메뉴 건너뛰기




Volumn 62, Issue 17, 2005, Pages 1901-1912

Synaptic dysfunction in Huntington's disease: A new perspective

Author keywords

Endocytosis; Exocytosis; Huntington's disease; Neurotransmission; Pathophysiology; Synaptic protein

Indexed keywords

HUNTINGTIN;

EID: 24344461460     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-005-5084-5     Document Type: Review
Times cited : (136)

References (135)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • 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
  • 4
    • 0030712094 scopus 로고    scopus 로고
    • Transgenic mouse models of neurodegenerative disease caused by CAG/polyglutamine expansions
    • Bates G. P. and Davies S. W. (1997) Transgenic mouse models of neurodegenerative disease caused by CAG/polyglutamine expansions. Mol. Med. Today 3: 508-515
    • (1997) Mol. Med. Today , vol.3 , pp. 508-515
    • Bates, G.P.1    Davies, S.W.2
  • 6
    • 0032052003 scopus 로고    scopus 로고
    • Huntingtin protein colocalizes with lesions of neurodegenerative diseases: An investigation in Huntington's, Alzheimer's and Pick's diseases
    • Singhrao S. K., Thomas P., Wood J. D., MacMillan J. C., Neal J. W., Harper P. S. et al. (1998) Huntingtin protein colocalizes with lesions of neurodegenerative diseases: an investigation in Huntington's, Alzheimer's and Pick's diseases. Exp. Neurol. 150: 213-222
    • (1998) Exp. Neurol. , vol.150 , pp. 213-222
    • Singhrao, S.K.1    Thomas, P.2    Wood, J.D.3    MacMillan, J.C.4    Neal, J.W.5    Harper, P.S.6
  • 7
    • 0033007867 scopus 로고    scopus 로고
    • Expression of the Huntington's disease gene is regulated in astrocytes in the arcuate nucleus of the hypothalamus of postpartum rats
    • Hebb M. O., Denovan-Wright E. M. and Robertson H. A. (1999) Expression of the Huntington's disease gene is regulated in astrocytes in the arcuate nucleus of the hypothalamus of postpartum rats. FASEB J. 13: 1099-1106
    • (1999) FASEB J. , vol.13 , pp. 1099-1106
    • Hebb, M.O.1    Denovan-Wright, E.M.2    Robertson, H.A.3
  • 8
    • 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., Hanson S. A., Strand A. D., Bergstrom D. A., Chun W., Peters N. L. et al. (2002) Dysregulation of gene expression in the R6/2 model of polyglutamine disease: parallel changes in muscle and brain. Hum. Mol. Genet. 11: 1911-1926
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1911-1926
    • Luthi-Carter, R.1    Hanson, S.A.2    Strand, A.D.3    Bergstrom, D.A.4    Chun, W.5    Peters, N.L.6
  • 9
    • 0141866674 scopus 로고    scopus 로고
    • Inclusion formation in Huntington's disease R6/2 mouse muscle cultures
    • Orth M., Cooper J. M., Bates G. P. and Schapira A. H. (2003) Inclusion formation in Huntington's disease R6/2 mouse muscle cultures. J. Neurochem. 87: 1-6
    • (2003) J. Neurochem. , vol.87 , pp. 1-6
    • Orth, M.1    Cooper, J.M.2    Bates, G.P.3    Schapira, A.H.4
  • 10
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I., Levine M. S. and Zeitlin S. (2000) Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat. Genet. 26: 300-306
    • (2000) Nat. Genet. , vol.26 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 11
    • 0037002444 scopus 로고    scopus 로고
    • Huntington's disease of the endocrine pancreas: Insulin deficiency and diabetes mellitus due to impaired insulin gene expression
    • Andreassen O. A., Dedeoglu A., Stanojevic V., Hughes D. B., Browne S. E., Leech C. A. et al. (2002) Huntington's disease of the endocrine pancreas: insulin deficiency and diabetes mellitus due to impaired insulin gene expression. Neurobiol. Dis. 11: 410-424
    • (2002) Neurobiol. Dis. , vol.11 , pp. 410-424
    • Andreassen, O.A.1    Dedeoglu, A.2    Stanojevic, V.3    Hughes, D.B.4    Browne, S.E.5    Leech, C.A.6
  • 12
    • 20044392282 scopus 로고    scopus 로고
    • The R6/2 transgenic mouse model of Huntington's disease develops diabetes due to deficient {beta}-cell mass and exocytosis
    • in press
    • Bjorkqvist M., Fex M., Renstrom E., Wierup N., Petersen A., Gil J. et al. (2005) The R6/2 transgenic mouse model of Huntington's disease develops diabetes due to deficient {beta}-cell mass and exocytosis. Hum. Mol. Genet., in press
    • (2005) Hum. Mol. Genet.
