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Volumn 353, Issue 3, 2005, Pages 642-654

Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: Trapping early oligomers of non-expanded ataxin-3

Author keywords

Amyloid; Neurodegenerative; Polyglutamine; SCA3; Self assembly domain

Indexed keywords

AMYLOID PROTEIN; ATAXIN 3; EPITOPE; OLIGOMER; POLYGLUTAMINE; POLYMER;

EID: 26244434741     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.061     Document Type: Article
Times cited : (64)

References (61)
  • 1
    • 0034640011 scopus 로고    scopus 로고
    • Fourteen and counting: Unraveling trinucleotide repeat diseases
    • C.J. Cummings, and H.Y. Zoghbi Fourteen and counting: unraveling trinucleotide repeat diseases Hum. Mol. Genet. 9 2000 909 916
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 909-916
    • Cummings, C.J.1    Zoghbi, H.Y.2
  • 2
    • 0027988041 scopus 로고
    • Polar zippers: Their role in human disease
    • M. Perutz Polar zippers: their role in human disease Protein Sci. 3 1994 1629 1637
    • (1994) Protein Sci. , vol.3 , pp. 1629-1637
    • Perutz, M.1
  • 3
    • 0032904145 scopus 로고    scopus 로고
    • Intracellular inclusions, pathological markers in diseases caused by expanded polyglutamine tracts?
    • D.C. Rubinsztein, A. Wyttenbach, and J. Rankin Intracellular inclusions, pathological markers in diseases caused by expanded polyglutamine tracts? J. Med. Genet. 36 1999 265 270
    • (1999) J. Med. Genet. , vol.36 , pp. 265-270
    • Rubinsztein, D.C.1    Wyttenbach, A.2    Rankin, J.3
  • 4
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • M.F. Perutz, T. Johnson, M. Suzuki, and J.T. Finch Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases Proc. Natl Acad. Sci. USA 91 1994 5355 5358
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 5
    • 0036669907 scopus 로고    scopus 로고
    • Glutamine repeats: Structural hypotheses and neurodegeneration
    • L. Masino, and A. Pastore Glutamine repeats: structural hypotheses and neurodegeneration Biochem. Soc. Trans. 30 2002 548 551
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 548-551
    • Masino, L.1    Pastore, A.2
  • 6
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • S. Chen, V. Berthelier, J.B. Hamilton, B. O'Nuallain, and R. Wetzel Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41 2002 7391 7399
    • (2002) Biochemistry , vol.41 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 7
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • E. Scherzinger, R. Lurz, M. Turmaine, L. Mangiarini, B. Hollenbach, and R. Hasenbank Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo Cell 90 1997 549 558
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3    Mangiarini, L.4    Hollenbach, B.5    Hasenbank, R.6
  • 8
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates parallel beta-fibrils
    • A.E. Bevivino, and P.J. Loll An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates parallel beta-fibrils Proc. Natl Acad. Sci. USA 98 2001 11955 11960
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 9
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • M.A. Poirier, H. Li, J. Macosko, S. Cai, M. Amzel, and C.A. Ross Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization J. Biol. Chem. 277 2002 41032 41037
    • (2002) J. Biol. Chem. , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    MacOsko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 11
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • B. O'Nuallain, and R. Wetzel Conformational Abs recognizing a generic amyloid fibril epitope Proc. Natl Acad. Sci. USA 99 2002 1485 1490
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 12
    • 0141891215 scopus 로고    scopus 로고
    • Pathogenesis of polyglutamine disorders: Aggregation revisited
    • A. Michalik, and C. Van Broeckhoven Pathogenesis of polyglutamine disorders: aggregation revisited Hum. Mol. Genet. 12 2003 R173 R186
    • (2003) Hum. Mol. Genet. , vol.12
    • Michalik, A.1    Van Broeckhoven, C.2
  • 13
    • 0345701297 scopus 로고    scopus 로고
    • Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
    • S. Iuchi, G. Hoffner, P. Verbeke, P. Djian, and H. Green Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine Proc. Natl Acad. Sci. USA 100 2003 2409 2414
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2409-2414
    • Iuchi, S.1    Hoffner, G.2    Verbeke, P.3    Djian, P.4    Green, H.5
  • 14
    • 0141668882 scopus 로고    scopus 로고
    • Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization
    • M. Tanaka, Y. Machida, Y. Nishikawa, T. Akagi, T. Hashikawa, T. Fujisawa, and N. Nukina Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization J. Biol. Chem. 278 2003 34717 34724
