Role of Aromatic Side Chains in Amyloid β-Protein Aggregation

Documenti analoghi

• Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
  di: Hellstrand, Erik, et al.
  Pubblicazione: (2009)
• On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations
  di: Yang, Xiaoting, et al.
  Pubblicazione: (2018)
• Distinct thermodynamic signature of oligomer generation in the aggregation of the amyloid-β peptide
  di: Cohen, Samuel I. A., et al.
  Pubblicazione: (2018)
• Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils
  di: Törnquist, Mattias, et al.
  Pubblicazione: (2020)
• Mutations that replace aromatic side chains promote aggregation of the Alzheimer’s Aβ peptide
  di: Armstrong, Anne H., et al.
  Pubblicazione: (2011)