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Volumn 290, Issue 36, 2015, Pages 21996-22004

Aggregation of polyglutamine-expanded ataxin 7 protein specifically sequesters ubiquitin-specific protease 22 and deteriorates its deubiquitinating function in the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; EXPANSION; ZINC;

EID: 84941312987     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.631663     Document Type: Article
Times cited : (32)

References (60)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H. Y., and Orr, H. T. (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
  • 2
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr, H. T., and Zoghbi, H. Y. (2007) Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30, 575-621
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 3
    • 84883541737 scopus 로고    scopus 로고
    • PolyQ disease: Misfiring of a developmental cell death program?
    • Blum, E. S., Schwendeman, A. R., and Shaham, S. (2013) PolyQ disease: misfiring of a developmental cell death program? Trends Cell Biol. 23, 168-174
    • (2013) Trends Cell Biol. , vol.23 , pp. 168-174
    • Blum, E.S.1    Schwendeman, A.R.2    Shaham, S.3
  • 6
    • 0028304397 scopus 로고
    • Autosomal dominant cerebellar ataxia with pigmentary macular dystrophy. A clinical and genetic study of eight families
    • Enevoldson, T. P., Sanders, M. D., and Harding, A. E. (1994) Autosomal dominant cerebellar ataxia with pigmentary macular dystrophy. A clinical and genetic study of eight families. Brain 117, 445-460
    • (1994) Brain , vol.117 , pp. 445-460
    • Enevoldson, T.P.1    Sanders, M.D.2    Harding, A.E.3
  • 7
    • 0035288035 scopus 로고    scopus 로고
    • Ataxin-7 expression analysis in controls and spinocerebellar ataxia type 7 patients
    • Einum, D. D., Townsend, J. J., Ptácek, L. J., and Fu, Y. H. (2001) Ataxin-7 expression analysis in controls and spinocerebellar ataxia type 7 patients. Neurogenetics 3, 83-90
    • (2001) Neurogenetics , vol.3 , pp. 83-90
    • Einum, D.D.1    Townsend, J.J.2    Ptácek, L.J.3    Fu, Y.H.4
  • 11
    • 84883490794 scopus 로고    scopus 로고
    • Structural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7
    • Jiang, Y. J., Zhou, C. J., Zhou, Z. R., Wu, M., and Hu, H. Y. (2013) Structural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7. FEBS Lett. 587, 2905-2911
    • (2013) FEBS Lett. , vol.587 , pp. 2905-2911
    • Jiang, Y.J.1    Zhou, C.J.2    Zhou, Z.R.3    Wu, M.4    Hu, H.Y.5
  • 14
    • 84871823260 scopus 로고    scopus 로고
    • Reelin is a target of polyglutamine expanded ataxin-7 in human spinocerebellar ataxia type 7 (SCA7) astrocytes
    • McCullough, S. D., Xu, X., Dent, S. Y., Bekiranov, S., Roeder, R. G., and Grant, P. A. (2012) Reelin is a target of polyglutamine expanded ataxin-7 in human spinocerebellar ataxia type 7 (SCA7) astrocytes. Proc. Natl. Acad. Sci. U.S.A. 109, 21319-21324
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 21319-21324
    • McCullough, S.D.1    Xu, X.2    Dent, S.Y.3    Bekiranov, S.4    Roeder, R.G.5    Grant, P.A.6
  • 16
    • 34547879583 scopus 로고    scopus 로고
    • The SAGA continues: Expanding the cellular role of a transcriptional co-activator complex
    • Baker, S. P., and Grant, P. A. (2007) The SAGA continues: expanding the cellular role of a transcriptional co-activator complex. Oncogene 26, 5329-5340
    • (2007) Oncogene , vol.26 , pp. 5329-5340
    • Baker, S.P.1    Grant, P.A.2
  • 17
    • 68249129270 scopus 로고    scopus 로고
    • Insights into SAGA function during gene expression
    • Rodríguez-Navarro, S. (2009) Insights into SAGA function during gene expression. EMBO Rep. 10, 843-850
    • (2009) EMBO Rep. , vol.10 , pp. 843-850
    • Rodríguez-Navarro, S.1
  • 18
    • 34547864553 scopus 로고    scopus 로고
    • Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation
    • Nagy, Z., and Tora, L. (2007) Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation. Oncogene 26, 5341-5357
    • (2007) Oncogene , vol.26 , pp. 5341-5357
    • Nagy, Z.1    Tora, L.2
  • 20
    • 80052597874 scopus 로고    scopus 로고
    • The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements
