메뉴 건너뛰기




Volumn 121, Issue 1, 2005, Pages 63-72

Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID;

EID: 17044381327     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.01.034     Document Type: Article
Times cited : (235)

References (51)
  • 1
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • A. Aguzzi, and M. Polymenidou Mammalian prion biology: one century of evolving concepts Cell 116 2004 313 327
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 2
    • 67349189383 scopus 로고
    • The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
    • C.B. Anfinsen, E. Haber, M. Sela, and F.H. White Jr. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain Proc. Natl. Acad. Sci. USA 47 1961 1309 1314
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1309-1314
    • Anfinsen, C.B.1    Haber, E.2    Sela, M.3    White Jr., F.H.4
  • 3
    • 1542379868 scopus 로고    scopus 로고
    • Autocatalytic conversion of recombinant prion protein displays a species barrier
    • I.V. Baskakov Autocatalytic conversion of recombinant prion protein displays a species barrier J. Biol. Chem. 279 2003 7671 7677
    • (2003) J. Biol. Chem. , vol.279 , pp. 7671-7677
    • Baskakov, I.V.1
  • 4
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • R.A. Bessen, and R.F. Marsh Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy J. Virol. 68 1994 7859 7868
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 6
    • 0025836628 scopus 로고
    • Scrapie strain variation and its implications
    • M.E. Bruce, and H. Fraser Scrapie strain variation and its implications Curr. Top. Microbiol. Immunol. 172 1991 125 138
    • (1991) Curr. Top. Microbiol. Immunol. , vol.172 , pp. 125-138
    • Bruce, M.E.1    Fraser, H.2
  • 8
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • B. Caughey Interactions between prion protein isoforms: the kiss of death? Trends Biochem. Sci. 26 2001 235 242
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 235-242
    • Caughey, B.1
  • 9
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in β-sheet conformations of abnormal prion protein
    • B. Caughey, G.J. Raymond, and R.A. Bessen Strain-dependent differences in β-sheet conformations of abnormal prion protein J. Biol. Chem. 273 1998 32230 32235
    • (1998) J. Biol. Chem. , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 10
    • 8844238368 scopus 로고    scopus 로고
    • Amyloidogenic domains, prions and structural inheritance: Rudiments of early life or recent acquisition?
    • Y.O. Chernoff Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition? Curr. Opin. Chem. Biol. 8 2004 665 671
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 665-671
    • Chernoff, Y.O.1
  • 11
    • 0035826236 scopus 로고    scopus 로고
    • Conformational diversity in a yeast prion dictates its seeding specificity
    • P. Chien, and J.S. Weissman Conformational diversity in a yeast prion dictates its seeding specificity Nature 410 2001 223 227
    • (2001) Nature , vol.410 , pp. 223-227
    • Chien, P.1    Weissman, J.S.2
  • 12
    • 0042358923 scopus 로고    scopus 로고
    • Generation of prion transmission barriers by mutational control of amyloid conformations
    • P. Chien, A.H. DePace, S.R. Collins, and J.S. Weissman Generation of prion transmission barriers by mutational control of amyloid conformations Nature 424 2003 948 951
    • (2003) Nature , vol.424 , pp. 948-951
    • Chien, P.1    Depace, A.H.2    Collins, S.R.3    Weissman, J.S.4
  • 13
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • P. Chien, J.S. Weissman, and A.H. DePace Emerging principles of conformation-based prion inheritance Annu. Rev. Biochem. 73 2004 617 656
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    Depace, A.H.3
  • 14
    • 0033600407 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease
    • J. Collinge Variant Creutzfeldt-Jakob disease Lancet 354 1999 317 323
    • (1999) Lancet , vol.354 , pp. 317-323
    • Collinge, J.1
  • 15
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • J. Collinge Prion diseases of humans and animals: their causes and molecular basis Annu. Rev. Neurosci. 24 2001 519 550
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 16
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • J.H. Come, P.E. Fraser, and P.T. Lansbury Jr. A kinetic model for amyloid formation in the prion diseases: importance of seeding Proc. Natl. Acad. Sci. USA 90 1993 5959 5963
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury Jr., P.T.3
  • 21
    • 0017336439 scopus 로고
    • Characteristics of a short incubation model of scrapie in the golden hamster
    • R.H. Kimberlin, and C.A. Walker Characteristics of a short incubation model of scrapie in the golden hamster J. Gen. Virol. 34 1977 295 304
    • (1977) J. Gen. Virol. , vol.34 , pp. 295-304
    • Kimberlin, R.H.1    Walker, C.A.2
  • 22
    • 0017866857 scopus 로고
    • Evidence for the transmission of one source of scrapie agent to hamster involves separation of agent strains from a mixture
    • R.H. Kimberlin, and C.A. Walker Evidence for the transmission of one source of scrapie agent to hamster involves separation of agent strains from a mixture J. Gen. Virol. 39 1978 487 496
    • (1978) J. Gen. Virol. , vol.39 , pp. 487-496
