J. Knops

TL;DR: A membrane-bound enzyme activity that cleaves full-length APP at the β-secretase cleavage site is described and found to be the predominant β-cleavage activity in human brain, and it is found that human brain β- secretase is a new membrane- bound aspartic proteinase.

TL;DR: Immunolabeling of the tau-expressing Sf9 cells demonstrated tau reactivity in the induced processes, and EM that microtubule bundles were present in the processes, since taxol treatment did not alter the overall cell shape, despite the induction of microtubules bundling within the cell body.

TL;DR: Intacellular acidic processes are rate-limiting for β-secretase cleavage and Aβ production from SW APP, but not WT APP, in the peripheral 293 cell line, indicating that such acidic processes also play a rate- Limiting role in Aβ release from human central nervous system-derived cells, including HMBC.

TL;DR: The development of statine-based peptidomimetic inhibitors of human β-secretase (BACE) and the identification of the cell-permeable BACE inhibitor 38 that demonstrated BACE-mechanism-selective inhibition of Aβ secretion in human embryonic kidney cells are described.

TL;DR: Densitometric analyses suggest that this non-secretory pathway of APP degradation, mediated by cysteine proteases in an intracellular acidic compartment, accounts for approximately 70% of total APP metabolism and that a key processing intermediate in this pathway is a 22-kDa, beta-peptide-containing APP carboxyl-terminal fragment.