    • Lang, G., Bonnet, J., Umlauf, D., Karmodiya, K., Koffler, J., Stierle, M., Devys, D., and Tora, L. (2011) The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements. Mol. Cell. Biol. 31, 3734-3744
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3734-3744
    • Lang, G.1    Bonnet, J.2    Umlauf, D.3    Karmodiya, K.4    Koffler, J.5    Stierle, M.6    Devys, D.7    Tora, L.8
  • 21
    • 45849133054 scopus 로고    scopus 로고
    • USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A
    • Zhang, X. Y., Pfeiffer, H. K., Thorne, A. W., and McMahon, S. B. (2008) USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell Cycle 7, 1522-1524
    • (2008) Cell Cycle , vol.7 , pp. 1522-1524
    • Zhang, X.Y.1    Pfeiffer, H.K.2    Thorne, A.W.3    McMahon, S.B.4
  • 22
    • 38149078715 scopus 로고    scopus 로고
    • The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression
    • Zhang, X. Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L., and McMahon, S. B. (2008) The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol. Cell 29, 102-111
    • (2008) Mol. Cell , vol.29 , pp. 102-111
    • Zhang, X.Y.1    Varthi, M.2    Sykes, S.M.3    Phillips, C.4    Warzecha, C.5    Zhu, W.6    Wyce, A.7    Thorne, A.W.8    Berger, S.L.9    McMahon, S.B.10
  • 23
    • 84861594601 scopus 로고    scopus 로고
    • The enigmatic role of H2Bub1 in cancer
    • Johnsen, S. A. (2012) The enigmatic role of H2Bub1 in cancer. FEBS Lett. 586, 1592-1601
    • (2012) FEBS Lett. , vol.586 , pp. 1592-1601
    • Johnsen, S.A.1
  • 24
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake, V. M., and Workman, J. L. (2008) Histone ubiquitination: triggering gene activity. Mol. Cell 29, 653-663
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 25
    • 33748695582 scopus 로고    scopus 로고
    • Transcriptional alterations and chromatin remodeling in polyglutamine diseases
    • Helmlinger, D., Tora, L., and Devys, D. (2006) Transcriptional alterations and chromatin remodeling in polyglutamine diseases. Trends Genet. 22, 562-570
    • (2006) Trends Genet. , vol.22 , pp. 562-570
    • Helmlinger, D.1    Tora, L.2    Devys, D.3
  • 26
    • 77149137999 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-7 causes cerebellar dysfunction by inducing transcriptional dysregulation
    • Chou, A. H., Chen, C. Y., Chen, S. Y., Chen, W. J., Chen, Y. L., Weng, Y. S., and Wang, H. L. (2010) Polyglutamine-expanded ataxin-7 causes cerebellar dysfunction by inducing transcriptional dysregulation. Neurochem. Int. 56, 329-339
    • (2010) Neurochem. Int. , vol.56 , pp. 329-339
    • Chou, A.H.1    Chen, C.Y.2    Chen, S.Y.3    Chen, W.J.4    Chen, Y.L.5    Weng, Y.S.6    Wang, H.L.7
  • 29
    • 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., 3rd, and Grant, P. A. (2005) Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity. Proc. Natl. Acad. Sci. U.S.A. 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
  • 32
    • 84896730064 scopus 로고    scopus 로고
    • Autoinhibitory structure of theWWdomain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin
    • Gao, Y. G., Yang, H., Zhao, J., Jiang, Y. J., and Hu, H. Y. (2014) Autoinhibitory structure of theWWdomain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin. Structure 22, 378-386
    • (2014) Structure , vol.22 , pp. 378-386
    • Gao, Y.G.1    Yang, H.2    Zhao, J.3    Jiang, Y.J.4    Hu, H.Y.5
  • 33
    • 79960114652 scopus 로고    scopus 로고
    • Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA)
    • Jiang, Y. J., Che, M. X., Yuan, J. Q., Xie, Y. Y., Yan, X. Z., and Hu, H. Y. (2011) Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA). J. Biol. Chem. 286, 25236-25245
    • (2011) J. Biol. Chem. , vol.286 , pp. 25236-25245
    • Jiang, Y.J.1    Che, M.X.2    Yuan, J.Q.3    Xie, Y.Y.4    Yan, X.Z.5    Hu, H.Y.6
  • 34
    • 75149167931 scopus 로고    scopus 로고
    • Interaction with synphilin-1 promotes inclusion formation of synuclein: Mechanistic insights and pathological implication
    • Xie, Y. Y., Zhou, C. J., Zhou, Z. R., Hong, J., Che, M. X., Fu, Q. S., Song, A. X., Lin, D. H., and Hu, H. Y. (2010) Interaction with synphilin-1 promotes inclusion formation of synuclein: mechanistic insights and pathological implication. FASEB J. 24, 196-205
