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Volumn 124, Issue 7, 2014, Pages 3080-3092

TorsinA hypofunction causes abnormal twisting movements and sensorimotor circuit neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; NESTIN; PROTEIN; PROTEIN DYT 1; TORSINA; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84903773326     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI72830     Document Type: Article
Times cited : (108)

References (62)
  • 2
    • 79952702136 scopus 로고    scopus 로고
    • Genetic and clinical features of primary torsion dystonia
    • Ozelius LJ, Bressman SB. Genetic and clinical features of primary torsion dystonia. Neurobiol Dis. 2011;42(2):127-135.
    • (2011) Neurobiol Dis , vol.42 , Issue.2 , pp. 127-135
    • Ozelius, L.J.1    Bressman, S.B.2
  • 3
    • 84880772785 scopus 로고    scopus 로고
    • Phenomenology and classification of dystonia: A consensus update
    • Albanese A, et al. Phenomenology and classification of dystonia: a consensus update. Mov Disord. 2013; 28(7):863-873.
    • (2013) Mov Disord , vol.28 , Issue.7 , pp. 863-873
    • Albanese, A.1
  • 4
    • 79952693973 scopus 로고    scopus 로고
    • Update on the pathology of dystonia
    • Standaert DG. Update on the pathology of dystonia. Neurobiol Dis. 2011;42(2):148-151.
    • (2011) Neurobiol Dis , vol.42 , Issue.2 , pp. 148-151
    • Standaert, D.G.1
  • 5
    • 0034702033 scopus 로고    scopus 로고
    • Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells
    • Hewett J, et al. Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells. Hum Mol Genet. 2000; 9(9):1403-1413.
    • (2000) Hum Mol Genet , vol.9 , Issue.9 , pp. 1403-1413
    • Hewett, J.1
  • 6
    • 0034623158 scopus 로고    scopus 로고
    • Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations
    • Kustedjo K, Bracey MH, Cravatt BF. Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations. J Biol Chem. 2000; 275(36):27933-27939.
    • (2000) J Biol Chem , vol.275 , Issue.36 , pp. 27933-27939
    • Kustedjo, K.1    Bracey, M.H.2    Cravatt, B.F.3
  • 7
    • 1642433201 scopus 로고    scopus 로고
    • Mislocalization to the nuclear envelope: An effect of the dystonia-causing torsinA mutation
    • Goodchild RE, Dauer WT. Mislocalization to the nuclear envelope: an effect of the dystonia-causing torsinA mutation. Proc Natl Acad Sci U S A. 2004; 101(3):847-852.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.3 , pp. 847-852
    • Goodchild, R.E.1    Dauer, W.T.2
  • 8
    • 29144460260 scopus 로고    scopus 로고
    • Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope
    • Goodchild RE, Kim CE, Dauer WT. Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope. Neuron. 2005; 48(6):923-932.
    • (2005) Neuron , vol.48 , Issue.6 , pp. 923-932
    • Goodchild, R.E.1    Kim, C.E.2    Dauer, W.T.3
  • 9
    • 70350463845 scopus 로고    scopus 로고
    • Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion
    • Naismith TV, Dalal S, Hanson PI. Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion. J Biol Chem. 2009;284(41):27866-27874.
    • (2009) J Biol Chem , vol.284 , Issue.41 , pp. 27866-27874
    • Naismith, T.V.1    Dalal, S.2    Hanson, P.I.3
  • 11
    • 27744533560 scopus 로고    scopus 로고
    • Silencing primary dystonia: Lentiviral-mediated RNA interference therapy for DYT1 dystonia
    • Gonzalez-Alegre P, Bode N, Davidson BL, Paulson HL. Silencing primary dystonia: lentiviral-mediated RNA interference therapy for DYT1 dystonia. J Neurosci. 2005;25(45):10502-10509.
