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Volumn 1643, Issue , 2016, Pages 103-112

Atypical ubiquitination by E3 ligase WWP1 inhibits the proteasome-mediated degradation of mutant huntingtin

Author keywords

E3 ligase; Huntingtin; Huntington's disease; Ubiquitin proteasome system; Ubiquitination; WWP1

Indexed keywords

GAMMA TUBULIN; HUNTINGTIN; PROTEASOME; PROTEIN AGGREGATE; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE E3 WWP1; UNCLASSIFIED DRUG; HTT PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; WWP1 PROTEIN, MOUSE;

EID: 84966431237     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2016.03.027     Document Type: Article
Times cited : (29)

References (76)
  • 1
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • W. Baumeister, J. Walz, F. Zuhl, and E. Seemuller The proteasome: paradigm of a self-compartmentalizing protease Cell 92 1998 367 380
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 2
    • 2342598416 scopus 로고    scopus 로고
    • Experimental therapeutics in transgenic mouse models of Huntington's disease
    • M.F. Beal, and R.J. Ferrante Experimental therapeutics in transgenic mouse models of Huntington's disease Nat. Rev. Neurosci. 5 2004 373 384
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 373-384
    • Beal, M.F.1    Ferrante, R.J.2
  • 3
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • N.F. Bence, R.M. Sampat, and R.R. Kopito Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 4
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • E.J. Bennett, N.F. Bence, R. Jayakumar, and R.R. Kopito Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation Mol. Cell 17 2005 351 365
    • (2005) Mol. Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 6
    • 65249181587 scopus 로고    scopus 로고
    • The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease
    • J.S. Bett, C. Cook, L. Petrucelli, and G.P. Bates The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease PLoS One 4 2009 e5128
    • (2009) PLoS One , vol.4 , pp. e5128
    • Bett, J.S.1    Cook, C.2    Petrucelli, L.3    Bates, G.P.4
  • 7
    • 29644433718 scopus 로고    scopus 로고
    • Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: Exclusion of proteasome activator REGgamma as a therapeutic target
    • J.S. Bett, G.M. Goellner, B. Woodman, G. Pratt, M. Rechsteiner, and G.P. Bates Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGgamma as a therapeutic target Hum. Mol. Genet. 15 2006 33 44
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 33-44
    • Bett, J.S.1    Goellner, G.M.2    Woodman, B.3    Pratt, G.4    Rechsteiner, M.5    Bates, G.P.6
  • 8
    • 84870498174 scopus 로고    scopus 로고
    • Dysregulation of core components of SCF complex in poly-glutamine disorders
    • S. Bhutani, A. Das, M. Maheshwari, S.C. Lakhotia, and N.R. Jana Dysregulation of core components of SCF complex in poly-glutamine disorders Cell Death Dis. 3 2012 e428
    • (2012) Cell Death Dis. , vol.3 , pp. e428
    • Bhutani, S.1    Das, A.2    Maheshwari, M.3    Lakhotia, S.C.4    Jana, N.R.5
  • 9
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • A.B. Bowman, S.Y. Yoo, N.P. Dantuma, and H.Y. Zoghbi Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation Hum. Mol. Genet. 14 2005 679 691
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 13
    • 34248546185 scopus 로고    scopus 로고
    • The amplified WWP1 gene is a potential molecular target in breast cancer
    • C. Chen, Z. Zhou, J.S. Ross, W. Zhou, and J.T. Dong The amplified WWP1 gene is a potential molecular target in breast cancer Int. J. Cancer 121 2007 80 87
    • (2007) Int. J. Cancer , vol.121 , pp. 80-87
    • Chen, C.1    Zhou, Z.2    Ross, J.S.3    Zhou, W.4    Dong, J.T.5
  • 14
    • 84857015643 scopus 로고    scopus 로고
    • Identification of common genetic modifiers of neurodegenerative diseases from an integrative analysis of diverse genetic screens in model organisms
    • X. Chen, and R.D. Burgoyne Identification of common genetic modifiers of neurodegenerative diseases from an integrative analysis of diverse genetic screens in model organisms BMC Genom. 13 2012 71
    • (2012) BMC Genom. , vol.13 , pp. 71
    • Chen, X.1    Burgoyne, R.D.2
  • 15
    • 84860115678 scopus 로고    scopus 로고
    • Degradation of mutant huntingtin via the ubiquitin/proteasome system is modulated by FE65
    • W.N. Chow, H.W. Luk, H.Y. Chan, and K.F. Lau Degradation of mutant huntingtin via the ubiquitin/proteasome system is modulated by FE65 Biochem. J. 443 2012 681 689
    • (2012) Biochem. J. , vol.443 , pp. 681-689
    • Chow, W.N.1    Luk, H.W.2    Chan, H.Y.3    Lau, K.F.4
  • 16
