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Volumn 4, Issue 6, 2009, Pages

Nucleocytoplasmic shuttling activity of ataxin-3

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; ATAXIN 3; EXPORTIN 1; GREEN FLUORESCENT PROTEIN; LEPTOMYCIN B; LYSINE; POLYGLUTAMINE; PROTEIN JOSEPHIN; UBIQUITIN; UNCLASSIFIED DRUG; ATXN3 PROTEIN, HUMAN; NERVE PROTEIN; NUCLEAR PROTEIN; REPRESSOR PROTEIN;

EID: 67149129949     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005834     Document Type: Article
Times cited : (40)

References (68)
  • 1
    • 0942287194 scopus 로고    scopus 로고
    • Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways
    • Chai Y, Berke SS, Cohen RE, Paulson HL (2004) Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways. J Biol Chem 279: 3605-3611.
    • (2004) J Biol Chem , vol.279 , pp. 3605-3611
    • Chai, Y.1    Berke, S.S.2    Cohen, R.E.3    Paulson, H.L.4
  • 2
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B, Li F, Pittman RN (2003) The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum Mol Genet 12: 3195-3205.
    • (2003) Hum Mol Genet , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 3
    • 0041563693 scopus 로고    scopus 로고
    • Domain architecture of the polyglutamine protein ataxin-3: A globular domain followed by a flexible tail
    • Masino L, Musi V, Menon RP, Fusi P, Kelly G, et al. (2003) Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. FEBS Lett 549: 21-25.
    • (2003) FEBS Lett , vol.549 , pp. 21-25
    • Masino, L.1    Musi, V.2    Menon, R.P.3    Fusi, P.4    Kelly, G.5
  • 4
    • 0034756334 scopus 로고    scopus 로고
    • Improvement in the molecular diagnosis of Machado-Joseph disease
    • Maciel P, Costa MC, Ferro A, Rousseau M, Santos CS, et al. (2001) Improvement in the molecular diagnosis of Machado-Joseph disease. Arch Neurol 58: 1821-1827.
    • (2001) Arch Neurol , vol.58 , pp. 1821-1827
    • Maciel, P.1    Costa, M.C.2    Ferro, A.3    Rousseau, M.4    Santos, C.S.5
  • 5
    • 0031803642 scopus 로고    scopus 로고
    • Ataxin-3 is transported into the nucleus and associates with the nuclear matrix
    • Tait D, Riccio M, Sittler A, Scherzinger E, Santi S, et al. (1998) Ataxin-3 is transported into the nucleus and associates with the nuclear matrix. Hum Mol Genet 7: 991-997.
    • (1998) Hum Mol Genet , vol.7 , pp. 991-997
    • Tait, D.1    Riccio, M.2    Sittler, A.3    Scherzinger, E.4    Santi, S.5
  • 6
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson HL, Perez MK, Trottier Y, Trojanowski JQ, Subramony SH, et al. (1997) Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19: 333-344.
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3    Trojanowski, J.Q.4    Subramony, S.H.5
  • 7
    • 0032425541 scopus 로고    scopus 로고
    • Heterogeneous intracellular localization and expression of ataxin-3
    • Trottier Y, Cancel G, An-Gourfinkel I, Lutz Y, Weber C, et al. (1998) Heterogeneous intracellular localization and expression of ataxin-3. Neurobiol Dis 5: 335-347.
    • (1998) Neurobiol Dis , vol.5 , pp. 335-347
    • Trottier, Y.1    Cancel, G.2    An-Gourfinkel, I.3    Lutz, Y.4    Weber, C.5
  • 8
    • 15944419824 scopus 로고    scopus 로고
    • Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin-associated mechanism
    • Warrick JM, Morabito LM, Bilen J, Gordesky-Gold B, Faust LZ, et al. (2005) Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin-associated mechanism. Mol Cell 18: 37-48.
    • (2005) Mol Cell , vol.18 , pp. 37-48
    • Warrick, J.M.1    Morabito, L.M.2    Bilen, J.3    Gordesky-Gold, B.4    Faust, L.Z.5
  • 9
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • Burnett BG, Pittman RN (2005) The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Proc Natl Acad Sci U S A 102: 4330-4335.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 10
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • Wang Q, Li L, Ye Y (2006) Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J Cell Biol 174: 963-971.