    • (2010) FASEB J. , vol.24 , pp. 196-205
    • Xie, Y.Y.1    Zhou, C.J.2    Zhou, Z.R.3    Hong, J.4    Che, M.X.5    Fu, Q.S.6    Song, A.X.7    Lin, D.H.8    Hu, H.Y.9
  • 35
    • 84923380331 scopus 로고    scopus 로고
    • Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: Implication in a loss-of-function pathology
    • Yang, H., Li, J. J., Liu, S., Zhao, J., Jiang, Y. J., Song, A. X., and Hu, H. Y. (2014) Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology. Sci. Rep. 4, 6410
    • (2014) Sci. Rep. , vol.4 , pp. 6410
    • Yang, H.1    Li, J.J.2    Liu, S.3    Zhao, J.4    Jiang, Y.J.5    Song, A.X.6    Hu, H.Y.7
  • 36
    • 33646596978 scopus 로고    scopus 로고
    • Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization
    • Bao, W. J., Gao, Y. G., Chang, Y. G., Zhang, T. Y., Lin, X. J., Yan, X. Z., and Hu, H. Y. (2006) Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization. Protein Expr. Purif. 47, 599-606
    • (2006) Protein Expr. Purif. , vol.47 , pp. 599-606
    • Bao, W.J.1    Gao, Y.G.2    Chang, Y.G.3    Zhang, T.Y.4    Lin, X.J.5    Yan, X.Z.6    Hu, H.Y.7
  • 37
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu, F. E., Horton, J. R., Mullally, J. E., Heroux, A., Cheng, X., and Wilkinson, K. D. (2006) The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 124, 1197-1208
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5    Wilkinson, K.D.6
  • 38
    • 0035976953 scopus 로고    scopus 로고
    • The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease
    • Chai, Y., Wu, L., Griffin, J. D., and Paulson, H. L. (2001) The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease. J. Biol. Chem. 276, 44889-44897
    • (2001) J. Biol. Chem. , vol.276 , pp. 44889-44897
    • Chai, Y.1    Wu, L.2    Griffin, J.D.3    Paulson, H.L.4
  • 40
    • 84861461517 scopus 로고    scopus 로고
    • USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development
    • Lin, Z., Yang, H., Kong, Q., Li, J., Lee, S. M., Gao, B., Dong, H., Wei, J., Song, J., Zhang, D. D., and Fang, D. (2012) USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development. Mol. Cell 46, 484-494
    • (2012) Mol. Cell , vol.46 , pp. 484-494
    • Lin, Z.1    Yang, H.2    Kong, Q.3    Li, J.4    Lee, S.M.5    Gao, B.6    Dong, H.7    Wei, J.8    Song, J.9    Zhang, D.D.10    Fang, D.11
  • 41
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • Borodovsky, A., Kessler, B. M., Casagrande, R., Overkleeft, H. S., Wilkinson, K. D., and Ploegh, H. L. (2001) A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J. 20, 5187-5196
    • (2001) EMBO J. , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 42
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., 3rd, Koonin, E. V., and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 43
    • 0242361623 scopus 로고    scopus 로고
    • Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8
    • Henry, K. W., Wyce, A., Lo, W. S., Duggan, L. J., Emre, N. C., Kao, C. F., Pillus, L., Shilatifard, A., Osley, M. A., and Berger, S. L. (2003) Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Genes Dev. 17, 2648-2663
    • (2003) Genes Dev. , vol.17 , pp. 2648-2663
    • Henry, K.W.1    Wyce, A.2    Lo, W.S.3    Duggan, L.J.4    Emre, N.C.5    Kao, C.F.6    Pillus, L.7    Shilatifard, A.8    Osley, M.A.9    Berger, S.L.10
  • 44
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
    • Park, S. H., Kukushkin, Y., Gupta, R., Chen, T., Konagai, A., Hipp, M. S., Hayer-Hartl, M., and Hartl, F. U. (2013) PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154, 134-145
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5    Hipp, M.S.6    Hayer-Hartl, M.7    Hartl, F.U.8
  • 47
    • 84898779814 scopus 로고    scopus 로고
    • Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition
    • Yu, A., Shibata, Y., Shah, B., Calamini, B., Lo, D. C., and Morimoto, R. I. (2014) Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition. Proc. Natl. Acad. Sci. U.S.A. 111, E1481-1490
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. E1481-1490
    • Yu, A.1    Shibata, Y.2    Shah, B.3    Calamini, B.4    Lo, D.C.5    Morimoto, R.I.6
