Accès gratuit
Numéro
Med Sci (Paris)
Volume 23, Numéro 12, Décembre 2007
Page(s) 1148 - 1158
Section M/S revues
DOI https://doi.org/10.1051/medsci/200723121148
Publié en ligne 15 décembre 2007
  1. Prusiner SB, Scott MR, Dearmond SJ, Cohen FE. Prion protein biology. Cell 1998; 93 : 337–48.
  2. Caughey B, Race RE, Chesebro B. Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines. J Gen Virol 1988; 69 : 711–6.
  3. Meyer RK, McKinley MP, Bowman KA, et al. Separation and properties of cellular and scrapie prion proteins. Proc Natl Acad Sci USA 1986; 83 : 2310–4.
  4. Aguzzi A, Haass C. Games played by rogue proteins in prion disorders and Alzheimer’s disease. Science 2003; 302 : 814–8.
  5. Cuille J, Chelle P. La maladie dite tremblante du mouton est-elle inoculable ? CR Acad Sci Paris 1936; 1552–4.
  6. Andreoletti O, Lacroux C, Chabert A, et al. PrP(Sc) accumulation in placentas of ewes exposed to natural scrapie: influence of fetal PrP genotype and effect on ewe-to-lamb transmission. J Gen Virol 2002; 83 : 2607–16.
  7. Goldmann W, Hunter N, Smith G, et al. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J Gen Virol 1994; 75 : 989–95.
  8. Wilesmith JW. An epidemiologist’s view of bovine spongiform encephalopathy. Philos Trans R Soc Lond B Biol Sci 1994; 343 : 357–61.
  9. Biacabe AG, Laplanche JL, Ryder S, Baron T. Distinct molecular phenotypes in bovine prion diseases. EMBO Rep 2004; 5 : 110–5.
  10. Pearson GR, Gruffydd-Jones TJ, Wyatt JM, et al. Feline spongiform encephalopathy. Vet Rec 1991; 128 : 532.
  11. Baron T, Belli P, Madec JY, et al. Spongiform encephalopathy in an imported cheetah in France. Vet Rec 1997; 141 : 270–1.
  12. Lezmi S, Martin S, Simon S, et al. Comparative molecular analysis of the abnormal prion protein in field scrapie cases and experimental bovine spongiform encephalopathy in sheep by use of Western blotting and immunohistochemical methods. J Virol 2004; 78 : 3654–62.
  13. Baron TG, Biacabe AG. Molecular analysis of the abnormal prion protein during coinfection of mice by bovine spongiform encephalopathy and a scrapie agent. J Virol 2001; 75 : 107–14.
  14. Eloit M, Adjou K, Coulpier M, et al. BSE agent signatures in a goat. Vet Rec 2005; 156 : 523–4.
  15. Buschmann A, Biacabe AG, Ziegler U, et al. Atypical scrapie cases in Germany and France are identified by discrepant reaction patterns in BSE rapid tests. J Virol Methods 2004; 117 : 27–36.
  16. Miller MW, Williams ES. Chronic wasting disease of cervids. Curr Top Microbiol Immunol 2004; 284 : 193–214.
  17. Kong Q, Huang S, Zou W, et al. Chronic wasting disease of elk: transmissibility to humans examined by transgenic mouse models. J Neurosci 2005; 25 : 7944–9.
  18. Creutzfeldt H. Über eine eigenartige herdförmige Erkrankung des Zentralnervensystems. Zeitschrift für die Gesamte Neurologie und Psychiatrie 1920; 57 : 1–18.
  19. Jakob A. Über eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswerten anatomischen Befunde (spastische Pseudosklerose-Encephalomyelopathie mit disseminierten Degenerationsherden). Deutsche Zeitschrift für Nervenheilkunde 1921; 70 : 132–46.
  20. Parchi P, Gambetti P. Human prion diseases. Curr Opin Neurol 1995; 8 : 286–93.
  21. Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 1996; 347 : 921–5.
  22. Ghani AC, Donnelly CA, Ferguson NM, Anderson RM. Updated projections of future vCJD deaths in the UK. BMC Infect Dis 2003; 3 : 4.
  23. Hilton DA, Ghani AC, Conyers L, et al. Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J Pathol 2004; 203 : 733–9.
  24. Ironside JW. Variant Creutzfeldt-Jakob disease: risk of transmission by blood transfusion and blood therapies. Haemophilia 2006; 12 (suppl 1) : 8–15.
  25. Ironside JW, Bishop MT, Connolly K, et al. Variant Creutzfeldt-Jakob disease: prion protein genotype analysis of positive appendix tissue samples from a retrospective prevalence study. Br Med J 2006; 332 : 1186–8.
  26. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216 : 136–44.
  27. Lasmezas CI, Deslys JP, Robain O, et al. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 1997; 275 : 402–5.
  28. Manson JC, Jamieson E, Baybutt H, et al. A single amino acid alteration (101L) introduced into murine PrP dramatically alters incubation time of transmissible spongiform encephalopathy. EMBO J 1999; 18 : 6855–64.
