Samuel W Ness

Learn More
We describe the isolation and detailed structural characterization of stable toxic oligomers of α-synuclein that have accumulated during the process of amyloid formation. Our approach has allowed us to identify distinct subgroups of oligomers and to probe their molecular architectures by using cryo-electron microscopy (cryoEM) image reconstruction(More)
The formation of reactive oxygen species (ROS) is linked to the pathogenesis of neurodegenerative diseases. Here we have investigated the effect of soluble and aggregated amyloid-β (Aβ) and α-synuclein (αS), associated with Alzheimer's and Parkinson's diseases, respectively, on the Cu(2+)-catalyzed formation of ROS in vitro in the presence of a biological(More)
The C11A mutant of SV40 large T antigen is unable to support the replication of viral origin containing DNA (ori-DNA) in vivo or in vitro. The mutation within C11A at residue 522 (pro-->ser) is located within the presumptive ATPase region of T antigen. While C11A T antigen was previously reported to be defective in ATPase and DNA helicase activities, it was(More)
High-throughput studies have been widely used to identify protein-protein interactions; however, few of these candidate interactions have been confirmed in vitro. We have used a combination of isothermal titration calorimetry and fluorescence anisotropy to screen candidate interactions within the pantothenate biosynthetic pathway. In particular, we observed(More)
  • 1