ReviewThe Journal of biological chemistry2009
The right to choose: multiple pathways for activating copper,zinc superoxide dismutase.
Review in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 105 citations in OpenAlex.
- From copper transport to cuproptosis: emerging therapeutic targets in cardiovascular disease.Molecular and cellular biochemistry · 2026Review
- Mammalian copper homeostasis: physiological roles and molecular mechanisms.Physiological reviews · 2025Review
- Role of copper homeostasis and cuproptosis in heart failure pathogenesis: implications for therapeutic strategies.Frontiers in pharmacology · 2024Review
- Superoxide Radicals in the Execution of Cell Death.Antioxidants (Basel, Switzerland) · 2022Review
- Dynamic and cell-specific transport networks for intracellular copper ions.Journal of cell science · 2021Review
- The Crossroads between Host Copper Metabolism and Influenza Infection.International journal of molecular sciences · 2021Review
- Role of Oxidative Stress in the Pathogenesis of Amyotrophic Lateral Sclerosis: Antioxidant Metalloenzymes and Therapeutic Strategies.Biomolecules · 2021Review
- Article
- Copper Sources for Sod1 Activation.Antioxidants (Basel, Switzerland) · 2020Review
- Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019Article
- Review
- Copper transporters and copper chaperones: roles in cardiovascular physiology and disease.American journal of physiology. Cell physiology · 2018Review
- A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.Scientific reports · 2017Article
- Unraveling new functions of superoxide dismutase using yeast model system: Beyond its conventional role in superoxide radical scavenging.Journal of microbiology (Seoul, Korea) · 2017Review
- Copper trafficking to the secretory pathway.Metallomics : integrated biometal science · 2016Review
- Histone H3 and TORC1 prevent organelle dysfunction and cell death by promoting nuclear retention of HMGB proteins.Epigenetics & chromatin · 2016Article
- Cellular sensing and transport of metal ions: implications in micronutrient homeostasis.The Journal of nutritional biochemistry · 2015Review
- Essential metals at the host-pathogen interface: nutritional immunity and micronutrient assimilation by human fungal pathogens.FEMS yeast research · 2015Review
- Diabetic cardiomyopathy is associated with defective myocellular copper regulation and both defects are rectified by divalent copper chelation.Cardiovascular diabetology · 2014Article
- Species-specific activation of Cu/Zn SOD by its CCS copper chaperone in the pathogenic yeast Candida albicans.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Since the discovery of SOD1 in 1969, there have been numerous achievements made in our understanding of the enzyme's biochemical reactivity and its role in oxidative stress protection and as a genetic determinant in amyotrophic lateral sclerosis. Many recent advances have also been made in understanding the "activation" of SOD1, i.e. the process by which an inert polypeptide is converted to a mature active enzyme through post-translational modifications. To date, two such activation pathways have been identified: one requiring the CCS copper chaperone and one that works independently of CCS to insert copper and activate SOD1 through oxidation of an intramolecular disulfide. Depending on an organism's lifestyle and complexity, different eukaryotes have evolved to favor one pathway over the other. Some organisms rely solely on CCS for activating SOD1, and others can only activate SOD1 independently of CCS, whereas the majority of eukaryotes appear to have evolved to use both pathways. In this minireview, we shall highlight recent advances made in understanding the mechanisms by which the CCS-dependent and CCS-independent pathways control the activity, structure, and intracellular localization of copper,zinc superoxide dismutase, with relevance to amyotrophic lateral sclerosis and an emphasis on evolutionary biology.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.