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • A. Ciechanover Proteolysis: from the lysosome to ubiquitin and the proteasome Nat. Rev. Mol. Cell Biol. 6 2005 79 87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 17
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • A. Ciechanover, and P. Brundin The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg Neuron 40 2003 427 446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 18
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • C.J. Cummings, M.A. Mancini, B. Antalffy, D.B. DeFranco, H.T. Orr, and H.Y. Zoghbi Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 Nat. Genet. 19 1998 148 154
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 21
    • 33845898194 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases
    • R. de Pril, D.F. Fischer, R.A. Roos, and F.W. van Leeuwen Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases Mol. Cell. Neurosci. 34 2007 10 19
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 10-19
    • De Pril, R.1    Fischer, D.F.2    Roos, R.A.3    Van Leeuwen, F.W.4
  • 22
    • 34249085552 scopus 로고    scopus 로고
    • Proteasomes: Machines for all reasons
    • G.N. Demartino, and T.G. Gillette Proteasomes: machines for all reasons Cell 129 2007 659 662
    • (2007) Cell , vol.129 , pp. 659-662
    • Demartino, G.N.1    Gillette, T.G.2
  • 23
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • L. Deng, C. Wang, E. Spencer, L. Yang, A. Braun, J. You, C. Slaughter, C. Pickart, and Z.J. Chen Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain Cell 103 2000 351 361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 25
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • M. DiFiglia, E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, J.P. Vonsattel, and N. Aronin 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    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 26
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • M.L. Duennwald, and S. Lindquist Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity Genes Dev. 22 2008 3308 3319
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 27
    • 84864233715 scopus 로고    scopus 로고
    • Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation
    • B. Gong, C. Kielar, and A.J. Morton Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation PLoS One 7 2012 e41450
    • (2012) PLoS One , vol.7 , pp. e41450
    • Gong, B.1    Kielar, C.2    Morton, A.J.3
  • 29
    • 79151485014 scopus 로고    scopus 로고
    • Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease
    • A.N. Hegde, and S.C. Upadhya Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease Biochim. Biophys. Acta 1809 2011 128 140
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 128-140
    • Hegde, A.N.1    Upadhya, S.C.2
  • 32
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • R.M. Hofmann, and C.M. Pickart Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair Cell 96 1999 645 653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 36
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • G.R. Jackson, I. Salecker, X. Dong, X. Yao, N. Arnheim, P.W. Faber, M.E. MacDonald, and S.L. Zipursky Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons Neuron 21 1998 633 642
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.R.1    Salecker, I.2    Dong, X.3    Yao, X.4    Arnheim, N.5    Faber, P.W.6    MacDonald, M.E.7    Zipursky, S.L.8
  • 37
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • N.R. Jana, P. Dikshit, A. Goswami, S. Kotliarova, S. Murata, K. Tanaka, and N. Nukina Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes J. Biol. Chem. 280 2005 11635 11640
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 38
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • N.R. Jana, E.A. Zemskov, G. Wang, and N. Nukina Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release Hum. Mol. Genet. 10 2001 1049 1059
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 39
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Y. Kawaguchi, J.J. Kovacs, A. McLaurin, J.M. Vance, A. Ito, and T.P. Yao The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress Cell 115 2003 727 738
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 40
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • Z. Kostova, Y.C. Tsai, and A.M. Weissman Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation Semin. Cell Dev. Biol. 18 2007 770 779
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 41
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series
    • C. Landles, and G.P. Bates Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series EMBO Rep. 5 2004 958 963
    • (2004) EMBO Rep. , vol.5 , pp. 958-963
