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Science 10 October 1997:
Vol. 278. no. 5336, pp. 245 - 251
DOI: 10.1126/science.278.5336.245
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Articles

Note: Due to the interest in this article, Science is offering its readers free access to the full text

Prion Diseases and the BSE Crisis

Stanley B. Prusiner

Bovine spongiform encephalopathy (BSE) and human Creutzfeldt-Jakob disease (CJD) are among the most notable central nervous system degenerative disorders caused by prions. CJD may present as a sporadic, genetic, or infectious illness. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrPSc). The normal, cellular prion protein (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high beta -sheet content. It is thought that BSE is a result of cannibalism in which faulty industrial practices produced prion-contaminated feed for cattle. There is now considerable concern that bovine prions may have been passed to humans, resulting in a new form of CJD.

Department of Neurology (address for correspondence) and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.

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   Abstract »    Full Text »    PDF »
Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible.
D. G. Donne, J. H. Viles, D. Groth, I. Mehlhorn, T. L. James, F. E. Cohen, S. B. Prusiner, P. E. Wright, and H. J. Dyson (1997)
PNAS 94, 13452-13457
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Folding of Prion Protein to Its Native alpha -Helical Conformation Is under Kinetic Control.
I. V. Baskakov, G. Legname, S. B. Prusiner, and F. E. Cohen (2001)
J. Biol. Chem. 276, 19687-19690
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pH-dependent Prion Protein Conformation in Classical Creutzfeldt-Jakob Disease.
G. Zanusso, A. Farinazzo, M. Fiorini, M. Gelati, A. Castagna, P. G. Righetti, N. Rizzuto, and S. Monaco (2001)
J. Biol. Chem. 276, 40377-40380
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A Monomer-Dimer Equilibrium of a Cellular Prion Protein (PrPC) Not Observed with Recombinant PrP.
R. K. Meyer, A. Lustig, B. Oesch, R. Fatzer, A. Zurbriggen, and M. Vandevelde (2000)
J. Biol. Chem. 275, 38081-38087
   Abstract »    Full Text »    PDF »
Prion protein: Evolution caught en route.
P. Tompa, G. E. Tusnady, M. Cserzo, and I. Simon (2001)
PNAS 98, 4431-4436
   Abstract »    Full Text »    PDF »
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro.
M. Ramirez-Alvarado, J. S. Merkel, and L. Regan (2000)
PNAS 97, 8979-8984
   Abstract »    Full Text »    PDF »


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