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Volumn 50, Issue 33, 2011, Pages 7111-7116

Seeding specificity and ultrastructural characteristics of infectious recombinant prions

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBERS; ATOMIC FORCE; COFACTORS; IN-VITRO; MOUSE BRAIN; PRION INFECTIVITY; PRION PROTEIN; PROTEIN MISFOLDING; SPHERICAL AGGREGATES; WILD TYPES;

EID: 80051714126     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200786p     Document Type: Article
Times cited : (37)

References (31)
  • 1
    • 77649213673 scopus 로고    scopus 로고
    • Wang, F.; et al. (2010) Science 327, 1132
    • (2010) Science , vol.327 , pp. 1132
    • Wang, F.1
  • 2
    • 77649214076 scopus 로고    scopus 로고
    • Colby, D. W.; et al. (2010) PLoS Pathog. 387, e1000736
    • (2010) PLoS Pathog. , vol.387 , pp. 1000736
    • Colby, D.W.1
  • 3
    • 77649213673 scopus 로고    scopus 로고
    • Generating a Prion with Bacterially Expressed Recombinant Prion Protein
    • Wang, F., Wang, X., Yuan, C. G., and Ma, J. (2010) Generating a Prion with Bacterially Expressed Recombinant Prion Protein Science 327, 1132-1135
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 5
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie Science 216, 136-144 (Pubitemid 12089840)
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 6
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey, B. and Raymond, G. J. (1991) The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive J. Biol. Chem. 266, 18217-18223 (Pubitemid 21908068)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.27 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 11
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • DOI 10.1038/nature03680
    • Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. O., Riekel, C., Grothe, R., and Eisenberg, D. (2005) Structure of the cross-beta spine of amyloid-like fibrils Nature 435, 773-778 (Pubitemid 40839722)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5    Grothe, R.6    Eisenberg, D.7
  • 12
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly, J. W. (2000) Mechanisms of amyloidogenesis Nat. Struct. Biol. 7, 824-826
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 13
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • DOI 10.1146/annurev.med.57.121304.131243
    • Pepys, M. B. (2006) Amyloidosis Annu. Rev. Med. 57, 223-241 (Pubitemid 43261989)
    • (2006) Annual Review of Medicine , vol.57 , pp. 223-241
    • Pepys, M.B.1
  • 14
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
    • Cobb, N. J., Sonnichsen, F. D., McHaourab, H., and Surewicz, W. K. (2007) Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure Proc. Natl. Acad. Sci. U. S. A. 104, 18946-18951
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sonnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 15
    • 67049087912 scopus 로고    scopus 로고
    • Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration
    • Shewmaker, F., Kryndushkin, D., Chen, B., Tycko, R., and Wickner, R. B. (2009) Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration Biochemistry 48, 5074-5082
    • (2009) Biochemistry , vol.48 , pp. 5074-5082
    • Shewmaker, F.1    Kryndushkin, D.2    Chen, B.3    Tycko, R.4    Wickner, R.B.5
  • 17
    • 84934442254 scopus 로고    scopus 로고
    • Methods for conversion of prion protein into amyloid fibrils
    • Breydo, L., Makarava, N., and Baskakov, I. V. (2008) Methods for conversion of prion protein into amyloid fibrils Methods Mol. Biol. 459, 105-115
    • (2008) Methods Mol. Biol. , vol.459 , pp. 105-115
    • Breydo, L.1    Makarava, N.2    Baskakov, I.V.3
  • 19
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy
    • Anderson, M., Bocharova, O. V., Makarava, N., Breydo, L., Salnikov, V. V., and Baskakov, I. V. (2006) Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy J. Mol. Biol. 358, 580-596
    • (2006) J. Mol. Biol. , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Makarava, N.3    Breydo, L.4    Salnikov, V.V.5    Baskakov, I.V.6
  • 20
    • 0033913783 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?
