메뉴 건너뛰기




Volumn 287, Issue 3, 2012, Pages 2068-2078

Polyglutamine expansion alters the dynamics and molecular architecture of aggregates in dentatorubropallidoluysian atrophy

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR TOXICITIES; CLINICAL FEATURES; COMPOSITION ANALYSIS; CYTOPLASMIC INCLUSION; DYNAMIC IMAGING; MOLECULAR ARCHITECTURE; MOLECULAR SPECIES; MUTANT PROTEINS; NEURODEGENERATION; NEURODEGENERATIVE DISORDERS; POLYGLUTAMINE; POLYGLUTAMINE (POLYQ); SLOW DYNAMICS;

EID: 84862968848     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.318915     Document Type: Article
Times cited : (8)

References (58)
  • 1
    • 77956184558 scopus 로고    scopus 로고
    • Neurotoxic protein oligomerization associated with polyglutamine diseases
    • Hands, S. L., and Wyttenbach, A. (2010) Neurotoxic protein oligomerization associated with polyglutamine diseases. Acta Neuropathol. 120, 419-437
    • (2010) Acta Neuropathol. , vol.120 , pp. 419-437
    • Hands, S.L.1    Wyttenbach, A.2
  • 2
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • DOI 10.1146/annurev.neuro.29.051605.113042
    • Orr, H. T., and Zoghbi, H. Y. (2007) Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30, 575-621 (Pubitemid 47218768)
    • (2007) Annual Review of Neuroscience , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 4
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • DOI 10.1016/S0968-0004(03)00168-3
    • Harjes, P., and Wanker, E. E. (2003) The hunt for huntingtin function. Interaction partners tell many different stories. Trends Biochem. Sci. 28, 425-433 (Pubitemid 36976745)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.8 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 5
    • 0034605071 scopus 로고    scopus 로고
    • Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription
    • Wood, J. D., Nucifora, F. C., Jr., Duan, K., Zhang, C., Wang, J., Kim, Y., Schilling, G., Sacchi, N., Liu, J. M., and Ross, C. A. (2000) Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription. J. Cell Biol. 150, 939-948
    • (2000) J. Cell Biol. , vol.150 , pp. 939-948
    • Wood, J.D.1    Nucifora Jr., F.C.2    Duan, K.3    Zhang, C.4    Wang, J.5    Kim, Y.6    Schilling, G.7    Sacchi, N.8    Liu, J.M.9    Ross, C.A.10
  • 9
    • 28444444502 scopus 로고    scopus 로고
    • Polyglutamine is not all: The functional role of the AXH domain in the ataxin-1 protein
    • DOI 10.1016/j.jmb.2005.09.083, PII S0022283605011629
    • de Chiara, C., Menon, R. P., Dal Piaz, F., Calder, L., and Pastore, A. (2005) Polyglutamine is not all. The functional role of the AXH domain in the ataxin-1 protein. J. Mol. Biol. 354, 883-893 (Pubitemid 41735509)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.4 , pp. 883-893
    • De Chiara, C.1    Menon, R.P.2    Dal, P.F.3    Calder, L.4    Pastore, A.5
  • 10
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • Ellisdon, A. M., Thomas, B., and Bottomley, S. P. (2006) The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J. Biol. Chem. 281, 16888-16896
    • (2006) J. Biol. Chem. , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 11
    • 71449084004 scopus 로고    scopus 로고
    • The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
    • Tam, S., Spiess, C., Auyeung, W., Joachimiak, L., Chen, B., Poirier, M. A., and Frydman, J. (2009) The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat. Struct. Mol. Biol. 16, 1279-1285
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1279-1285
    • Tam, S.1    Spiess, C.2    Auyeung, W.3    Joachimiak, L.4    Chen, B.5    Poirier, M.A.6    Frydman, J.7
  • 14
    • 15544372340 scopus 로고    scopus 로고
    • A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: Evidence for a compact beta-sheet structure
    • DOI 10.1093/hmg/ddi071
    • Poirier, M. A., Jiang, H., and Ross, C. A. (2005) A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity. Evidence for a compact β-sheet structure. Hum. Mol. Genet. 14, 765-774 (Pubitemid 40403273)
    • (2005) Human Molecular Genetics , vol.14 , Issue.6 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 15
