Abstract
Autocatalytic changes in the conformation and aggregation state of prion protein appear to be fundamental to transmissible spongiform encephalopathies or prion diseases. Here we review the considerable progress that has been made in describing the normal properties of prion protein and the changes that occur during these devastating neurodegenerative diseases.
MeSH terms
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Animals
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Dimerization
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Humans
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Macromolecular Substances
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Models, Molecular
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Mutation
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PrPSc Proteins / chemistry
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PrPSc Proteins / genetics
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PrPSc Proteins / metabolism
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Prion Diseases / genetics
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Prion Diseases / metabolism*
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Prions / chemistry*
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Prions / genetics
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Prions / metabolism
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Protein Conformation
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Protein Folding
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Protein Structure, Quaternary
Substances
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Macromolecular Substances
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PrPSc Proteins
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Prions