메뉴 건너뛰기




Volumn 20, Issue 3, 2004, Pages 146-154

Huntingtin-protein interactions and the pathogenesis of Huntington's disease

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; CYSTATHIONINE BETA SYNTHASE; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HUNTINGTIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; POLYGLUTAMINE; TATA BINDING PROTEIN; TATA BINDING PROTEIN ASSOCIATED FACTOR; TRANSCRIPTION FACTOR; UBIQUITIN CONJUGATING ENZYME;

EID: 1242338856     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2004.01.008     Document Type: Review
Times cited : (465)

References (88)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi H.Y., Orr H.T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23:2000;217-247.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 2
    • 0035393427 scopus 로고    scopus 로고
    • SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein
    • Nakamura K., et al. SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. Hum. Mol. Genet. 10:2001;1441-1448.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1441-1448
    • Nakamura, K.1
  • 3
    • 0022395922 scopus 로고
    • Neuropathological classification of Huntington's disease
    • Vonsattel J.P., et al. Neuropathological classification of Huntington's disease. J. Neuropathol. Exp. Neurol. 44:1985;559-577.
    • (1985) J. Neuropathol. Exp. Neurol. , vol.44 , pp. 559-577
    • Vonsattel, J.P.1
  • 4
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes P., Wanker E.E. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem. Sci. 28:2003;425-433.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 5
    • 0141742228 scopus 로고    scopus 로고
    • The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor
    • Takano, H. and Gusella, J.F. (2002) The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor. BMC Neurosci. 3, 15 ( www.biomedcentral.com/1471-2202/3/15 ).
    • (2002) BMC Neurosci. , vol.3 , pp. 15
    • Takano, H.1    Gusella, J.F.2
  • 6
    • 0033782987 scopus 로고    scopus 로고
    • HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions
    • Neuwald A.F., Hirano T. HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions. Genome Res. 10:2000;1445-1452.
    • (2000) Genome Res. , vol.10 , pp. 1445-1452
    • Neuwald, A.F.1    Hirano, T.2
  • 7
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia M., et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron. 14:1995;1075-1081.
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • Difiglia, M.1
  • 8
    • 0029034511 scopus 로고
    • Widespread expression of Huntington's disease gene (IT15) protein product
    • Sharp A.H., et al. Widespread expression of Huntington's disease gene (IT15) protein product. Neuron. 14:1995;1065-1074.
    • (1995) Neuron , vol.14 , pp. 1065-1074
    • Sharp, A.H.1
  • 9
    • 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., et al. The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): comparison with huntingtin in rat and human. J. Neurosci. 18:1998;7674-7686.
    • (1998) J. Neurosci. , vol.18 , pp. 7674-7686
    • Gutekunst, C.A.1
  • 10
    • 0035282594 scopus 로고    scopus 로고
    • Loss of normal huntingtin function: New developments in Huntington's disease research
    • Cattaneo E., et al. Loss of normal huntingtin function: new developments in Huntington's disease research. Trends Neurosci. 24:2001;182-188.
    • (2001) Trends Neurosci. , vol.24 , pp. 182-188
    • Cattaneo, E.1
  • 11
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I., et al. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat. Genet. 26:2000;300-306.
    • (2000) Nat. Genet. , vol.26 , pp. 300-306
    • Dragatsis, I.1
  • 12
    • 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. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell. 90:1997;537-548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1
  • 13
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • Reddy P.H., et al. Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA. Nat. Genet. 20:1998;198-202.
    • (1998) Nat. Genet. , vol.20 , pp. 198-202
    • Reddy, P.H.1
  • 14
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling G., et al. Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8:1999;397-407.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1
  • 15
    • 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., et al. A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron. 23:1999;181-192.
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1
  • 16
    • 0032101287 scopus 로고    scopus 로고
    • The influence of huntingtin protein size on nuclear localization and cellular toxicity
    • Hackam A.S., et al. The influence of huntingtin protein size on nuclear localization and cellular toxicity. J. Cell Biol. 141:1998;1097-1105.
