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Updated: Mar 12, 2026

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells
Published on: October 4, 2017
Commentary: alpha-synuclein interacts with SOD1 and promotes its oligomerization
Anika M Helferich1, Pamela J McLean2, Jochen H Weishaupt1
1Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, Germany.
Abstract:
Alpha-synuclein and Cu, Zn superoxide dismutase (SOD1) are both aggregation-prone proteins that are associated with Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS), respectively. Recently, we showed that alpha-synuclein interacts with SOD1 in various cell types and tissues. Using a cell culture model, we also found that alpha-synuclein nucleates the polymerization of SOD1. Here, we discuss the current literature regarding their interaction and their co-localization in aggregates of human post-mortem tissue. Furthermore we comment on the reported alpha-synuclein-induced SOD1 polymerization in terms of cross-seeding effects in neurodegeneration.
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