. 97, 11910-11915
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 67
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
    • Elden, A.C. et al. (2010) Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 466, 1069-1075
    • (2010) Nature , vol.466 , pp. 1069-1075
    • Elden, A.C.1
  • 68
    • 77955647254 scopus 로고    scopus 로고
    • Towards the treatment of polyglutamine diseases: the modulatory role of protein context
    • Robertson, A.L. and Bottomley, S.P. (2010) Towards the treatment of polyglutamine diseases: the modulatory role of protein context. Curr. Med. Chem. 17, 3058-3068
    • (2010) Curr. Med. Chem. , vol.17 , pp. 3058-3068
    • Robertson, A.L.1    Bottomley, S.P.2
  • 70
    • 28944446477 scopus 로고    scopus 로고
    • Oligoproline effects on polyglutamine conformation and aggregation
    • Bhattacharyya, A. et al. (2006) Oligoproline effects on polyglutamine conformation and aggregation. J. Mol. Biol. 355, 524-535
    • (2006) J. Mol. Biol. , vol.355 , pp. 524-535
    • Bhattacharyya, A.1
  • 71
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong, H. et al. (2009) Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 137, 60-72
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1
  • 72
    • 72849148037 scopus 로고    scopus 로고
    • Posttranslational modification of ataxin-7 at lysine 257 prevents autophagy-mediated turnover of an N-terminal caspase-7 cleavage fragment
    • Mookerjee, S. et al. (2009) Posttranslational modification of ataxin-7 at lysine 257 prevents autophagy-mediated turnover of an N-terminal caspase-7 cleavage fragment. J. Neurosci. 29, 15134-15144
    • (2009) J. Neurosci. , vol.29 , pp. 15134-15144
    • Mookerjee, S.1
  • 73
    • 70350380989 scopus 로고    scopus 로고
    • Phosphorylation of threonine 3, implications for Huntingtin aggregation and neurotoxicity
    • Aiken, C.T. et al. (2009) Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity. J. Biol. Chem. 284, 29427-29436
    • (2009) J. Biol. Chem. , vol.284 , pp. 29427-29436
    • Aiken, C.T.1
  • 74
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of fulllength human mutant huntingtin induced disease pathogenesis in HD mice
    • Gu, X. et al. (2009) Serines 13 and 16 are critical determinants of fulllength human mutant huntingtin induced disease pathogenesis in HD mice. Neuron 64, 828-840
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1
  • 75
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • Thompson, L.M. et al. (2009) IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J. Cell Biol. 187, 1083-1099
    • (2009) J. Cell Biol. , vol.187 , pp. 1083-1099
    • Thompson, L.M.1
  • 76
    • 77957007354 scopus 로고    scopus 로고
    • SCA1-like disease in mice expressing wild-type ataxin-1 with a serine to aspartic acid replacement at residue 776
    • Duvick, L. et al. (2010) SCA1-like disease in mice expressing wild-type ataxin-1 with a serine to aspartic acid replacement at residue 776. Neuron 67, 929-935
    • (2010) Neuron , vol.67 , pp. 929-935
    • Duvick, L.1
  • 77
    • 42049086100 scopus 로고    scopus 로고
    • Opposing effects of polyglutamine expansion on native protein complexes contribute to SCA1
    • Lim, J. et al. (2008) Opposing effects of polyglutamine expansion on native protein complexes contribute to SCA1. Nature 452, 713-718
    • (2008) Nature , vol.452 , pp. 713-718
    • Lim, J.1
  • 78
    • 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. (2002) Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron 35, 843-854
    • (2002) Neuron , vol.35 , pp. 843-854
    • Katsuno, M.1
  • 79
    • 0037194896 scopus 로고    scopus 로고
    • Androgen-dependent neurodegeneration by polyglutamine-expanded human androgen receptor in Drosophila
    • Takeyama, K-I. et al. (2002) Androgen-dependent neurodegeneration by polyglutamine-expanded human androgen receptor in Drosophila. Neuron 35, 855-864
    • (2002) Neuron , vol.35 , pp. 855-864
    • Takeyama, K.-I.1
  • 80
    • 77957011660 scopus 로고    scopus 로고
    • Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy
    • Nedelsky, N.B. et al. (2010) Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy. Neuron 67, 936-952
    • (2010) Neuron , vol.67 , pp. 936-952
    • Nedelsky, N.B.1
  • 81
    • 36749043765 scopus 로고    scopus 로고
    • Overexpression of wild-type androgen receptor in muscle recapitulates polyglutamine disease
    • Monks, D.A. et al. (2007) Overexpression of wild-type androgen receptor in muscle recapitulates polyglutamine disease. Proc. Natl. Acad. Sci. U.S.A. 104, 18259-18264
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18259-18264
    • Monks, D.A.1
  • 82
    • 0028829596 scopus 로고