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • DOI 10.1074/jbc.M205809200
    • Poirier, M. A., Li, H., Macosko, J., Cai, S., Amzel, M., and Ross, C. A. (2002) Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. 277, 41032-41037 (Pubitemid 35215693)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Macosko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 16
    • 0033791230 scopus 로고    scopus 로고
    • Protein aggregation and pathogenesis of Huntington's disease. Mechanisms and correlations
    • Wanker, E. E. (2000) Protein aggregation and pathogenesis of Huntington's disease. Mechanisms and correlations. Biol. Chem. 381, 937-942
    • (2000) Biol. Chem. , vol.381 , pp. 937-942
    • Wanker, E.E.1
  • 20
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • DOI 10.1038/502
    • Cummings, C. J., Mancini, M. A., Antalffy, B., DeFranco, D. B., Orr, H. T., and Zoghbi, H. Y. (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148-154 (Pubitemid 28248795)
    • (1998) Nature Genetics , vol.19 , Issue.2 , 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
  • 26
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • DOI 10.1038/ncb859
    • Stenoien, D. L., Mielke, M., and Mancini, M. A. (2002) Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat. Cell Biol. 4, 806-810 (Pubitemid 35214775)
    • (2002) Nature Cell Biology , vol.4 , Issue.10 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 27
    • 0029015557 scopus 로고
    • Abnormal gene product identified in hereditary dentatorubralpallidoluysian atrophy (DRPLA) brain
    • Yazawa, I., Nukina, N., Hashida, H., Goto, J., Yamada, M., and Kanazawa, I. (1995) Abnormal gene product identified in hereditary dentatorubralpallidoluysian atrophy (DRPLA) brain. Nat. Genet. 10, 99-103
    • (1995) Nat. Genet. , vol.10 , pp. 99-103
    • Yazawa, I.1    Nukina, N.2    Hashida, H.3    Goto, J.4    Yamada, M.5    Kanazawa, I.6
  • 29
    • 0035149350 scopus 로고    scopus 로고
    • Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases
    • Yamada, M., Sato, T., Shimohata, T., Hayashi, S., Igarashi, S., Tsuji, S., and Takahashi, H. (2001) Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases. Am. J. Pathol. 159, 1785-1795 (Pubitemid 33062521)
    • (2001) American Journal of Pathology , vol.159 , Issue.5 , pp. 1785-1795
    • Yamada, M.1    Sato, T.2    Shimohata, T.3    Hayashi, S.4    Igarashi, S.5    Tsuji, S.6    Takahashi, H.7
  • 30
    • 0035112686 scopus 로고    scopus 로고
    • Widespread occurrence of intranuclear atrophin-1 accumulation in the central nervous system neurons of patients with dentatorubral-pallidoluysian atrophy
    • DOI 10.1002/1531-8249(200101)49:1<14::AID-ANA5>3.0.CO;2-X
    • Yamada, M., Wood, J. D., Shimohata, T., Hayashi, S., Tsuji, S., Ross, C. A., and Takahashi, H. (2001) Widespread occurrence of intranuclear atrophin-1 accumulation in the central nervous system neurons of patients with dentatorubral-pallidoluysian atrophy. Ann. Neurol. 49, 14-23 (Pubitemid 32163001)
    • (2001) Annals of Neurology , vol.49 , Issue.1 , pp. 14-23
    • Yamada, M.1    Wood, J.D.2    Shimohata, T.3    Hayashi, S.4    Tsuji, S.5    Ross, C.A.6    Takahashi, H.7
  • 31
    • 0033012401 scopus 로고    scopus 로고
    • Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate
    • DOI 10.1093/hmg/8.6.947
    • Okamura-Oho, Y., Miyashita, T., Ohmi, K., and Yamada, M. (1999) Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate. Hum. Mol. Genet. 8, 947-957 (Pubitemid 29250882)
    • (1999) Human Molecular Genetics , vol.8 , Issue.6 , pp. 947-957
    • Okamura-Oho, Y.1    Miyashita, T.2    Ohmi, K.3    Yamada, M.4
  • 32
    • 0032504549 scopus 로고    scopus 로고
    • Intracellular aggregate formation of dentatorubral-pallidoluysian atrophy (DRPLA) protein with the extended polyglutamine
    • DOI 10.1006/bbrc.1998.9096
    • Miyashita, T., Nagao, K., Ohmi, K., Yanagisawa, H., Okamura-Oho, Y., and Yamada, M. (1998) Intracellular aggregate formation of dentatorubral- pallidoluysian atrophy (DRPLA) protein with the extended polyglutamine. Biochem. Biophys. Res. Commun. 249, 96-102 (Pubitemid 28418701)