    • Bjorkqvist, M.1    Fex, M.2    Renstrom, E.3    Wierup, N.4    Petersen, A.5    Gil, J.6
  • 13
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia M., Sapp E., Chase K., Schwarz C., Meloni A., Young C. et al. (1995) Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14: 1075-1081
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3    Schwarz, C.4    Meloni, A.5    Young, C.6
  • 14
    • 0031867231 scopus 로고    scopus 로고
    • Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways
    • Velier J., Kim M., Schwarz C., Kim T. W., Sapp E., Chase K. et al. (1998) Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways. Exp. Neurol. 152: 34-40
    • (1998) Exp. Neurol. , vol.152 , pp. 34-40
    • Velier, J.1    Kim, M.2    Schwarz, C.3    Kim, T.W.4    Sapp, E.5    Chase, K.6
  • 15
    • 0032190391 scopus 로고    scopus 로고
    • The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): Comparison with huntingtin in rat and human
    • Gutekunst C. A., Li S. H., Yi H., Ferrante R. J., Li X. J. and Hersch S. M. (1998) The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): comparison with huntingtin in rat and human. J. Neurosci. 18: 7674-7686
    • (1998) J. Neurosci. , vol.18 , pp. 7674-7686
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3    Ferrante, R.J.4    Li, X.J.5    Hersch, S.M.6
  • 17
    • 0029055717 scopus 로고
    • Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes
    • Nasir J., Floresco S. B., O'Kusky J. R., Diewert V. M., Richman J. M., Zeisler J. et al. (1995) Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioral and morphological changes in heterozygotes. Cell 81: 811-823
    • (1995) Cell , vol.81 , pp. 811-823
    • Nasir, J.1    Floresco, S.B.2    O'Kusky, J.R.3    Diewert, V.M.4    Richman, J.M.5    Zeisler, J.6
  • 19
    • 0037131263 scopus 로고    scopus 로고
    • Calcium-dependent cleavage of endogenous wild-type huntingtin in primary cortical neurons
    • Goffredo D., Rigamonti D., Tartari M., De Micheli A., Verderio C., Matteoli M. et al. (2002) Calcium-dependent cleavage of endogenous wild-type huntingtin in primary cortical neurons. J. Biol. Chem. 277: 39594-39598
    • (2002) J. Biol. Chem. , vol.277 , pp. 39594-39598
    • Goffredo, D.1    Rigamonti, D.2    Tartari, M.3    De Micheli, A.4    Verderio, C.5    Matteoli, M.6
  • 20
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li S. H. and Li X. J. (2004) Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet. 20: 146-154
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 21
    • 0030726894 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 (HAP1) interacts with the p150(Glued) subunit of dynactin
    • Engelender S., Sharp A. H., Colomer V., Tokito M. K., Lanahan A., Worley P. et al. (1997) Huntingtin-associated protein 1 (HAP1) interacts with the p150(Glued) subunit of dynactin. Hum. Mol. Genet. 6: 2205-2212
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 2205-2212
    • Engelender, S.1    Sharp, A.H.2    Colomer, V.3    Tokito, M.K.4    Lanahan, A.5    Worley, P.6
  • 23
    • 4444316194 scopus 로고    scopus 로고
    • Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro
    • Trushina E., Dyer R. B., Badger J. D. 2nd, Ure D., Eide L., Tran D. D. et al. (2004) Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro. Mol. Cell. Biol. 24: 8195-8209
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8195-8209
    • Trushina, E.1    Dyer, R.B.2    Badger II, J.D.3    Ure, D.4    Eide, L.5    Tran, D.D.6
  • 24
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • Gauthier L. R., Charrin B. C., Borrell-Pages M., Dompierre J. P., Rangone H., Cordelieres F. P. et al. (2004) Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell 118: 127-138
    • (2004) Cell , vol.118 , pp. 127-138
    • Gauthier, L.R.1    Charrin, B.C.2    Borrell-Pages, M.3    Dompierre, J.P.4    Rangone, H.5    Cordelieres, F.P.6
  • 25
    • 0029152808 scopus 로고
    • Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies
    • Gutekunst C. A., Levey A. I., Heilman C. J., Whaley W. L., Yi H., Nash N. R. et al. (1995) Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc. Natl. Acad. Sci. USA 92: 8710-8714
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8710-8714
    • Gutekunst, C.A.1    Levey, A.I.2    Heilman, C.J.3    Whaley, W.L.4    Yi, H.5    Nash, N.R.6
  • 26
    • 0036500862 scopus 로고    scopus 로고
    • Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: Relevance to Huntington's disease
    • Hoffner G., Kahlem P. and Djian P. (2002) Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease. J. Cell Sci. 115: 941-948
    • (2002) J. Cell Sci. , vol.115 , pp. 941-948
    • Hoffner, G.1    Kahlem, P.2    Djian, P.3
  • 27
    • 10744224530 scopus 로고    scopus 로고
    • Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport
    • Szebenyi G., Morfini G. A., Babcock A., Gould M., Selkoe K., Stenoien D. L. et al. (2003) Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron 40: 41-52
    • (2003) Neuron , vol.40 , pp. 41-52
    • Szebenyi, G.1    Morfini, G.A.2    Babcock, A.3    Gould, M.4    Selkoe, K.5    Stenoien, D.L.6
  • 28
    • 0141750470 scopus 로고    scopus 로고
    • Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila
    • Gunawardena S., Her L. S., Brusch R. G., Laymon R. A., Niesman I. R., Gordesky-Gold B. et al. (2003) Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila. Neuron 40: 25-40
    • (2003) Neuron , vol.40 , pp. 25-40
    • Gunawardena, S.1    Her, L.S.2    Brusch, R.G.3    Laymon, R.A.4    Niesman, I.R.5    Gordesky-Gold, B.6
  • 29
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A. and Brundin P. (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40: 427-446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 30
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink A. L. (1999) Chaperone-mediated protein folding. Physiol. Rev. 79: 425-449
    • (1999) Physiol. Rev. , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 31
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F. U. and Hayer-Hartl M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 32
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes A., Lindenberg K. S., Ben-Haiem L., Weber C., Devys D., Landwehrmeyer G. B. et al. (2002) Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol. Cell. 10: 259-269
    • (2002) Mol. Cell. , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3    Weber, C.4    Devys, D.5    Landwehrmeyer, G.B.6
  • 33
    • 0042921188 scopus 로고    scopus 로고
    • Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release
    • Li H., Wyman T., Yu Z. X., Li S. H. and Li X. J. (2003) Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release. Hum. Mol. Genet. 12: 2021-2030
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2021-2030
    • Li, H.1    Wyman, T.2    Yu, Z.X.3    Li, S.H.4    Li, X.J.5
  • 34
    • 0842322740 scopus 로고    scopus 로고
    • Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction
    • Qin Z. H., Wang Y., Sapp E., Cuiffo B., Wanker E., Hayden M. R. et al. (2004) Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction. J. Neurosci. 24: 269-281
    • (2004) J. Neurosci. , vol.24 , pp. 269-281
    • Qin, Z.H.1    Wang, Y.2    Sapp, E.3    Cuiffo, B.4    Wanker, E.5    Hayden, M.R.6
  • 35
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S., Boeddrich A., Lurz R., Scherzinger E., Lueder G., Lehrach H. et al. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell 12: 1393-1407
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6
  • 36
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi H., Mitsui K., Kurosawa M., Machida Y., Kuroiwa Y. and Nukina N. (2004) Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett. 571: 171-176
    • (2004) FEBS Lett. , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 38
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H., Breuer P., Hayer-Hartl M. K. and Hartl F. U. (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl. Acad. Sci. USA 99 (suppl. 4): 16412-16418
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.4 SUPPL. , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 40
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora F. C. Jr, Sasaki M., Peters M. F., Huang H., Cooper J. K., Yamada M. et al. (2001) Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291: 2423-2428.