    • CAG expansion affects the expression of mutant Huntingtin in the Huntington's disease brain
    • Aronin, N. et al. (1995) CAG expansion affects the expression of mutant Huntingtin in the Huntington's disease brain. Neuron 15, 1193-1201
    • (1995) Neuron , vol.15 , pp. 1193-1201
    • Aronin, N.1
  • 83
    • 0029014180 scopus 로고
    • Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals
    • Servadio, A. et al. (1995) Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals. Nat. Genet. 10, 94-98
    • (1995) Nat. Genet. , vol.10 , pp. 94-98
    • Servadio, A.1
  • 84
    • 0030294345 scopus 로고    scopus 로고
    • Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats
    • Imbert, G. et al. (1996) Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats. Nat. Genet. 14, 285-291
    • (1996) Nat. Genet. , vol.14 , pp. 285-291
    • Imbert, G.1
  • 85
    • 33646884427 scopus 로고    scopus 로고
    • Stochastic kinetics of intracellular huntingtin aggregate formation
    • Colby, D.W. et al. (2006) Stochastic kinetics of intracellular huntingtin aggregate formation. Nat. Chem. Biol. 2, 319-323
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 319-323
    • Colby, D.W.1
  • 86
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
    • Subramaniam, S. et al. (2009) Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science 324, 1327-1330
    • (2009) Science , vol.324 , pp. 1327-1330
    • Subramaniam, S.1
  • 87
    • 0033568070 scopus 로고    scopus 로고
    • Rhes: a striatal-specific Ras homolog related to Dexras1
    • Falk, J.D. et al. (1999) Rhes: a striatal-specific Ras homolog related to Dexras1. J. Neurosci. Res. 57, 782-788
    • (1999) J. Neurosci. Res. , vol.57 , pp. 782-788
    • Falk, J.D.1
  • 88
    • 79952615363 scopus 로고    scopus 로고
    • Preferential accumulation of N-terminal mutant huntingtin in the nuclei of striatal neurons is regulated by phosphorylation
    • Havel, L.S. et al. (2011) Preferential accumulation of N-terminal mutant huntingtin in the nuclei of striatal neurons is regulated by phosphorylation. Hum. Mol. Genet. 20, 1424-1437
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1424-1437
    • Havel, L.S.1
  • 89
    • 29644433445 scopus 로고    scopus 로고
    • Selective degeneration and nuclear localization of mutant huntingtin in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk, J.M. et al. (2005) Selective degeneration and nuclear localization of mutant huntingtin in the YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 14, 3823-3835
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3823-3835
    • Van Raamsdonk, J.M.1
  • 90
    • 84355161952 scopus 로고    scopus 로고
    • Excitation-induced ataxin-3 aggregation in neurons from patients with Machado-Joseph disease
    • Koch, P. et al. (2011) Excitation-induced ataxin-3 aggregation in neurons from patients with Machado-Joseph disease. Nature 480, 543-546
    • (2011) Nature , vol.480 , pp. 543-546
    • Koch, P.1
  • 92
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley, J.F. et al. (2002) The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 99, 10417-10422
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10417-10422
    • Morley, J.F.1
  • 93
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • Ben-Zvi, A. et al. (2009) Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc. Natl. Acad. Sci. U.S.A. 106, 14914-14919
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1
  • 94
    • 84864332905 scopus 로고    scopus 로고
    • dSarm/Sarm1 is required for activation of an injury-induced axon death pathway
    • Osterloh, J.M. et al. (2012) dSarm/Sarm1 is required for activation of an injury-induced axon death pathway. Science 337, 481-484
    • (2012) Science , vol.337 , pp. 481-484
    • Osterloh, J.M.1
  • 95
    • 0035839104 scopus 로고    scopus 로고
    • The p400 complex is an essential E1A transformation target
    • Fuchs, M. et al. (2001) The p400 complex is an essential E1A transformation target. Cell 106, 297-307
    • (2001) Cell , vol.106 , pp. 297-307
    • Fuchs, M.1
  • 96
    • 80054097980 scopus 로고    scopus 로고
    • MED12, the mediator complex subunit 12 gene, is mutated at high frequency in uterine leiomyomas
    • Makinen, N. et al. (2011) MED12, the mediator complex subunit 12 gene, is mutated at high frequency in uterine leiomyomas. Science 334, 252-255
    • (2011) Science , vol.334 , pp. 252-255
    • Makinen, N.1
  • 97
    • 33646687963 scopus 로고    scopus 로고
    • A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration
    • Lim, J. et al. (2006) A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. Cell 125, 801-814
    • (2006) Cell , vol.125 , pp. 801-814
    • Lim, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.