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Volumn 56, Issue 2, 2010, Pages 329-339

Polyglutamine-expanded ataxin-7 causes cerebellar dysfunction by inducing transcriptional dysregulation

Author keywords

Ataxin 7; Cerebellum; Polyglutamine expanded ataxin 7; SCA7 transgenic mice; Spinocerebellar ataxia type 7

Indexed keywords

ATAXIN 7; MESSENGER RNA; POLYGLUTAMINE;

EID: 77149137999     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2009.11.003     Document Type: Article
Times cited : (51)

References (61)
  • 2
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam J., Ozer R.S., Safer D., Halpain S., Milligan R.A. MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J. Cell Biol. 2002, 157:1187-1196.
    • (2002) J. Cell Biol. , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 3
    • 0036889724 scopus 로고    scopus 로고
    • Developmentally regulated expression of Neuro-p24 and its possible function in neurite extension
    • Araki M., Nagata K., Satoh Y., Kadota Y., Hisha H., Adachi Y., Taketani S. Developmentally regulated expression of Neuro-p24 and its possible function in neurite extension. Neurosci. Res. 2002, 44:379-389.
    • (2002) Neurosci. Res. , vol.44 , pp. 379-389
    • Araki, M.1    Nagata, K.2    Satoh, Y.3    Kadota, Y.4    Hisha, H.5    Adachi, Y.6    Taketani, S.7
  • 4
    • 36148945617 scopus 로고    scopus 로고
    • RGS proteins: regulation of G-protein signaling and beyond
    • Bansal G., Druey K.M., Xie Z.H. RGS proteins: regulation of G-protein signaling and beyond. Pharmacol. Ther. 2007, 116:473-495.
    • (2007) Pharmacol. Ther. , vol.116 , pp. 473-495
    • Bansal, G.1    Druey, K.M.2    Xie, Z.H.3
  • 5
    • 33748928786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
    • Butler R., Bates G.P. Histone deacetylase inhibitors as therapeutics for polyglutamine disorders. Nat. Rev. Neurosci. 2006, 7:784-796.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 784-796
    • Butler, R.1    Bates, G.P.2
  • 6
    • 0347287040 scopus 로고    scopus 로고
    • Interference of Crx-dependent transcription by ataxin-7 involves interaction between the glutamine regions and requires the ataxin-7 carboxyl-terminal region for nuclear localization
    • Chen S.M., Peng G.H., Wang X.J., Smith A.C., Grote S.K., Sopher B.L., La Spada A.R. Interference of Crx-dependent transcription by ataxin-7 involves interaction between the glutamine regions and requires the ataxin-7 carboxyl-terminal region for nuclear localization. Hum. Mol. Genet. 2004, 13:53-67.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 53-67
    • Chen, S.M.1    Peng, G.H.2    Wang, X.J.3    Smith, A.C.4    Grote, S.K.5    Sopher, B.L.6    La Spada, A.R.7
  • 7
    • 33947506515 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein-mediated signaling in central nervous system pathophysiology
    • Chen Y., Aulia S., Tang B.L. Myelin-associated glycoprotein-mediated signaling in central nervous system pathophysiology. Mol. Neurobiol. 2006, 34:81-92.
    • (2006) Mol. Neurobiol. , vol.34 , pp. 81-92
    • Chen, Y.1    Aulia, S.2    Tang, B.L.3
  • 8
    • 45049085458 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-3 causes cerebellar dysfunction of SCA3 transgenic mice by inducing transcriptional dysregulation
    • Chou A.H., Yeh T.H., Ouyang P., Chen Y.L., Chen S.Y., Wang H.L. Polyglutamine-expanded ataxin-3 causes cerebellar dysfunction of SCA3 transgenic mice by inducing transcriptional dysregulation. Neurobiol. Dis. 2008, 31:89-101.
    • (2008) Neurobiol. Dis. , vol.31 , pp. 89-101
    • Chou, A.H.1    Yeh, T.H.2    Ouyang, P.3    Chen, Y.L.4    Chen, S.Y.5    Wang, H.L.6
  • 9
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in neurodegenerative diseases: sometimes the chicken, sometimes the egg
    • Ciechanover A., Brundin P. The ubiquitin-proteasome pathway in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003, 40:427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 10
    • 0030864463 scopus 로고    scopus 로고
    • Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations
    • Clark H.B., Burright E.N., Yunis W.S., Larson S., Wilcox C., Hartman B., Matilla A., Zoghbi H.Y., Orr H.T. Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations. J. Neurosci. 1997, 17:7385-7395.
