Over 100 mutations in the SOD1 protein have been linked to ALS, but how all these distinct mutations lead to the same disease is still a matter of debate. A new study published October 14 in Proceedings of the National Academy of Sciences applied sophisticated biophysical methods to examine how mutations in the SOD1 protein affect protein stability and aggregation dynamics. The researchers, led by Elizabeth Getzhoff and John Tainer at The Scripps Research Institute in La Jolla, California, together with colleagues from the Lawrence Berkeley National Laboratories in Berkeley, California and University of Georgia, found that in all SOD1 mutations analyzed, the mutations increased protein instability and reduced copper retention. Interestingly, SOD1 mutations that led to more rapid protein aggregation were also associated with faster progression of clinical symptoms. Click here to read more.
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