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Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN5777061
Luchinat, Barbieri, Rubino, Kozyreva, Cantini, Banci: In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. in Nature communications 2014
Weak significance was observed for a protective effect of the TT genotype of rs1041740 in the SOD1 gene relative to Type 1 Diabetes development (OR 0.318, 95% CI 0.092-0.959, p = 0.056).
SOD1 is S-acetylated in spinal cord homogenates from ALS (show IGFALS Proteins) and non-ALS (show IGFALS Proteins) subjects. The degree of S-acylation is highest for SOD1-CCS (show CCS Proteins) heterodimers and lowest for SOD1 monomers.
Metallation and oxidation of SOD1 stabilize the native, mature conformation and decrease the number of detected excited conformational states.
results thus shed light on the role of local unfolding and conformational dynamics in aggregation of SOD1
Certain SOD1 mutants, viz. His80Arg and Asp83Gly, were recognized that were more damaging to the Zn binding loop than all other mutants, leading to a loss of Zn binding with altered coordination of the Zn ion. Furthermore, the conformational stability, compactness, and secondary structural alteration of the His80Arg and Asp83Gly mutants were monitored using distinct parameters.
describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 and TARDP genes
that global changes in DNA methylation (show HELLS Proteins) might contribute to the ALS (show IGFALS Proteins) phenotype in carriers of not fully penetrant SOD1 mutations
The present study indicating that although the Ins (show INS Proteins)/Del polymorphism of SOD1 is associated with the SOD1 expression levels, this polymorphism is not associated with the risk of dependency to heroin.
The mutant human SOD1-G93A protein induced axonal and myelin degeneration during the progression of Amyotrophic Lateral Sclerosis in a mouse model and participated in axon remyelination and regeneration in response to injury.
SOD1 oligomer and not the mature form of aggregated fibril is critical for the neurotoxic effects in the model of amyotrophic lateral sclerosis.
the cytosolic SOD-null syndrome is largely consistent across sex and genetic background, but also significantly influenced by both.
The functional SOD1 and SOD2 (show SOD2 Proteins) genes knockout and their overexpression in neurons and glial tissue increase the sensitivity of Drosophila melanogaster to oxidative stress conditions.
Expression of zinc-deficient human superoxide dismutase (show SOD2 Proteins) in Drosophila neurons produces a locomotor defect linked to mitochondrial dysfunction.
curcumin increases mean lifespan of Drosophila via regulating gene expression of the key enzyme SOD and reducing accumulation of MDA and lipid peroxidation.
The activity of carbohydrate metabolizing enzymes, lipid and triglyceride concentration, and steady state NADPH:NADP(+) in SOD1-null and control transgenic rescue flies, was analysed.
Overexpression of Cu,ZnSOD and MnSOD (show SOD2 Proteins) in transgenic Drosophila.
Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity.
SOD1 and SOD2 (show SOD2 Proteins) provide independent protection to compartment-specific protein iron-sulfur clusters against attack by superoxide generated under oxidative stress
A 1140 base pair region, composed of the single sod1 intron along with exon 2, was found to be essential for permitting spatial and temporal expression patterns that approximate normal endogenous expression.
Cu/Zn superoxide dismutase has a role in preventing spontaneous DNA damage
Presence of mutated SOD1 protein affects the MHC class I molecules expression and is associated with facial injured motoneurons.
These results suggest that overexpression of SQSTM1 (show SQSTM1 Proteins) in SOD1 (H46R) mice accelerates disease onset by compromising the protein degradation pathways.
Results support the concept that impaired redox signaling, rather than oxidative damage, in peripheral nerve plays a key role in muscle loss in Sod1(-/-) mice and potentially sarcopenia during aging
This evidence favours mutant SOD1-containing astrocytes releasing destructive species that alter the biology of adjacent astrocytes
Given the close association of stress granules and TDP-43 (show TARDBP Proteins), we wondered whether internalisation of SOD1 aggregates stimulated TDP-43 (show TARDBP Proteins) cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 (show TARDBP Proteins) to the cytoplasm where it was still accumulated after 48 h.
Distinct roles for motor neuron autophagy early and late in the SOD1(G93A) mouse model of ALS.
It was observed that global AQP4 (show AQP4 Proteins) expression increased in the spinal cord of SOD1G93A mice as the disease progressed. However, AQP4 (show AQP4 Proteins) polarization decreased as the disease progressed, and AQP4 (show AQP4 Proteins) polarized localization at the endfeet of astrocytes was decreased in the spinal ventral horn of SOD1G93A mice at the disease onset and end stages.