    • (2003) J. Biol. Chem. , vol.278 , pp. 34717-34724
    • Tanaka, M.1    MacHida, Y.2    Nishikawa, Y.3    Akagi, T.4    Hashikawa, T.5    Fujisawa, T.6    Nukina, N.7
  • 15
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • R. Tycko Progress towards a molecular-level structural understanding of amyloid fibrils Curr. Opin. Struct. Biol. 14 2004 96 103
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 17
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • R. Kayed, Y. Sokolov, B. Edmonds, T.M. McIntire, S.C. Milton, J.E. Hall, and C.G. Glabe Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases J. Biol. Chem. 279 2004 46363 46366
    • (2004) J. Biol. Chem. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 18
    • 0030936575 scopus 로고    scopus 로고
    • Machado-Joseph disease gene product is a cytoplasmic protein widely expressed in brain
    • H.L. Paulson, S.S. Das, P.B. Crino, M.K. Perez, S.C. Patel, and D. Gotsdiner Machado-Joseph disease gene product is a cytoplasmic protein widely expressed in brain Ann. Neurol. 41 1997 453 462
    • (1997) Ann. Neurol. , vol.41 , pp. 453-462
    • Paulson, H.L.1    Das, S.S.2    Crino, P.B.3    Perez, M.K.4    Patel, S.C.5    Gotsdiner, D.6
  • 19
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • B. Burnett, F. Li, and R.N. Pittman The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity Hum. Mol. Genet. 12 2003 3195 3205
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 20
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • B.G. Burnett, and R.N. Pittman The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation Proc. Natl Acad. Sci. USA 102 2005 4330 4335
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 21
    • 0942287194 scopus 로고    scopus 로고
    • Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways
    • Y. Chai, S.S. Berke, R.E. Cohen, and H.L. Paulson Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways J. Biol. Chem. 279 2004 3605 3611
    • (2004) J. Biol. Chem. , vol.279 , pp. 3605-3611
    • Chai, Y.1    Berke, S.S.2    Cohen, R.E.3    Paulson, H.L.4
  • 23
    • 0041563693 scopus 로고    scopus 로고
    • Domain architecture of the polyglutamine protein ataxin-3: A globular domain followed by a flexible tail
    • L. Masino, V. Musi, R.P. Menon, P. Fusi, G. Kelly, and T.A. Frenkiel Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail FEBS Letters 549 2003 21 25
    • (2003) FEBS Letters , vol.549 , pp. 21-25
    • Masino, L.1    Musi, V.2    Menon, R.P.3    Fusi, P.4    Kelly, G.5    Frenkiel, T.A.6
  • 24
    • 0242693202 scopus 로고    scopus 로고
    • Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics
    • H. Scheel, S. Tomiuk, and K. Hofmann Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics Hum. Mol. Genet. 12 2003 2845 2852
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2845-2852
    • Scheel, H.1    Tomiuk, S.2    Hofmann, K.3
  • 25
    • 0030747914 scopus 로고    scopus 로고
    • Machado-Joseph disease gene products carrying different carboxyl termini
    • J. Goto, M. Watanabe, Y. Ichikawa, S.B. Yee, N. Ihara, and K. Endo Machado-Joseph disease gene products carrying different carboxyl termini Neurosci. Res. 28 1997 373 377
    • (1997) Neurosci. Res. , vol.28 , pp. 373-377
    • Goto, J.1    Watanabe, M.2    Ichikawa, Y.3    Yee, S.B.4    Ihara, N.5    Endo, K.6
  • 27
    • 0347481134 scopus 로고    scopus 로고
    • Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36)
    • E. Shehi, P. Fusi, F. Secundo, S. Pozzuolo, A. Bairati, and P. Tortora Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36) Biochemistry 42 2003 14626 14632
    • (2003) Biochemistry , vol.42 , pp. 14626-14632
    • Shehi, E.1    Fusi, P.2    Secundo, F.3    Pozzuolo, S.4    Bairati, A.5    Tortora, P.6
  • 28
    • 0042357191 scopus 로고    scopus 로고
    • Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature
    • S. Marchal, E. Shehi, M.C. Harricane, P. Fusi, F. Heitz, P. Tortora, and R. Lange Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature J. Biol. Chem. 278 2003 31554 31563
    • (2003) J. Biol. Chem. , vol.278 , pp. 31554-31563
    • Marchal, S.1    Shehi, E.2    Harricane, M.C.3    Fusi, P.4    Heitz, F.5    Tortora, P.6    Lange, R.7
  • 29
    • 0345118103 scopus 로고    scopus 로고
    • Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: A model for misfolding in polyglutamine disease
    • M.K. Chow, H.L. Paulson, and S.P. Bottomley Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease J. Mol. Biol. 335 2004 333 341
    • (2004) J. Mol. Biol. , vol.335 , pp. 333-341