    • (2006) J Cell Biol , vol.174 , pp. 963-971
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 11
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li F, Macfarlan T, Pittman RN, Chakravarti D (2002) Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J Biol Chem 277: 45004-45012.
    • (2002) J Biol Chem , vol.277 , pp. 45004-45012
    • Li, F.1    Macfarlan, T.2    Pittman, R.N.3    Chakravarti, D.4
  • 12
    • 33750962224 scopus 로고    scopus 로고
    • Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation
    • Evert BO, Araujo J, Vieira-Saecker AM, de Vos RA, Harendza S, et al. (2006) Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation. J Neurosci 26: 11474-11486.
    • (2006) J Neurosci , vol.26 , pp. 11474-11486
    • Evert, B.O.1    Araujo, J.2    Vieira-Saecker, A.M.3    de Vos, R.A.4    Harendza, S.5
  • 14
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY, Orr HT (2000) Glutamine repeats and neurodegeneration. Annu Rev Neurosci 23: 217-247.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 15
    • 34547627141 scopus 로고    scopus 로고
    • Differential effects of polyglutamine proteins on nuclear organization and artificial reporter splicing
    • Sun J, Xu H, Negi S, Subramony SH, Hebert MD (2007) Differential effects of polyglutamine proteins on nuclear organization and artificial reporter splicing. J Neurosci Res 85: 2306-2317.
    • (2007) J Neurosci Res , vol.85 , pp. 2306-2317
    • Sun, J.1    Xu, H.2    Negi, S.3    Subramony, S.H.4    Hebert, M.D.5
  • 16
    • 0027356605 scopus 로고
    • Epidemiology and clinical aspects of Machado-Joseph disease
    • Sequeiros J, Coutinho P (1993) Epidemiology and clinical aspects of Machado-Joseph disease. Adv Neurol 61: 139-153.
    • (1993) Adv Neurol , vol.61 , pp. 139-153
    • Sequeiros, J.1    Coutinho, P.2
  • 17
    • 7344234800 scopus 로고    scopus 로고
    • An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients
    • Schmidt T, Landwehrmeyer GB, Schmitt I, Trottier Y, Auburger G, et al. (1998) An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Brain Pathol 8: 669-679.
    • (1998) Brain Pathol , vol.8 , pp. 669-679
    • Schmidt, T.1    Landwehrmeyer, G.B.2    Schmitt, I.3    Trottier, Y.4    Auburger, G.5
  • 18
    • 0035871295 scopus 로고    scopus 로고
    • Beyond the Qs in the polyglutamine diseases
    • Orr HT (2001) Beyond the Qs in the polyglutamine diseases. Genes Dev 15: 925-932.
    • (2001) Genes Dev , vol.15 , pp. 925-932
    • Orr, H.T.1
  • 19
    • 0038379383 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Minding your Ps and Qs
    • Paulson H (2003) Polyglutamine neurodegeneration: minding your Ps and Qs. Nat Med 9: 825-826.
    • (2003) Nat Med , vol.9 , pp. 825-826
    • Paulson, H.1
  • 21
    • 11144356369 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxias: Clinical features, genetics, and pathogenesis
    • Schols L, Bauer P, Schmidt T, Schulte T, Riess O (2004) Autosomal dominant cerebellar ataxias: clinical features, genetics, and pathogenesis. Lancet Neurol 3: 291-304.
    • (2004) Lancet Neurol , vol.3 , pp. 291-304
    • Schols, L.1    Bauer, P.2    Schmidt, T.3    Schulte, T.4    Riess, O.5
  • 22
    • 0033811788 scopus 로고    scopus 로고
    • Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human
    • Huynh DP, Figueroa K, Hoang N, Pulst SM (2000) Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human. Nat Genet 26: 44-50.
    • (2000) Nat Genet , vol.26 , pp. 44-50
    • Huynh, D.P.1    Figueroa, K.2    Hoang, N.3    Pulst, S.M.4
  • 23
    • 0036670407 scopus 로고    scopus 로고
    • Huntingtin fragments that aggregate go their separate ways
    • DiFiglia M (2002) Huntingtin fragments that aggregate go their separate ways. Mol Cell 10: 224-225.
