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

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

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

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

A β-barrel-like tetramer formed by a β-hairpin derived from Aβ

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

Flanking regions, amyloid cores, and polymorphism: the potential

Analyzing Morphological Properties of Early-Stage Toxic Amyloid β Oligomers by Atomic Force Microscopy

A glimpse into the structural properties of α‐synuclein oligomers

Andres Arango

Exploring amyloid oligomers with peptide model systems - ScienceDirect

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

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

Andres Arango