Aβ(1-42) tetramer and octamer structures reveal edge conductivity
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Structure of AqpZ tetramer and location of mutations. The
The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide
Frontiers Binding mechanism of full-length Aβ40 peptide to a mixed lipid bilayer
Eduard PUIG GOMÀ-CAMPS, Postdoctoral Associate
PDF) Aβ(1-42) tetramer and octamer structures reveal edge pores as a mechanism for membrane damage
Amyloid-Beta's Atomic Structure Reveals Alzheimer's Disease Toxicity Mechanism
Amphiphilic stilbene derivatives attenuate the neurotoxicity of soluble Aβ 42 oligomers by controlling their interactions with cell membranes - Chemical Science (RSC Publishing) DOI:10.1039/D2SC02654F
Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization - Journal of Biological Chemistry
A β-barrel-like tetramer formed by a β-hairpin derived from Aβ - Chemical Science (RSC Publishing) DOI:10.1039/D3SC05185D
A β-barrel-like tetramer formed by a β-hairpin derived from Aβ - Chemical Science (RSC Publishing) DOI:10.1039/D3SC05185D
Exploring amyloid oligomers with peptide model systems - ScienceDirect
Structure of amyloid β25–35 in lipid environment and cholesterol-dependent membrane pore formation
RCSB PDB - 6RHY: Structure of pore-forming amyloid-beta tetramers
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