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Each lifecycle of the Hepatitis C virus (HCV) produces structural and non-structural (NS) proteins in equimolar. Structural proteins were either assembled or degraded by host proteolysis systems, while NS proteins remain inside the host cells and don’t accumulate. Therefore, they must be degraded. Here, NS3 and NS5A half-lives were quantified in the presence of autolysosome and proteasome different modulators. Inhibitors of both systems increased the half-life, while inducers decreased the half-life. Furthermore, polyubiquitination of NS3 and NS5A was observed. Additionally, their intracellular co-localization with autolysosome (LAMP2) and proteasome (PSMB5) was observed, and inhibitors of both systems increased the degree of co-localization. A better understanding of NS protein degradation might help to improve medical interventions during HCV infections in the future.
The main purpose of Points is to give an insight into SAFE's two principal fields of activity – conducting research in finance and providing policy advice – and to introduce you to the people behind these two pillars of the institute. For both pillars, it is essential to point out the problems and phenomena the researchers at SAFE deal with and to have a point and state it clearly.
As such, Points also serves to keep readers informed about new perspectives as they open up in the development of SAFE. Initially, the magazine will be published once a year free of charge and advertising and is intended as a complementary product to SAFE's digital newsletter, which is currently published six times a year.