Faculty Opinions recommendation of Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers.

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Neuronal calcium signaling: function and dysfunction (2014, background): “the cellular prion protein that may function as the receptor [175], may enhance Ca2+ entry through the ROC (e.”
An Overview of APP Processing Enzymes and Products (2010, neutral): “One interesting interaction that has been reported recently is between Aβ and cellular prion protein (PrP) (Lauren et al., 2009).”
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Subsequent studies showed that oAβ, especially high-molecular weight oligomers [88], preferentially bind to PrPC within an N-terminal 95-111aa segment [87].”
Extracellular Vesicles: Unique Intercellular Delivery Vehicles. (2017, background): “However, a protective function of EVs in Alzheimer’s disease has also been reported, as PrPC, present on the surface of EVs serves as a receptor for toxic Abeta42 peptide [134] and can thus sequester β-amyloid assemblies in vivo [135].”
The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy (2016, background): “These oligomers were also shown to bind to the PrPc and lead to a series of events disrupting synaptic function in hippocampal neurons (Freir et al., 2011; Lauren et al., 2009; Um et al., 2012).”