Accès gratuit
Numéro |
Med Sci (Paris)
Volume 18, Numéro 1, Janvier 2002
|
|
---|---|---|
Page(s) | 62 - 69 | |
Section | M/S Revues : Articles de Synthèse | |
DOI | https://doi.org/10.1051/medsci/200218162 | |
Publié en ligne | 15 janvier 2002 |
- Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95: 13363–83. [Google Scholar]
- Laurent M. Les maladies à prion : l’hypothèse de la “protéine seule” et ses conséquences dynamiques. Med Sci 1996; 12 : 774–85. [Google Scholar]
- Caughey B., Interactions between prion protein isoforms: the kiss of death? Trends Biochem Sci 2001; 26 : 235–42. [Google Scholar]
- Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K. NMR structure of the mouse prion protein domain PrP (121-231). Nature 1996; 382 : 180–2. [Google Scholar]
- Liemann S, Glockshuber R. Influence of amino acid substitution related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 1999; 38 : 3258–67. [Google Scholar]
- Wildegger G, Liemann S, Glockshuber R. Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat Struct Biol 1999; 6 : 550–3. [Google Scholar]
- Swietnicki W, Morillas M, Chen S, Gambetti P, Surewicz WK. Aggregation and fibrilization of the recombinant human prion protein huPrP90-231. Biochemistry 2000; 39 : 421–31. [Google Scholar]
- Corne 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. [Google Scholar]
- Baskakov IV, Legname G, Prusiner SB, Cohen FE. Folding of prion protein to its native a-helical conformation is under kinetic control. J Biol Chem 2001; 276 : 19687–90. [Google Scholar]
- Morange M. Protéines chaperons. Med Sci 2000; 16 : 630–4. [Google Scholar]
- Liautard JP. Prions and molecular chaperones. Arch Virol 1993; 7 : 227–43. [Google Scholar]
- Edenhofer F, Rieger R, Famulok M, Wendler W, Weiss S, Winnacker EL. Prion protein PrPC interacts with molecular chaperones of the Hsp60 family. J Virol 1996; 70 : 4724–8. [Google Scholar]
- Guerin MC, Bettache S, Aumelas A, Chiche L, Liautard JP. Use of surface plasmon resonance to analyse recombinant prion protein interaction with molecular chaperones. Int J Biochromatogr 2001 [Google Scholar]
- Telling GC, Scott M, Mastrianni J, et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995; 83 : 79–90. [Google Scholar]
- Raeber AJ, Borchelt DR, Scott M, Prusiner SB. Attempts to convert the cellular prion protein into the scrapie isoform in cell-free Systems.J Virol 1992; 66 : 6155–63. [Google Scholar]
- Caughey BW, Kocisko DA, Raymond GJ, Lansburry PT. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the proteaseresistant state. Curr Biol 1996; 2 : 807–17. [Google Scholar]
- Deburman SK, Raymond GJ, Caughey B, Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc Natl Acad Sci USA 1997; 94 : 13938–43. [Google Scholar]
- Horiuchi M, Priola SA, Chabry J, Caughey B. Interactions between heterologous forms of prion protein : binding, inhibition of conversion and species barriers. Proc Natl Acad Sci USA 2000; 97 : 5836–41. [Google Scholar]
- Hill AF, Antoniou M, Collinge J. Protease-resistant prion protein produced in vitro lacks detectabble infectivivty. J Gen Virol 1999; 80 : 11–4. [Google Scholar]
- Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001; 411 : 810–3. [Google Scholar]
Les statistiques affichées correspondent au cumul d'une part des vues des résumés de l'article et d'autre part des vues et téléchargements de l'article plein-texte (PDF, Full-HTML, ePub... selon les formats disponibles) sur la platefome Vision4Press.
Les statistiques sont disponibles avec un délai de 48 à 96 heures et sont mises à jour quotidiennement en semaine.
Le chargement des statistiques peut être long.