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora Jr., F.C.1    Sasaki, M.2    Peters, M.F.3    Huang, H.4    Cooper, J.K.5    Yamada, M.6
  • 41
    • 1042289730 scopus 로고    scopus 로고
    • Decreased cAMP response element-mediated transcription: An early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis
    • Sugars K. L., Brown R., Cook L. J., Swartz J. and Rubinsztein D. C. (2004) Decreased cAMP response element-mediated transcription: an early event in exon 1 and full-length cell models of Huntington's disease that contributes to polyglutamine pathogenesis. J. Biol. Chem. 279: 4988-4999
    • (2004) J. Biol. Chem. , vol.279 , pp. 4988-4999
    • Sugars, K.L.1    Brown, R.2    Cook, L.J.3    Swartz, J.4    Rubinsztein, D.C.5
  • 42
    • 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., Swartz J., Kita H., Thykjaer T., Carmichael J., Bradley J. et al. (2001) 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: 1829-1845
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1    Swartz, J.2    Kita, H.3    Thykjaer, T.4    Carmichael, J.5    Bradley, J.6
  • 43
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato C., Tartari M., Crotti A., Goffredo D., Valenza M., Conti L. et al. (2003) Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat. Genet. 35: 76-83
    • (2003) Nat. Genet. , vol.35 , pp. 76-83
    • Zuccato, C.1    Tartari, M.2    Crotti, A.3    Goffredo, D.4    Valenza, M.5    Conti, L.6
  • 44
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator sp1
    • Li S. H., Cheng A. L., Zhou H., Lam S., Rao M., Li H. et al. (2002) Interaction of Huntington disease protein with transcriptional activator sp1. Mol. Cell. Biol. 22: 1277-1287
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1277-1287
    • Li, S.H.1    Cheng, A.L.2    Zhou, H.3    Lam, S.4    Rao, M.5    Li, H.6
  • 45
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah A. W., Jeong H., Griffin A., Kim Y. M., Standaert D. G., Hersch S. M. et al. (2002) Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296: 2238-2243
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3    Kim, Y.M.4    Standaert, D.G.5    Hersch, S.M.6
  • 46
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars K. L. and Rubinsztein D. C. (2003) Transcriptional abnormalities in Huntington disease. Trends Genet. 19: 233-238
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 47
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease
    • Landles C. and Bates G. P. (2004) Huntingtin and the molecular pathogenesis of Huntington's disease. EMBO Rep. 5: 958-963
    • (2004) EMBO Rep. , vol.5 , pp. 958-963
    • Landles, C.1    Bates, G.P.2
  • 48
    • 0742287915 scopus 로고    scopus 로고
    • CRE-mediated transcription is increased in Huntington's disease transgenic mice
    • Obrietan K. and Hoyt K. R. (2004) CRE-mediated transcription is increased in Huntington's disease transgenic mice. J. Neurosci. 24: 791-796
    • (2004) J. Neurosci. , vol.24 , pp. 791-796
    • Obrietan, K.1    Hoyt, K.R.2
  • 49
    • 0037090927 scopus 로고    scopus 로고
    • Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice
    • Yu Z. X., Li S. H., Nguyen H. P. and Li X. J. (2002) Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice. Hum. Mol. Genet. 11: 905-914
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 905-914
    • Yu, Z.X.1    Li, S.H.2    Nguyen, H.P.3    Li, X.J.4
  • 50
    • 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., Strand A. D., Hanson S. A., Kooperberg C., Schilling G., La Spada A. R. et al. (2002) Polyglutamine and transcription: gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects. Hum. Mol. Genet. 11: 1927-1937
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1927-1937
    • Luthi-Carter, R.1    Strand, A.D.2    Hanson, S.A.3    Kooperberg, C.4    Schilling, G.5    La Spada, A.R.6
  • 51
    • 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., Luthi-Carter R., Strand A., Solano S. M., Hanson S. A., DeJohn M. M. et al. (2002) Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease. Hum. Mol. Genet. 11: 1939-1951
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1939-1951
    • Chan, E.Y.1    Luthi-Carter, R.2    Strand, A.3    Solano, S.M.4    Hanson, S.A.5    DeJohn, M.M.6
  • 52
    • 0037101839 scopus 로고    scopus 로고
    • Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analyses
    • Sipione S., Rigamonti D., Valenza M., Zuccato C., Conti L., Pritchard J. et al. (2002) Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analyses. Hum. Mol. Genet. 11: 1953-1965
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1953-1965
    • Sipione, S.1    Rigamonti, D.2    Valenza, M.3    Zuccato, C.4    Conti, L.5    Pritchard, J.6
  • 53
    • 0029796093 scopus 로고    scopus 로고
    • Identification of potential target genes for the neuron restrictive silencer factor
    • Schoenherr C. J., Paquette A. J. and Anderson D. J. (1996) Identification of potential target genes for the neuron restrictive silencer factor. Proc. Natl. Acad. Sci. USA 93: 9881-9886
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9881-9886
    • Schoenherr, C.J.1    Paquette, A.J.2    Anderson, D.J.3
  • 54
    • 0142184100 scopus 로고    scopus 로고
    • Huntington's disease: A synaptopathy?
    • Li J. Y., Plomann M. and Brundin P. (2003) Huntington's disease: a synaptopathy? Trends Mol. Med. 9: 414-420
    • (2003) Trends Mol. Med. , vol.9 , pp. 414-420
    • Li, J.Y.1    Plomann, M.2    Brundin, P.3
  • 55
  • 56
    • 0035030442 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotransmitter release
    • Fon E. A. and Edwards R. H. (2001) Molecular mechanisms of neurotransmitter release. Muscle Nerve 24: 581-601
    • (2001) Muscle Nerve , vol.24 , pp. 581-601
    • Fon, E.A.1    Edwards, R.H.2
  • 57
    • 2342544141 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of presynaptic assembly
    • Ziv N. E. and Garner C. C. (2004) Cellular and molecular mechanisms of presynaptic assembly. Nat. Rev. Neurosci. 5: 385-399
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 385-399
    • Ziv, N.E.1    Garner, C.C.2
  • 58