    • Landles, C.1    Bates, G.P.2
  • 42
    • 53749088439 scopus 로고    scopus 로고
    • Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases
    • X. Li, H. Li, and X.J. Li Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases Brain Res. Rev. 59 2008 245 252
    • (2008) Brain Res. Rev. , vol.59 , pp. 245-252
    • Li, X.1    Li, H.2    Li, X.J.3
  • 43
    • 77955291545 scopus 로고    scopus 로고
    • Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments
    • X. Li, C.E. Wang, S. Huang, X. Xu, X.J. Li, H. Li, and S. Li Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments Hum. Mol. Genet. 19 2010 2445 2455
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2445-2455
    • Li, X.1    Wang, C.E.2    Huang, S.3    Xu, X.4    Li, X.J.5    Li, H.6    Li, S.7
  • 44
    • 77955447356 scopus 로고    scopus 로고
    • Clearance of mutant huntingtin
    • X.J. Li, H. Li, and S. Li Clearance of mutant huntingtin Autophagy 6 2010 663 664
    • (2010) Autophagy , vol.6 , pp. 663-664
    • Li, X.J.1    Li, H.2    Li, S.3
  • 46
    • 84865528947 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin ligase Ube3a may be associated with synaptic pathophysiology in a mouse model of Huntington disease
    • M. Maheshwari, A. Samanta, S.K. Godavarthi, R. Mukherjee, and N.R. Jana Dysfunction of the ubiquitin ligase Ube3a may be associated with synaptic pathophysiology in a mouse model of Huntington disease J. Biol. Chem. 287 2012 29949 29957
    • (2012) J. Biol. Chem. , vol.287 , pp. 29949-29957
    • Maheshwari, M.1    Samanta, A.2    Godavarthi, S.K.3    Mukherjee, R.4    Jana, N.R.5
  • 47
    • 79955017869 scopus 로고    scopus 로고
    • Modifiers and mechanisms of multi-system polyglutamine neurodegenerative disorders: Lessons from fly models
    • M. Mallik, and S.C. Lakhotia Modifiers and mechanisms of multi-system polyglutamine neurodegenerative disorders: lessons from fly models J. Genet 89 2010 497 526
    • (2010) J. Genet , vol.89 , pp. 497-526
    • Mallik, M.1    Lakhotia, S.C.2
  • 50
    • 43149120469 scopus 로고    scopus 로고
    • E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity
    • A. Mishra, P. Dikshit, S. Purkayastha, J. Sharma, N. Nukina, and N.R. Jana E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity J. Biol. Chem. 283 2008 7648 7656
    • (2008) J. Biol. Chem. , vol.283 , pp. 7648-7656
    • Mishra, A.1    Dikshit, P.2    Purkayastha, S.3    Sharma, J.4    Nukina, N.5    Jana, N.R.6
  • 51
    • 63249135140 scopus 로고    scopus 로고
    • Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease
    • S. Mitra, A.S. Tsvetkov, and S. Finkbeiner Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease J. Biol. Chem. 284 2009 4398 4403
    • (2009) J. Biol. Chem. , vol.284 , pp. 4398-4403
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 52
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • H.T. Orr, and H.Y. Zoghbi Trinucleotide repeat disorders Annu. Rev. Neurosci. 30 2007 575 621
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 53
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • C.M. Pickart Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 54
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions: A common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?
    • C.A. Ross Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 19 1997 1147 1150
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 55
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med 10 Suppl 2004 S10 S17
    • (2004) Nat. Med , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 56
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • D. Rotin, O. Staub, and R. Haguenauer-Tsapis Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases J. Membr. Biol. 176 2000 1 17
    • (2000) J. Membr. Biol. , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 57
    • 52049085768 scopus 로고    scopus 로고
    • Pathophysiology of Huntington's disease: From huntingtin functions to potential treatments
    • E. Roze, F. Saudou, and J. Caboche Pathophysiology of Huntington's disease: from huntingtin functions to potential treatments Curr. Opin. Neurol. 21 2008 497 503
    • (2008) Curr. Opin. Neurol. , vol.21 , pp. 497-503
    • Roze, E.1    Saudou, F.2    Caboche, J.3
  • 58
    • 77950386683 scopus 로고    scopus 로고
    • Genomic imprinting of experience-dependent cortical plasticity by the ubiquitin ligase gene Ube3a
    • M. Sato, and M.P. Stryker Genomic imprinting of experience-dependent cortical plasticity by the ubiquitin ligase gene Ube3a Proc. Natl. Acad. Sci. U.S.A. 107 2010 5611 5616
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5611-5616
    • Sato, M.1    Stryker, M.P.2