    • (1998) J. Cell Biol. , vol.141 , pp. 1097-1105
    • Hackam, A.S.1
  • 17
    • 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
  • 18
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim Y.J., et al. Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc. Natl. Acad. Sci. U. S. A. 98:2001;12784-12789.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12784-12789
    • Kim, Y.J.1
  • 19
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J., Ellerby L.M. Calpain activation in Huntington's disease. J. Neurosci. 22:2002;4842-4849.
    • (2002) J. Neurosci. , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 20
    • 0037107151 scopus 로고    scopus 로고
    • Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease
    • Wellington C.L., et al. Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease. J. Neurosci. 22:2002;7862-7872.
    • (2002) J. Neurosci. , vol.22 , pp. 7862-7872
    • Wellington, C.L.1
  • 21
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes A., et al. Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol. Cell. 10:2002;259-269.
    • (2002) Mol. Cell , vol.10 , pp. 259-269
    • Lunkes, A.1
  • 22
    • 0141891952 scopus 로고    scopus 로고
    • Huntingtin forms toxic N-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity
    • Zhou H., et al. Huntingtin forms toxic N-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity. J. Cell Biol. 163:2003;109-118.
    • (2003) J. Cell Biol. , vol.163 , pp. 109-118
    • Zhou, H.1
  • 23
    • 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
  • 24
    • 0032899021 scopus 로고    scopus 로고
    • Genetic regulation of glutamate receptor ion channels
    • Myers S.J., et al. Genetic regulation of glutamate receptor ion channels. Annu. Rev. Pharmacol. Toxicol. 39:1999;221-241.
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 221-241
    • Myers, S.J.1
  • 25
    • 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
  • 26
    • 23444458415 scopus 로고
    • Transcriptional activation modulated by homopolymeric glutamine and proline stretches
    • Gerber H.P., et al. Transcriptional activation modulated by homopolymeric glutamine and proline stretches. Science. 263:1994;808-811.
    • (1994) Science , vol.263 , pp. 808-811
    • Gerber, H.P.1
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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 Jr., F.C.1
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante R.J., et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23:2003;9418-9427.
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 33
    • 0037386621 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent oxidative neuronal death independent of expanded polyglutamine repeats via an Sp1-dependent pathway
    • Ryu H., et al. Histone deacetylase inhibitors prevent oxidative neuronal death independent of expanded polyglutamine repeats via an Sp1-dependent pathway. Proc. Natl. Acad. Sci. U. S. A. 100:2003;4281-4286.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4281-4286
    • Ryu, H.1
  • 34
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz M.F., et al. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. U. S. A. 91:1994;5355-5358.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5355-5358
    • Perutz, M.F.1
  • 35
    • 0032450856 scopus 로고    scopus 로고
    • Amyloid formation by mutant huntingtin: Threshold, progressivity and recruitment of normal polyglutamine proteins
    • Huang C.C., et al. Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins. Somat. Cell Mol. Genet. 24:1998;217-233.
    • (1998) Somat. Cell Mol. Genet. , vol.24 , pp. 217-233
    • Huang, C.C.1
  • 36
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • Perez M.K., et al. Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J. Cell Biol. 143:1998;1457-1470.
    • (1998) J. Cell Biol. , vol.143 , pp. 1457-1470
    • Perez, M.K.1
  • 37
    • 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
  • 38
    • 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
  • 39
    • 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
  • 40
    • 0037101839 scopus 로고    scopus 로고
    • Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analyses
    • Sipione S., et al. Early transcriptional profiles in huntingtin- inducible striatal cells by microarray analyses. Hum. Mol. Genet. 11:2002;1953-1965.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1953-1965
    • Sipione, S.1
  • 41
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • Li S.H., et al. Interaction of Huntington disease protein with transcriptional activator Sp1. Mol. Cell. Biol. 22:2002;1277-1287.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1277-1287
    • Li, S.H.1
  • 42
    • 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
  • 43
    • 0034283877 scopus 로고    scopus 로고
    • Transcriptional dysregulation in Huntington's disease
    • Cha J.H. Transcriptional dysregulation in Huntington's disease. Trends Neurosci. 23:2000;387-392.
