Madhuri Chattopadhyay

TL;DR: It is shown that a small amount of disulfide-reduced apo-SOD1 can rapidly initiate fibrillation of this exceptionally stable and highly structured protein under mild, physiologically accessible conditions, thus providing an unusual demonstration of a specific, physiological relevant form of a protein acting as an initiating agent for the fibrilation of another form of the same protein.

TL;DR: This work provides the first complete characterization of all dominant copper coordination modes at pH 7.4, and identifies three distinct coordination modes that are clearly identified at low copper stoichiometry.

TL;DR: Recent research on the significance, causes, and mechanisms of SOD1 fibril formation from a biophysical perspective is reviewed.

TL;DR: It is demonstrated that the octarepeat domain is responsive to a remarkably wide copper concentration range covering approximately 5 orders of magnitude, which suggests that PrP may function to protect cells by scavenging excess copper.

TL;DR: A picture of copper and zinc in the cell is provided as well as the importance of these metals in understanding SOD1-ALS pathology to support the hypothesis that immature nascent S OD1 is the substrate for aggregation.