메뉴 건너뛰기




Volumn 21, Issue 6-7, 2005, Pages 634-640

Prion proteins: Folding and aggregation properties;Protéines prions: Propriétés de repliement et d'agrégation

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; POLYPEPTIDE; PRION PROTEIN;

EID: 22144467370     PISSN: 07670974     EISSN: None     Source Type: Journal    
DOI: 10.1051/medsci/2005216-7634     Document Type: Review
Times cited : (2)

References (36)
  • 1
    • 0001289828 scopus 로고
    • Pathologie animale. La maladie dite tremblante du mouton est-elle inoculable?
    • Cuille J, Chelle PL. Pathologie animale. La maladie dite tremblante du mouton est-elle inoculable? CR Acad Sci (Paris) 1936; 203: 1552-4.
    • (1936) CR Acad Sci (Paris) , vol.203 , pp. 1552-1554
    • Cuille, J.1    Chelle, P.L.2
  • 2
    • 49749220574 scopus 로고
    • Scrapie and Kuru
    • Hadlow WJ. Scrapie and Kuru. Lancet 1959; 2: 289-90.
    • (1959) Lancet , vol.2 , pp. 289-290
    • Hadlow, W.J.1
  • 3
    • 49749206702 scopus 로고
    • Encephalopathy in mice produced by inoculation with scrapie brain material
    • Chandler RL. Encephalopathy in mice produced by inoculation with scrapie brain material. Lancet 1961; 1: 1378-9.
    • (1961) Lancet , vol.1 , pp. 1378-1379
    • Chandler, R.L.1
  • 4
    • 0024211952 scopus 로고
    • Transmissible and non-transmissible amyloidoses: Autocatalytic post-translational conversion of host precursor proteins to β-pleated conformations
    • Gajdusek DC. Transmissible and non-transmissible amyloidoses: autocatalytic post-translational conversion of host precursor proteins to β-pleated conformations. J Neuroimmunol 1988; 20: 95-110.
    • (1988) J Neuroimmunol , vol.20 , pp. 95-110
    • Gajdusek, D.C.1
  • 6
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. Self-replication and scrapie. Nature 1967; 215: 1043-4.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 7
    • 0019324430 scopus 로고
    • Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent
    • Prusiner SB, Groth DF, Cochran SP, et al. Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent. Biochemistry 1980; 19: 4883-91.
    • (1980) Biochemistry , vol.19 , pp. 4883-4891
    • Prusiner, S.B.1    Groth, D.F.2    Cochran, S.P.3
  • 9
    • 0020285570 scopus 로고
    • Further purification and characterization of scrapie prions
    • Prusiner SB, Bolton DC, Groth DF, et al. Further purification and characterization of scrapie prions. Biochemistry 1982; 26: 6942-50.
    • (1982) Biochemistry , vol.26 , pp. 6942-6950
    • Prusiner, S.B.1    Bolton, D.C.2    Groth, D.F.3
  • 10
    • 0021019026 scopus 로고
    • Scrapie prions aggregate to form amyloid-like birefringent rods
    • Prusiner SB, McKinley MP, Bowman KA, et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983; 35: 349-58.
    • (1983) Cell , vol.35 , pp. 349-358
    • Prusiner, S.B.1    McKinley, M.P.2    Bowman, K.A.3
  • 11
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner SB, Groth DF, Bolton DC, et al. Purification and structural studies of a major scrapie prion protein. Cell 1984; 38: 127-34.
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3
  • 12
    • 0028343093 scopus 로고
    • No propagation of prions in mice devoid of PrP
    • Sailer A, Bueler H, Fischer M, et al. No propagation of prions in mice devoid of PrP. Cell 1994; 77: 967-8.
    • (1994) Cell , vol.77 , pp. 967-968
    • Sailer, A.1    Bueler, H.2    Fischer, M.3
  • 13
    • 0028962532 scopus 로고
    • Prion protein gene variation among primates
    • Schätzl HM, Da Costa M, Taylor L, et al. Prion protein gene variation among primates. J Mol Biol 1995; 254: 362-74.
    • (1995) J Mol Biol , vol.254 , pp. 362-374
    • Schätzl, H.M.1    Da Costa, M.2    Taylor, L.3
  • 14
    • 0024434503 scopus 로고
    • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
    • Endo T, Groth D, Prusiner SB, Kobata A. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 1989; 28: 8380-8.
    • (1989) Biochemistry , vol.28 , pp. 8380-8388
    • Endo, T.1    Groth, D.2    Prusiner, S.B.3    Kobata, A.4
  • 15
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N, Borchelt DR, Hsiao K, Prusiner SB. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 1987; 51: 229-40.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 16
    • 0344239773 scopus 로고    scopus 로고
    • Glycosylation differences between the normal and pathogenic prion protein isoforms
    • Rudd PM, Endo T, Colominas C, et al. Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc Natl Acad Sci USA 1999; 96: 13044-9.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13044-13049
    • Rudd, P.M.1    Endo, T.2    Colominas, C.3
  • 17
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP(l21-32l)
    • Riek R, Hornemann S, Wider G, et al. NMR structure of the mouse prion protein domain PrP(l21-32l). Nature 1996; 382: 180-2.
    • (1996) Nature , vol.382 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3
  • 18
