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MeSH Review

Prion Diseases

 
 
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Disease relevance of Prion Diseases

 

Psychiatry related information on Prion Diseases

  • The appearance of a novel human prion disease, variant CJD, and the clear experimental evidence that it is caused by exposure to BSE has highlighted the need to understand the molecular basis of prion propagation, pathogenesis, and the barriers limiting intermammalian transmission [6].
  • Amyloid fibrils are associated with a variety of neurodegenerative maladies including Alzheimer's disease and the prion diseases [7].
  • Why this family with prion disease (PrP-A117V) should present with ataxia instead of dementia, which was found in two previously identified families with the same PrP gene mutation, remains to be established [8].
 

High impact information on Prion Diseases

 

Chemical compound and disease context of Prion Diseases

 

Biological context of Prion Diseases

 

Anatomical context of Prion Diseases

 

Gene context of Prion Diseases

 

Analytical, diagnostic and therapeutic context of Prion Diseases

References

  1. Cell-free formation of protease-resistant prion protein. Kocisko, D.A., Come, J.H., Priola, S.A., Chesebro, B., Raymond, G.J., Lansbury, P.T., Caughey, B. Nature (1994) [Pubmed]
  2. Variant Creutzfeldt-Jakob disease. Collinge, J. Lancet (1999) [Pubmed]
  3. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Come, J.H., Fraser, P.E., Lansbury, P.T. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease. Lecerf, J.M., Shirley, T.L., Zhu, Q., Kazantsev, A., Amersdorfer, P., Housman, D.E., Messer, A., Huston, J.S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  5. Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP. Ghetti, B., Piccardo, P., Spillantini, M.G., Ichimiya, Y., Porro, M., Perini, F., Kitamoto, T., Tateishi, J., Seiler, C., Frangione, B., Bugiani, O., Giaccone, G., Prelli, F., Goedert, M., Dlouhy, S.R., Tagliavini, F. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  6. Prion diseases of humans and animals: their causes and molecular basis. Collinge, J. Annu. Rev. Neurosci. (2001) [Pubmed]
  7. Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Wang, W., Hecht, M.H. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  8. Prion disease (PrP-A117V) presenting with ataxia instead of dementia. Mastrianni, J.A., Curtis, M.T., Oberholtzer, J.C., Da Costa, M.M., DeArmond, S., Prusiner, S.B., Garbern, J.Y. Neurology (1995) [Pubmed]
  9. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Glover, J.R., Kowal, A.S., Schirmer, E.C., Patino, M.M., Liu, J.J., Lindquist, S. Cell (1997) [Pubmed]
  10. A novel erythroid-specific marker of transmissible spongiform encephalopathies. Miele, G., Manson, J., Clinton, M. Nat. Med. (2001) [Pubmed]
  11. Allelic origin of the abnormal prion protein isoform in familial prion diseases. Chen, S.G., Parchi, P., Brown, P., Capellari, S., Zou, W., Cochran, E.J., Vnencak-Jones, C.L., Julien, J., Vital, C., Mikol, J., Lugaresi, E., Autilio-Gambetti, L., Gambetti, P. Nat. Med. (1997) [Pubmed]
  12. PrP-expressing tissue required for transfer of scrapie infectivity from spleen to brain. Blättler, T., Brandner, S., Raeber, A.J., Klein, M.A., Voigtländer, T., Weissmann, C., Aguzzi, A. Nature (1997) [Pubmed]
  13. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond. Soto, C., Saborio, G.P., Anderes, L. Trends Neurosci. (2002) [Pubmed]
  14. New insights into prion structure and toxicity. Harris, D.A., True, H.L. Neuron (2006) [Pubmed]
  15. Quinacrine does not prolong survival in a murine Creutzfeldt-Jakob disease model. Collins, S.J., Lewis, V., Brazier, M., Hill, A.F., Fletcher, A., Masters, C.L. Ann. Neurol. (2002) [Pubmed]
  16. Clinical features of fatal familial insomnia: phenotypic variability in relation to a polymorphism at codon 129 of the prion protein gene. Montagna, P., Cortelli, P., Avoni, P., Tinuper, P., Plazzi, G., Gallassi, R., Portaluppi, F., Julien, J., Vital, C., Delisle, M.B., Gambetti, P., Lugaresi, E. Brain Pathol. (1998) [Pubmed]
  17. Inherited prion disease with an alanine to valine mutation at codon 117 in the prion protein gene. Mallucci, G.R., Campbell, T.A., Dickinson, A., Beck, J., Holt, M., Plant, G., de Pauw, K.W., Hakin, R.N., Clarke, C.E., Howell, S., Davies-Jones, G.A., Lawden, M., Smith, C.M., Ince, P., Ironside, J.W., Bridges, L.R., Dean, A., Weeks, I., Collinge, J. Brain (1999) [Pubmed]
