Fibrillization of 40-residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms

Podobne zapisy

• Fibrillization of 40-Residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms
  od: Qinghui Cheng, i wsp.
  Wydane: (2020-06-01)
• The on-fibrillation-pathway membrane content leakage and off-fibrillation-pathway lipid mixing induced by 40-residue β-amyloid peptides in biologically relevant model liposomes
  od: Cheng, Qinghui, i wsp.
  Wydane: (2018)
• Polymorphic Fibril Formation by Residues 10–40 of the Alzheimer's β-Amyloid Peptide
  od: Paravastu, Anant K., i wsp.
  Wydane: (2006)
• Distinct Membrane Disruption Pathways Are Induced by 40-Residue β-Amyloid Peptides
  od: Delgado, Dennis A., i wsp.
  Wydane: (2016)
• Phosphorylation at Ser(8) as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) Fibrils
  od: Hu, Zhi-Wen, i wsp.
  Wydane: (2017)