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Volumn 19, Issue 5, 2003, Pages 233-238

Transcriptional abnormalities in Huntington disease

Author keywords

[No Author keywords available]

Indexed keywords

CAGA PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; ENKEPHALIN; GROWTH FACTOR; HUNTINGTIN; MUTANT PROTEIN; NEUROPEPTIDE; NEUROTRANSMITTER RECEPTOR; NUCLEAR PROTEIN; POLYGLUTAMINE; PROTEIN; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR SP1; UNCLASSIFIED DRUG;

EID: 0037408279     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9525(03)00074-X     Document Type: Review
Times cited : (480)

References (40)
  • 1
    • 0035164243 scopus 로고    scopus 로고
    • The molecular biology of huntington's disease
    • Ho L., et al. The molecular biology of huntington's disease. Psychol. Med. 31:2001;3-14.
    • (2001) Psychol. Med. , vol.31 , pp. 3-14
    • Ho, L.1
  • 2
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., et al. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature. 421:2003;373-379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1
  • 3
    • 17344363559 scopus 로고    scopus 로고
    • Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates
    • Martindale D., et al. Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat. Genet. 18:1998;150-154.
    • (1998) Nat. Genet. , vol.18 , pp. 150-154
    • Martindale, D.1
  • 4
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science. 277:1997;1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 5
    • 0035179456 scopus 로고    scopus 로고
    • Mutant protein in Huntington disease is resistant to proteolysis in affected brain
    • Dyer R.B., McMurray C.T. Mutant protein in Huntington disease is resistant to proteolysis in affected brain. Nat. Genet. 29:2001;270-278.
    • (2001) Nat. Genet. , vol.29 , pp. 270-278
    • Dyer, R.B.1    McMurray, C.T.2
  • 6
    • 18544368523 scopus 로고    scopus 로고
    • Huntingtin is present in the nucleus, interacts with the transcriptional corepressor C-terminal binding protein, and represses transcription
    • Kegel K.B., et al. Huntingtin is present in the nucleus, interacts with the transcriptional corepressor C-terminal binding protein, and represses transcription. J. Biol. Chem. 277:2002;7466-7476.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7466-7476
    • Kegel, K.B.1
  • 7
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative disorders
    • Stott K., et al. Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative disorders. Proc. Natl. Acad. Sci. U. S. A. 92:1995;6509-6513.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6509-6513
    • Stott, K.1
  • 8
    • 0001408324 scopus 로고    scopus 로고
    • Evidence for a recruitment and sequestration mechanism in Huntington's disease
    • P.S. Harper, & M. et al. Perutz. Oxford University Press
    • Preisinger E., et al. Evidence for a recruitment and sequestration mechanism in Huntington's disease. Harper P.S., Perutz M., et al. Glutamine Repeats and Neurodegenerative Diseases: Molecular Aspects. 2001;127-139 Oxford University Press.
    • (2001) Glutamine Repeats and Neurodegenerative Diseases: Molecular Aspects , pp. 127-139
    • Preisinger, E.1
  • 9
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease
    • Wyttenbach A., et al. Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease. Hum. Mol. Genet. 10:2001;1829-1845.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1
  • 10
    • 0037106523 scopus 로고    scopus 로고
    • Modulation of polyglutamine-induced cell death by genes identified by expression profiling
    • Kita H., et al. Modulation of polyglutamine-induced cell death by genes identified by expression profiling. Hum. Mol. Genet. 11:2002;2279-2287.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2279-2287
    • Kita, H.1
  • 11
    • 0037101835 scopus 로고    scopus 로고
    • Dysregulation of gene expression in the R6/2 model of polyglutamine disease parallel changes in muscle and brain
    • Luthi-Carter R., et al. Dysregulation of gene expression in the R6/2 model of polyglutamine disease parallel changes in muscle and brain. Hum. Mol. Genet. 11:2002;1911-1926.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1911-1926
    • Luthi-Carter, R.1
  • 12
    • 0037101837 scopus 로고    scopus 로고
    • Polyglutamine and transcription: Gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects
