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

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

Single-molecule Mapping of Amyloid-β Oligomer Insertion into Lipid

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

Single-molecule Mapping of Amyloid-β Oligomer Insertion into Lipid

Eduard Puig, Ph.D. - Freelance

Frontiers Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer's disease

Frontiers On the Role of Platelet-Generated Amyloid Beta Peptides in Certain Amyloidosis Health Complications

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

The structure of tyrosine-10 favors ionic conductance of

Transmembrane Structures for Alzheimer's Aβ1−42 Oligomers

3D structure of the Aβ(1-42) tetramer prepared in DPC a Ribbon diagram

Atomic Structure of Aβ Protein Assemblies Revealed

Frontiers High Speed AFM and NanoInfrared Spectroscopy