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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

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

Uptake of Aβ by OATPs might be a new pathophysiological mechanism of Alzheimer disease, BMC Neuroscience

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

In vivo synaptic activity-independent co-uptakes of amyloid β1–42 and Zn2+ into dentate granule cells in the normal brain

A delay in vesicle endocytosis by a C-terminal fragment of N-cadherin enhances Aβ synaptotoxicity

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

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Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1–42 aggregates - Zhaliazka - 2023 - The FEBS Journal - Wiley Online Library

Physiological Roles of Monomeric Amyloid-β and Implications for Alzheimer's Disease Therapeutics