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2) and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach A., Carmichael J., Swartz J., Furlong R. A., Narain Y., Rankin J. et al. (2000) Effects of heat shock, heat shock protein 40 (HDJ-2) and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl. Acad. Sci. USA 97: 2898-2903
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5    Rankin, J.6
  • 59
    • 0036382909 scopus 로고    scopus 로고
    • Abnormal phosphorylation of synapsin I predicts a neuronal transmission impairment in the R6/2 Huntington's disease transgenic mice
    • Lievens J. C., Woodman B., Mahal A. and Bates G. P. (2002) Abnormal phosphorylation of synapsin I predicts a neuronal transmission impairment in the R6/2 Huntington's disease transgenic mice. Mol. Cell. Neurosci. 20: 638-648
    • (2002) Mol. Cell. Neurosci. , vol.20 , pp. 638-648
    • Lievens, J.C.1    Woodman, B.2    Mahal, A.3    Bates, G.P.4
  • 60
    • 0036673069 scopus 로고    scopus 로고
    • Snares and Munc18 in synaptic vesicle fusion
    • Rizo J. and Sudhof T. C. (2002) Snares and Munc18 in synaptic vesicle fusion. Nat. Rev. Neurosci. 3: 64-653
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 64-653
    • Rizo, J.1    Sudhof, T.C.2
  • 61
    • 0035158533 scopus 로고    scopus 로고
    • Progressive depletion of complexin II in a transgenic mouse model of Huntington's disease
    • Morton A. J. and Edwardson J. M. (2001) Progressive depletion of complexin II in a transgenic mouse model of Huntington's disease. J. Neurochem. 76: 166-172
    • (2001) J. Neurochem. , vol.76 , pp. 166-172
    • Morton, A.J.1    Edwardson, J.M.2
  • 62
    • 0035883175 scopus 로고    scopus 로고
    • Abnormalities in the synaptic vesicle fusion machinery in Huntington's disease
    • Morton A. J., Faull R. L. and Edwardson J. M. (2001) Abnormalities in the synaptic vesicle fusion machinery in Huntington's disease. Brain Res. Bull. 56: 111-117
    • (2001) Brain Res. Bull. , vol.56 , pp. 111-117
    • Morton, A.J.1    Faull, R.L.2    Edwardson, J.M.3
  • 63
    • 0041731977 scopus 로고    scopus 로고
    • Expression of mutant huntingtin blocks exocytosis in PC12 cells by depletion of complexin II
    • Edwardson J. M., Wang C. T., Gong B., Wyttenbach A., Bai J., Jackson M. B. et al. (2003) Expression of mutant huntingtin blocks exocytosis in PC12 cells by depletion of complexin II. J. Biol. Chem. 278: 30849-30853
    • (2003) J. Biol. Chem. , vol.278 , pp. 30849-30853
    • Edwardson, J.M.1    Wang, C.T.2    Gong, B.3    Wyttenbach, A.4    Bai, J.5    Jackson, M.B.6
  • 64
    • 0141618325 scopus 로고    scopus 로고
    • Complexin II is essential for normal neurological function in mice
    • Glynn D., Bortnick R. A. and Morton A. J. (2003) Complexin II is essential for normal neurological function in mice. Hum. Mol. Genet. 12: 2431-2448
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2431-2448
    • Glynn, D.1    Bortnick, R.A.2    Morton, A.J.3
  • 65
    • 24344444735 scopus 로고    scopus 로고
    • Depletion of rabphilin 3A in a transgenic mouse model (R6/1) of Huntington's disease, a possible culprit in synaptic dysfunction
    • in press
    • Smith R., Petersen A., Bates G., Brundin P. and Li J. Y. (2005) Depletion of rabphilin 3A in a transgenic mouse model (R6/1) of Huntington's disease, a possible culprit in synaptic dysfunction. Neurobiol. Dis., in press
    • (2005) Neurobiol. Dis.
    • Smith, R.1    Petersen, A.2    Bates, G.3    Brundin, P.4    Li, J.Y.5
  • 66
    • 0029077932 scopus 로고
    • Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells
    • Chung S. H., Takai Y. and Holz R. W. (1995) Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells. J. Biol. Chem. 270: 16714-16718
    • (1995) J. Biol. Chem. , vol.270 , pp. 16714-16718
    • Chung, S.H.1    Takai, Y.2    Holz, R.W.3
  • 67
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Valtorta F., Czernik A. J. and Benfenati F. (1993) Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259: 780-785
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 68
    • 0022630780 scopus 로고
    • Synapsin I is a microtubule-bundling protein
    • Baines A. J. and Bennett V. (1986) Synapsin I is a microtubule-bundling protein. Nature 319: 145-147
    • (1986) Nature , vol.319 , pp. 145-147
    • Baines, A.J.1    Bennett, V.2
  • 69
    • 0035783462 scopus 로고    scopus 로고
    • Resistance to NMDA toxicity correlates with appearance of nuclear inclusions, behavioural deficits and changes in calcium homeostasis in mice transgenic for exon 1 of the huntington gene
    • Hansson O., Guatteo E., Mercuri N. B., Bernardi G., Li X. J., Castilho R. F. et al. (2001) Resistance to NMDA toxicity correlates with appearance of nuclear inclusions, behavioural deficits and changes in calcium homeostasis in mice transgenic for exon 1 of the huntington gene. Eur. J. Neurosci. 14: 1492-1504
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 1492-1504
    • Hansson, O.1    Guatteo, E.2    Mercuri, N.B.3    Bernardi, G.4    Li, X.J.5    Castilho, R.F.6
  • 70
    • 0346101741 scopus 로고    scopus 로고
    • Cysteine string protein (CSP) inhibition of N-type calcium channels is blocked by mutant huntingtin
    • Miller L. C., Swayne L. A., Chen L., Feng Z. P., Wacker J. L., Muchowski P. J. et al. (2003) Cysteine string protein (CSP) inhibition of N-type calcium channels is blocked by mutant huntingtin. J. Biol. Chem. 278: 53072-53081
    • (2003) J. Biol. Chem. , vol.278 , pp. 53072-53081
    • Miller, L.C.1    Swayne, L.A.2    Chen, L.3    Feng, Z.P.4    Wacker, J.L.5    Muchowski, P.J.6
  • 71
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1
    • Tang T. S., Tu H., Chan E. Y., Maximov A., Wang Z., Wellington C. L. et al. (2003) Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39: 227-239
    • (2003) Neuron , vol.39 , pp. 227-239
    • Tang, T.S.1    Tu, H.2    Chan, E.Y.3    Maximov, A.4    Wang, Z.5    Wellington, C.L.6
  • 72
    • 0032568517 scopus 로고    scopus 로고
    • Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human Huntington disease gene
    • Cha J. H., Kosinski C. M., Kerner J. A., Alsdorf S. A., Mangiarini L., Davies S. W. et al. (1998) Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human Huntington disease gene. Proc. Natl. Acad. Sci. USA 95: 6480-6485