    • (2000) Trends Neurosci. , vol.23 , pp. 387-392
    • Cha, J.H.1
  • 44
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars K.L., Rubinsztein D.C. Transcriptional abnormalities in Huntington disease. Trends Genet. 19:2003;233-238.
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 45
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato C., et al. Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat. Genet. 35:2003;76-83.
    • (2003) Nat. Genet. , vol.35 , pp. 76-83
    • Zuccato, C.1
  • 46
    • 0030726894 scopus 로고    scopus 로고
    • Glued subunit of dynactin
    • Glued subunit of dynactin. Hum. Mol. Genet. 6:1997;2205-2212.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 2205-2212
    • Engelender, S.1
  • 47
    • 0032519646 scopus 로고    scopus 로고
    • Glued
    • Glued. J. Neurosci. 18:1998;1261-1269.
    • (1998) J. Neurosci. , vol.18 , pp. 1261-1269
    • Li, S.H.1
  • 48
    • 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., et al. Huntingtin-associated protein 1 interacts with hepatocyte growth factor-regulated tyrosine kinase substrate and functions in endosomal trafficking. J. Biol. Chem. 277:2002;28212-28221.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28212-28221
    • Li, Y.1
  • 49
    • 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., et al. Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron. 39:2003;227-239.
    • (2003) Neuron , vol.39 , pp. 227-239
    • Tang, T.S.1
  • 50
    • 0042423684 scopus 로고    scopus 로고
    • Stimulation of NeuroD activity by huntingtin and huntingtin-associated proteins HAP1 and MLK2
    • Marcora E., et al. Stimulation of NeuroD activity by huntingtin and huntingtin-associated proteins HAP1 and MLK2. Proc. Natl. Acad. Sci. U. S. A. 100:2003;9578-9583.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9578-9583
    • Marcora, E.1
  • 51
    • 0030878098 scopus 로고    scopus 로고
    • Fast transport and retrograde movement of huntingtin and HAP 1 in axons
    • Block-Galarza J., et al. Fast transport and retrograde movement of huntingtin and HAP 1 in axons. Neuroreport. 8:1997;2247-2251.
    • (1997) Neuroreport , vol.8 , pp. 2247-2251
    • Block-Galarza, J.1
  • 52
    • 0037091010 scopus 로고    scopus 로고
    • Targeted disruption of Huntingtin-associated protein-1 (Hap1) results in postnatal death due to depressed feeding behavior
    • Chan E.Y., et al. Targeted disruption of Huntingtin-associated protein-1 (Hap1) results in postnatal death due to depressed feeding behavior. Hum. Mol. Genet. 11:2002;945-959.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 945-959
    • Chan, E.Y.1
  • 53
    • 0041632303 scopus 로고    scopus 로고
    • Lack of huntingtin-associated protein-1 causes neuronal death resembling hypothalamic degeneration in Huntington's disease
    • Li S.H., et al. Lack of huntingtin-associated protein-1 causes neuronal death resembling hypothalamic degeneration in Huntington's disease. J. Neurosci. 23:2003;6956-6964.
    • (2003) J. Neurosci. , vol.23 , pp. 6956-6964
    • Li, S.H.1
  • 54
    • 0030986659 scopus 로고    scopus 로고
    • HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain
    • Kalchman M.A., et al. HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nat. Genet. 16:1997;44-53.