  18. Antibody to DNA detects scrapie but not normal prion protein. Zou, W.Q., Zheng, J., Gray, D.M., Gambetti, P., Chen, S.G. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  19. Prion protein NMR structure and species barrier for prion diseases. Billeter, M., Riek, R., Wider, G., Hornemann, S., Glockshuber, R., Wüthrich, K. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  20. Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties. Cancellotti, E., Wiseman, F., Tuzi, N.L., Baybutt, H., Monaghan, P., Aitchison, L., Simpson, J., Manson, J.C. J. Biol. Chem. (2005) [Pubmed]
  21. Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease. Mastrianni, J.A., Iannicola, C., Myers, R.M., DeArmond, S., Prusiner, S.B. Neurology (1996) [Pubmed]
  22. Studies in aging of the brain: IV. Familial Alzheimer disease: Relation to transmissible dementia, aneuploidy, and microtubular defects. Cook, R.H., Ward, B.E., Austin, J.H. Neurology (1979) [Pubmed]
  23. Prion protein amyloidosis. Ghetti, B., Piccardo, P., Frangione, B., Bugiani, O., Giaccone, G., Young, K., Prelli, F., Farlow, M.R., Dlouhy, S.R., Tagliavini, F. Brain Pathol. (1996) [Pubmed]
  24. Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons. Roucou, X., Guo, Q., Zhang, Y., Goodyer, C.G., LeBlanc, A.C. J. Biol. Chem. (2003) [Pubmed]
  25. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. Leucht, C., Simoneau, S., Rey, C., Vana, K., Rieger, R., Lasmézas, C.I., Weiss, S. EMBO Rep. (2003) [Pubmed]
  26. Sphingosine kinase-dependent migration of immature dendritic cells in response to neurotoxic prion protein fragment. Kaneider, N.C., Kaser, A., Dunzendorfer, S., Tilg, H., Wiedermann, C.J. J. Virol. (2003) [Pubmed]
  27. Expression of excitatory amino acid transporter-1 (EAAT-1) in brain macrophages and microglia of patients with prion diseases. Chrétien, F., Le Pavec, G., Vallat-Decouvelaere, A.V., Delisle, M.B., Uro-Coste, E., Ironside, J.W., Gambetti, P., Parchi, P., Créminon, C., Dormont, D., Mikol, J., Gray, F., Gras, G. J. Neuropathol. Exp. Neurol. (2004) [Pubmed]
  28. Spontaneous mutations in the prion protein gene causing transmissible spongiform encephalopathy. Dagvadorj, A., Petersen, R.B., Lee, H.S., Cervenakova, L., Shatunov, A., Budka, H., Brown, P., Gambetti, P., Goldfarb, L.G. Ann. Neurol. (2002) [Pubmed]
  29. Nonenzymatic glycation at the N terminus of pathogenic prion protein in transmissible spongiform encephalopathies. Choi, Y.G., Kim, J.I., Jeon, Y.C., Park, S.J., Choi, E.K., Rubenstein, R., Kascsak, R.J., Carp, R.I., Kim, Y.S. J. Biol. Chem. (2004) [Pubmed]
  30. APOE in non-Alzheimer amyloidoses: transmissible spongiform encephalopathies. Chapman, J., Cervenáková, L., Petersen, R.B., Lee, H.S., Estupinan, J., Richardson, S., Vnencak-Jones, C.L., Gajdusek, D.C., Korczyn, A.D., Brown, P., Goldfarb, L.G. Neurology (1998) [Pubmed]
  31. Analysis of sequence variability of the bovine prion protein gene (PRNP) in German cattle breeds. Sander, P., Hamann, H., Pfeiffer, I., Wemheuer, W., Brenig, B., Groschup, M.H., Ziegler, U., Distl, O., Leeb, T. Neurogenetics (2004) [Pubmed]
  32. Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies. Ishikawa, K., Doh-ura, K., Kudo, Y., Nishida, N., Murakami-Kubo, I., Ando, Y., Sawada, T., Iwaki, T. J. Gen. Virol. (2004) [Pubmed]
  33. Western blot mapping of disease-specific amyloid in various animal species and humans with transmissible spongiform encephalopathies using a high-yield purification method. Beekes, M., Baldauf, E., Cassens, S., Diringer, H., Keyes, P., Scott, A.C., Wells, G.A., Brown, P., Gibbs, C.J., Gajdusek, D.C. J. Gen. Virol. (1995) [Pubmed]
  34. Phenotypic variability in the brains of a family with a prion disease characterized by a 144-base pair insertion in the prion protein gene. King, A., Doey, L., Rossor, M., Mead, S., Collinge, J., Lantos, P. Neuropathol. Appl. Neurobiol. (2003) [Pubmed]
  35. Use of capillary electrophoresis and fluorescent labeled peptides to detect the abnormal prion protein in the blood of animals that are infected with a transmissible spongiform encephalopathy. Schmerr, M.J., Jenny, A.L., Bulgin, M.S., Miller, J.M., Hamir, A.N., Cutlip, R.C., Goodwin, K.R. Journal of chromatography. A. (1999) [Pubmed]
  36. Novel approaches in diagnosis and therapy of Creutzfeldt-Jakob disease. Müller, W.E., Laplanche, J.L., Ushijima, H., Schröder, H.C. Mech. Ageing Dev. (2000) [Pubmed]
  37. Sequence analysis of the PrP protein from two species of antelope susceptible to transmissible spongiform encephalopathy. Poidinger, M., Kirkwood, J., Almond, W. Arch. Virol. (1993) [Pubmed]
 
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