    • (1997) J. Neurosci. , vol.17 , pp. 7385-7395
    • Clark, H.B.1    Burright, E.N.2    Yunis, W.S.3    Larson, S.4    Wilcox, C.5    Hartman, B.6    Matilla, A.7    Zoghbi, H.Y.8    Orr, H.T.9
  • 11
    • 34547107623 scopus 로고    scopus 로고
    • Receptor activity-modifying proteins 2 and 3 have distinct physiological functions from embryogenesis to old age
    • Dackor R., Fritz-Six K., Smithies O., Caron K. Receptor activity-modifying proteins 2 and 3 have distinct physiological functions from embryogenesis to old age. J. Biol. Chem. 2007, 282:18094-18099.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18094-18099
    • Dackor, R.1    Fritz-Six, K.2    Smithies, O.3    Caron, K.4
  • 14
    • 35448989687 scopus 로고    scopus 로고
    • Conditional knock-out of Kir4.1 leads to glial membrane depolarization, inhibition of potassium and glutamate uptake, and enhanced short-term synaptic potentiation
    • Djukic B., Casper K.B., Philpot B.D., Chin L.S., McCarthy K.D. Conditional knock-out of Kir4.1 leads to glial membrane depolarization, inhibition of potassium and glutamate uptake, and enhanced short-term synaptic potentiation. J. Neurosci. 2007, 27:11354-11365.
    • (2007) J. Neurosci. , vol.27 , pp. 11354-11365
    • Djukic, B.1    Casper, K.B.2    Philpot, B.D.3    Chin, L.S.4    McCarthy, K.D.5
  • 15
    • 0042817834 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinase put PI4,5P(2) in its place
    • Doughman R.L., Firestone A.J., Anderson R.A. Phosphatidylinositol phosphate kinase put PI4,5P(2) in its place. J. Membr. Biol. 2003, 194:77-89.
    • (2003) J. Membr. Biol. , vol.194 , pp. 77-89
    • Doughman, R.L.1    Firestone, A.J.2    Anderson, R.A.3
  • 16
    • 33745088678 scopus 로고    scopus 로고
    • Molecular pathogenesis of spinocerebellar ataxias
    • Duenas A.M., Goold R., Giunti P. Molecular pathogenesis of spinocerebellar ataxias. Brain 2006, 129:1357-1370.
    • (2006) Brain , vol.129 , pp. 1357-1370
    • Duenas, A.M.1    Goold, R.2    Giunti, P.3
  • 17
    • 8144228406 scopus 로고    scopus 로고
    • Trinucleotide repeats and neurodegenerative disease
    • Everett C.M., Wood N.W. Trinucleotide repeats and neurodegenerative disease. Brain 2004, 127:2385-2405.
    • (2004) Brain , vol.127 , pp. 2385-2405
    • Everett, C.M.1    Wood, N.W.2
  • 18
    • 36448930958 scopus 로고    scopus 로고
    • Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration
    • Friedman M.J., Shah A.G., Fang Z.A., Ward E.G., Warren S.T., Li S.H., Li X.J. Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat. Neurosci. 2007, 10:1519-1528.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1519-1528
    • Friedman, M.J.1    Shah, A.G.2    Fang, Z.A.3    Ward, E.G.4    Warren, S.T.5    Li, S.H.6    Li, X.J.7
  • 19
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin stabilizing protein to dendritic spines
    • Fujii R., Takumi T. TLS facilitates transport of mRNA encoding an actin stabilizing protein to dendritic spines. J. Cell Sci. 2005, 118:5755-5765.
    • (2005) J. Cell Sci. , vol.118 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 20
    • 65849122227 scopus 로고    scopus 로고
    • Molecular pathogenesis and cellular pathology of spinocerebellar ataxia type 7 neurodegeneration
    • Garden A.G., La Spada A.R. Molecular pathogenesis and cellular pathology of spinocerebellar ataxia type 7 neurodegeneration. Cerebellum 2008, 22:138-149.
    • (2008) Cerebellum , vol.22 , pp. 138-149
    • Garden, A.G.1    La Spada, A.R.2
  • 21
    • 0037660062 scopus 로고    scopus 로고
    • Secretoneurin promotes pertussis toxin-sensitive neurite outgrowth in cerebellar granule cells
    • Gasser M.C., Berti I., Hauser K.F., Fischer-Colbrie R., Saria A. Secretoneurin promotes pertussis toxin-sensitive neurite outgrowth in cerebellar granule cells. J. Neurochem. 2003, 85:662-669.
