Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant

Eitemau Tebyg

• Probing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide.
  gan: Massi, F, et al.
  Cyhoeddwyd: (2001)
• Association Thermodynamics and Conformational Stability of β-Sheet Amyloid β(17-42) Oligomers: Effects of E22Q (Dutch) Mutation and Charge Neutralization
  gan: Blinov, Nikolay, et al.
  Cyhoeddwyd: (2010)
• Aqueous urea solution destabilizes Aβ(16–22) oligomers
  gan: Klimov, D. K., et al.
  Cyhoeddwyd: (2004)
• Kinetic theory of fibrillogenesis of amyloid β-protein
  gan: Lomakin, Aleksey, et al.
  Cyhoeddwyd: (1997)
• Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15–28 fragment of the Alzheimer amyloid-β protein
  gan: Baumketner, Andrij, et al.
  Cyhoeddwyd: (2008)