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Updated: Nov 28, 2025
11:12
Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells
Published on: October 4, 2017
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SOD1, more than just an antioxidant
Elis Cristina Araujo Eleutherio1, Rayne Stfhany Silva Magalhães1, Aline de Araújo Brasil1
1Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Brazil.
Archives of Biochemistry and Biophysics
|December 1, 2020
Summary
Human copper-zinc superoxide dismutase (SOD1) enzyme protects cells from damaging superoxide radicals. This review explores SOD1’s structure, functions, modifications, and roles in diseases like ALS.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Cellular respiration produces damaging superoxide radicals.
- Cu/Zn Superoxide Dismutase (SOD1) neutralizes superoxide radicals.
- SOD1 also exhibits non-canonical functions, including gene transcription regulation and RNA binding.
Purpose of the Study:
- To provide a comprehensive review of human SOD1 (hSOD1).
- To detail hSOD1 structure, properties, and modifications.
- To explore hSOD1's diverse functions and disease relevance.
Main Methods:
- Literature review of existing studies on hSOD1.
- Analysis of transcriptional and post-translational modifications (PTM).
- Discussion of current analytical strategies for hSOD1.
Main Results:
- hSOD1 possesses diverse functions beyond radical scavenging.
- Transcriptional and PTMs significantly impact hSOD1 activity and roles.
- hSOD1 is implicated in neurodegenerative diseases and cancer.
Conclusions:
- Understanding hSOD1's multifaceted nature is crucial.
- Further research into hSOD1 modifications and functions can reveal therapeutic targets.
- hSOD1 plays a significant role in cellular health and disease pathogenesis.
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