Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases

Structure. 1997 May 15;5(5):595-600. doi: 10.1016/s0969-2126(97)00215-3.

Abstract

The assembly and misassembly of normally soluble proteins into fibrilar structures is thought to be a causative agent in a variety of human amyloid and prion diseases. Structural and mechanistic studies of this process are beginning to elucidate the conformational changes required for the conversion of a normally soluble and functional protein into a defined quaternary structure.

Publication types

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

MeSH terms

  • Amyloid / chemistry*
  • Amyloidosis / etiology*
  • Humans
  • Models, Chemical
  • Prealbumin / chemistry*
  • Prion Diseases / etiology*
  • Protein Conformation
  • Protein Denaturation
  • Protein Folding

Substances

  • Amyloid
  • Prealbumin