    • (2003) J. Neurochem. , vol.85 , pp. 662-669
    • Gasser, M.C.1    Berti, I.2    Hauser, K.F.3    Fischer-Colbrie, R.4    Saria, A.5
  • 22
    • 33750501125 scopus 로고    scopus 로고
    • Opposite effects of PSD-95 and MPP3 PDZ proteins on serotonin 5-hydroxytryptamine2C receptor desensitization and membrane stability
    • Gavarini S., Becamel C., Altier C., Lory P., Poncet J., Bockaert J., Marin P. Opposite effects of PSD-95 and MPP3 PDZ proteins on serotonin 5-hydroxytryptamine2C receptor desensitization and membrane stability. Mol. Biol. Cell 2006, 17:4619-4631.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4619-4631
    • Gavarini, S.1    Becamel, C.2    Altier, C.3    Lory, P.4    Poncet, J.5    Bockaert, J.6    Marin, P.7
  • 23
    • 0037031819 scopus 로고    scopus 로고
    • TATA binding protein-free TAF-containing complex (TFTC) and p300 are both required for efficient transcriptional activation
    • Hardy S., Brand M., Mittler G., Yanagisawa J., Kato S., Meisterernst M., Tora L. TATA binding protein-free TAF-containing complex (TFTC) and p300 are both required for efficient transcriptional activation. J. Biol. Chem. 2002, 277:32875-32882.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32875-32882
    • Hardy, S.1    Brand, M.2    Mittler, G.3    Yanagisawa, J.4    Kato, S.5    Meisterernst, M.6    Tora, L.7
  • 24
    • 0030973352 scopus 로고    scopus 로고
    • Dendritic and somatic receptor channels in rat cerebellar Purkinje cells
    • Hausser M., Roth A. Dendritic and somatic receptor channels in rat cerebellar Purkinje cells. J. Physiol. 1997, 501:77-95.
    • (1997) J. Physiol. , vol.501 , pp. 77-95
    • Hausser, M.1    Roth, A.2
  • 25
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay D.G., Sathasivam K., Tobaben S., Stahl B., Marber M., Mestril R., Mahal A., Smith D.L., Woodman B., Bates G.P. Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 2004, 13:1389-1405.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 26
    • 33748695582 scopus 로고    scopus 로고
    • Transcriptional alterations and chromatin remodeling in polyglutamine diseases
    • Helmlinger D., Tora L., Devys D. Transcriptional alterations and chromatin remodeling in polyglutamine diseases. Trends Genet. 2006, 22:562-570.
    • (2006) Trends Genet. , vol.22 , pp. 562-570
    • Helmlinger, D.1    Tora, L.2    Devys, D.3
  • 27
  • 28
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa N., Takemura R. Molecular motors and mechanisms of directional transport in neurons. Nat. Rev. Neurosci. 2005, 6:201-211.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 201-211
    • Hirokawa, N.1    Takemura, R.2
  • 29
    • 34548103304 scopus 로고    scopus 로고
    • Multiple functions of junctin and junctate, two distinct isoforms of aspartyl beta-hydroxylase
    • Hong C.S., Kwon S.J., Kim D.H. Multiple functions of junctin and junctate, two distinct isoforms of aspartyl beta-hydroxylase. Biochem. Biophys. Res. Commun. 2007, 362:1-4.
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 1-4
    • Hong, C.S.1    Kwon, S.J.2    Kim, D.H.3
  • 30
    • 15444363703 scopus 로고    scopus 로고
    • PLP1-related inherited dysmyelinating disorders: Pelizaeus-Merzbacher disease and spastic paraplegia type 2
    • Inoue K. PLP1-related inherited dysmyelinating disorders: Pelizaeus-Merzbacher disease and spastic paraplegia type 2. Neurogenetics 2005, 6:1-16.
    • (2005) Neurogenetics , vol.6 , pp. 1-16
    • Inoue, K.1
  • 31
    • 29244488777 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2)-deficient mice display motor deficits
    • Jaworski D.M., Soloway P., Caterina J., Falls W.A. Tissue inhibitor of metalloproteinase-2 (TIMP-2)-deficient mice display motor deficits. J. Neurobiol. 2006, 66:82-94.
    • (2006) J. Neurobiol. , vol.66 , pp. 82-94
    • Jaworski, D.M.1    Soloway, P.2    Caterina, J.3    Falls, W.A.4
  • 33
    • 24944475554 scopus 로고    scopus 로고
    • Functions and pathophysiological roles of phospholipase D in the brain
    • Klein J. Functions and pathophysiological roles of phospholipase D in the brain. J. Neurochem. 2005, 94:1473-1487.
