Aβ(1-42) tetramer and octamer structures reveal edge conductivity
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Atomic Structure of Alzheimer's Amyloid Protein Reveals New Toxicity Mechanism
A β-barrel-like tetramer formed by a β-hairpin derived from Aβ
PDF] Alzheimer´s Disease-associated Aβ42 Peptide: Expression and Purification for NMR Structural Studies
Computational Structural Biology and Molecular Biophysics
The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide aggregation in membrane-mimetic environments. - Abstract - Europe PMC
Frontiers Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer's disease
Structural architecture of amyloid-β oligomers, curvilinear protofibrils and annular assemblies, imaged by cryo-EM and cryo-ET
PDF] Alzheimer´s Disease-associated Aβ42 Peptide: Expression and Purification for NMR Structural Studies
Amentoflavone: A Bifunctional Metal Chelator that Controls the
Atomic Structure of Alzheimer's Amyloid Protein Reveals New Toxicity Mechanism
A common pathway for detergent-assisted oligomerization of Aβ42
Andres Arango
The structure of tyrosine-10 favors ionic conductance of
A β-barrel-like tetramer formed by a β-hairpin derived from Aβ - Chemical Science (RSC Publishing) DOI:10.1039/D3SC05185D
Architecture of the Aβ(1-42) tetramer a Amide resonance assignments of
42-year woman with palpable left breast lump. (A) Standard mammogram
First Look: The Fortis N-42 Novonaut, The Return of a Space Classic
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