    • Kimberlin, R.H.1    Walker, C.A.2
  • 23
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • C.-Y. King, and R. Diaz-Avalos Protein-only transmission of three yeast prion strains Nature 428 2004 319 323
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.-Y.1    Diaz-Avalos, R.2
  • 24
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
    • D.A. Kocisko, S.A. Priola, G.J. Raymond, B. Chesebro, P.T. Lansbury Jr., and B. Caughey Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier Proc. Natl. Acad. Sci. USA 92 1995 3923 3927
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    Lansbury Jr., P.T.5    Caughey, B.6
  • 25
    • 0142091396 scopus 로고    scopus 로고
    • Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: Structural clues for prion propagation
    • B. Kundu, N.R. Maiti, E.M. Jones, K.A. Surewicz, D.L. Vanik, and W.K. Surewicz Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation Proc. Natl. Acad. Sci. USA 100 2003 12069 12074
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12069-12074
    • Kundu, B.1    Maiti, N.R.2    Jones, E.M.3    Surewicz, K.A.4    Vanik, D.L.5    Surewicz, W.K.6
  • 26
    • 0042320356 scopus 로고    scopus 로고
    • Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process
    • S. Lee, and D. Eisenberg Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process Nat. Struct. Biol. 10 2003 725 730
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 725-730
    • Lee, S.1    Eisenberg, D.2
  • 29
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • M. Morillas, W. Swietnicki, P. Gambetti, and W.K. Surewicz Membrane environment alters the conformational structure of the recombinant human prion protein J. Biol. Chem. 274 1999 36859 36865
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 31
    • 0028822204 scopus 로고
    • A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells
    • S.A. Priola, and B. Chesebro A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells J. Virol. 69 1995 7754 7758
    • (1995) J. Virol. , vol.69 , pp. 7754-7758
    • Priola, S.A.1    Chesebro, B.2
  • 32
    • 0035041973 scopus 로고    scopus 로고
    • Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155
    • S.A. Priola, J. Chabry, and K. Chan Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155 J. Virol. 75 2001 4673 4680
    • (2001) J. Virol. , vol.75 , pp. 4673-4680
    • Priola, S.A.1    Chabry, J.2    Chan, K.3
  • 33
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • S.B. Prusiner Novel proteinaceous infectious particles cause scrapie Science 216 1982 136 144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 39
    • 17044382824 scopus 로고    scopus 로고
    • Transgenetic investigations of the species barrier and prion strains
    • S.B. Prusiner Second Edition Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • M. Scott, D. Peretz, R.M. Ridley, H.F. Baker, S.J. DeArmond, and S.B. Prusiner Transgenetic investigations of the species barrier and prion strains S.B. Prusiner Prion Biology and Diseases Second Edition 2004 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 435 482
    • (2004) Prion Biology and Diseases , pp. 435-482
    • Scott, M.1    Peretz, D.2    Ridley, R.M.3    Baker, H.F.4    Dearmond, S.J.5    Prusiner, S.B.6
  • 41
    • 3042760011 scopus 로고    scopus 로고
    • Prion protein conversion in vitro
    • S. Supattapone Prion protein conversion in vitro J. Mol. Med. 82 2004 348 356
    • (2004) J. Mol. Med. , vol.82 , pp. 348-356
    • Supattapone, S.1
  • 42
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • W.K. Surewicz, and H.H. Mantsch New insight into protein secondary structure from resolution-enhanced infrared spectra Biochim. Biophys. Acta 952 1988 115 130
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 43
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • M. Tanaka, P. Chien, N. Naber, R. Cooke, and J.S. Weissman Conformational variations in an infectious protein determine prion strain differences Nature 428 2004 323 328
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 44
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • G.C. Telling, M. Scott, J. Mastrianni, R. Gabizon, M. Torchia, F.E. Cohen, S.J. DeArmond, and S.B. Prusiner Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein Cell 83 1995 79 90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    Dearmond, S.J.7    Prusiner, S.B.8
  • 46
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • S.M. Uptain, and S. Lindquist Prions as protein-based genetic elements Annu. Rev. Microbiol. 56 2002 703 741
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 47
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • D.L. Vanik, K.A. Surewicz, and W.K. Surewicz Molecular basis of barriers for interspecies transmissibility of mammalian prions Mol. Cell 14 2004 139 145
    • (2004) Mol. Cell , vol.14 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3
  • 48
  • 51
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • G. Zandomeneghi, M.R.H. Krebs, M.G. McCammon, and M. Fandrich FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils Protein Sci. 13 2004 3314 3321
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fandrich, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.