    • 0030790431 scopus 로고    scopus 로고
    • Prion protein NMR structure and species barrier for prion diseases
    • Billeter M, Riek R, Wider G, et al. Prion protein NMR structure and species barrier for prion diseases. Proc Natl Acad Sci USA 1997; 94: 7281-5.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7281-7285
    • Billeter, M.1    Riek, R.2    Wider, G.3
  • 19
    • 0030342679 scopus 로고    scopus 로고
    • Scrapie prions: A three-dimensional model of an infectious fragment
    • Huang Z, Prusiner SB, Cohen FE. Scrapie prions: a three-dimensional model of an infectious fragment. Folding Des 1996; 1: 13-9.
    • (1996) Folding des , vol.1 , pp. 13-19
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 21
    • 0033583190 scopus 로고    scopus 로고
    • Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
    • Jackson GS, Hosszu LL, Power A, et al. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 1999; 283: 1935-7.
    • (1999) Science , vol.283 , pp. 1935-1937
    • Jackson, G.S.1    Hosszu, L.L.2    Power, A.3
  • 22
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill AF, Antoniou M, Collinge. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J Gen Virol 1999; 80: 11-4.
    • (1999) J Gen Virol , vol.80 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge3
  • 24
    • 3442898738 scopus 로고    scopus 로고
    • An end to the prion debate? Don't count on it
    • Couzin J. An end to the prion debate? Don't count on it. Science 2004; 305: 589.
    • (2004) Science , vol.305 , pp. 589
    • Couzin, J.1
  • 25
    • 84966138908 scopus 로고
    • PSI, a cytoplasmic suppressor of super-suppressor in yeast
    • Cox BS. PSI, a cytoplasmic suppressor of super-suppressor in yeast. Heredity 1965; 20: 505-21.
    • (1965) Heredity , vol.20 , pp. 505-521
    • Cox, B.S.1
  • 26
    • 0015056102 scopus 로고
    • Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast
    • Lacroute F. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J Bacterial 1971; 106: 519-22.
    • (1971) J Bacterial , vol.106 , pp. 519-522
    • Lacroute, F.1
  • 27
    • 0028308104 scopus 로고
    • Evidence for a prion analog in S. cerevisiae: The [URE3] non-Mendelian genetic element as an altered URE2 protein
    • Wickner RB. Evidence for a prion analog in S. cerevisiae: The [URE3] non-Mendelian genetic element as an altered URE2 protein. Science 1994; 264: 566-9.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 28
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio TR, Cashikar AG, Kowal AS, et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000; 289: 1317-21.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3
  • 29
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
    • Bousset L, Thomson NH, Radford SE, Melki R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J 2002; 21: 2903-11.
    • (2002) EMBO J , vol.21 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 30
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde M, Serpell LC, Bartlam M, et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 1997; 273: 729-39.
    • (1997) J Mol Biol , vol.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3
  • 31
    • 0034834580 scopus 로고    scopus 로고
    • Preparation and characterization of purified amyloid fibrils
    • Zurdo J, Guijarro JI, Dobson CM. Preparation and characterization of purified amyloid fibrils. J Am Chem Soc 2001; 123: 8141-2.
    • (2001) J Am Chem Soc , vol.123 , pp. 8141-8142
    • Zurdo, J.1    Guijarro, J.I.2    Dobson, C.M.3
  • 32
    • 0037291995 scopus 로고    scopus 로고
    • The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils
    • Bousset L, Briki F, Doucet J, Melki R. The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils. J Struct Biol 2003; 141: 132-42.
    • (2003) J Struct Biol , vol.141 , pp. 132-142
    • Bousset, L.1    Briki, F.2    Doucet, J.3    Melki, R.4
  • 33
    • 0040865398 scopus 로고
    • In vitro formation of flagella-like filaments and other structure from flagellin
    • Abram D, Koffler H. In vitro formation of flagella-like filaments and other structure from flagellin. J Mol Biol 1964; 9: 168-85.
    • (1964) J Mol Biol , vol.9 , pp. 168-185
    • Abram, D.1    Koffler, H.2
  • 34
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas DA, Carrell RW. Serpinopathies and the conformational dementias. Nat Rev Genet 2002; 3: 759-68.
    • (2002) Nat Rev Genet , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 35
    • 0242636317 scopus 로고    scopus 로고
    • Propagation of yeast prions
    • Tuite MF, Cox BS. Propagation of yeast prions. Nat Rev 2003; 4: 878-89.
    • (2003) Nat Rev , vol.4 , pp. 878-889
    • Tuite, M.F.1    Cox, B.S.2
  • 36
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • Bousset L, Belrhali H, Janin J, et al. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 2001; 9: 39-46.
    • (2001) Structure , vol.9 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.