메뉴 건너뛰기




Volumn 100, Issue 8, 2011, Pages 2033-2042

The Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79959686811     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.02.056     Document Type: Article
Times cited : (42)

References (35)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F., and C. M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 23444450224 scopus 로고    scopus 로고
    • Protein fibers as performance proteins: New technologies and applications
    • DOI 10.1016/j.copbio.2005.05.005, PII S095816690500087X, Protein Technologies and Commercial Enzymes
    • Scheibel, T. 2005. Protein fibers as performance proteins: new technologies and applications. Curr. Opin. Biotechnol. 16:427-433. (Pubitemid 41111529)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.4 , pp. 427-433
    • Scheibel, T.1
  • 4
    • 0034578144 scopus 로고    scopus 로고
    • Trinucleotide repeats: Mechanisms and pathophysiology
    • Cummings, C. J., and H. Y. Zoghbi. 2000. Trinucleotide repeats: mechanisms and pathophysiology. Annu. Rev. Genomics Hum. Genet. 1:281-328.
    • (2000) Annu. Rev. Genomics Hum. Genet , vol.1 , pp. 281-328
    • Cummings, C.J.1    Zoghbi, H.Y.2
  • 5
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • DOI 10.1006/jmbi.2001.4850
    • Chen, S., V. Berthelier, R. Wetzel. 2001. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol. 311:173-182. (Pubitemid 32735322)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.1 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 6
    • 35648992125 scopus 로고    scopus 로고
    • The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils
    • Bulone, D., L. Masino, A. Pastore. 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    Pastore, A.3
  • 7
    • 77949775195 scopus 로고    scopus 로고
    • Repeat expansion disease: Progress and puzzles in disease pathogenesis
    • La Spada, A. R., and J. P. Taylor. 2010. Repeat expansion disease: progress and puzzles in disease pathogenesis. Nat. Rev. Genet. 11:247-258.
    • (2010) Nat. Rev. Genet , vol.11 , pp. 247-258
    • La Spada, A.R.1    Taylor, J.P.2
  • 8
    • 77955647254 scopus 로고    scopus 로고
    • Towards the treatment of polyglutamine diseases: The modulatory role of protein context
    • Robertson, A. L., and S. P. Bottomley. 2010. Towards the treatment of polyglutamine diseases: the modulatory role of protein context. Curr. Med. Chem. 17:3058-3068.
    • (2010) Curr. Med. Chem , vol.17 , pp. 3058-3068
    • Robertson, A.L.1    Bottomley, S.P.2
  • 9
    • 0042357191 scopus 로고    scopus 로고
    • Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature
    • DOI 10.1074/jbc.M304205200
    • Marchal, S., E. Shehi, R. Lange. 2003. Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature. J. Biol. Chem. 278:31554-31563. (Pubitemid 37048333)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , 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
  • 10
    • 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., G. Nicastro, A. Pastore. 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
  • 12
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • Ellisdon, A. M., B. Thomas, and S. P. Bottomley. 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
  • 13
    • 33947586837 scopus 로고    scopus 로고
    • Mechanisms of Ataxin-3 Misfolding and Fibril Formation: Kinetic Analysis of a Disease-associated Polyglutamine Protein
    • DOI 10.1016/j.jmb.2007.02.058, PII S0022283607002392
    • Ellisdon, A. M., M. C. Pearce, and S. P. Bottomley. 2007. Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein. J. Mol. Biol. 368:595-605. (Pubitemid 46483496)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 595-605
    • Ellisdon, A.M.1    Pearce, M.C.2    Bottomley, S.P.3
  • 14
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils
    • DOI 10.1073/pnas.211305198
    • Bevivino, A. E., and P. J. Loll. 2001. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils. Proc. Natl. Acad. Sci. USA. 98:11955-11960. (Pubitemid 32959808)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.21 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 15
    • 79251572023 scopus 로고    scopus 로고
    • Functional interactions as a survival strategy against abnormal aggregation
    • Masino, L., G. Nicastro, A. Pastore. 2011. Functional interactions as a survival strategy against abnormal aggregation. FASEB J. 25:45-54.
    • (2011) FASEB J , vol.25 , pp. 45-54
    • Masino, L.1    Nicastro, G.2    Pastore, A.3
  • 16
    • 0041563693 scopus 로고    scopus 로고
    • Domain architecture of the polyglutamine protein ataxin-3: A globular domain followed by a flexible tail
