Molecular Modeling of Two Distinct Triangular Oligomers in Amyloid β-protein

This publication has 49 references indexed in Scilit:

• A Kinetic Model for β-Amyloid Adsorption at the Air/Solution Interface and Its Implication to the β-Amyloid Aggregation Process
  The Journal of Physical Chemistry B, 2009
• Atomic structures of peptide self-assembly mimics
  Proceedings of the National Academy of Sciences, 2006
• Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
  Science, 2005
• Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
  Nature Neuroscience, 2004
• Annular Oligomeric Amyloid Intermediates Observed by in Situ Atomic Force Microscopy
  Journal of Biological Chemistry, 2004
• Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
  Science, 2003
• Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
  Nature, 2002
• Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology
  The FASEB Journal, 2001
• Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular beta-amyloid or A4 peptides.
  Proceedings of the National Academy of Sciences, 1993
• Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide.
  Proceedings of the National Academy of Sciences, 1993