Sod1, short for superoxide dismutase 1, is well-known for its ROS scavenging activity. It also plays additional roles in modulating metabolism, maintaining redox balance, and regulating transcription [2].

Mutations in the Sod1 gene are responsible for 15% of familial amyotrophic lateral sclerosis (ALS) cases, and Sod1 dysfunction may be involved in sporadic ALS as well [1]. In ALS, mutant Sod1 proteins misfold and aggregate, leading to mitochondrial dysfunction, which is an important pathogenic mechanism [4]. The mitochondrial accumulation of mutant Sod1 can lead to motor neuron pathology and death [4]. Also, the efficacy of Sod1 folding impacts neuronal loss in motor system neurodegenerative diseases [3].

In conclusion, Sod1 is crucial for multiple cellular functions such as ROS scavenging, metabolism modulation, etc. Its role in ALS, especially through mutant-induced misfolding, aggregation, and mitochondrial dysfunction, has been well-demonstrated. The study of Sod1, especially in the context of ALS, helps in understanding the disease mechanism and may lead to potential therapeutic strategies [1,2,3,4].