Jun Zhao

TL;DR: Transgenic mice that express high levels of human mutant APP support a primary role for APP/Aβ in the genesis of AD and could provide a preclinical model for testing therapeutic drugs.

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: In this article, the β-amyloid precursor protein (βAPP) is monitored by detecting the secretion of a soluble amino-terminal fragment or βAPP (ATF-βAPP).

TL;DR: Strong in vivo evidence is provided that the major source of Aβ in brain is from neurons and not from astrocytes, and the β-secretase cleavage necessary for generation of β-s-APP and Aβ is efficiently performed in neurons.

TL;DR: In this article, a transgene encoding an APP polypeptide comprising the Swedish mutation was proposed. But it was not suitable for transgenic non-human animals and transgenic mammalian cells.