    • (2002) Mol Cell , vol.10 , pp. 224-225
    • DiFiglia, M.1
  • 24
    • 4344636957 scopus 로고    scopus 로고
    • Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice
    • Schilling G, Savonenko AV, Klevytska A, Morton JL, Tucker SM, et al. (2004) Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice. Hum Mol Genet 13: 1599-1610.
    • (2004) Hum Mol Genet , vol.13 , pp. 1599-1610
    • Schilling, G.1    Savonenko, A.V.2    Klevytska, A.3    Morton, J.L.4    Tucker, S.M.5
  • 25
    • 27544477225 scopus 로고    scopus 로고
    • Contribution of nuclear and extranuclear polyQ to neurological phenotypes in mouse models of Huntington's disease
    • Benn CL, Landles C, Li H, Strand AD, Woodman B, et al. (2005) Contribution of nuclear and extranuclear polyQ to neurological phenotypes in mouse models of Huntington's disease. Hum Mol Genet 14: 3065-3078.
    • (2005) Hum Mol Genet , vol.14 , pp. 3065-3078
    • Benn, C.L.1    Landles, C.2    Li, H.3    Strand, A.D.4    Woodman, B.5
  • 26
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang W, Dunlap JR, Andrews RB, Wetzel R (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet 11: 2905-2917.
    • (2002) Hum Mol Genet , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 27
    • 0038104366 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport signals affect the age at onset of abnormalities in knock-in mice expressing polyglutamine within an ectopic protein context
    • Jackson WS, Tallaksen-Greene SJ, Albin RL, Detloff PJ (2003) Nucleocytoplasmic transport signals affect the age at onset of abnormalities in knock-in mice expressing polyglutamine within an ectopic protein context. Hum Mol Genet 12: 1621-1629.
    • (2003) Hum Mol Genet , vol.12 , pp. 1621-1629
    • Jackson, W.S.1    Tallaksen-Greene, S.J.2    Albin, R.L.3    Detloff, P.J.4
  • 28
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, et al. (1998) Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95: 41-53.
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5
  • 29
    • 14044266141 scopus 로고    scopus 로고
    • RNA association and nucleocytoplasmic shuttling by ataxin-1
    • Irwin S, Vandelft M, Pinchev D, Howell JL, Graczyk J, et al. (2005) RNA association and nucleocytoplasmic shuttling by ataxin-1. J Cell Sci 118: 233-242.
    • (2005) J Cell Sci , vol.118 , pp. 233-242
    • Irwin, S.1    Vandelft, M.2    Pinchev, D.3    Howell, J.L.4    Graczyk, J.5
  • 30
    • 0032858212 scopus 로고    scopus 로고
    • Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7
    • Kaytor MD, Duvick LA, Skinner PJ, Koob MD, Ranum LP, et al. (1999) Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7. Hum Mol Genet 8: 1657-1664.
    • (1999) Hum Mol Genet , vol.8 , pp. 1657-1664
    • Kaytor, M.D.1    Duvick, L.A.2    Skinner, P.J.3    Koob, M.D.4    Ranum, L.P.5
  • 31
    • 0035959998 scopus 로고    scopus 로고
    • Qs in the nucleus
    • Orr HT (2001) Qs in the nucleus. Neuron 31: 875-876.
    • (2001) Neuron , vol.31 , pp. 875-876
    • Orr, H.T.1
  • 32
    • 33646378692 scopus 로고    scopus 로고
    • Ataxin-7 can export from the nucleus via a conserved exportin-dependent signal
    • Taylor J, Grote SK, Xia J, Vandelft M, Graczyk J, et al. (2006) Ataxin-7 can export from the nucleus via a conserved exportin-dependent signal. J Biol Chem 281: 2730-2739.
    • (2006) J Biol Chem , vol.281 , pp. 2730-2739
    • Taylor, J.1    Grote, S.K.2    Xia, J.3    Vandelft, M.4    Graczyk, J.5
  • 33
    • 0037701612 scopus 로고    scopus 로고
    • Huntingtin contains a highly conserved nuclear export signal
    • Xia J, Lee DH, Taylor J, Vandelft M, Truant R (2003) Huntingtin contains a highly conserved nuclear export signal. Hum Mol Genet 12: 1393-1403.