    • Chow, M.K.1    Paulson, H.L.2    Bottomley, S.P.3
  • 30
    • 0035976953 scopus 로고    scopus 로고
    • The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease
    • Y. Chai, L. Wu, D. Griffin James, and L. Paulson Henry The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease J. Biol. Chem. 276 2001 44889 44897
    • (2001) J. Biol. Chem. , vol.276 , pp. 44889-44897
    • Chai, Y.1    Wu, L.2    Griffin James, D.3    Paulson Henry, L.4
  • 31
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the josephin domain of the polyglutamine-containing protein ataxin-3
    • L. Masino, G. Nicastro, R.P. Menon, F.D. Piaz, L. Calder, and A. Pastore Characterization of the structure and the amyloidogenic properties of the josephin domain of the polyglutamine-containing protein ataxin-3 J. Mol. Biol. 344 2004 1021 1035
    • (2004) J. Mol. Biol. , vol.344 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Piaz, F.D.4    Calder, L.5    Pastore, A.6
  • 32
    • 0036295080 scopus 로고    scopus 로고
    • Transthyretin fibrillogenesis entails the assembly of monomers: A molecular model for in vitro assembled transthyretin amyloid-like fibrils
    • I. Cardoso, C.S. Goldsbury, S.A. Muller, V. Olivieri, S. Wirtz, and A.M. Damas Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils J. Mol. Biol. 317 2002 683 695
    • (2002) J. Mol. Biol. , vol.317 , pp. 683-695
    • Cardoso, I.1    Goldsbury, C.S.2    Muller, S.A.3    Olivieri, V.4    Wirtz, S.5    Damas, A.M.6
  • 33
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • J.C. Rochet, K.A. Conway, and P.T. Lansbury Jr Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein Biochemistry 39 2000 10619 10626
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.C.1    Conway, K.A.2    Lansbury Jr., P.T.3
  • 34
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • S. Chen, F.A. Ferrone, and R. Wetzel Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc. Natl Acad. Sci. USA 99 2002 11884 11889
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 35
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • S. Chen, V. Berthelier, W. Yang, and R. Wetzel Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity J. Mol. Biol. 311 2001 173 182
    • (2001) J. Mol. Biol. , vol.311 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 36
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in ataxin-3 does not affect protein stability: Implications for misfolding and disease
    • M.K. Chow, A.M. Ellisdon, L.D. Cabrita, and S.P. Bottomley Polyglutamine expansion in ataxin-3 does not affect protein stability: Implications for misfolding and disease J. Biol. Chem. 279 2004 47643 47651
    • (2004) J. Biol. Chem. , vol.279 , pp. 47643-47651
    • Chow, M.K.1    Ellisdon, A.M.2    Cabrita, L.D.3    Bottomley, S.P.4
  • 37
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • A. Demuro, E. Mina, R. Kayed, S.C. Milton, I. Parker, and C.G. Glabe Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers J. Biol. Chem. 280 2005 17294 17300
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 38
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81 2003 678 699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 39
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize - Implications for neurodegenerative diseases
    • K. Stott, J.M. Blackburn, P.J.G. Butler, and M. Perutz Incorporation of glutamine repeats makes protein oligomerize - implications for neurodegenerative diseases Proc. Natl Acad. Sci. USA 92 1995 6509 6513
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.G.3    Perutz, M.4
  • 40
    • 0000522537 scopus 로고    scopus 로고
    • Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat
    • Y.W. Chen, K. Stott, and M.F. Perutz Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat Proc. Natl Acad. Sci. USA 96 1999 1257 1261
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1257-1261
    • Chen, Y.W.1    Stott, K.2    Perutz, M.F.3
  • 41
    • 0034814752 scopus 로고    scopus 로고
    • Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions
    • J.G. Duncan, R.J. Carbajo, K. Stott, and D. Neuhaus Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions Biochem. Biophys. Res. Commun. 280 2001 855 860
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 855-860
    • Duncan, J.G.1    Carbajo, R.J.2    Stott, K.3    Neuhaus, D.4
  • 42
    • 4143058003 scopus 로고    scopus 로고
    • The evolving role of 3D domain swapping in proteins
    • M.J. Bennett, and D. Eisenberg The evolving role of 3D domain swapping in proteins Structure 12 2004 1339 1341
    • (2004) Structure , vol.12 , pp. 1339-1341