    • DOI 10.1038/77476
    • Caughey, B. (2000) Transmissible spongiform encephalopathies, amyloidoses and yeast prions: common threads? Nature Med. 6, 751-754 (Pubitemid 30469422)
    • (2000) Nature Medicine , vol.6 , Issue.7 , pp. 751-754
    • Caughey, B.1
  • 21
    • 0033850051 scopus 로고    scopus 로고
    • Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein
    • Wille, H., Prusiner, S. B., and Cohen, F. E. (2000) Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein J. Struct. Biol. 130, 323-338
    • (2000) J. Struct. Biol. , vol.130 , pp. 323-338
    • Wille, H.1    Prusiner, S.B.2    Cohen, F.E.3
  • 23
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • DOI 10.1074/jbc.M603964200
    • Saa, P., Castilla, J., and Soto, C. (2006) Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification J. Biol. Chem. 281, 35245-35252 (Pubitemid 46036562)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35245-35252
    • Saa, P.1    Castilla, J.2    Soto, C.3
  • 24
    • 34547096014 scopus 로고    scopus 로고
    • Generation of genuine prion infectivity by serial PMCA
    • DOI 10.1016/j.vetmic.2007.04.004, PII S037811350700171X, Recent Progress in Prion Research Scientific Advances Reported at the Concluding Meeting of the German TSE Research Platform
    • Weber, P., Giese, A., Piening, N., Mitteregger, G., Thomzig, A., Beekes, M., and Kretzschmar, H. A. (2007) Generation of genuine prion infectivity by serial PMCA Vet. Microbiol. 123, 346-357 (Pubitemid 47096769)
    • (2007) Veterinary Microbiology , vol.123 , Issue.4 , pp. 346-357
    • Weber, P.1    Giese, A.2    Piening, N.3    Mitteregger, G.4    Thomzig, A.5    Beekes, M.6    Kretzschmar, H.A.7
  • 25
    • 77649205447 scopus 로고    scopus 로고
    • Biochemistry. What makes a prion infectious?
    • Supattapone, S. (2010) Biochemistry. What makes a prion infectious? Science 327, 1091-1092
    • (2010) Science , vol.327 , pp. 1091-1092
    • Supattapone, S.1
  • 26
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen, R. A. and Marsh, R. F. (1992) Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent J. Virol. 66, 2096-2101
    • (1992) J. Virol. , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 27
    • 12644272790 scopus 로고    scopus 로고
    • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
    • DOI 10.1126/science.274.5295.2079
    • Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J., Lugaresi, E., Gambetti, P., and Prusiner, S. B. (1996) Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity Science 274, 2079-2082 (Pubitemid 27020700)
    • (1996) Science , vol.274 , Issue.5295 , pp. 2079-2082
    • Telling, G.C.1    Parchi, P.2    DeArmond, S.J.3    Cortelli, P.4    Montagna, P.5    Gabizon, R.6    Mastrianni, J.7    Lugaresi, E.8    Gambetti, P.9    Prusiner, S.B.10
  • 28
    • 0035086136 scopus 로고    scopus 로고
    • Strain-specified relative conformational stability of the scrapie prion protein
    • DOI 10.1110/ps.39201
    • Peretz, D., Scott, M. R., Groth, D., Williamson, R. A., Burton, D. R., Cohen, F. E., and Prusiner, S. B. (2001) Strain-specified relative conformational stability of the scrapie prion protein Protein Sci. 10, 854-863 (Pubitemid 32240511)
    • (2001) Protein Science , vol.10 , Issue.4 , pp. 854-863
    • Peretz, D.1    Scott, M.R.2    Groth, D.3    Williamson, R.A.4    Burton, D.R.5    Cohen, F.E.6    Prusiner, S.B.7
  • 29
    • 77951923337 scopus 로고    scopus 로고
    • Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro
    • Deleault, N. R., Kascsak, R., Geoghegan, J. C., and Supattapone, S. (2010) Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro Biochemistry 49, 3928-3934
    • (2010) Biochemistry , vol.49 , pp. 3928-3934
    • Deleault, N.R.1    Kascsak, R.2    Geoghegan, J.C.3    Supattapone, S.4
  • 30
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova, O. V., Breydo, L., Parfenov, A. S., Salnikov, V. V., and Baskakov, I. V. (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc) J. Mol. Biol. 346, 645-659
    • (2005) J. Mol. Biol. , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.