Bibliografia:

 

  1. Prusiner S.B., "The Prion Diseases", Scientific American, January 1995
  2. Cohen F.E., Pan K.M., Huang Z., Baldwin M., Fletterick R.J., Prusiner S.B., "Structural clues to prion replication", Science (1994) 264, 530-531
  3. Come J.H., Fraser P.E., Lansbury P.T., "A kinetic model for amyloid formation in the prion diseases: importance of seeding", Proc. Natl. Acad. Sci. USA (1993) 90, 5959-5963
  4. Cantor C.R., Schimmel P.R., "BIOPHYSICAL CHEMISTRY II, Techniques for the study of biological structure and function", W.H. Freeman – San Francisco, 409-433
  5. Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R.J., Cohen F.E., Prusiner S.B., "Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins", Biochemistry (1993) 90, 10962-10966
  6. Inouye H., Kirschner D.A., "X-ray diffraction analysis of scrapie prion: intermediate and folded structure in a peptide containing two putative a-helices", J. Mol. Biol. (1997) 268, 375-389
  7. Safar J., Roller P.P., Gajdusek D.C., Gibbs C.J., "Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein, J. Biol. Chem. (1993) 268, 20276-20284
  8. Zhang S., Rich A., "Direct conversion of an oligopeptide from a b-sheet to an a-helix: a model for amyloid formation", Proc. Natl. Acad. Sci. USA (1997) 94, 23-28
  9. Hornemann S., Glockshuber R., "Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein", J. Mol. Biol. (1996) 262, 614-619
  10. Hornemann S., Glockshuber R., "A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH", Proc. Natl. Acad. Sci. USA (1998) 95, 6010-6014
  11. Wildegger G., Liemann S., Glockshuber R., "Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates", Nature Structural Biology (1999) 6, 550-553
  12. Jobling M.F., Stewart L.R., White A.R., McLean C., Friedhuber A., Mather F., Beyreuther K., Masters C.L., Barrow C.J., Collins S.J., Cappai R., "The hydrophobic core sequence modulates the neurotoxic and secondary structure properties of the prion peptide 106-126", J. Neurochem. (1999) 73, 1557-1565
  13. Prince R.C., Gunson D.E., "Prions are copper-binding proteins" Trends Biochem. Sci. (1998) 23, 197-198
  14. "Structure of the prion repeat region", URL:http://www.mad-cow.org/~tom/prion_proline.html
  15. Stockel J., Safar J., Wallace A.C., Cohen F.E., Prusiner S.B., "Prion protein selectively binds copper(II) ions", Biochemistry (1998) 37, 7185-7193

 

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