    • Luthi-Carter R., et al. Polyglutamine and transcription: gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects. Hum. Mol. Genet. 11:2002;1927-1937.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1927-1937
    • Luthi-Carter, R.1
  • 13
    • 0037101838 scopus 로고    scopus 로고
    • Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease
    • Chan E.Y.W., et al. Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease. Hum. Mol. Genet. 11:2002;1939-1951.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1939-1951
    • Chan, E.Y.W.1
  • 14
    • 0037101839 scopus 로고    scopus 로고
    • Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analysis
    • Sipione S., et al. Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analysis. Hum. Mol. Genet. 11:2002;1953-1965.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1953-1965
    • Sipione, S.1
  • 15
    • 0036720019 scopus 로고    scopus 로고
    • Mouse and fly models of neurodegeneration
    • Zoghbi H.Y., Botas J. Mouse and fly models of neurodegeneration. Trends Genet. 18:2002;463-471.
    • (2002) Trends Genet. , vol.18 , pp. 463-471
    • Zoghbi, H.Y.1    Botas, J.2
  • 16
    • 0035862874 scopus 로고    scopus 로고
    • Abnormalities in the functioning of adipocytes from R6/2 mice that are transgenic for the Huntington's disease mutation
    • Fain J.N., et al. Abnormalities in the functioning of adipocytes from R6/2 mice that are transgenic for the Huntington's disease mutation. Hum. Mol. Genet. 10:2001;145-152.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 145-152
    • Fain, J.N.1
  • 17
    • 0037101970 scopus 로고    scopus 로고
    • Function and Regulation of CREB family transcription factors in the nervous system
    • Lonze B.E., Ginty D.D. Function and Regulation of CREB family transcription factors in the nervous system. Neuron. 35:2002;605-623.
    • (2002) Neuron , vol.35 , pp. 605-623
    • Lonze, B.E.1    Ginty, D.D.2
  • 18
    • 0035937523 scopus 로고    scopus 로고
    • Interference by Huntingtin and Atrophin-1 with CBP-mediated transcription leading to cellular toxicity
    • Nucifora F.C. Jr, et al. Interference by Huntingtin and Atrophin-1 with CBP-mediated transcription leading to cellular toxicity. Science. 291:2001;2423-2428.
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora F.C., Jr.1
  • 19
    • 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. 9:2000;2197-2202.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2197-2202
    • McCampbell, A.1
  • 20
    • 0033818112 scopus 로고    scopus 로고
    • II130, interfering with CREB-dependent transcription
    • II130, interfering with CREB-dependent transcription. Nat. Genet. 26:2000;29-36.
    • (2000) Nat. Genet. , vol.26 , pp. 29-36
    • Shimohata, T.1
  • 21
    • 0036578784 scopus 로고    scopus 로고
    • Disruption of CREB function in brain leads to neurodegeneration
    • Mantamadiotis T., et al. Disruption of CREB function in brain leads to neurodegeneration. Nat. Genet. 31:2002;47-54.
    • (2002) Nat. Genet. , vol.31 , pp. 47-54
    • Mantamadiotis, T.1
  • 22
    • 0035976953 scopus 로고    scopus 로고
    • The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease
    • Chai Y., et al. The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease. J. Biol. Chem. 276:2001;44889-44897.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44889-44897
    • Chai, Y.1
  • 23
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan J.S., et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature. 413:2001;739-743.
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1
  • 24
    • 0037090927 scopus 로고    scopus 로고
    • Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice
    • Yu Z.-X., et al. Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice. Hum. Mol. Genet. 11:2002;905-914.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 905-914
    • Yu, Z.-X.1
  • 25
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien D.L., et al. Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat. Cell Biol. 4:2002;806-810.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 806-810
    • Stenoien, D.L.1
  • 26
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
    • Chai Y., et al. Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 99:2002;9310-9315.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9310-9315
    • Chai, Y.1
  • 27
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah A.W., et al. Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science. 296:2002;2238-2243.
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1
  • 28