    • (2005) J Neurosci , vol.25 , Issue.45 , pp. 10502-10509
    • Gonzalez-Alegre, P.1    Bode, N.2    Davidson, B.L.3    Paulson, H.L.4
  • 12
    • 8144230422 scopus 로고    scopus 로고
    • Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystoniaassociated DeltaE-torsinA mutant
    • Torres GE, Sweeney AL, Beaulieu J-M, Shashidharan P, Caron MG. Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystoniaassociated DeltaE-torsinA mutant. Proc Natl Acad Sci U S A. 2004;101(44):15650-15655.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.44 , pp. 15650-15655
    • Torres, G.E.1    Sweeney, A.L.2    Beaulieu, J.-M.3    Shashidharan, P.4    Caron, M.G.5
  • 13
    • 79960292775 scopus 로고    scopus 로고
    • TorsinA participates in endoplasmic reticulum-associated degradation
    • Nery FC, et al. TorsinA participates in endoplasmic reticulum-associated degradation. Nat Commun. 2011;2:393.
    • (2011) Nat Commun , vol.2 , pp. 393
    • Nery, F.C.1
  • 14
    • 77956113164 scopus 로고    scopus 로고
    • The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response
    • Chen P, et al. The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response. Hum Mol Genet. 2010;19(18):3502-3515.
    • (2010) Hum Mol Genet , vol.19 , Issue.18 , pp. 3502-3515
    • Chen, P.1
  • 15
    • 43049088486 scopus 로고    scopus 로고
    • SiRNA knock-down of mutant torsinA restores processing through secretory pathway in DYT1 dystonia cells
    • Hewett JW, et al. siRNA knock-down of mutant torsinA restores processing through secretory pathway in DYT1 dystonia cells. Hum Mol Genet. 2008; 17(10):1436-1445.
    • (2008) Hum Mol Genet , vol.17 , Issue.10 , pp. 1436-1445
    • Hewett, J.W.1
  • 16
    • 34249850241 scopus 로고    scopus 로고
    • Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells
    • Hewett JW, et al. Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells. Proc Natl Acad Sci U S A. 2007; 104(17):7271-7276.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.17 , pp. 7271-7276
    • Hewett, J.W.1
  • 17
    • 1642290757 scopus 로고    scopus 로고
    • Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia
    • Gonzalez-Alegre P, Paulson HL. Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia. J Neurosci. 2004; 24(11):2593-2601.
    • (2004) J Neurosci , vol.24 , Issue.11 , pp. 2593-2601
    • Gonzalez-Alegre, P.1    Paulson, H.L.2
  • 18
    • 15444374750 scopus 로고    scopus 로고
    • The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein
    • Goodchild RE, Dauer WT. The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein. J Cell Biol. 2005; 168(6):855-862.
    • (2005) J Cell Biol , vol.168 , Issue.6 , pp. 855-862
    • Goodchild, R.E.1    Dauer, W.T.2
  • 20
    • 79957650385 scopus 로고    scopus 로고
    • The nuclear envelope localization of DYT1 dystonia torsinA-?E requires the SUN1 LINC complex component
    • Jungwirth MT, Kumar D, Jeong DY, Goodchild RE. The nuclear envelope localization of DYT1 dystonia torsinA-?E requires the SUN1 LINC complex component. BMC Cell Biol. 2011;12:24.
    • (2011) BMC Cell Biol , vol.12 , pp. 24
    • Jungwirth, M.T.1    Kumar, D.2    Jeong, D.Y.3    Goodchild, R.E.4
  • 21
    • 56349160730 scopus 로고    scopus 로고
    • TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton
    • Nery FC, et al. TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. J Cell Sci. 2008; 121(pt 20):3476-3486.
    • (2008) J Cell Sci , vol.121 , Issue.PART 20 , pp. 3476-3486
    • Nery, F.C.1
  • 22
    • 34447641630 scopus 로고    scopus 로고
    • Overexpression of human wildtype torsinA and human DeltaGAG torsinA in a transgenic mouse model causes phenotypic abnormalities
    • Grundmann K, et al. Overexpression of human wildtype torsinA and human DeltaGAG torsinA in a transgenic mouse model causes phenotypic abnormalities. Neurobiol Dis. 2007;27(2):190-206.
    • (2007) Neurobiol Dis , vol.27 , Issue.2 , pp. 190-206
    • Grundmann, K.1
  • 23
    • 20044374519 scopus 로고    scopus 로고
    • Impaired motor learning in mice expressing torsinA with the DYT1 dystonia mutation
    • Sharma N, et al. Impaired motor learning in mice expressing torsinA with the DYT1 dystonia mutation. J Neurosci. 2005;25(22):5351-5355.