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6480-6485
    • Cha, J.H.1    Kosinski, C.M.2    Kerner, J.A.3    Alsdorf, S.A.4    Mangiarini, L.5    Davies, S.W.6
  • 73
    • 0036850524 scopus 로고    scopus 로고
    • HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis
    • Singaraja R. R., Hadano S., Metzler M., Givan S., Wellington C. L., Warby S. et al. (2002) HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis. Hum. Mol. Genet. 11: 2815-2828
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2815-2828
    • Singaraja, R.R.1    Hadano, S.2    Metzler, M.3    Givan, S.4    Wellington, C.L.5    Warby, S.6
  • 74
    • 0036796261 scopus 로고    scopus 로고
    • PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains
    • Modregger J., DiProspero N. A., Charles V., Tagle D. A. and Plomann M. (2002) PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains. Hum. Mol. Genet. 11: 2547-2558
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2547-2558
    • Modregger, J.1    DiProspero, N.A.2    Charles, V.3    Tagle, D.A.4    Plomann, M.5
  • 75
    • 0030986659 scopus 로고    scopus 로고
    • HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain
    • Kalchman M. A., Koide H. B., McCutcheon K., Graham R. K., Nichol K., Nishiyama K. et al. (1997) HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nat. Genet.16: 44-53
    • (1997) Nat. Genet. , vol.16 , pp. 44-53
    • Kalchman, M.A.1    Koide, H.B.2    McCutcheon, K.3    Graham, R.K.4    Nichol, K.5    Nishiyama, K.6
  • 76
    • 0032186107 scopus 로고    scopus 로고
    • SH3GL3 associates with the huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates
    • Sittler A., Walter S., Wedemeyer N., Hasenbank R., Scherzinger E., Eickhoff H. et al. (1998) SH3GL3 associates with the huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates. Mol. Cell. 2: 427-436
    • (1998) Mol. Cell , vol.2 , pp. 427-436
    • Sittler, A.1    Walter, S.2    Wedemeyer, N.3    Hasenbank, R.4    Scherzinger, E.5    Eickhoff, H.6
  • 78
    • 0028803757 scopus 로고
    • A huntingtin-associated protein enriched in brain with implications for pathology
    • Li X. J., Li S. H., Sharp A. H., Nucifora F. C. Jr, Schilling G., Lanahan A. et al. (1995) A huntingtin-associated protein enriched in brain with implications for pathology. Nature 378: 398-402
    • (1995) Nature , vol.378 , pp. 398-402
    • Li, X.J.1    Li, S.H.2    Sharp, A.H.3    Nucifora Jr., F.C.4    Schilling, G.5    Lanahan, A.6
  • 79
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill S. R., Schroer T. A., Szilak I., Steuer E. R., Sheetz M. P. and Cleveland D. W. (1991) Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 115: 1639-1650
    • (1991) J. Cell Biol. , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 80
    • 0037008677 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 interacts with hepatocyte growth factor-regulated tyrosine kinase substrate and functions in endosomal trafficking
    • Li Y., Chin L. S., Levey A. I. and Li L. (2002) Huntingtin-associated protein 1 interacts with hepatocyte growth factor-regulated tyrosine kinase substrate and functions in endosomal trafficking. J. Biol. Chem. 277: 28212-28221
    • (2002) J. Biol. Chem. , vol.277 , pp. 28212-28221
    • Li, Y.1    Chin, L.S.2    Levey, A.I.3    Li, L.4
  • 81
    • 0033611051 scopus 로고    scopus 로고
    • An actin-binding protein of the Sla2/huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles
    • Engqvist-Goldstein A. E., Kessels M. M., Chopra V. S., Hayden M. R. and Drubin D. G. (1999) An actin-binding protein of the Sla2/huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J. Cell Biol. 147: 1503-1518
    • (1999) J. Cell Biol. , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, A.E.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 82
    • 0037205440 scopus 로고    scopus 로고
    • HIP1 and HIP12 display differential binding to F-actin, AP2 and clathrin. Identification of a novel interaction with clathrin light chain
    • Legendre-Guillemin V., Metzler M., Charbonneau M., Gan L., Chopra V., Philie J. et al. (2002) HIP1 and HIP12 display differential binding to F-actin, AP2 and clathrin. Identification of a novel interaction with clathrin light chain. J. Biol. Chem. 277: 19897-19904
    • (2002) J. Biol. Chem. , vol.277 , pp. 19897-19904
    • Legendre-Guillemin, V.1    Metzler, M.2    Charbonneau, M.3    Gan, L.4    Chopra, V.5    Philie, J.6
  • 83
    • 0037423214 scopus 로고    scopus 로고
    • Characterization of endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1
    • Modregger J., Schmidt A. A., Ritter B., Huttner W. B. and Plomann M. (2003) Characterization of endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1. J. Biol. Chem. 278: 4160-4167
    • (2003) J. Biol. Chem. , vol.278 , pp. 4160-4167
    • Modregger, J.1    Schmidt, A.A.2    Ritter, B.3    Huttner, W.B.4    Plomann, M.5
  • 84
    • 0035180327 scopus 로고    scopus 로고
    • Altered striatal amino acid neurotransmitter release monitored using microdialysis in R6/1 Huntington transgenic mice
    • Nicniocaill B., Haraldsson B., Hansson O., O'Connor W. T. and Brundin P. (2001) Altered striatal amino acid neurotransmitter release monitored using microdialysis in R6/1 Huntington transgenic mice. Eur. J. Neurosci. 13: 206-210
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 206-210
    • Nicniocaill, B.1    Haraldsson, B.2    Hansson, O.3    O'Connor, W.T.4    Brundin, P.5
  • 85
    • 0036345741 scopus 로고    scopus 로고
    • Impaired glutamate transport and glutamate-glutamine cycling: Downstream effects of the Huntington mutation
    • Behrens P. F., Franz P., Woodman B., Lindenberg K. S. and Landwehrmeyer G. B. (2002) Impaired glutamate transport and glutamate-glutamine cycling: downstream effects of the Huntington mutation. Brain 125: 1908-1922
    • (2002) Brain , vol.125 , pp. 1908-1922
    • Behrens, P.F.1    Franz, P.2    Woodman, B.3    Lindenberg, K.S.4    Landwehrmeyer, G.B.5
  • 86
    • 0031930027 scopus 로고    scopus 로고
    • Immunohistochemical localization of metabotropic glutamate receptors mGluR1a and mGluR2/3 in the rat basal ganglia