    • (2005) J. Neurochem. , vol.94 , pp. 1473-1487
    • Klein, J.1
  • 34
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • Kuhn U., Wahle E. Structure and function of poly(A) binding proteins. Biochem. Biophys. Acta 2004, 1678:67-84.
    • (2004) Biochem. Biophys. Acta , vol.1678 , pp. 67-84
    • Kuhn, U.1    Wahle, E.2
  • 35
    • 0033919033 scopus 로고    scopus 로고
    • Expression analysis of ataxin-7 mRNA and protein in human brain: evidence for a widespread distribution and focal protein accumulation
    • Lindenberg K.S., Yvert G., Müller K., Landwehrmeyer G.B. Expression analysis of ataxin-7 mRNA and protein in human brain: evidence for a widespread distribution and focal protein accumulation. Brain Pathol. 2000, 10:385-394.
    • (2000) Brain Pathol. , vol.10 , pp. 385-394
    • Lindenberg, K.S.1    Yvert, G.2    Müller, K.3    Landwehrmeyer, G.B.4
  • 37
    • 20844441094 scopus 로고    scopus 로고
    • Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity
    • McMahon S.J., Pray-Grant M.G., Schieltz D., Yates J.R., Grant P.A. Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:8478-8482.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8478-8482
    • McMahon, S.J.1    Pray-Grant, M.G.2    Schieltz, D.3    Yates, J.R.4    Grant, P.A.5
  • 38
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 2005, 6:11-22.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 39
    • 0042869974 scopus 로고    scopus 로고
    • Polyglutamine diseases: a transcription disorder?
    • Okazawa H. Polyglutamine diseases: a transcription disorder?. Cell. Mol. Life Sci. 2003, 60:1427-1439.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1427-1439
    • Okazawa, H.1
  • 40
  • 42
    • 29244447354 scopus 로고    scopus 로고
    • Human class-I restricted T cell associated molecule is highly expressed in the cerebellum and is a marker for activated NKT and CD8+ T lymphocytes
    • Patino-Lopez G., Hevezi P., Lee J., Willhite D., Verge G.M., Lechner S., Ortiz-Navarrete M., Zlotnik V.A. Human class-I restricted T cell associated molecule is highly expressed in the cerebellum and is a marker for activated NKT and CD8+ T lymphocytes. J. Neuroimmunol. 2006, 171:145-155.
    • (2006) J. Neuroimmunol. , vol.171 , pp. 145-155
    • Patino-Lopez, G.1    Hevezi, P.2    Lee, J.3    Willhite, D.4    Verge, G.M.5    Lechner, S.6    Ortiz-Navarrete, M.7    Zlotnik, V.A.8
  • 43
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing a-synuclein from the platelet-derived growth factor and thy-1 promoters
    • Rockenstein E., Mallory M., Hashimoto M., Song D., Shults C.W., Lang I., Masliah E. Differential neuropathological alterations in transgenic mice expressing a-synuclein from the platelet-derived growth factor and thy-1 promoters. J. Neurosci. Res. 2002, 68:568-578.
    • (2002) J. Neurosci. Res. , vol.68 , pp. 568-578
    • Rockenstein, E.1    Mallory, M.2    Hashimoto, M.3    Song, D.4    Shults, C.W.5    Lang, I.6    Masliah, E.7
  • 46
    • 19544374135 scopus 로고    scopus 로고
    • Gene profiling links SCA1 pathophysiology to glutamate signaling in Purkinje cells of transgenic mice
    • Serra H.G., Byam C.E., Lande J.D., Tousey S.K., Zoghbi H.Y., Orr H.T. Gene profiling links SCA1 pathophysiology to glutamate signaling in Purkinje cells of transgenic mice. Hum. Mol. Genet. 2004, 13:2535-2543.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2535-2543
    • Serra, H.G.1    Byam, C.E.2    Lande, J.D.3    Tousey, S.K.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 47
    • 34547535639 scopus 로고    scopus 로고
    • The functions of UCH-L1 and its relation to neurodegenerative diseases
    • Setsuie R., Wada K. The functions of UCH-L1 and its relation to neurodegenerative diseases. Neurochem. Int. 2007, 51:105-111.
    • (2007) Neurochem. Int. , vol.51 , pp. 105-111
    • Setsuie, R.1    Wada, K.2
  • 48
    • 34247478454 scopus 로고    scopus 로고
    • LKB1/STRAD promotes axon initiation during neuronal polarization
    • Shelly M., Cancedda L., Heilshorn S., Sumbre G., Poo M.M. LKB1/STRAD promotes axon initiation during neuronal polarization. Cell 2007, 129:565-577.
