Chunjiang Yu

TL;DR: This chapter outlines protocols that produce homogenous preparations of oligomeric and fibrillar amyloid-β peptide (Aβ), developed and characterized by using atomic force microscopy (AFM) to identify the structurally discrete species formed by Aβ42 under specific solution conditions.

TL;DR: APOE differentially regulates multiple aspects of Aβ accumulation, and its effects on plaque morphology, intraneuronal Aβ, soluble Aβ42, and oligomeric Aβ (oAβ) are determined using new EFAD transgenic mice.

TL;DR: It is demonstrated that APOE4 predisposes to inflammation, which could contribute to its association with Alzheimer's disease and other disorders, as measured by three markers: PSD‐95, drebin, and synaptophysin.

TL;DR: While multiple forms of Aβ have cognition impairing activity, there are significant differences in effective concentration and potency.

TL;DR: Evidence is provided that apoE/Aβ levels isoform-specifically modulate soluble oAβ clearance, suggesting a basis for APOE4-induced AD risk and a mechanistic approach to AD biomarkers.