    • (2005) J Neurosci , vol.25 , Issue.22 , pp. 5351-5355
    • Sharma, N.1
  • 24
    • 77954956971 scopus 로고    scopus 로고
    • Cell-autonomous alteration of dopaminergic transmission by wild type and mutant (DeltaE) TorsinA in transgenic mice
    • Page ME, et al. Cell-autonomous alteration of dopaminergic transmission by wild type and mutant (DeltaE) TorsinA in transgenic mice. Neurobiol Dis. 2010;39(3):318-326.
    • (2010) Neurobiol Dis , vol.39 , Issue.3 , pp. 318-326
    • Page, M.E.1
  • 25
    • 84861231595 scopus 로고    scopus 로고
    • Generation of a novel rodent model for DYT1 dystonia
    • Grundmann K, et al. Generation of a novel rodent model for DYT1 dystonia. Neurobiol Dis. 2012; 47(1):61-74.
    • (2012) Neurobiol Dis , vol.47 , Issue.1 , pp. 61-74
    • Grundmann, K.1
  • 26
    • 27744567561 scopus 로고    scopus 로고
    • Generation and characterization of Dyt1 DeltaGAG knock-in mouse as a model for earlyonset dystonia
    • Dang MT, et al. Generation and characterization of Dyt1 DeltaGAG knock-in mouse as a model for earlyonset dystonia. Exp Neurol. 2005;196(2):452-463.
    • (2005) Exp Neurol , vol.196 , Issue.2 , pp. 452-463
    • Dang, M.T.1
  • 27
    • 84857678883 scopus 로고    scopus 로고
    • Genetic background modulates the phenotype of a mouse model of DYT1 dystonia
    • Tanabe LM, Martin C, Dauer WT. Genetic background modulates the phenotype of a mouse model of DYT1 dystonia. PLoS One. 2012; 7(2):e32245.
    • (2012) PLoS One , vol.7 , Issue.2
    • Tanabe, L.M.1    Martin, C.2    Dauer, W.T.3
  • 28
    • 84863422091 scopus 로고    scopus 로고
    • Cholinergic dysregulation produced by selective inactivation of the dystoniaassociated protein torsinA
    • Sciamanna G, et al. Cholinergic dysregulation produced by selective inactivation of the dystoniaassociated protein torsinA. Neurobiol Dis. 2012; 47(3):416-427.
    • (2012) Neurobiol Dis , vol.47 , Issue.3 , pp. 416-427
    • Sciamanna, G.1
  • 29
    • 80052634773 scopus 로고    scopus 로고
    • Motor deficits and decreased striatal dopamine receptor 2 binding activity in the striatum-specific Dyt1 conditional knockout mice
    • Yokoi F, Dang MT, Li J, Standaert DG, Li Y. Motor deficits and decreased striatal dopamine receptor 2 binding activity in the striatum-specific Dyt1 conditional knockout mice. PLoS One. 2011; 6(9):e24539.
    • (2011) PLoS One , vol.6 , Issue.9
    • Yokoi, F.1    Dang, M.T.2    Li, J.3    Standaert, D.G.4    Li, Y.5
  • 30
    • 79953173585 scopus 로고    scopus 로고
    • Altered dendritic morphology of Purkinje cells in Dyt1 ?GAG knock-in and purkinje cell-specific Dyt1 conditional knockout mice
    • Zhang L, et al. Altered dendritic morphology of Purkinje cells in Dyt1 ?GAG knock-in and purkinje cell-specific Dyt1 conditional knockout mice. PLoS One. 2011;6(3):e18357.
    • (2011) PLoS One , vol.6 , Issue.3
    • Zhang, L.1
  • 31
    • 79955633670 scopus 로고    scopus 로고
    • Cerebellothalamocortical pathway abnormalities in torsinA DYT1 knock-in mice
    • Ulug AM, et al. Cerebellothalamocortical pathway abnormalities in torsinA DYT1 knock-in mice. Proc Natl Acad Sci U S A. 2011;108(16):6638-6643.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.16 , pp. 6638-6643
    • Ulug, A.M.1
  • 32
    • 68549092937 scopus 로고    scopus 로고
    • Cerebellothalamocortical connectivity regulates penetrance in dystonia
    • Argyelan M, et al. Cerebellothalamocortical connectivity regulates penetrance in dystonia. J Neurosci. 2009;29(31):9740-9747.
