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

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

Structural details of amyloid β oligomers in complex with human

Carulla Laβ (@carullalab) / X

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

Andres Arango

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

Architecture of the Aβ(1-42) tetramer a Amide resonance assignments of

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

알츠하이머병 - AD 뇌의 신경세포 막에서 Aβ가 만드는 pore로 인해 neurotoxicity가 유도 됨. Reference: Aβ( 1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage (Nature Communications, 2020).

Aβ-Peptide Production and Conformational Behavior

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