1. Volume 5, Issue 5, Pages 595-600 (May 1997)
Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases 
Jeffery W Kelly 
Structure 
Volume 5, Issue 5, Pages (May 1997)
DOI: /S (97)

2. Figure 1
Outline of the role that conformational changes play in the conversion of a normally soluble and functional protein into amyloid. Amyloidogenic proteins appear to adopt alternative conformations which have common structural features.
Structure 1997 5, DOI: ( /S (97) )

3. Figure 2
The pH-dependent denaturation/amyloid fibril formation pathway exhibited by transthyretin (TTR).
Structure 1997 5, DOI: ( /S (97) )

4. Figure 3
Ligand binding stabilizes the normal fold of the amyloidogenic protein transthyretin (TTR), thus preventing the formation of the alternative conformation which leads to amyloid fibril formation.
Structure 1997 5, DOI: ( /S (97) )