    • Testa C. M., Friberg I. K., Weiss S. W. and Standaert D. G. (1998) Immunohistochemical localization of metabotropic glutamate receptors mGluR1a and mGluR2/3 in the rat basal ganglia. J. Comp. Neurol. 390: 5-19
    • (1998) J. Comp. Neurol. , vol.390 , pp. 5-19
    • Testa, C.M.1    Friberg, I.K.2    Weiss, S.W.3    Standaert, D.G.4
  • 87
    • 0033844601 scopus 로고    scopus 로고
    • Regulation of neurotransmitter release by metabotropic glutamate receptors
    • Cartmell J. and Schoepp D. D. (2000) Regulation of neurotransmitter release by metabotropic glutamate receptors. J. Neurochem. 75: 889-907
    • (2000) J. Neurochem. , vol.75 , pp. 889-907
    • Cartmell, J.1    Schoepp, D.D.2
  • 88
    • 0033571743 scopus 로고    scopus 로고
    • Enhanced sensitivity to N-methyl-D-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease
    • Levine M. S., Klapstein G. J., Koppel A., Gruen E., Cepeda C., Vargas M. E. et al. (1999) Enhanced sensitivity to N-methyl-D-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease. J. Neurosci. Res. 58: 515-532
    • (1999) J. Neurosci. Res. , vol.58 , pp. 515-532
    • Levine, M.S.1    Klapstein, G.J.2    Koppel, A.3    Gruen, E.4    Cepeda, C.5    Vargas, M.E.6
  • 89
    • 0033136692 scopus 로고    scopus 로고
    • A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity and selective striatal neurodegeneration
    • Hodgson J. G., Agopyan N., Gutekunst C. A., Leavitt B. R., LePiane F., Singaraja R. et al. (1999) A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity and selective striatal neurodegeneration. Neuron 23: 181-192
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1    Agopyan, N.2    Gutekunst, C.A.3    Leavitt, B.R.4    LePiane, F.5    Singaraja, R.6
  • 90
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95
    • Sun Y., Savanenin A., Reddy P. H. and Liu Y. F. (2001) Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95. J. Biol. Chem. 276: 24713-24718
    • (2001) J. Biol. Chem. , vol.276 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3    Liu, Y.F.4
  • 91
    • 10744223572 scopus 로고    scopus 로고
    • Complex alteration of NMDA receptors in transgenic Huntington's disease mouse brain: Analysis of mRNA and protein expression, plasma membrane association, interacting proteins and phosphorylation
    • Luthi-Carter R., Apostol B. L., Dunah A. W., DeJohn M. M., Farrell L. A., Bates G. P. et al. (2003) Complex alteration of NMDA receptors in transgenic Huntington's disease mouse brain: analysis of mRNA and protein expression, plasma membrane association, interacting proteins and phosphorylation. Neurobiol. Dis. 14: 624-636
    • (2003) Neurobiol. Dis. , vol.14 , pp. 624-636
    • Luthi-Carter, R.1    Apostol, B.L.2    Dunah, A.W.3    DeJohn, M.M.4    Farrell, L.A.5    Bates, G.P.6
  • 92
    • 0030708576 scopus 로고    scopus 로고
    • Changes of NMDA receptor subunit (NR1, NR2B) and glutamate transporter (GLT1) mRNA expression in Huntington's disease - An in situ hybridization study
    • Arzberger T., Krampfl K., Leimgruber S. and Weindl A. (1997) Changes of NMDA receptor subunit (NR1, NR2B) and glutamate transporter (GLT1) mRNA expression in Huntington's disease - an in situ hybridization study. J. Neuropathol. Exp. Neurol. 56: 440-454
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 440-454
    • Arzberger, T.1    Krampfl, K.2    Leimgruber, S.3    Weindl, A.4
  • 93
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
    • Wyszynski M., Lin J., Rao A., Nigh E., Beggs A. H., Craig A. M. et al. (1997) Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature 385: 439-442
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6
  • 94
    • 0029731554 scopus 로고    scopus 로고
    • Physical and functional interaction of rabphilin-3A with alpha-actinin
    • Kato M., Sasaki T., Ohya T., Nakanishi H., Nishioka H., Imamura M. et al. (1996) Physical and functional interaction of rabphilin-3A with alpha-actinin. J. Biol. Chem. 271: 31775-31778
    • (1996) J. Biol. Chem. , vol.271 , pp. 31775-31778
    • Kato, M.1    Sasaki, T.2    Ohya, T.3    Nakanishi, H.4    Nishioka, H.5    Imamura, M.6
  • 95
    • 14844314896 scopus 로고    scopus 로고
    • Enhanced striatal NR2B-containing N-methyl-D-aspartate receptor mediated synaptic currents in a mouse model of Huntington disease
    • Li L., Murphy T. H., Hayden M. R. and Raymond L. A. (2004) Enhanced striatal NR2B-containing N-methyl-D-aspartate receptor mediated synaptic currents in a mouse model of Huntington disease. J. Neurophysiol. 92: 2738-2746
    • (2004) J. Neurophysiol. , vol.92 , pp. 2738-2746
    • Li, L.1    Murphy, T.H.2    Hayden, M.R.3    Raymond, L.A.4
  • 96
    • 1542346231 scopus 로고    scopus 로고
    • Regulation of proteins affecting NMDA receptor-induced excitotoxicity in a Huntington's mouse model
    • Jarabek B. R., Yasuda R. P. and Wolfe B. B. (2004) Regulation of proteins affecting NMDA receptor-induced excitotoxicity in a Huntington's mouse model. Brain 127: 505-516
    • (2004) Brain , vol.127 , pp. 505-516
    • Jarabek, B.R.1    Yasuda, R.P.2    Wolfe, B.B.3
  • 97
    • 0033587760 scopus 로고    scopus 로고
    • Transgenic mice expressing a Huntington's disease mutation are resistant to quinolinic acid-induced striatal excitotoxicity
    • Hansson O., Petersén Å., Leist M., Nicotera P., Castilho R. F. and Brundin P. (1999) Transgenic mice expressing a Huntington's disease mutation are resistant to quinolinic acid-induced striatal excitotoxicity. Proc. Natl. Acad. Sci. USA 96: 8727-8732
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8727-8732
    • Hansson, O.1    Petersén, Å.2    Leist, M.3    Nicotera, P.4    Castilho, R.F.5    Brundin, P.6
  • 98
    • 0034889544 scopus 로고    scopus 로고
    • Partial resistance to malonate-induced striatal cell death in transgenic mouse models of Huntington's disease is dependent on age and CAG repeat length
    • Hansson O., Castilho R. F., Korhonen L., Lindholm D., Bates G. P. and Brundin P. (2001) Partial resistance to malonate-induced striatal cell death in transgenic mouse models of Huntington's disease is dependent on age and CAG repeat length. J. Neurochem. 78: 694-703
    • (2001) J. Neurochem. , vol.78 , pp. 694-703