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transciptional activator Sp1
    • Li S.-H., et al. Interaction of Huntington disease protein with transciptional activator Sp1. Mol. Cell. Biol. 22:2002;1277-1287.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1277-1287
    • Li, S.-H.1
  • 29
    • 0035038460 scopus 로고    scopus 로고
    • Extended polyglutamine selectively interacts with caspase-8 and -10 in nuclear aggregates
    • U M., et al. Extended polyglutamine selectively interacts with caspase-8 and -10 in nuclear aggregates. Cell Death Differ. 8:2001;377-386.
    • (2001) Cell Death Differ. , vol.8 , pp. 377-386
    • U, M.1
  • 30
    • 0036848793 scopus 로고    scopus 로고
    • Purification of polyglutamine aggregates and identification of elongation factor-1a and heat shock protein 84 as aggregate-interacting proteins
    • Mitsui K., et al. Purification of polyglutamine aggregates and identification of elongation factor-1a and heat shock protein 84 as aggregate-interacting proteins. J. Neurosci. 22:2002;9267-9277.
    • (2002) J. Neurosci. , vol.22 , pp. 9267-9277
    • Mitsui, K.1
  • 31
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Neil F., et al. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Neil, F.1
  • 32
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease
    • Hockly E., et al. Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 100:2003;2041-2046.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2041-2046
    • Hockly, E.1
  • 33
    • 0037150524 scopus 로고    scopus 로고
    • A glutamine-rich trail leads to transcription factors
    • Freiman R.N., Tjian R. A glutamine-rich trail leads to transcription factors. Science. 296:2002;2149-2150.
    • (2002) Science , vol.296 , pp. 2149-2150
    • Freiman, R.N.1    Tjian, R.2
  • 34
    • 12944263711 scopus 로고    scopus 로고
    • The huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription
    • Steffan J.S., et al. The huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc. Natl. Acad. Sci. U. S. A. 97:2000;6763-6768.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6763-6768
    • Steffan, J.S.1
  • 35
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone binding protein with two independent transcriptional corepressor activities
    • Li F., et al. Ataxin-3 is a histone binding protein with two independent transcriptional corepressor activities. J. Biol. Chem. 277:2002;45004-45012.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45004-45012
    • Li, F.1
  • 36
    • 0032833981 scopus 로고    scopus 로고
    • Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin
    • Boutell J.M., et al. Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin. Hum. Mol. Genet. 8:1999;1647-1655.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1647-1655
    • Boutell, J.M.1
  • 37
    • 0141742228 scopus 로고    scopus 로고
    • The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-κB/Rel/dorsal family transcription factor
    • Takano H., Gusella J.F. The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-κB/Rel/dorsal family transcription factor. BMC Neurosci. 3:2002;15-27.
    • (2002) BMC Neurosci. , vol.3 , pp. 15-27
    • Takano, H.1    Gusella, J.F.2
  • 38
    • 0035852687 scopus 로고    scopus 로고
    • The Gln-Ala repeat transcriptional activitor CA150 interacts with huntingtin: Neuropathologic and genetic eveidence for a role in Huntington's disease pathogenesis
    • Holbert S., et al. The Gln-Ala repeat transcriptional activitor CA150 interacts with huntingtin: neuropathologic and genetic eveidence for a role in Huntington's disease pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 98:2001;1811-1816.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1811-1816
    • Holbert, S.1
  • 39
    • 0036797242 scopus 로고    scopus 로고
    • Polyglutamine protein aggregates are dynamic
    • Kim S., et al. Polyglutamine protein aggregates are dynamic. Nat. Cell Biol. 4:2002;826-831.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 826-831
    • Kim, S.1
  • 40
    • 0037072807 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3b inhibitors prevent cellular polyglutamine toxicity caused by the Huntington's disease mutation
    • Carmichael J., et al. Glycogen synthase kinase-3b inhibitors prevent cellular polyglutamine toxicity caused by the Huntington's disease mutation. J. Biol. Chem. 277:2002;33791-33798.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33791-33798
    • Carmichael, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.