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Cu-Zn Superoxide Dismutase

Known as: EC 1.15.1.1, Superoxide Dismutase [Cu-Zn], hSod1 
Superoxide dismutase [Cu-Zn] (154 aa, ~16 kDa) is encoded by the human SOD1 gene. This protein is involved in the conversion of superoxides into… 
National Institutes of Health

Related topics

Related topics

15 relations
CytoplasmEnzyme GeneFlumazenil Cardioprotection PathwayFree Radical Induced Apoptosis Pathway

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2015
Highly Cited
2015
NLRP3 inflammasome is expressed by astrocytes in the SOD1 mouse model of ALS and in human sporadic ALS patients
Amyotrophic lateral sclerosis (ALS) is characterized by the degeneration of motoneurons in the cerebral cortex, brainstem and… 
Review
2011
Review
2011
Glial Cells in Amyotrophic Lateral Sclerosis
Amyotrophic lateral sclerosis (ALS) is an adult motor neuron disease characterized by premature death of upper and lower motor… 
Highly Cited
2009
Highly Cited
2009
Hitchhiking of Cu/Zn Superoxide Dismutase to Peroxisomes – Evidence for a Natural Piggyback Import Mechanism in Mammals
Most newly synthesized peroxisomal proteins are imported in a receptor‐mediated fashion, depending on the interaction of a… 
Highly Cited
2006
Highly Cited
2006
Complete Dissociation of Motor Neuron Death from Motor Dysfunction by Bax Deletion in a Mouse Model of ALS
The death of cranial and spinal motoneurons (MNs) is believed to be an essential component of the pathogenesis of amyotrophic… 
Highly Cited
2005
Highly Cited
2005
Increased persistent Na+ current and its effect on excitability in motoneurones cultured from mutant SOD1 mice
Mutations in the enzyme superoxide dismutase 1 (SOD1) initiate a progressive motoneurone degeneration in amyotrophic lateral… 
Highly Cited
2004
Highly Cited
2004
The Unusually Stable Quaternary Structure of Human Cu,Zn-Superoxide Dismutase 1 Is Controlled by Both Metal Occupancy and Disulfide Status*
The eukaryotic copper,zinc superoxide dismutases are remarkably stable dimeric proteins that maintain an intrasubunit disulfide… 
Highly Cited
2002
Highly Cited
2002
Mutated Human SOD1 Causes Dysfunction of Oxidative Phosphorylation in Mitochondria of Transgenic Mice*
A growing body of evidence suggests that impaired mitochondrial energy production and increased oxidative radical damage to the… 
Highly Cited
2000
Highly Cited
2000
Human Cu/Zn Superoxide Dismutase (SOD1) Overexpression in Mice Causes Mitochondrial Vacuolization, Axonal Degeneration, and Premature Motoneuron Death and Accelerates Motoneuron Disease in Mice…
Cytosolic Cu/Zn superoxide dismutase (SOD1) is a ubiquitous small cytosolic metalloenzyme that catalyzes the conversion of… 
Review
2000
Review
2000
The biochemistry of aging.
Highly Cited
1995
Highly Cited
1995
Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons.
Mutation in superoxide dismutase 1 (SOD1), a Cu/Zn enzyme that removes oxygen radicals and protects against oxidative injury, has… 
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