Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 35, Issue -, Pages 974-979Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0350974
Keywords
beta-site amyloid precursor protein-cleaving enzyme (BACE); amyloid precursor protein (APP); Golgi-associated gamma-adaptin ear homology domain ADP-ribosylation factor (Arf)-interacting protein-1 (GGA-1); isoprenylation; palmitoylation; subcellular trafficking
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The correct assembly of the BACE (beta-site amyloid precursor protein-cleaving enzyme or beta-secretase) complex and its subsequent trafficking to cellular compartments where it associates with the APP (amyloid precursor protein) is essential for the production of A beta (amyloid beta-pepticle), the protein whose aggregation into senile plaques is thought to be responsible for the pathogenesis of AD (Alzheimer's disease). These processes rely upon both transient and permanent BACE-protein interactions. This review will discuss what is currently known about these BACE-protein interactions and how they may reveal novel therapeutic targets for the treatment of AD.
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