    • DOI 10.1016/S0014-5793(03)00748-8
    • Masino, L., V. Musi, A. Pastore. 2003. Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. FEBS Lett. 549:21-25. (Pubitemid 36959836)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 21-25
    • Masino, L.1    Musi, V.2    Menon, R.P.3    Fusi, P.4    Kelly, G.5    Frenkiel, T.A.6    Trottier, Y.7    Pastore, A.8
  • 17
    • 33646392477 scopus 로고    scopus 로고
    • Structural and mechanical study of a self-assembling protein nanotube
    • Graveland-Bikker, J. F., I. A. Schaap, C. G. de Kruif. 2006. Structural and mechanical study of a self-assembling protein nanotube. Nano Lett. 6:616-621.
    • (2006) Nano Lett , vol.6 , pp. 616-621
    • Graveland-Bikker, J.F.1    Schaap, I.A.2    De Kruif, C.G.3
  • 18
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • DOI 10.1083/jcb.120.4.923
    • Gittes, F., B. Mickey, J. Howard. 1993. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:923-934. (Pubitemid 23056298)
    • (1993) Journal of Cell Biology , vol.120 , Issue.4 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 19
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • DOI 10.1006/jmbi.1996.0687
    • Rivetti, C., M. Guthold, and C. Bustamante. 1996. Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis. J. Mol. Biol. 264:919-932. (Pubitemid 27019483)
    • (1996) Journal of Molecular Biology , vol.264 , Issue.5 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 20
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama, N., and R. W. Woody. 2000. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:252-260. (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 22
    • 77950643588 scopus 로고    scopus 로고
    • Detection of populations of amyloid-like protofibrils with different physical properties
    • Relini, A., S. Torrassa, A. Gliozzi. 2010. Detection of populations of amyloid-like protofibrils with different physical properties. Biophys. J. 98:1277-1284.
    • (2010) Biophys. J , vol.98 , pp. 1277-1284
    • Relini, A.1    Torrassa, S.2    Gliozzi, A.3
  • 25
    • 37549063068 scopus 로고    scopus 로고
    • Role of intermolecular forces in defining material properties of protein nanofibrils
    • Knowles, T. P., A. W. Fitzpatrick, M. E. Welland. 2007. Role of intermolecular forces in defining material properties of protein nanofibrils. Science. 318:1900-1903.
    • (2007) Science , vol.318 , pp. 1900-1903
    • Knowles, T.P.1    Fitzpatrick, A.W.2    Welland, M.E.3
  • 26
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • DOI 10.1038/35069000
    • Vollrath, F., and D. P. Knight. 2001. Liquid crystalline spinning of spider silk. Nature. 410:541-548. (Pubitemid 32267190)
    • (2001) Nature , vol.410 , Issue.6828 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 29
    • 9744228666 scopus 로고    scopus 로고
    • Fibrillar β-lactoglobulin gels: Part 1. Fibril formation and structure
    • DOI 10.1021/bm049659d
    • Gosal, W. S., A. H. Clark, and S. B. Ross-Murphy. 2004. Fibrillar β-lactoglobulin gels. Part 1. Fibril formation and structure. Biomacromolecules. 5:2408-2419. (Pubitemid 39585296)
    • (2004) Biomacromolecules , vol.5 , Issue.6 , pp. 2408-2419
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 30
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • DOI 10.1074/jbc.M205809200
    • Poirier, M. A., H. Li, C. A. Ross. 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
  • 33
    • 0037819879 scopus 로고    scopus 로고
    • Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy
    • Kad, N. M., S. L. Myers, N. H. Thomson. 2003. Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 330:785-797.
    • (2003) J. Mol. Biol , vol.330 , pp. 785-797
    • Kad, N.M.1    Myers, S.L.2    Thomson, N.H.3
  • 34
    • 77953799932 scopus 로고    scopus 로고
    • Small heatshock proteins interact with a flanking domain to suppress polyglutamine aggregation
    • Robertson, A. L., S. J. Headey, S. P. Bottomley. 2010. Small heatshock proteins interact with a flanking domain to suppress polyglutamine aggregation. Proc. Natl. Acad. Sci. USA. 107:10424-10429.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 10424-10429
    • Robertson, A.L.1    Headey, S.J.2    Bottomley, S.P.3
  • 35
    • 71749115321 scopus 로고    scopus 로고
    • Josephin domain of ataxin-3 contains two distinct ubiquitin-binding sites
    • Nicastro, G., L. Masino, A. Pastore. 2009. Josephin domain of ataxin-3 contains two distinct ubiquitin-binding sites. Biopolymers. 91:1203-1214.
    • (2009) Biopolymers , vol.91 , pp. 1203-1214
    • Nicastro, G.1    Masino, L.2    Pastore, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.