    • (1998) Biochemical and Biophysical Research Communications , vol.249 , Issue.1 , pp. 96-102
    • Miyashita, T.1    Nagao, K.2    Ohmi, K.3    Yanagisawa, H.4    Okamura-Oho, Y.5    Yamada, M.6
  • 33
    • 33645214602 scopus 로고    scopus 로고
    • Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells
    • DOI 10.1074/jbc.M509201200
    • Matsumoto, G., Kim, S., and Morimoto, R. I. (2006) Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells. J. Biol. Chem. 281, 4477-4485 (Pubitemid 43847879)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 4477-4485
    • Matsumoto, G.1    Kim, S.2    Morimoto, R.I.3
  • 35
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine- containing protein aggregates
    • DOI 10.1016/S0076-6879(99)09026-6
    • Wanker, E. E., Scherzinger, E., Heiser, V., Sittler, A., Eickhoff, H., and Lehrach, H. (1999) Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates. Methods Enzymol. 309, 375-386 (Pubitemid 29446461)
    • (1999) Methods in Enzymology , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5    Lehrach, H.6
  • 36
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 38
    • 9144223729 scopus 로고    scopus 로고
    • Inefficient degradation of truncated polyglutamine proteins by the proteasome
    • DOI 10.1038/sj.emboj.7600426
    • Holmberg, C. I., Staniszewski, K. E., Mensah, K. N., Matouschek, A., and Morimoto, R. I. (2004) Inefficient degradation of truncated polyglutamine proteins by the proteasome. EMBO J. 23, 4307-4318 (Pubitemid 39546168)
    • (2004) EMBO Journal , vol.23 , Issue.21 , pp. 4307-4318
    • Holmberg, C.I.1    Staniszewski, K.E.2    Mensah, K.N.3    Matouschek, A.4    Morimoto, R.I.5
  • 39
    • 45149120561 scopus 로고    scopus 로고
    • Polyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation
    • Krol, H. A., Krawczyk, P. M., Bosch, K. S., Aten, J. A., Hol, E. M., and Reits, E. A. (2008) Polyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation. PLoS ONE 3, e1503
    • (2008) PLoS ONE , vol.3
    • Krol, H.A.1    Krawczyk, P.M.2    Bosch, K.S.3    Aten, J.A.4    Hol, E.M.5    Reits, E.A.6
  • 40
    • 55049100926 scopus 로고    scopus 로고
    • Focal distortion of the nuclear envelope by huntingtin aggregates revealed by lamin immunostaining
    • Chapple, J. P., Bros-Facer, V., Butler, R., and Gallo, J. M. (2008) Focal distortion of the nuclear envelope by huntingtin aggregates revealed by lamin immunostaining. Neurosci. Lett. 447, 172-174
    • (2008) Neurosci. Lett. , vol.447 , pp. 172-174
    • Chapple, J.P.1    Bros-Facer, V.2    Butler, R.3    Gallo, J.M.4
  • 41
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lueder, G., Lehrach, H., and Wanker, E. E. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell 12, 1393-1407 (Pubitemid 33044419)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.5 , 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
  • 43
    • 41849138304 scopus 로고    scopus 로고
    • Orthogonal cross-seeding: an approach to explore protein aggregates in living cells
    • DOI 10.1021/bi800002j
    • Hinz, J., Gierasch, L. M., and Ignatova, Z. (2008) Orthogonal cross-seeding. An approach to explore protein aggregates in living cells. Biochemistry 47, 4196-4200 (Pubitemid 351499875)
    • (2008) Biochemistry , vol.47 , Issue.14 , pp. 4196-4200
    • Hinz, J.1    Gierasch, L.M.2    Ignatova, Z.3
  • 44
    • 0035826236 scopus 로고    scopus 로고
    • Conformational diversity in a yeast prion dictates its seeding specificity
    • DOI 10.1038/35065632
    • Chien, P., and Weissman, J. S. (2001) Conformational diversity in a yeast prion dictates its seeding specificity. Nature 410, 223-227 (Pubitemid 32216596)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 223-227
    • Chien, P.1    Weissman, J.S.2
  • 45
    • 37549011420 scopus 로고    scopus 로고
    • In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence
    • Ignatova, Z., Thakur, A. K., Wetzel, R., and Gierasch, L. M. (2007) In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. J. Biol. Chem. 282, 36736-36743
    • (2007) J. Biol. Chem. , vol.282 , pp. 36736-36743