    • (1997) Nat. Genet. , vol.16 , pp. 44-53
    • Kalchman, M.A.1
  • 55
    • 0035914402 scopus 로고    scopus 로고
    • HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2
    • Metzler M., et al. HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2. J. Biol. Chem. 276:2001;39271-39276.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39271-39276
    • Metzler, M.1
  • 56
    • 0035880457 scopus 로고    scopus 로고
    • The huntingtin interacting protein HIP1 is a clathrin and α-adaptin-binding protein involved in receptor-mediated endocytosis
    • Waelter S., et al. The huntingtin interacting protein HIP1 is a clathrin and α-adaptin-binding protein involved in receptor-mediated endocytosis. Hum. Mol. Genet. 10:2001;1807-1817.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1807-1817
    • Waelter, S.1
  • 57
    • 0035824673 scopus 로고    scopus 로고
    • Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins
    • Mishra S.K., et al. Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins. J. Biol. Chem. 276:2001;46230-46236.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46230-46236
    • Mishra, S.K.1
  • 58
    • 0037926396 scopus 로고    scopus 로고
    • Disruption of the endocytic protein HIP1 results in neurological deficits and decreased AMPA receptor trafficking
    • Metzler M., et al. Disruption of the endocytic protein HIP1 results in neurological deficits and decreased AMPA receptor trafficking. EMBO J. 22:2003;3254-3266.
    • (2003) EMBO J. , vol.22 , pp. 3254-3266
    • Metzler, M.1
  • 59
    • 1242266718 scopus 로고    scopus 로고
    • Altered receptor trafficking in huntingtin interacting protein 1-transformed cells
    • Rao D.S., et al. Altered receptor trafficking in huntingtin interacting protein 1-transformed cells. Cancer Cell. 3:2003;471-482.
    • (2003) Cancer Cell , vol.3 , pp. 471-482
    • Rao, D.S.1
  • 60
    • 0034731370 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain
    • Hackam A.S., et al. Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain. J. Biol. Chem. 275:2000;41299-41308.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41299-41308
    • Hackam, A.S.1
  • 61
    • 0036173770 scopus 로고    scopus 로고
    • Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi
    • Gervais F.G., et al. Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi. Nat. Cell Biol. 4:2002;95-105.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 95-105
    • Gervais, F.G.1
  • 62
    • 0036850524 scopus 로고    scopus 로고
    • HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis
    • Singaraja R.R., et al. HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis. Hum. Mol. Genet. 11:2002;2815-2828.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2815-2828
    • Singaraja, R.R.1
  • 63
    • 0036796261 scopus 로고    scopus 로고
    • PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains
    • Modregger J., et al. PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains. Hum. Mol. Genet. 11:2002;2547-2558.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2547-2558
    • Modregger, J.1
  • 64
    • 0032186107 scopus 로고    scopus 로고
    • SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates
    • Sittler A., et al. SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates. Mol. Cell. 2:1998;427-436.
    • (1998) Mol. Cell , vol.2 , pp. 427-436
    • Sittler, A.1
  • 65
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95
    • Sun Y., et al. Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95. J. Biol. Chem. 276:2001;24713-24718.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24713-24718
    • Sun, Y.1
  • 66
    • 0035889535 scopus 로고    scopus 로고
    • NMDA receptor function in mouse models of Huntington disease
    • Cepeda C., et al. NMDA receptor function in mouse models of Huntington disease. J. Neurosci. Res. 66:2001;525-539.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 525-539
    • Cepeda, C.1
  • 67
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron M.M., et al. Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron. 33:2002;849-860.
    • (2002) Neuron , vol.33 , pp. 849-860
    • Zeron, M.M.1
  • 68
    • 0042921188 scopus 로고    scopus 로고
    • Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release
    • Li H., et al. Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release. Hum. Mol. Genet. 12:2003;2021-2030.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2021-2030
    • Li, H.1
  • 69
    • 0032811511 scopus 로고    scopus 로고
    • Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice
    • Li H., et al. Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice. Hum. Mol. Genet. 8:1999;1227-1236.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1227-1236
    • Li, H.1
  • 70
    • 0035503511 scopus 로고    scopus 로고
    • Huntingtin aggregate-associated axonal degeneration is an early pathological event in Huntington's disease mice
    • Li H., et al. Huntingtin aggregate-associated axonal degeneration is an early pathological event in Huntington's disease mice. J. Neurosci. 21:2001;8473-8481.
