Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)

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Amyloid-beta peptides 40 and 42 employ distinct molecular pathways for cell entry and intracellular transit at the BBB endothelium

The amyloid-β degradation intermediate Aβ34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer's disease, Acta Neuropathologica Communications

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Uptake of Aβ(1-40), Aβ(1-42) and Trf in SH-SY5Y cells under conditions

The amyloid-β degradation intermediate Aβ34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer's disease, Acta Neuropathologica Communications

Alzheimer's disease linked Aβ42 exerts product feedback inhibition on γ-secretase impairing downstream cell signaling

Shared cerebral metabolic pathology in non-transgenic animal models of Alzheimer's and Parkinson's disease

Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42) - ScienceDirect

Designed Cell-Penetrating Peptide Inhibitors of Amyloid-beta Aggregation and Cytotoxicity - ScienceDirect

Towards the integrative theory of Alzheimer's disease: linking molecular mechanisms of neurotoxicity, beta-amyloid biomarkers, and the diagnosis

Intracellular tracing of amyloid vaccines through direct fluorescent labelling

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Pathways of clathrin-independent endocytosis