    • (2009) J Neurosci , vol.29 , Issue.31 , pp. 9740-9747
    • Argyelan, M.1
  • 33
    • 79954415475 scopus 로고    scopus 로고
    • Exploring the influence of torsinA expression on protein quality control
    • Gordon KL, Glenn KA, Gonzalez-Alegre P. Exploring the influence of torsinA expression on protein quality control. Neurochem Res. 2011;36(3):452-459.
    • (2011) Neurochem Res , vol.36 , Issue.3 , pp. 452-459
    • Gordon, K.L.1    Glenn, K.A.2    Gonzalez-Alegre, P.3
  • 34
    • 79960804408 scopus 로고    scopus 로고
    • TorsinA and the torsinAinteracting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast
    • Valastyan JS, Lindquist S. TorsinA and the torsinAinteracting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast. PLoS One. 2011;6(7):e22744.
    • (2011) PLoS One , vol.6 , Issue.7
    • Valastyan, J.S.1    Lindquist, S.2
  • 35
    • 77955710947 scopus 로고    scopus 로고
    • The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro
    • Burdette AJ, Churchill PF, Caldwell GA, Caldwell KA. The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro. Cell Stress Chaperones. 2010; 15(5):605-617.
    • (2010) Cell Stress Chaperones , vol.15 , Issue.5 , pp. 605-617
    • Burdette, A.J.1    Churchill, P.F.2    Caldwell, G.A.3    Caldwell, K.A.4
  • 36
    • 0029572439 scopus 로고
    • The metabolic topography of idiopathic torsion dystonia
    • Eidelberg D, et al. The metabolic topography of idiopathic torsion dystonia. Brain. 1995; 118(pt 6):1473-1484.
    • (1995) Brain , vol.118 , Issue.PART 6 , pp. 1473-1484
    • Eidelberg, D.1
  • 37
    • 0027988344 scopus 로고
    • Dystonia in Ashkenazi Jews: Clinical characterization of a founder mutation
    • Bressman SB, et al. Dystonia in Ashkenazi Jews: clinical characterization of a founder mutation. Ann Neurol. 1994;36(5):771-777.
    • (1994) Ann Neurol , vol.36 , Issue.5 , pp. 771-777
    • Bressman, S.B.1
  • 38
    • 0032754787 scopus 로고    scopus 로고
    • Distribution of the mRNAs encoding torsinA and torsinB in the normal adult human brain
    • Augood SJ, et al. Distribution of the mRNAs encoding torsinA and torsinB in the normal adult human brain. Ann Neurol. 1999;46(5):761-769.
    • (1999) Ann Neurol , vol.46 , Issue.5 , pp. 761-769
    • Augood, S.J.1
  • 39
    • 18344378034 scopus 로고    scopus 로고
    • Molecular cloning and expression of rat torsinA in the normal and genetically dystonic (dt) rat
    • Ziefer P, et al. Molecular cloning and expression of rat torsinA in the normal and genetically dystonic (dt) rat. Brain Res Mol Brain Res. 2002;101(1-2):132-135.
    • (2002) Brain Res Mol Brain Res , vol.101 , Issue.1-2 , pp. 132-135
    • Ziefer, P.1
  • 40
    • 0034635370 scopus 로고    scopus 로고
    • Ethanol-induced apoptotic neurodegeneration and fetal alcohol syndrome
    • Ikonomidou C, et al. Ethanol-induced apoptotic neurodegeneration and fetal alcohol syndrome. Science. 2000;287(5455):1056-1060.
    • (2000) Science , vol.287 , Issue.5455 , pp. 1056-1060
    • Ikonomidou, C.1
  • 41
    • 77953090863 scopus 로고    scopus 로고
    • A molecular mechanism underlying the neural-specific defect in torsinA mutant mice
    • Kim CE, Perez A, Perkins G, Ellisman MH, Dauer WT. A molecular mechanism underlying the neural-specific defect in torsinA mutant mice. Proc Natl Acad Sci U S A. 2010;107(21):9861-9866.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.21 , pp. 9861-9866
    • Kim, C.E.1    Perez, A.2    Perkins, G.3    Ellisman, M.H.4    Dauer, W.T.5
  • 42
    • 33644963223 scopus 로고    scopus 로고
    • Developmental patterns of torsinA and torsinB expression
    • Vasudevan A, Breakefield XO, Bhide PG. Developmental patterns of torsinA and torsinB expression. Brain Res. 2006;1073-1074:139-145.