    • Bennett, M.J.1    Eisenberg, D.2
  • 43
    • 0035757051 scopus 로고    scopus 로고
    • 3D domain swapping, protein oligomerization, and amyloid formation
    • M. Jaskolski 3D domain swapping, protein oligomerization, and amyloid formation Acta Biochim. Pol. 48 2001 807 827
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 807-827
    • Jaskolski, M.1
  • 47
    • 0035504113 scopus 로고    scopus 로고
    • Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death
    • X. Fan, P. Dion, J. Laganiere, B. Brais, and G.A. Rouleau Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death Hum. Mol. Genet 10 2001 2341 2351
    • (2001) Hum. Mol. Genet , vol.10 , pp. 2341-2351
    • Fan, X.1    Dion, P.2    Laganiere, J.3    Brais, B.4    Rouleau, G.A.5
  • 48
    • 0038379383 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Minding your Ps and Qs
    • H. Paulson Polyglutamine neurodegeneration: minding your Ps and Qs Nature Med. 9 2003 825 826
    • (2003) Nature Med. , vol.9 , pp. 825-826
    • Paulson, H.1
  • 49
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • S. Chen, A. Ferrone Frank, and R. Wetzel Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc. Natl Acad. Sci. USA 99 2002 11884 11889
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone Frank, A.2    Wetzel, R.3
  • 50
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • J.D. Harper, and P.T. Lansbury Jr Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 51
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini, E. Giannoni, F. Chiti, F. Baroni, L. Formigli, and J. Zurdo Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 52
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • D.M. Walsh, and D.J. Selkoe Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration Protein Pept. Letters 11 2004 213 228
    • (2004) Protein Pept. Letters , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 53
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation
    • G. Schaffar, P. Breuer, R. Boteva, C. Behrends, N. Tzvetkov, and N. Strippel Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation Mol. Cell. 15 2004 95 105
    • (2004) Mol. Cell. , vol.15 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3    Behrends, C.4    Tzvetkov, N.5    Strippel, N.6
  • 55
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • M. Arrasate, S. Mitra, E.S. Schweitzer, M.R. Segal, and S. Finkbeiner Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 431 2004 805 810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 56
    • 0033802841 scopus 로고    scopus 로고
    • Ataxin-3 is translocated into the nucleus for the formation of intranuclear inclusions in normal and Machado-Joseph disease brains
    • H. Fujigasaki, T. Uchihara, S. Koyano, K. Iwabuchi, S. Yagishita, and T. Makifuchi Ataxin-3 is translocated into the nucleus for the formation of intranuclear inclusions in normal and Machado-Joseph disease brains Expt. Neurol. 165 2000 248 256
    • (2000) Expt. Neurol. , vol.165 , pp. 248-256
    • Fujigasaki, H.1    Uchihara, T.2    Koyano, S.3    Iwabuchi, K.4    Yagishita, S.5    Makifuchi, T.6
  • 57
    • 0034807238 scopus 로고    scopus 로고
    • Preferential recruitment of ataxin-3 independent of expanded polyglutamine: An immunohistochemical study on Marinesco bodies
    • H. Fujigasaki, T. Uchihara, J. Takahashi, H. Matsushita, A. Nakamura, and S. Koyano Preferential recruitment of ataxin-3 independent of expanded polyglutamine: an immunohistochemical study on Marinesco bodies J. Neurol. Neurosurg. Psychiatry 71 2001 518 520
    • (2001) J. Neurol. Neurosurg. Psychiatry , vol.71 , pp. 518-520
    • Fujigasaki, H.1    Uchihara, T.2    Takahashi, J.3    Matsushita, H.4    Nakamura, A.5    Koyano, S.6
  • 59
    • 0038514252 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization
    • L. Gales, I. Cardoso, B. Fayard, A. Quintanilha, M.J. Saraiva, and A.M. Damas X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization J. Biol. Chem. 278 2003 11654 11660
    • (2003) J. Biol. Chem. , vol.278 , pp. 11654-11660
    • Gales, L.1    Cardoso, I.2    Fayard, B.3    Quintanilha, A.4    Saraiva, M.J.5    Damas, A.M.6
  • 60
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • O. Poirot, E. O'Toole, and C. Notredame Tcoffee@igs: a web server for computing, evaluating and combining multiple sequence alignments Nucl. Acids Res. 31 2003 3503 3506
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 61
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • G.J. Barton ALSCRIPT: a tool to format multiple sequence alignments Protein Eng. 6 1993 37 40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.