    • (2003) Hum Mol Genet , vol.12 , pp. 1393-1403
    • Xia, J.1    Lee, D.H.2    Taylor, J.3    Vandelft, M.4    Truant, R.5
  • 34
    • 13944275615 scopus 로고    scopus 로고
    • Polyglutamine expansion of huntingtin impairs its nuclear export
    • Cornett J, Cao F, Wang CE, Ross CA, Bates GP, et al. (2005) Polyglutamine expansion of huntingtin impairs its nuclear export. Nat Genet 37: 198-204.
    • (2005) Nat Genet , vol.37 , pp. 198-204
    • Cornett, J.1    Cao, F.2    Wang, C.E.3    Ross, C.A.4    Bates, G.P.5
  • 35
    • 34447520352 scopus 로고    scopus 로고
    • Nuclear localization of ataxin-3 is required for the manifestation of symptoms in SCA3: In vivo evidence
    • Bichelmeier U, Schmidt T, Hubener J, Boy J, Ruttiger L, et al. (2007) Nuclear localization of ataxin-3 is required for the manifestation of symptoms in SCA3: in vivo evidence. J Neurosci 27: 7418-7428.
    • (2007) J Neurosci , vol.27 , pp. 7418-7428
    • Bichelmeier, U.1    Schmidt, T.2    Hubener, J.3    Boy, J.4    Ruttiger, L.5
  • 36
    • 46249122383 scopus 로고    scopus 로고
    • Striatal and nigral pathology in a lentiviral rat model of Machado-Joseph disease
    • Alves S, Regulier E, Nascimento-Ferreira I, Hassig R, Dufour N, et al. (2008) Striatal and nigral pathology in a lentiviral rat model of Machado-Joseph disease. Hum Mol Genet 17: 2071-2083.
    • (2008) Hum Mol Genet , vol.17 , pp. 2071-2083
    • Alves, S.1    Regulier, E.2    Nascimento-Ferreira, I.3    Hassig, R.4    Dufour, N.5
  • 37
    • 58149375272 scopus 로고    scopus 로고
    • Deranged calcium signaling and neurodegeneration in spinocerebellar ataxia type 3
    • Chen X, Tang TS, Tu H, Nelson O, Pook M, et al. (2008) Deranged calcium signaling and neurodegeneration in spinocerebellar ataxia type 3. J Neurosci 28: 12713-12724.
    • (2008) J Neurosci , vol.28 , pp. 12713-12724
    • Chen, X.1    Tang, T.S.2    Tu, H.3    Nelson, O.4    Pook, M.5
  • 38
    • 20844462057 scopus 로고    scopus 로고
    • A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration
    • Goti D, Katzen SM, Mez J, Kurtis N, Kiluk J, et al. (2004) A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration. J Neurosci 24: 10266-10279.
    • (2004) J Neurosci , vol.24 , pp. 10266-10279
    • Goti, D.1    Katzen, S.M.2    Mez, J.3    Kurtis, N.4    Kiluk, J.5
  • 39
    • 0034005718 scopus 로고    scopus 로고
    • A genetic system for detection of protein nuclear import and export
    • Rhee Y, Gurel F, Gafni Y, Dingwall C, Citovsky V (2000) A genetic system for detection of protein nuclear import and export. Nat Biotechnol 18: 433-437.
    • (2000) Nat Biotechnol , vol.18 , pp. 433-437
    • Rhee, Y.1    Gurel, F.2    Gafni, Y.3    Dingwall, C.4    Citovsky, V.5
  • 41
    • 0022054094 scopus 로고
    • A Tn3 lacZ transposon for the random generation of beta-galactosidase gene fusions: Application to the analysis of gene expression in Agrobacterium
    • Stachel SE, An G, Flores C, Nester EW (1985) A Tn3 lacZ transposon for the random generation of beta-galactosidase gene fusions: application to the analysis of gene expression in Agrobacterium. Embo J 4: 891-898.
    • (1985) Embo J , vol.4 , pp. 891-898
    • Stachel, S.E.1    An, G.2    Flores, C.3    Nester, E.W.4
  • 42
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson BR, Eleftheriou A (2000) A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp Cell Res 256: 213-224.