    • (2006) Brain Res , vol.1073-1074 , pp. 139-145
    • Vasudevan, A.1    Breakefield, X.O.2    Bhide, P.G.3
  • 43
    • 80054004851 scopus 로고    scopus 로고
    • A functional role for TorsinA in herpes simplex virus 1 nuclear egress
    • Maric M, et al. A functional role for TorsinA in herpes simplex virus 1 nuclear egress. J Virol. 2011; 85(19):9667-9679.
    • (2011) J Virol , vol.85 , Issue.19 , pp. 9667-9679
    • Maric, M.1
  • 44
    • 84876955658 scopus 로고    scopus 로고
    • Torsin mediates primary envelopment of large ribonucleoprotein granules at the nuclear envelope
    • Jokhi V, et al. Torsin mediates primary envelopment of large ribonucleoprotein granules at the nuclear envelope. Cell Rep. 2013;3(4):988-995.
    • (2013) Cell Rep , vol.3 , Issue.4 , pp. 988-995
    • Jokhi, V.1
  • 45
    • 43149084144 scopus 로고    scopus 로고
    • Immunohistochemical localization of a ubiquitin ligase HRD1 in murine brain
    • Omura T, Kaneko M, Tabei N, Okuma Y, Nomura Y. Immunohistochemical localization of a ubiquitin ligase HRD1 in murine brain. J Neurosci Res. 2008; 86(7):1577-1587.
    • (2008) J Neurosci Res , vol.86 , Issue.7 , pp. 1577-1587
    • Omura, T.1    Kaneko, M.2    Tabei, N.3    Okuma, Y.4    Nomura, Y.5
  • 46
    • 20044394518 scopus 로고    scopus 로고
    • Essential role of synoviolin in embryogenesis
    • Yagishita N, et al. Essential role of synoviolin in embryogenesis. J Biol Chem. 2005;280(9):7909-7916.
    • (2005) J Biol Chem , vol.280 , Issue.9 , pp. 7909-7916
    • Yagishita, N.1
  • 47
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng M, Hochstrasser M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature. 2006;443(7113):827-831.
    • (2006) Nature , vol.443 , Issue.7113 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 48
    • 69249150847 scopus 로고    scopus 로고
    • Printor, a novel torsinAinteracting protein implicated in dystonia pathogenesis
    • Giles LM, Li L, Chin LS. Printor, a novel torsinAinteracting protein implicated in dystonia pathogenesis.J Biol Chem. 2009;284(32):21765-21775.
    • (2009) J Biol Chem , vol.284 , Issue.32 , pp. 21765-21775
    • Giles, L.M.1    Li, L.2    Chin, L.S.3
  • 49
    • 0027978063 scopus 로고
    • The behavioural and motor consequences of focal lesions of the basal ganglia in man
    • Bhatia KP, Marsden CD. The behavioural and motor consequences of focal lesions of the basal ganglia in man. Brain. 1994;117(pt 4):859-876.
    • (1994) Brain , vol.117 , Issue.PART 4 , pp. 859-876
    • Bhatia, K.P.1    Marsden, C.D.2
  • 50
    • 0028017280 scopus 로고
    • Movement disorders following lesions of the thalamus or subthalamic region
    • Lee MS, Marsden CD. Movement disorders following lesions of the thalamus or subthalamic region. Mov Disord. 1994;9(5):493-507.
    • (1994) Mov Disord , vol.9 , Issue.5 , pp. 493-507
    • Lee, M.S.1    Marsden, C.D.2
  • 51
    • 84866652556 scopus 로고    scopus 로고
    • Limited regional cerebellar dysfunction induces focal dystonia in mice
    • Raike RS, et al. Limited regional cerebellar dysfunction induces focal dystonia in mice. Neurobiol Dis. 2012;49C:200-210.