    • (2007) Cell , vol.129 , pp. 565-577
    • Shelly, M.1    Cancedda, L.2    Heilshorn, S.3    Sumbre, G.4    Poo, M.M.5
  • 49
  • 50
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., Suzuki K. Structure and physiological function of calpains. Biochem. J. 1997, 326:721-732.
    • (1997) Biochem. J. , vol.326 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 52
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof T.C. The synaptic vesicle cycle. Annu. Rev. Neurosci. 2004, 27:509-547.
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 54
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: an ancient motor protein involved in multiple modes of transport
    • Vallee R.B., Williams J.C., Varma D., Barnhart L.E. Dynein: an ancient motor protein involved in multiple modes of transport. J. Neurobiol. 2004, 58:189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 55
    • 33645278637 scopus 로고    scopus 로고
    • Bex1, a novel interactor of the p75 neurotrophin receptor, links neurotrophin signaling to the cell cycle
    • Vilar M., Murillo-Carretero M., Mira H., Magnusson K., Besset V., Ibanez C.F. Bex1, a novel interactor of the p75 neurotrophin receptor, links neurotrophin signaling to the cell cycle. EMBO J. 2006, 25:1219-1230.
    • (2006) EMBO J. , vol.25 , pp. 1219-1230
    • Vilar, M.1    Murillo-Carretero, M.2    Mira, H.3    Magnusson, K.4    Besset, V.5    Ibanez, C.F.6
  • 56
    • 29044445801 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-7 activates mitochondrial apoptotic pathway of cerebellar neurons by upregulating Bax and downregulating Bcl-xL
    • Wang H.L., Yeh T.H., Chou A.H., Kuo Y.L., Luo L.J., He C.Y., Huang P.C., Li A.H. Polyglutamine-expanded ataxin-7 activates mitochondrial apoptotic pathway of cerebellar neurons by upregulating Bax and downregulating Bcl-xL. Cell. Signal. 2006, 18:541-552.
    • (2006) Cell. Signal. , vol.18 , pp. 541-552
    • Wang, H.L.1    Yeh, T.H.2    Chou, A.H.3    Kuo, Y.L.4    Luo, L.J.5    He, C.Y.6    Huang, P.C.7    Li, A.H.8
  • 57
    • 33846220180 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-7 decreases nuclear translocation of NF-κB p65 and impairs NF-κB activity by inhibiting proteasome activity of cerebellar neurons
    • Wang H.L., He C.Y., Chou A.H., Yeh T.H., Chen Y.L., Chou A.H., Li A. Polyglutamine-expanded ataxin-7 decreases nuclear translocation of NF-κB p65 and impairs NF-κB activity by inhibiting proteasome activity of cerebellar neurons. Cell. Signal. 2007, 19:573-581.
    • (2007) Cell. Signal. , vol.19 , pp. 573-581
    • Wang, H.L.1    He, C.Y.2    Chou, A.H.3    Yeh, T.H.4    Chen, Y.L.5    Chou, A.H.6    Li, A.7
  • 58
    • 13844276513 scopus 로고    scopus 로고
    • Myelinogenesis and axonal recognition by oligodendrocytes in brain are uncoupled in Olig1-null mice
    • Xin M., Yue T., Ma Z., Wu F., Gow A., Lu Q.R. Myelinogenesis and axonal recognition by oligodendrocytes in brain are uncoupled in Olig1-null mice. J. Neurosci. 2005, 25:1354-1365.
    • (2005) J. Neurosci. , vol.25 , pp. 1354-1365
    • Xin, M.1    Yue, T.2    Ma, Z.3    Wu, F.4    Gow, A.5    Lu, Q.R.6
  • 60
    • 77149154048 scopus 로고    scopus 로고
    • Expanded polyglutamines induce neurodegeneration and trans-neuronal alterations in cerebellum and retina of SCA7 transgenic mice
    • Yvert G., Lindenberg K.S., Picaud S., Landwehrmeyer G.B., Sahel J.A., Mandel J.L. Expanded polyglutamines induce neurodegeneration and trans-neuronal alterations in cerebellum and retina of SCA7 transgenic mice. Hum. Mol. Genet. 2001, 10:2569-2579.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2569-2579
    • Yvert, G.1    Lindenberg, K.S.2    Picaud, S.3    Landwehrmeyer, G.B.4    Sahel, J.A.5    Mandel, J.L.6
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.