The structure of prion: is it enough for interpreting the diverse phenotypes of prion diseases?

Acta Biochim Biophys Sin (Shanghai). 2013 Jun;45(6):429-34. doi: 10.1093/abbs/gmt021. Epub 2013 Mar 3.

Abstract

Prion diseases, or transmissible spongiform encephalopathies, are neurodegenerative diseases, which affect human and many species of animals with 100% fatality rate. The most accepted etiology for prion disease is 'prion', which arises from the conversion from cellular PrP(C) to the pathological PrP(Sc). This review discussed the characteristic structure of PrP, including PRNP gene, PrP(C), PrP(Sc), PrP amyloid, and prion strains.

Keywords: PrP; PrP structure; PrPC; prion disease.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyloid / chemistry
  • Animals
  • Humans
  • Prion Diseases / classification*
  • Prions / chemistry*
  • Prions / genetics
  • Protein Conformation

Substances

  • Amyloid
  • Prions