Zhuohua Zhang

TL;DR: It is shown that presenilin-1 forms a complex with β-catenin in vivo that increases β-Catenin stability, which increases neuronal vulnerability to apoptosis induced by amyloid-β protein.

TL;DR: It is shown both in vitro and in vivo that nitrosative stress leads to S-nitrosylation of wild-type parkin and, initially, to a dramatic increase followed by a decrease in the E3 ligase-ubiquitin-proteasome degradative pathway, which may provide a molecular link between free radical toxicity and protein accumulation in sporadic Parkinson's disease.

TL;DR: Presenilins are required for γ -secretase cleavage of β -APP and transmembrane cleaving of Notch-1 and trans Membrane Cleavage of NotCh-1.

TL;DR: It is shown that phosphorylated β-catenin is specifically recognized by β-Trcp, an F-box/WD40-repeat protein that also associates with Skp1, an essential component of the ubiquitination apparatus, thus providing a molecular explanation for why these mutations cause β- catenin accumulation that leads to cancer.

TL;DR: It is shown that Parkin, PINK1, and DJ-1 formed a complex to promote ubiquitination and degradation of Parkin substrates, including Parkin itself and Synphilin-1 in neuroblastoma cells and human brain lysates and suggests that their PD-pathogenic mutations impair E3 ligase activity of the complex, which may constitute a mechanism underlying PD pathogenesis.