Voelcker Academy

Research Symposium 2009

 

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Michael Anderson

Crystallographic studies on Copper-Zinc Superoxide Dismutase (SOD1) involved in Amyotrophic Lateral Sclerosis Using X-Ray Diffraction

Michael Anderson

Mentor(s): John Hart, Ph.D

Copper-zinc superoxide dismutase (SOD1) detoxifies superoxide anion, a byproduct of cellular respiration, to molecular oxygen and hydrogen peroxide. In the early 1990s, mutations in the human gene encoding SOD1 were linked to the fatal progressive neurodegenerative disease of amyotrophic lateral sclerosis. Today, more than 100 distinct pathogenic mutations have been documented, with most resulting in single amino acid substitutions and a few in truncations of the SOD1 polypeptide. Currently, it is generally accepted that SOD1-linked ALS pathology is related to pathogenic SOD1 misfolding and/or aggregation; however, the mechanism of SOD1 mediated toxicity is not known.