    • (2012) Neurobiol Dis , vol.49 C , pp. 200-210
    • Raike, R.S.1
  • 52
    • 79952009635 scopus 로고    scopus 로고
    • The neural substrates of rapid-onset dystonia-parkinsonism
    • Calderon DP, Fremont R, Kraenzlin F, Khodakhah K. The neural substrates of rapid-onset Dystonia-Parkinsonism. Nat Neurosci. 2011;14(3):357-365.
    • (2011) Nat Neurosci , vol.14 , Issue.3 , pp. 357-365
    • Calderon, D.P.1    Fremont, R.2    Kraenzlin, F.3    Khodakhah, K.4
  • 53
    • 0025891961 scopus 로고
    • Effect of harmaline oncells of the inferior olive in the absence of tremor: Differential response of genetically dystonic and harmaline-tolerant rats
    • Stratton SE, Lorden JF. Effect of harmaline oncells of the inferior olive in the absence of tremor: differential response of genetically dystonic and harmaline-tolerant rats. Neuroscience. 1991; 41(2-3):543-549.
    • (1991) Neuroscience , vol.41 , Issue.2-3 , pp. 543-549
    • Stratton, S.E.1    Lorden, J.F.2
  • 54
    • 0027251669 scopus 로고
    • Cerebellectomy eliminates the motor syndrome of the genetically dystonic rat
    • LeDoux MS, Lorden JF, Ervin JM. Cerebellectomy eliminates the motor syndrome of the genetically dystonic rat. Exp Neurol. 1993;120(2):302-310.
    • (1993) Exp Neurol , vol.120 , Issue.2 , pp. 302-310
    • Ledoux, M.S.1    Lorden, J.F.2    Ervin, J.M.3
  • 55
    • 0036703466 scopus 로고    scopus 로고
    • Cortical excitatory neurons and glia, but not GABAergic neurons, are produced in the Emx1-expressing lineage
    • Gorski JA, et al. Cortical excitatory neurons and glia, but not GABAergic neurons, are produced in the Emx1-expressing lineage. J Neurosci. 2002; 22(15):6309-6314.
    • (2002) J Neurosci , vol.22 , Issue.15 , pp. 6309-6314
    • Gorski, J.A.1
  • 56
    • 0033748392 scopus 로고    scopus 로고
    • Topographical and physiological characterization of interneurons that express engrailed-1 in the embryonic chick spinal cord
    • Wenner P, O?Donovan MJ, Matise MP. Topographical and physiological characterization of interneurons that express engrailed-1 in the embryonic chick spinal cord. J Neurophysiol. 2000;84(5):2651-2657.
    • (2000) J Neurophysiol , vol.84 , Issue.5 , pp. 2651-2657
    • Wenner, P.1    O'Donovan, M.J.2    Matise, M.P.3
  • 57
    • 85114476016 scopus 로고    scopus 로고
    • Primary dystonia: Conceptualizing the disorder through a structural brain imaging lens
    • pii:tre-03-152-3638-4
    • Ramdhani RA, Simonyan K. Primary dystonia: conceptualizing the disorder through a structural brain imaging lens. Tremor Other Hyperkinet Mov (N Y). 2013;3.pii:tre-03-152-3638-4.
    • (2013) Tremor Other Hyperkinet Mov (N Y) , vol.3
    • Ramdhani, R.A.1    Simonyan, K.2
  • 58
    • 0037352031 scopus 로고    scopus 로고
    • A highly efficient recombineering-based method for generating conditional knockout mutations
    • Liu P, Jenkins NA, Copeland NG. A highly efficient recombineering-based method for generating conditional knockout mutations. Genome Res. 2003; 13(3):476-484.
    • (2003) Genome Res , vol.13 , Issue.3 , pp. 476-484
    • Liu, P.1    Jenkins, N.A.2    Copeland, N.G.3
  • 61
    • 16144368388 scopus 로고    scopus 로고
    • Mice lacking both subunits of lysosomal β-hexosaminidase display gangliosidosis and mucopolysaccharidosis
    • Sango K, et al. Mice lacking both subunits of lysosomal β-hexosaminidase display gangliosidosis and mucopolysaccharidosis. Nat Genet. 1996; 14(3):348-352.
    • (1996) Nat Genet , vol.14 , Issue.3 , pp. 348-352
    • Sango, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.