    • Hansson, O.1    Castilho, R.F.2    Korhonen, L.3    Lindholm, D.4    Bates, G.P.5    Brundin, P.6
  • 99
    • 0036469255 scopus 로고    scopus 로고
    • Immediate-early gene response to methamphetamine, haloperidol and quinolinic acid is not impaired in Huntington's disease transgenic mice
    • MacGibbon G. A., Hamilton L. C., Crocker S. F., Costain W. J., Murphy K. M., Robertson H. A. et al. (2002) Immediate-early gene response to methamphetamine, haloperidol and quinolinic acid is not impaired in Huntington's disease transgenic mice. J. Neurosci. Res. 67: 372-378
    • (2002) J. Neurosci. Res. , vol.67 , pp. 372-378
    • MacGibbon, G.A.1    Hamilton, L.C.2    Crocker, S.F.3    Costain, W.J.4    Murphy, K.M.5    Robertson, H.A.6
  • 100
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron M. M., Hansson O., Chen N., Wellington C. L., Leavitt B. R., Brundin P. et al. (2002) Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 33: 849-860
    • (2002) Neuron , vol.33 , pp. 849-860
    • Zeron, M.M.1    Hansson, O.2    Chen, N.3    Wellington, C.L.4    Leavitt, B.R.5    Brundin, P.6
  • 101
    • 0036254430 scopus 로고    scopus 로고
    • Maintenance of susceptibility to neurodegeneration following intrastriatal injections of quinolinic acid in a new transgenic mouse model of Huntington's disease
    • Petersen A., Chase K., Puschban Z., DiFiglia M., Brundin P. and Aronin N. (2002) Maintenance of susceptibility to neurodegeneration following intrastriatal injections of quinolinic acid in a new transgenic mouse model of Huntington's disease. Exp. Neurol. 175: 297-300
    • (2002) Exp. Neurol. , vol.175 , pp. 297-300
    • Petersen, A.1    Chase, K.2    Puschban, Z.3    DiFiglia, M.4    Brundin, P.5    Aronin, N.6
  • 102
    • 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., Sathasivam K., Seller M., Cozens B., Harper A., Hetherington C. 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    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5    Hetherington, C.6
  • 103
    • 0036453663 scopus 로고    scopus 로고
    • Evidence for dysfunction of the nigrostriatal pathway in the R6/1 line of transgenic Huntington's disease mice
    • Petersen A., Puschban Z., Lotharius J., NicNiocaill B., Wiekop P., O'Connor W. T. et al. (2002) Evidence for dysfunction of the nigrostriatal pathway in the R6/1 line of transgenic Huntington's disease mice. Neurobiol. Dis. 11: 134-146
    • (2002) Neurobiol. Dis. , vol.11 , pp. 134-146
    • Petersen, A.1    Puschban, Z.2    Lotharius, J.3    NicNiocaill, B.4    Wiekop, P.5    O'Connor, W.T.6
  • 104
    • 0034722642 scopus 로고    scopus 로고
    • N-Acetylaspartate and DARPP-32 levels decrease in the corpus striatum of Huntington's disease mice
    • van Dellen A., Welch J., Dixon R. M., Cordery P., York D., Styles P. et al. (2000) N-Acetylaspartate and DARPP-32 levels decrease in the corpus striatum of Huntington's disease mice. Neuroreport 11: 3751-3757
    • (2000) Neuroreport , vol.11 , pp. 3751-3757
    • Van Dellen, A.1    Welch, J.2    Dixon, R.M.3    Cordery, P.4    York, D.5    Styles, P.6
  • 106
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F., Finkbeiner S., Devys D. and Greenberg M. E. (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95: 55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 108
    • 0026077859 scopus 로고
    • The hypothalamic lateral tuberal nucleus and the characteristics of neuronal loss in Huntington's disease
    • Kremer H. P., Roos R. A., Dingjan G. M., Bots G. T., Bruyn G. W. and Hofman M. A. (1991) The hypothalamic lateral tuberal nucleus and the characteristics of neuronal loss in Huntington's disease. Neurosci. Lett. 132: 101-104
    • (1991) Neurosci. Lett. , vol.132 , pp. 101-104
    • Kremer, H.P.1    Roos, R.A.2    Dingjan, G.M.3    Bots, G.T.4    Bruyn, G.W.5    Hofman, M.A.6
  • 110
    • 0034049346 scopus 로고    scopus 로고
    • An autopsy case with clinically and molecular genetically diagnosed Huntington's disease with only minimal non-specific neuropathological findings
    • Mizuno H., Shibayama H., Tanaka F., Doyu M., Sobue G., Iwata H. et al. (2000) An autopsy case with clinically and molecular genetically diagnosed Huntington's disease with only minimal non-specific neuropathological findings. Clin. Neuropathol. 19: 94-103
    • (2000) Clin. Neuropathol. , vol.19 , pp. 94-103
    • Mizuno, H.1    Shibayama, H.2    Tanaka, F.3    Doyu, M.4    Sobue, G.5    Iwata, H.6
  • 111
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K. O., Davies S. W., Bates G. P., Vonsattel J. P. et al. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277: 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6
  • 112
    • 0021982117 scopus 로고
    • Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease
    • Graveland G. A., Williams R. S. and DiFiglia M. (1985) Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease. Science 227: 770-773
    • (1985) Science , vol.227 , pp. 770-773
    • Graveland, G.A.1    Williams, R.S.2    DiFiglia, M.3
  • 113
    • 0034994207 scopus 로고    scopus 로고
    • Early degenerative changes in transgenic mice expressing mutant huntingtin involve dendritic abnormalities but no impairment of mitochondrial energy production
    • Guidetti P., Charles V., Chen E. Y., Reddy P. H., Kordower J. H., Whetsell W. O. Jr. et al. (2001) Early degenerative changes in transgenic mice expressing mutant huntingtin involve dendritic abnormalities but no impairment of mitochondrial energy production. Exp. Neurol. 169: 340-350
    • (2001) Exp. Neurol. , vol.169 , pp. 340-350
    • Guidetti, P.1    Charles, V.2    Chen, E.Y.3    Reddy, P.H.4    Kordower, J.H.5    Whetsell Jr., W.O.6
  • 115
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling G., Becher M. W., Sharp A. H., Jinnah H. A., Duan K., Kotzuk J. A. et al. (1999) Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8: 397-407
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1    Becher, M.W.2    Sharp, A.H.3    Jinnah, H.A.4    Duan, K.5    Kotzuk, J.A.6
  • 117
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • Reddy P. H., Williams M., Charles V., Garrett L., Pike-Buchanan L., Whetsell W. O. Jr et al. (1998) Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA. Nat Genet 20: 198-202
