| Antioxidant defense | Catalyzes the dismutation of superoxide radical (O₂⁻) to hydrogen peroxide (H₂O₂) and molecular oxygen (O₂) |
| Cellular protection | Prevents oxidative damage to proteins, lipids, and nucleic acids |
| Metal ion homeostasis | Requires precise copper and zinc binding for proper folding and activity |
| Dimeric structure | Functions as a homodimer with each subunit requiring proper metalation |
| Intermediate species | Partially folded monomers and small oligomers are highly toxic |
| Aggregate formation | Insoluble aggregates accumulate in motor neurons and glia |
| Sequestration | Aggregates sequester essential cellular proteins including chaperones |
| Proteostasis overload | The cellular protein quality control systems become overwhelmed |
| Direct mitochondrial binding | Mutant SOD1 localizes to mitochondrial outer membranes |
| Electron transport chain impairment | Complex I and IV activities are reduced |
| Increased ROS production | Paradoxically increases oxidative stress despite antioxidant enzyme activity |
| Databases | OMIMOrphanetClinicalTrialsPubMed |
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