    • (2000) Exp Cell Res , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 43
    • 0037252650 scopus 로고    scopus 로고
    • NESbase version 1.0: A database of nuclear export signals. Nucleic Acids Res
    • la Cour T, Gupta R, Rapacki K, Skriver K, Poulsen FM, et al. (2003) NESbase version 1.0: a database of nuclear export signals. Nucleic Acids Res 31: 393-396.
    • (2003) , vol.31 , pp. 393-396
    • la Cour, T.1    Gupta, R.2    Rapacki, K.3    Skriver, K.4    Poulsen, F.M.5
  • 44
    • 0030936575 scopus 로고    scopus 로고
    • Machado-Joseph disease gene product is a cytoplasmic protein widely expressed in brain
    • Paulson HL, Das SS, Crino PB, Perez MK, Patel SC, et al. (1997) Machado-Joseph disease gene product is a cytoplasmic protein widely expressed in brain. Ann Neurol 41: 453-462.
    • (1997) Ann Neurol , vol.41 , pp. 453-462
    • Paulson, H.L.1    Das, S.S.2    Crino, P.B.3    Perez, M.K.4    Patel, S.C.5
  • 45
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai Y, Koppenhafer SL, Shoesmith SJ, Perez MK, Paulson HL (1999) Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum Mol Genet 8: 673-682.
    • (1999) Hum Mol Genet , vol.8 , pp. 673-682
    • Chai, Y.1    Koppenhafer, S.L.2    Shoesmith, S.J.3    Perez, M.K.4    Paulson, H.L.5
  • 46
    • 0030701840 scopus 로고    scopus 로고
    • Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins
    • Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, et al. (1997) Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J Biol Chem 272: 29742-29751.
    • (1997) J Biol Chem , vol.272 , pp. 29742-29751
    • Kudo, N.1    Khochbin, S.2    Nishi, K.3    Kitano, K.4    Yanagida, M.5
  • 47
    • 0032146749 scopus 로고    scopus 로고
    • Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1
    • Kudo N, Wolff B, Sekimoto T, Schreiner EP, Yoneda Y, et al. (1998) Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. Exp Cell Res 242: 540-547.
    • (1998) Exp Cell Res , vol.242 , pp. 540-547
    • Kudo, N.1    Wolff, B.2    Sekimoto, T.3    Schreiner, E.P.4    Yoneda, Y.5
  • 48
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: Definition, function, and interaction with importin alpha
    • Lange A, Mills RE, Lange CJ, Stewart M, Devine SE, et al. (2007) Classical nuclear localization signals: definition, function, and interaction with importin alpha. J Biol Chem 282: 5101-5105.
    • (2007) J Biol Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5
  • 49
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton LF, Paschal BM (2005) Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6: 187-198.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 51
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: Hierarchical regulation of nucleocytoplasmic transport
    • Terry LJ, Shows EB, Wente SR (2007) Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science 318: 1412-1416.
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 52
    • 0034662924 scopus 로고    scopus 로고
    • The virulence factor AvrXa7 of Xanthomonas oryzae pv. oryzae is a type III secretion pathway-dependent nuclear-localized double-stranded DNA-binding protein
    • Yang B, Zhu W, Johnson LB, White FF (2000) The virulence factor AvrXa7 of Xanthomonas oryzae pv. oryzae is a type III secretion pathway-dependent nuclear-localized double-stranded DNA-binding protein. Proc Natl Acad Sci U S A 97: 9807-9812.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9807-9812
    • Yang, B.1    Zhu, W.2    Johnson, L.B.3    White, F.F.4
  • 53
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel SS, Belmont BJ, Sante JM, Rexach MF (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129: 83-96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 54
    • 0345118103 scopus 로고    scopus 로고
    • Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: A model for misfolding in polyglutamine disease
    • Chow MK, Paulson HL, Bottomley SP (2004) Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease. J Mol Biol 335: 333-341.
    • (2004) J Mol Biol , vol.335 , pp. 333-341
    • Chow, M.K.1    Paulson, H.L.2    Bottomley, S.P.3
  • 55
    • 26244434741 scopus 로고    scopus 로고
    • Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: Trapping early oligomers of non-expanded ataxin-3
    • Gales L, Cortes L, Almeida C, Melo CV, do Carmo Costa M, et al. (2005) Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3. J Mol Biol 353: 642-654.