    • (1998) Nat Genet , vol.20 , pp. 198-202
    • Reddy, P.H.1    Williams, M.2    Charles, V.3    Garrett, L.4    Pike-Buchanan, L.5    Whetsell Jr., W.O.6
  • 120
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
    • Bogdanov M. B., Andreassen O. A., Dedeoglu A., Ferrante R. J. and Beal M. F. (2001) Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease. J. Neurochem. 79: 1246-1249
    • (2001) J. Neurochem. , vol.79 , pp. 1246-1249
    • Bogdanov, M.B.1    Andreassen, O.A.2    Dedeoglu, A.3    Ferrante, R.J.4    Beal, M.F.5
  • 121
    • 0034915234 scopus 로고    scopus 로고
    • Comparative analysis of superoxide dismutase activity between acute pharmacological models and a transgenic mouse model of Huntington's disease
    • Santamaria A., Perez-Severiano F., Rodriguez-Martinez E., Maldonado P. D., Pedraza-Chaverri J., Rios C. et al. (2001) Comparative analysis of superoxide dismutase activity between acute pharmacological models and a transgenic mouse model of Huntington's disease. Neurochem. Res. 26: 419-424
    • (2001) Neurochem. Res. , vol.26 , pp. 419-424
    • Santamaria, A.1    Perez-Severiano, F.2    Rodriguez-Martinez, E.3    Maldonado, P.D.4    Pedraza-Chaverri, J.5    Rios, C.6
  • 122
    • 0033982887 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and free radical damage in the Huntington R6/2 transgenic mouse
    • Tabrizi S. J., Workman J., Hart P. E., Mangiarini L., Mahal A., Bates G. et al. (2000) Mitochondrial dysfunction and free radical damage in the Huntington R6/2 transgenic mouse. Ann. Neurol. 47: 80-86
    • (2000) Ann. Neurol. , vol.47 , pp. 80-86
    • Tabrizi, S.J.1    Workman, J.2    Hart, P.E.3    Mangiarini, L.4    Mahal, A.5    Bates, G.6
  • 123
    • 0037183717 scopus 로고    scopus 로고
    • Age-dependent changes in nitric oxide synthase activity and protein expression in striata of mice transgenic for the Huntington's disease mutation
    • Perez-Severiano F., Escalante B., Vergara P., Rios C. and Segovia J. (2002) Age-dependent changes in nitric oxide synthase activity and protein expression in striata of mice transgenic for the Huntington's disease mutation. Brain Res. 951: 36-42
    • (2002) Brain Res. , vol.951 , pp. 36-42
    • Perez-Severiano, F.1    Escalante, B.2    Vergara, P.3    Rios, C.4    Segovia, J.5
  • 124
    • 0035900181 scopus 로고    scopus 로고
    • Reduced activity and protein expression of NOS in R6/2 HD transgenic mice: Effects of L-NAME on symptom progression
    • Deckel A. W., Gordinier A., Nuttal D., Tang V., Kuwada C., Freitas R. et al. (2001) Reduced activity and protein expression of NOS in R6/2 HD transgenic mice: effects of L-NAME on symptom progression. Brain Res. 919: 70-81
    • (2001) Brain Res. , vol.919 , pp. 70-81
    • Deckel, A.W.1    Gordinier, A.2    Nuttal, D.3    Tang, V.4    Kuwada, C.5    Freitas, R.6
  • 125
    • 0037036055 scopus 로고    scopus 로고
    • Altered neuronal nitric oxide synthase expression contributes to disease progression in Huntington's disease transgenic mice
    • Deckel A. W., Tang V., Nuttal D., Gary K. and Elder R. (2002) Altered neuronal nitric oxide synthase expression contributes to disease progression in Huntington's disease transgenic mice. Brain Res. 939: 76-86
    • (2002) Brain Res. , vol.939 , pp. 76-86
    • Deckel, A.W.1    Tang, V.2    Nuttal, D.3    Gary, K.4    Elder, R.5
  • 126
    • 0035364748 scopus 로고    scopus 로고
    • Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration
    • Petersen A., Larsen K. E., Behr G. G., Romero N., Przedborski S., Brundin P. et al. (2001) Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration. Hum. Mol. Genet. 10: 1243-1254
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1243-1254
    • Petersen, A.1    Larsen, K.E.2    Behr, G.G.3    Romero, N.4    Przedborski, S.5    Brundin, P.6
  • 127
    • 0037322570 scopus 로고    scopus 로고
    • Transient and progressive electrophysiological alterations in the corticostriatal pathway in a mouse model of Huntington's disease
    • Cepeda C., Hurst R. S., Calvert C. R., Hernandez-Echeagaray E., Nguyen O. K., Jocoy E. et al. (2003) Transient and progressive electrophysiological alterations in the corticostriatal pathway in a mouse model of Huntington's disease. J. Neurosci. 23: 961-969
    • (2003) J. Neurosci. , vol.23 , pp. 961-969
    • Cepeda, C.1    Hurst, R.S.2    Calvert, C.R.3    Hernandez-Echeagaray, E.4    Nguyen, O.K.5    Jocoy, E.6
  • 129
    • 0036074718 scopus 로고    scopus 로고
    • The role of dopamine in motor symptoms in the R6/2 transgenic mouse model of Huntington's disease
    • Hickey M. A., Reynolds G. P. and Morton A. J. (2002) The role of dopamine in motor symptoms in the R6/2 transgenic mouse model of Huntington's disease. J. Neurochem. 81: 46-59
    • (2002) J. Neurochem. , vol.81 , pp. 46-59
    • Hickey, M.A.1    Reynolds, G.P.2    Morton, A.J.3
  • 132
    • 0036736196 scopus 로고    scopus 로고
    • Inhibition of tryptophan hydroxylase activity and decreased 5-HT1A receptor binding in a mouse model of Huntington's disease
    • Yohrling I. G., Jiang G. C., DeJohn M. M., Robertson D. J., Vrana K. E. and Cha J. H. (2002) Inhibition of tryptophan hydroxylase activity and decreased 5-HT1A receptor binding in a mouse model of Huntington's disease. J. Neurochem. 82: 1416-1423
    • (2002) J. Neurochem. , vol.82 , pp. 1416-1423
    • Yohrling, I.G.1    Jiang, G.C.2    DeJohn, M.M.3    Robertson, D.J.4    Vrana, K.E.5    Cha, J.H.6
  • 135
    • 12744279625 scopus 로고    scopus 로고
    • Transcriptional dysregulation in striatal projection- and interneurons in a mouse model of Huntington's disease: Neuronal selectivity and potential neuroprotective role of HAP1
    • Zucker B., Luthi-Carter R., Kama J. A., Dunah A. W., Stern E. A., Fox J. H. et al. (2005) Transcriptional dysregulation in striatal projection- and interneurons in a mouse model of Huntington's disease: neuronal selectivity and potential neuroprotective role of HAP1. Hum. Mol. Genet. 14: 179-189
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 179-189
    • Zucker, B.1    Luthi-Carter, R.2    Kama, J.A.3    Dunah, A.W.4    Stern, E.A.5    Fox, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.