论文部分内容阅读
Misfolding, aggregation and formation of intracellular inclusions of SOD1, is a hallmark of ALS,and we have shown that in-vitro, SOD1 aggregation is driven by recruitment of globally unfolded protein.Consequently, large efforts have been focused on studies of early misfolding events in-vitro.From a molecular perspective extrapolation of in-vitro data to cellular conditions is questionable.To circumvent this problem, our strategy is direct analysis of the misfolding mechanism at atomistic resolution in living human cells.We deliver isotope labelled SOD1 into human cells to directly measure the effect on protein stability.