  • 59
    • 84867386032 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Huntington's disease: Are proteasomes impaired, initiators of disease, or coming to the rescue?
    • S. Schipper-Krom, K. Juenemann, and E.A. Reits The ubiquitin-proteasome system in Huntington's disease: are proteasomes impaired, initiators of disease, or coming to the rescue? Biochem. Res. Int. 2012 2012 837015
    • (2012) Biochem. Res. Int. , vol.2012 , pp. 837015
    • Schipper-Krom, S.1    Juenemann, K.2    Reits, E.A.3
  • 60
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • C. Soto Unfolding the role of protein misfolding in neurodegenerative diseases Nat. Rev. Neurosci. 4 2003 49 60
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 61
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • J. Spence, R.R. Gali, G. Dittmar, F. Sherman, M. Karin, and D. Finley Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain Cell 102 2000 67 76
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 62
    • 79954630190 scopus 로고    scopus 로고
    • Gene expression profiling of R6/2 transgenic mice with different CAG repeat lengths reveals genes associated with disease onset and progression in Huntington's disease
    • B. Tang, T. Seredenina, G. Coppola, A. Kuhn, D.H. Geschwind, R. Luthi-Carter, and E.A. Thomas Gene expression profiling of R6/2 transgenic mice with different CAG repeat lengths reveals genes associated with disease onset and progression in Huntington's disease Neurobiol. Dis. 42 2011 459 467
    • (2011) Neurobiol. Dis. , vol.42 , pp. 459-467
    • Tang, B.1    Seredenina, T.2    Coppola, G.3    Kuhn, A.4    Geschwind, D.H.5    Luthi-Carter, R.6    Thomas, E.A.7
  • 65
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Y.C. Tsai, P.S. Fishman, N.V. Thakor, and G.A. Oyler Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function J. Biol. Chem. 278 2003 22044 22055
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 66
    • 58149380769 scopus 로고    scopus 로고
    • Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons
    • S. Tydlacka, C.E. Wang, X. Wang, S. Li, and X.J. Li Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons J. Neurosci. 28 2008 13285 13295
    • (2008) J. Neurosci. , vol.28 , pp. 13285-13295
    • Tydlacka, S.1    Wang, C.E.2    Wang, X.3    Li, S.4    Li, X.J.5
  • 67
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • P. Venkatraman, R. Wetzel, M. Tanaka, N. Nukina, and A.L. Goldberg Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins Mol. Cell 14 2004 95 104
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 68
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • S. Waelter, A. Boeddrich, R. Lurz, E. Scherzinger, G. Lueder, H. Lehrach, and E.E. Wanker Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation Mol. Biol. Cell 12 2001 1393 1407
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 69
    • 49649117786 scopus 로고    scopus 로고
    • Accumulation of N-terminal mutant huntingtin in mouse and monkey models implicated as a pathogenic mechanism in Huntington's disease
    • C.E. Wang, S. Tydlacka, A.L. Orr, S.H. Yang, R.K. Graham, M.R. Hayden, S. Li, A.W. Chan, and X.J. Li Accumulation of N-terminal mutant huntingtin in mouse and monkey models implicated as a pathogenic mechanism in Huntington's disease Hum. Mol. Genet. 17 2008 2738 2751
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2738-2751
    • Wang, C.E.1    Tydlacka, S.2    Orr, A.L.3    Yang, S.H.4    Graham, R.K.5    Hayden, M.R.6    Li, S.7    Chan, A.W.8    Li, X.J.9
  • 71
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • A.M. Weissman Themes and variations on ubiquitylation Nat. Rev. Mol. Cell Biol. 2 2001 169 178
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 72
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • H. Yang, C. Liu, Y. Zhong, S. Luo, M.J. Monteiro, and S. Fang Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP PLoS One 5 2010 e8905
    • (2010) PLoS One , vol.5 , pp. e8905
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 74
    • 84862322449 scopus 로고    scopus 로고
    • WWP1: A versatile ubiquitin E3 ligase in signaling and diseases
    • X. Zhi, and C. Chen WWP1: a versatile ubiquitin E3 ligase in signaling and diseases Cell. Mol. Life Sci. 69 2012 1425 1434
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 1425-1434
    • Zhi, X.1    Chen, C.2
  • 75
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • C. Zuccato, M. Valenza, and E. Cattaneo Molecular mechanisms and potential therapeutical targets in Huntington's disease Physiol. Rev. 90 2010 905 981
    • (2010) Physiol. Rev. , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.