The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

By I. Benilova, E. Karran, B. de Strooper. Nature Neuroscience, 2012

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Oxidative stress, mitochondrial dysfunction and neurodegenerative diseases; a mechanistic insight. (2015, background): “Oligomers represent the most toxic aggregation stage of Ab, because they promote excitotoxicity by interacting with glutamate receptors, endoplasmic reticulum stress, mitochondrial dysfunction, altered acetyl-cholinergic neurotransmission, inflammation, and oxidative stress [98].”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “In the case of Alzheimer disease, for example, extracellular protein oligomers have been reported to interact with the phospholipid bilayers of the cell membrane, NMDA and AMPA receptors, the metabotropic glutamate receptor 5, the insulin receptor, the nicotinic acetylcholine receptor α7-nAcChR, PrP”
Oxidative stress and mitochondrial dysfunction-linked neurodegenerative disorders (2017, background): “dysfunction lead to cell death and dementia.[30,31] The transition metals, Cu2+, Zn2+, and Fe3+, have been found to be involved in Aβ aggregation and oxidative damage in AD patients.”
Amyloid Precursor Protein (APP)/APP-like Protein 2 (APLP2) Expression Is Required to Initiate Endosome-Nucleus-Autophagosome Trafficking of Glypican-1-derived Heparan Sulfate* (2014, neutral): “Such A assemblies, formed in vitro, can be toxic to cells (2).”