Common mechanisms of amyloid oligomer pathogenesis in degenerative disease

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity

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Amyloid pores from pathogenic mutations

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Amyloid β-Protein Fibrillogenesis

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Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦

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Permeabilization of Lipid Bilayers Is a Common Conformation-dependent Activity of Soluble Amyloid Oligomers in Protein Misfolding Diseases

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X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS

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Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

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The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

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X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

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Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro.

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Pore Formation by the Cytotoxic Islet Amyloid Peptide Amylin

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Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register

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Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils

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Amyloid peptides are toxic via a common oxidative mechanism.

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Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling

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Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity

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Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance

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Protofibrillar Islet Amyloid Polypeptide Permeabilizes Synthetic Vesicles by a Pore-like Mechanism that May Be Relevant to Type II Diabetes

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Tau Paired Helical Filaments from Alzheimer's Disease Brain and Assembled in Vitro Are Based on β-Structure in the Core Domain

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Soluble Amyloid Aβ-(1–40) Exists as a Stable Dimer at Low Concentrations

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Hyperactivation of Signal Transduction Systems in Alzheimer's Diseasea

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Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

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The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy

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