    • (2005) J Mol Biol , vol.353 , pp. 642-654
    • Gales, L.1    Cortes, L.2    Almeida, C.3    Melo, C.V.4    do Carmo5    Costa, M.6
  • 56
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3
    • Masino L, Nicastro G, Menon RP, Dal Piaz F, Calder L, et al. (2004) Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3. J Mol Biol 344: 1021-1035.
    • (2004) J Mol Biol , vol.344 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Dal Piaz, F.4    Calder, L.5
  • 57
    • 0032735135 scopus 로고    scopus 로고
    • Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix
    • Perez MK, Paulson HL, Pittman RN (1999) Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix. Hum Mol Genet 8: 2377-2385.
    • (1999) Hum Mol Genet , vol.8 , pp. 2377-2385
    • Perez, M.K.1    Paulson, H.L.2    Pittman, R.N.3
  • 58
    • 0042808497 scopus 로고    scopus 로고
    • Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates
    • Donaldson KM, Li W, Ching KA, Batalov S, Tsai CC, et al. (2003) Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates. Proc Natl Acad Sci U S A 100: 8892-8897.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8892-8897
    • Donaldson, K.M.1    Li, W.2    Ching, K.A.3    Batalov, S.4    Tsai, C.C.5
  • 59
    • 4444229456 scopus 로고    scopus 로고
    • Exportin 7 defines a novel general nuclear export pathway
    • Mingot JM, Bohnsack MT, Jakle U, Gorlich D (2004) Exportin 7 defines a novel general nuclear export pathway. Embo J 23: 3227-3236.
    • (2004) Embo J , vol.23 , pp. 3227-3236
    • Mingot, J.M.1    Bohnsack, M.T.2    Jakle, U.3    Gorlich, D.4
  • 60
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: Born to be weak
    • Kutay U, Guttinger S (2005) Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol 15: 121-124.
    • (2005) Trends Cell Biol , vol.15 , pp. 121-124
    • Kutay, U.1    Guttinger, S.2
  • 62
    • 1642543151 scopus 로고    scopus 로고
    • Nuclear export of alpha-catenin: Overlap between nuclear export signal sequences and the beta-catenin binding site
    • Giannini A, Mazor M, Orme M, Vivanco M, Waxman J, et al. (2004) Nuclear export of alpha-catenin: overlap between nuclear export signal sequences and the beta-catenin binding site. Exp Cell Res 295: 150-160.
    • (2004) Exp Cell Res , vol.295 , pp. 150-160
    • Giannini, A.1    Mazor, M.2    Orme, M.3    Vivanco, M.4    Waxman, J.5
  • 63
    • 4644362866 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): Identification of novel nuclear export and import signals in RIP3
    • Yang Y, Ma J, Chen Y, Wu M (2004) Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3. J Biol Chem 279: 38820-38829.
    • (2004) J Biol Chem , vol.279 , pp. 38820-38829
    • Yang, Y.1    Ma, J.2    Chen, Y.3    Wu, M.4
  • 64
    • 31144441675 scopus 로고    scopus 로고
    • Nuclear export of African swine fever virus p37 protein occurs through two distinct pathways and is mediated by three independent signals
    • Eulalio A, Nunes-Correia I, Carvalho AL, Faro C, Citovsky V, et al. (2006) Nuclear export of African swine fever virus p37 protein occurs through two distinct pathways and is mediated by three independent signals. J Virol 80: 1393-1404.
    • (2006) J Virol , vol.80 , pp. 1393-1404
    • Eulalio, A.1    Nunes-Correia, I.2    Carvalho, A.L.3    Faro, C.4    Citovsky, V.5
  • 65
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation
    • Perez MK, Paulson HL, Pendse SJ, Saionz SJ, Bonini NM, et al. (1998) Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol 143: 1457-1470.
    • (1998) J Cell Biol , vol.143 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5
  • 66
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
    • Chai Y, Shao J, Miller VM, Williams A, Paulson HL (2002) Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc Natl Acad Sci U S A 99: 9310-9315.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9310-9315
    • Chai, Y.1    Shao, J.2    Miller, V.M.3    Williams, A.4    Paulson, H.L.5
  • 67
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • Bilen J, Bonini NM (2007) Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genet 3: 1950-1964.
    • (2007) PLoS Genet , vol.3 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 68
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


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