Folding proteins in fatal ways

  title={Folding proteins in fatal ways},
  author={Dennis J. Selkoe},
  • D. Selkoe
  • Published 18 December 2003
  • Biology
  • Nature
Human diseases characterized by insoluble extracellular deposits of proteins have been recognized for almost two centuries. Such amyloidoses were once thought to represent arcane secondary phenomena of questionable pathogenic significance. But it is has now become clear that many different proteins can misfold and form extracellular or intracellular aggregates that initiate profound cellular dysfunction. Particularly challenging examples of such disorders occur in the post-mitotic environment… 

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