    • (2001) J. Neurosci. , vol.21 , pp. 8473-8481
    • Li, H.1
  • 71
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: Relationship to neuropathology
    • Gutekunst C.A., et al. Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology. J. Neurosci. 19:1999;2522-2534.
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1
  • 72
    • 0000790724 scopus 로고    scopus 로고
    • SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes
    • Liu Y.F., et al. SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes. J. Biol. Chem. 272:1997;8121-8124.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8121-8124
    • Liu, Y.F.1
  • 73
    • 0141926491 scopus 로고    scopus 로고
    • Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: A potential mechanism for loss of huntingtin function in Huntington's disease
    • Busch A., et al. Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: a potential mechanism for loss of huntingtin function in Huntington's disease. J. Biol. Chem. 278:2003;41452-41461.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41452-41461
    • Busch, A.1
  • 74
    • 0141531987 scopus 로고    scopus 로고
    • Depletion of wild-type huntingtin in mouse models of neurologic diseases
    • Zhang Y., et al. Depletion of wild-type huntingtin in mouse models of neurologic diseases. J. Neurochem. 87:2003;101-106.
    • (2003) J. Neurochem. , vol.87 , pp. 101-106
    • Zhang, Y.1
  • 76
    • 0035852687 scopus 로고    scopus 로고
    • The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: Neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis
    • Holbert S., et al. The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence 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
  • 77
    • 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
  • 78
    • 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
  • 79
    • 0031662269 scopus 로고    scopus 로고
    • Huntingtin interacts with a family of WW domain proteins
    • Faber P.W., et al. Huntingtin interacts with a family of WW domain proteins. Hum. Mol. Genet. 7:1998;1463-1474.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1463-1474
    • Faber, P.W.1
  • 80
    • 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
  • 81
    • 0031056478 scopus 로고    scopus 로고
    • HIP-I: A huntingtin interacting protein isolated by the yeast two-hybrid system
    • Wanker E.E., et al. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. Hum. Mol. Genet. 6:1997;487-495.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 487-495
    • Wanker, E.E.1
  • 82
    • 0030001072 scopus 로고    scopus 로고
    • Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin
    • Bao J., et al. Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin. Proc. Natl. Acad. Sci. U. S. A. 93:1996;5037-5042.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5037-5042
    • Bao, J.1
  • 83
    • 0344838402 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 binds to huntingtin: Neuropathologic and biological evidence for a role in Huntington's disease
    • Holbert S., et al. Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 100:2003;2712-2717.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2712-2717
    • Holbert, S.1
  • 84
    • 0031909798 scopus 로고    scopus 로고
    • Huntingtin interacts with cystathionine β-synthase
    • Boutell J.M., et al. Huntingtin interacts with cystathionine β-synthase. Hum. Mol. Genet. 7:1998;371-378.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 371-378
    • Boutell, J.M.1
  • 85
    • 0029664992 scopus 로고    scopus 로고
    • Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
    • Burke J.R., et al. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nat. Med. 2:1996;347-350.
    • (1996) Nat. Med. , vol.2 , pp. 347-350
    • Burke, J.R.1
  • 86
    • 9444239187 scopus 로고    scopus 로고
    • Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme
    • Kalchman M.A., et al. Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. J. Biol. Chem. 271:1996;19385-19394.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19385-19394
    • Kalchman, M.A.1
  • 87
    • 0141750470 scopus 로고    scopus 로고
    • Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila
    • Gunawardena S., et al. Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila. Neuron. 40:2003;25-40.
    • (2003) Neuron , vol.40 , pp. 25-40
    • Gunawardena, S.1
  • 88
    • 10744224530 scopus 로고    scopus 로고
    • Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport
    • Szebenyi G., et al. Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron. 40:2003;41-52.
    • (2003) Neuron , vol.40 , pp. 41-52
    • Szebenyi, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.