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Volumn 14, Issue 4, 1998, Pages 475-488

As;Les prions : Entre dogmes et réalités

(1)  Laurent, Michel a  

a CNRS   (France)

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[No Author keywords available]

Indexed keywords


EID: 33746330172     PISSN: 07670974     EISSN: None     Source Type: Journal    
DOI: 10.4267/10608/1066     Document Type: Article
Times cited : (2)

References (26)
  • 6
    • 0027958170 scopus 로고
    • Molecular biology of prion diseases
    • Weissmann C. Molecular biology of prion diseases. Trends Cell Biol 1994; 4: 10-4.
    • (1994) Trends Cell Biol , vol.4 , pp. 10-14
    • Weissmann, C.1
  • 7
    • 0028308104 scopus 로고
    • URE3 as an altered URE2 protein : Evidence for a prion analog in Saccharomyces rerevisiae
    • Wickner RB. URE3 as an altered URE2 protein : evidence for a prion analog in Saccharomyces rerevisiae. Science 1994; 264: 566-9.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 8
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison D, Wickner RB. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 1995; 270: 93-5.
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.1    Wickner, R.B.2
  • 9
    • 0028484034 scopus 로고
    • Prion-like factors in yeast
    • Cox B. Prion-like factors in yeast. Curr Biol 1994; 4: 744-8.
    • (1994) Curr Biol , vol.4 , pp. 744-748
    • Cox, B.1
  • 10
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of PSI+, a heritable pnon-like factor of S cerevisiae
    • Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of PSI+, a heritable pnon-like factor of S cerevisiae. Cell 1997; 89: 811-9.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5    Lindquist, S.6
  • 11
    • 0025731379 scopus 로고
    • Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation
    • Milner J, Medcalf EA. Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation. Cell 1991 ; 65: 765-74.
    • (1991) Cell , vol.65 , pp. 765-774
    • Milner, J.1    Medcalf, E.A.2
  • 13
    • 0013894066 scopus 로고
    • Salmonella flagella: In vitro reconstitution and over-all shapes of flagellar filaments
    • Asukura S, Eguchi G, lino T. Salmonella flagella: in vitro reconstitution and over-all shapes of flagellar filaments. J Mol Biol 1966; 16: 302-16.
    • (1966) J Mol Biol , vol.16 , pp. 302-316
    • Asukura, S.1    Eguchi, G.2    Lino, T.3
  • 14
    • 0016370644 scopus 로고
    • Assembly of Salmonella flagellin in vitro and in vivo
    • lino T. Assembly of Salmonella flagellin in vitro and in vivo. J Supramol Struct 1974; 2: 372-84.
    • (1974) J Supramol Struct , vol.2 , pp. 372-384
    • Lino, T.1
  • 16
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come JH, Fraser PE, Lansbury PT. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc Natl Acad Sci USA 1993; 90: 5959-63.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 18
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to pro tease-resistant forms: A model for the scrapie species barrier
    • Kocisko DA, Priola SA, Raymond G, Chesebro B, Lansbury PT, Caughey B. Species specificity in the cell-free conversion of prion protein to pro tease-resistant forms: a model for the scrapie species barrier. Proc Xatl Acad Sci USA 1995 ; 92: 3923-7.
    • (1995) Proc Xatl Acad Sci USA , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.3    Chesebro, B.4    Lansbury, P.T.5    Caughey, B.6
  • 19
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Pnisiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136-44.
    • (1982) Science , vol.216 , pp. 136-144
    • Pnisiner, S.B.1
  • 20
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Pnisiner SB. Molecular biology of prion diseases. Science 1991 ; 252: 1515-22.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Pnisiner, S.B.1
  • 21
    • 0030579560 scopus 로고    scopus 로고
    • Prionics or the kinetic basis of prion diseases
    • Eigen M. Prionics or the kinetic basis of prion diseases. Biophys Chem 1996; 63, A1-8.
    • (1996) Biophys Chem , vol.63
    • Eigen, M.1
  • 22
    • 0031582232 scopus 로고    scopus 로고
    • Aiitocatalytic processes in cooperative mechanisms of prion diseases
    • Laurent M. Aiitocatalytic processes in cooperative mechanisms of prion diseases. FEBS Lett 1997; 407: 1-6.
    • (1997) FEBS Lett , vol.407 , pp. 1-6
    • Laurent, M.1
  • 23
    • 0029897477 scopus 로고    scopus 로고
    • Les maladies àprions: L'hypothèse de la protéine seule et ses conséquences dynamiques
    • Laurent M. Les maladies àprions: l'hypothèse de la protéine seule et ses conséquences dynamiques. Med Sci 1996; 12 : 774-85.
    • (1996) Med Sci , vol.12 , pp. 774-785
    • Laurent, M.1
  • 24
    • 0029817344 scopus 로고    scopus 로고
    • Prion diseases and the «protein only» hypothesis: A theoretical dynamic study
    • Laurent M. Prion diseases and the «protein only» hypothesis: a theoretical dynamic study. Biochem J 1996; 318: 35-9.
    • (1996) Biochem J , vol.318 , pp. 35-39
    • Laurent, M.1
  • 25
    • 0030574088 scopus 로고    scopus 로고
    • How many phenotypes from one genotype? the case of prion diseases
    • Kacser H, Small JR. How many phenotypes from one genotype? The case of prion diseases. J Theoret Biol 1996 ; 182: 209-18.
    • (1996) J Theoret Biol , vol.182 , pp. 209-218
    • Kacser, H.1    Small, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.