    • Ignatova, Z.1    Thakur, A.K.2    Wetzel, R.3    Gierasch, L.M.4
  • 46
    • 2342444028 scopus 로고    scopus 로고
    • Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
    • DOI 10.1074/jbc.M311300200
    • O'Nuallain, B., Williams, A. D., Westermark, P., and Wetzel, R. (2004) Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 279, 17490-17499 (Pubitemid 38560512)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 47
    • 0034126815 scopus 로고    scopus 로고
    • The nuclear pore complex: Mediator of translocation between nucleus and cytoplasm
    • Allen, T. D., Cronshaw, J. M., Bagley, S., Kiseleva, E., and Goldberg, M. W. (2000) The nuclear pore complex. Mediator of translocation between nucleus and cytoplasm. J. Cell Sci. 113, 1651-1659 (Pubitemid 30333114)
    • (2000) Journal of Cell Science , vol.113 , Issue.10 , pp. 1651-1659
    • Allen, T.D.1    Cronshaw, J.M.2    Bagley, S.3    Kiseleva, E.4    Goldberg, M.W.5
  • 48
    • 59349096106 scopus 로고    scopus 로고
    • Atrophins' emerging roles in development and neurodegenerative disease
    • Shen, Y., and Peterson, A. S. (2009) Atrophins' emerging roles in development and neurodegenerative disease. Cell Mol. Life Sci. 66, 437-446
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 437-446
    • Shen, Y.1    Peterson, A.S.2
  • 49
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich, D., Kopito, R., and Frydman, J. (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454, 1088-1095
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 50
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • DOI 10.1126/science.289.5483.1317
    • Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., and Lindquist, S. L. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289, 1317-1321 (Pubitemid 30656041)
    • (2000) Science , vol.289 , Issue.5483 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6    Arnsdorf, M.F.7    Lindquist, S.L.8
  • 51
    • 35648992125 scopus 로고    scopus 로고
    • The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils
    • Bulone, D., Masino, L., Thomas, D. J., San Biagio, P. L., and Pastore, A. (2006) The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils. PLoS ONE 1, e111
    • (2006) PLoS ONE , vol.1
    • Bulone, D.1    Masino, L.2    Thomas, D.J.3    San Biagio, P.L.4    Pastore, A.5
  • 52
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3
    • DOI 10.1016/j.jmb.2004.09.065, PII S0022283604012239
    • Masino, L., Nicastro, G., Menon, R. P., Dal Piaz, F., Calder, L., and Pastore, A. (2004) Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3. J. Mol. Biol. 344, 1021-1035 (Pubitemid 39491247)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Piaz, F.D.4    Calder, L.5    Pastore, A.6
  • 53
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • DOI 10.2165/00822942-200403020-00005
    • Romero, P., Obradovic, Z., and Dunker, A. K. (2004) Natively disordered proteins. Functions and predictions. Appl. Bioinformatics 3, 105-113 (Pubitemid 41032063)
    • (2004) Applied Bioinformatics , vol.3 , Issue.2-3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 55
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutarnine- induced disease in SCA1 transgenic mice
    • DOI 10.1016/S0092-8674(00)81781-X
    • Klement, I. A., Skinner, P. J., Kaytor, M. D., Yi, H., Hersch, S. M., Clark, H. B., Zoghbi, H. Y., and Orr, H. T. (1998) Ataxin-1 nuclear localization and aggregation. Role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95, 41-53 (Pubitemid 28458023)
    • (1998) Cell , vol.95 , Issue.1 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 56
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D., and Greenberg, M. E. (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 58
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis: Confusion of the kinds?
    • DOI 10.1016/j.sbi.2006.01.011, PII S0959440X06000121
    • Rousseau, F., Schymkowitz, J., and Serrano, L. (2006) Protein aggregation and amyloidosis. Confusion of the kinds? Curr. Opin. Struct. Biol. 16, 118-126 (Pubitemid 43221880)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.