  • 50
    • 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. H., Ward, E. G., Warren, S. T., Li, S., and Li, X. J. (2007) Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat. Neurosci. 10, 1519-1528
    • (2007) Nat. Neurosci. , vol.10 , pp. 1519-1528
    • Friedman, M.J.1    Shah, A.G.2    Fang, Z.H.3    Ward, E.G.4    Warren, S.T.5    Li, S.6    Li, X.J.7
  • 51
    • 83755228990 scopus 로고    scopus 로고
    • Suppression of aggregate formation of mutant huntingtin potentiates CREB-binding protein sequestration and apoptotic cell death
    • Choi, Y. J., Kim, S. I., Lee, J. W., Kwon, Y. S., Lee, H. J., Kim, S. S., and Chun, W. (2012) Suppression of aggregate formation of mutant huntingtin potentiates CREB-binding protein sequestration and apoptotic cell death. Mol. Cell Neurosci 49, 127-137
    • (2012) Mol. Cell Neurosci , vol.49 , pp. 127-137
    • Choi, Y.J.1    Kim, S.I.2    Lee, J.W.3    Kwon, Y.S.4    Lee, H.J.5    Kim, S.S.6    Chun, W.7
  • 52
    • 84877877932 scopus 로고    scopus 로고
    • P62/SQSTM1 regulates cellular oxygen sensing by attenuating PHD3 activity through aggregate sequestration and enhanced degradation
    • Rantanen, K., Pursiheimo, J. P., Högel, H., Miikkulainen, P., Sundström, J., and Jaakkola, P. M. (2013) p62/SQSTM1 regulates cellular oxygen sensing by attenuating PHD3 activity through aggregate sequestration and enhanced degradation. J. Cell Sci. 126, 1144-1154
    • (2013) J. Cell Sci. , vol.126 , pp. 1144-1154
    • Rantanen, K.1    Pursiheimo, J.P.2    Högel, H.3    Miikkulainen, P.4    Sundström, J.5    Jaakkola, P.M.6
  • 54
    • 84863624498 scopus 로고    scopus 로고
    • Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI] yeast
    • Zhao, X., Park, Y. N., Todor, H., Moomau, C., Masison, D., Eisenberg, E., and Greene, L. E. (2012) Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI] yeast. J. Biol. Chem. 287, 23346-23355
    • (2012) J. Biol. Chem. , vol.287 , pp. 23346-23355
    • Zhao, X.1    Park, Y.N.2    Todor, H.3    Moomau, C.4    Masison, D.5    Eisenberg, E.6    Greene, L.E.7
  • 56
    • 84904696676 scopus 로고    scopus 로고
    • Defining the limits: Protein aggregation and toxicity in vivo
    • Holmes, W. M., Klaips, C. L., and Serio, T. R. (2014) Defining the limits: protein aggregation and toxicity in vivo. Crit. Rev. Biochem. Mol. Biol. 49, 294-303
    • (2014) Crit. Rev. Biochem. Mol. Biol. , vol.49 , pp. 294-303
    • Holmes, W.M.1    Klaips, C.L.2    Serio, T.R.3
  • 57
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation
    • Perez, M. K., Paulson, H. L., Pendse, S. J., Saionz, S. J., Bonini, N. M., and Pittman, R. N. (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    Pittman, R.N.6
  • 58
    • 84929163852 scopus 로고    scopus 로고
    • Poly(Q) Expansions inATXN7affect solubility but not activity of the SAGA deubiquitinating module
    • Lan, X., Koutelou, E., Schibler, A. C., Chen, Y. C., Grant, P. A., and Dent, S. Y. (2015) Poly(Q) Expansions inATXN7affect solubility but not activity of the SAGA deubiquitinating module. Mol. Cell. Biol. 35, 1777-1787
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 1777-1787
    • Lan, X.1    Koutelou, E.2    Schibler, A.C.3    Chen, Y.C.4    Grant, P.A.5    Dent, S.Y.6
  • 59
    • 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, S. L., Shoesmith, S. J., Perez, M. K., and Paulson, H. L. (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
  • 60
    • 0036198110 scopus 로고    scopus 로고
    • Protein surveillance machinery in brains with spinocerebellar ataxia type 3: Redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions
    • Schmidt, T., Lindenberg, K. S., Krebs, A., Schöls, L., Laccone, F., Herms, J., Rechsteiner, M., Riess, O., and Landwehrmeyer, G. B. (2002) Protein surveillance machinery in brains with spinocerebellar ataxia type 3: redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions. Ann. Neurol. 51, 302-310
    • (2002) Ann. Neurol. , vol.51 , pp. 302-310
    • Schmidt, T.1    Lindenberg, K.S.2    Krebs, A.3    Schöls, L.4    Laccone, F.5    Herms, J.6    Rechsteiner, M.7    Riess, O.8    Landwehrmeyer, G.B.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.