  29. Hsiao KK, Groth D, Scott M, et al. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc Natl Acad Sci USA 1994; 91 : 9126–30.
  30. Legname G, Baskakov IV, Nguyen HO, et al. Synthetic mammalian prions. Science 2004; 305 : 673–6.
  31. Castilla J, Saa P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell 2005; 121 : 195–206.
  32. Manuelidis L. A 25 nm virion is the likely cause of transmissible spongiform encephalopathies. J Cell Biochem 2007; 100 : 897–915.
  33. Manuelidis L. Dementias, neurodegeneration, and viral mechanisms of disease from the perspective of human transmissible encephalopathies. Ann NY Acad Sci 1994; 724 : 259–81.
  34. Leblanc P, Alais S, Porto-Carreiro I, et al. Retrovirus infection strongly enhances scrapie infectivity release in cell culture. EMBO J 2006; 25 : 2674–85.
  35. Wickner RB, Edskes HK, Maddelein ML, et al. Prions of yeast and fungi. Proteins as genetic material. J Biol Chem 1999; 274 : 555–8.
  36. Tuite MF, Cox BS. Propagation of yeast prions. Nat Rev Mol Cell Biol 2003; 4 : 878–90.
  37. Bueler H, Fischer M, Lang Y, et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992; 356 : 577–82.
  38. Mouillet-Richard S, Ermonval M, Chebassier C, et al. Signal transduction through prion protein. Science 2000; 289 : 1925–8.
  39. Lehmann S. Metal ions and prion diseases. Curr Opin Chem Biol 2002; 6 : 187–92.
  40. Chen S, Mange A, Dong L, Schachner M. Different signal transduction pathways are involved in neurite outgrowth and neuronal survival mediated by the prion protein. Mol Cell Neurosci 2003; 2 : 227–33.
  41. Simoneau S, Haik S, Leucht C, et al. Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP. Biol Chem 2003; 384 : 243–6.
  42. Cazaubon S, Viegas P, Couraud PO. Fonctions de la protéine prion PrPc.Med Sci (Paris) 2007; 23 : 741–5.
  43. Steele AD, Emsley JG, Ozdinler PH, et al. Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc Natl Acad Sci USA 2006; 103 : 3416–21.
  44. Zhang CC, Steele AD, Lindquist S, Lodish HF. Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proc Natl Acad Sci USA 2006; 103 : 2184–9.
  45. Zerr I, Bodemer M, Weber T. The 14-3-3 brain protein and transmissible spongiform encephalopathy. N Engl J Med 1997; 336 : 875.
  46. Brown P. Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy. Vox Sang 2005; 89 : 63–70.
  47. Brown P. Drug therapy in human and experimental transmissible spongiform encephalopathy. Neurology 2002; 58 : 1720–5.
  48. Todd NV, Morrow J, Doh-Ura K, et al. Cerebroventricular infusion of pentosan polysulphate in human variant Creutzfeldt-Jakob disease. J Infect 2005; 50 : 394–6.
  49. Aguzzi A, Glatzel M, Montrasio F, et al. Interventional strategies against prion diseases. Nat Rev Neurosci 2001; 2 : 745–9.
  50. Mallucci G, Dickinson A, Linehan J, et al. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. Science 2003; 302 : 871–4.
  51. Crozet C, Lin YL, Mettling C, et al. Inhibition of PrPSc formation by lentiviral gene transfer of PrP containing dominant negative mutations. J Cell Sci 2004; 117 : 5591–7.
  52. Fernandez-Bellot E, Guillemet E, Ness F, et al. The URE3 phenotype: evidence for a soluble prion in yeast. EMBO Rep 2002; 3 : 76–81.
  53. Saupe SJ, Clave C Begueret J. Vegetative incompatibility in filamentous fungi: Podospora and Neurospora provide some clues. Curr Opin Microbiol 2000; 3 : 608–12.
  54. Si K, Lindquist S, Kandel ER. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003; 115 : 879–91.
  55. Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005; 6 : 435–50.
  56. Cazaubon S, Viegas P, Couraud PO. Fonctions de la protéine prion PRPC. Med Sci (Paris) 2007; 23 : 741–5.
  57. Bousset L, Melki R. Protéines prions : propriétés de repliement et d’agrégation. Med Sci (Paris) 2005; 21 : 634–40.
  58. Madly B, Chrétien F. La structure de la protéine prion et la relation avec son infectiosité. Med Sci (Paris) 2005; 21 : 806–7.
  59. Février B, Laude H, Raposo G, Vilette D. Les exosomes : des convoyeurs de prions ? Med Sci (Paris) 2005; 21 : 132–3.
  60. Goggin K, Roucou X. La protéine prion ne se fait pas prier pour faire des agrégats moléculaires. Med Sci (Paris) 2006; 22 : 1013–4.

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.