Aβ(1-42) tetramer and octamer structures reveal edge conductivity

Eduard PUIG GOMÀ-CAMPS, Postdoctoral Associate

PDF) Aβ(1-42) tetramer and octamer structures reveal edge pores as a mechanism for membrane damage

Molecules, Free Full-Text

Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization - ScienceDirect

PDF] Alzheimer´s Disease-associated Aβ42 Peptide: Expression and Purification for NMR Structural Studies

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Frontiers Binding mechanism of full-length Aβ40 peptide to a mixed lipid bilayer

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RCSB PDB - 6RHY: Structure of pore-forming amyloid-beta tetramers

Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization - ScienceDirect

Frontiers High Speed AFM and NanoInfrared Spectroscopy

Atomic Structure of Alzheimer's Amyloid Protein Reveals New Toxicity Mechanism

Why are the root causes of amyloid-associated diseases so misunderstood and treatments so inadequate?