Prion protein interconversions and the transmissible spongiform encephalopathies

Structure. 1999 Oct 15;7(10):R231-40. doi: 10.1016/s0969-2126(00)80049-0.

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Dimerization
  • Humans
  • Macromolecular Substances
  • Models, Molecular
  • Mutation
  • PrPSc Proteins / chemistry
  • PrPSc Proteins / genetics
  • PrPSc Proteins / metabolism
  • Prion Diseases / genetics
  • Prion Diseases / metabolism*
  • Prions / chemistry*
  • Prions / genetics
  • Prions / metabolism
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Quaternary

Substances

  • Macromolecular Substances
  • PrPSc Proteins
  • Prions