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

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

Structural details of amyloid β oligomers in complex with human

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

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

Molecules, Free Full-Text

A β-barrel-like tetramer formed by a β-hairpin derived from Aβ - Chemical Science (RSC Publishing) DOI:10.1039/D3SC05185D

Aβ-Peptide Production and Conformational Behavior

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

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

Pharmaceutics, Free Full-Text

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