Superoxide dismutase 1 mutation is associated with amyotrophic lateral sclerosis.
Restrictive Lung Disease in the Cu/Zn Superoxide-Dismutase 1 G93A Amyotrophic Lateral Sclerosis Mouse Model.
Endogenous MIF (show MIF Proteins) reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of amyotrophic lateral sclerosis.
The results showed that 60-min ischemia of the porcine uterus conducted at the mid-secretory estrous phase caused decreased HIF-1alpha (show HIF1A Proteins) and increased SOD-2 (show SOD2 Proteins) gene expression.
CuZnSOD mRNA is a broad-spectrum expression gene, which was detected in brain, heart, spleen, liver, kidney, lung, large intestine, small intestine, spinal cord, muscle, backfat, and stomach
Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle.
SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability
antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase (show GPX1 Proteins), which show the changes in their expression during improper placental release
Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis.
ALOX5AP (show ALOX5AP Proteins), CPNE3 (show CPNE3 Proteins), IL1R2 (show IL1R2 Proteins), IL6 (show IL6 Proteins), TLR2, TLR4 (show TLR4 Proteins), and THY1 (show THY1 Proteins) were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows.
Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced (show SQSTM1 Proteins) by PGF (show PGF Proteins) during functional luteolysis.
At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase (show CAT Proteins).
Capillary electrophoresis and mass spectrometry to study the different structures of bovine SOD-1. In both cases, an average molecular mass corresponding to the apo (show C9orf3 Proteins)-monomer SOD-1 was calculated.
flexibility of the metal sites involved in present a single-crystal X-ray diffraction study of Cu,Zn superoxide dismutase in space group P212121 at 0.57 GPa (show GYPA Proteins). The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution.
expression profile in follicles: oocytes (SOD1 throughout ooplasm & nucleoplasm); cumulus cells (no SOD1 detected); granulosa cells (expressed SOD1); follicular fluid (small follicles show increased amounts of SOD1 in comparison with large follicles)
amyloid and oxidative stress-related disease proteins like SOD 1 is increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.
We found that guanylyl cyclases GCY-5 and GCY-22 and neuropeptide receptor NPR-1 act antagonistically to regulate SOD-1 expression in the gustatory neuron ASER.
These data suggest that SOD1 mutants are removed from the nucleus by CRM1 (show XPO1 Proteins) as a defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus.
the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS (show CCS Proteins) for activation
although several long-lived mutants of Caenorhabditis elegans have increased SOD levels, this phenomenon does not correlate with life span or growth rate.
SOD isoforms play no role in lifespan in ad lib or dietary restricted conditions, but mutational inactivation of SOD-1 reduces life extension by cold.
the ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
this suggests that the activity of SOD-1, which so far has been thought to act mainly in cytoplasm, helps to control the detoxification of *O2- also in the mitochondria.
fenofibrate almost completely abolished GM-induced reactive oxygen species generation, which seemed to be mediated at least in part by the restoration of the expression of PPARalphadependent antioxidant enzymes, including catalase (show CAT Proteins) and superoxide dismutase (SOD)-1.
The earliest event in the pathophysiology of amyotrohic lateral sclerosis in the mutant sod1 zebrafish model involves neuronal stress in inhibitory interneurons, resulting from mutant Sod1 expression.
A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a (show ATP7A Proteins), sp1 (show SP1 Proteins) and sod1 in zebrafish.
depresses cathepsin L activity stimulated by free radicals and prevents otic complications associated with bone erosion
Copper/zinc superoxide dismutase was cloned from the zebrafish ( Danio rerio). Evidence is presented that SOD protects against paraquat toxicity in fish.
Glia maturation factor-null cells ahow a concurrent decrease in CuZnSOD astrocytes.
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene.
, Cu/Zn superoxide dismutase
, SOD, soluble
, indophenoloxidase A
, superoxide dismutase [Cu-Zn]
, superoxide dismutase, cystolic
, Cu, Zn superoxide dismutase
, Cu-Zn superoxide dismutase
, Cu/Zn-Superoxide dismutase
, CuZn superoxide dismutase
, CuZn-superoxide dismutase
, CuZn-superoxide dismutase (SOD)1
, Cu[2+] Zn[2+] superoxide dismutase
, Cu[2+]Zn[2+] superoxide dismutase
, Mn superoxide dismutase
, complementation group G
, copper and zinc SOD
, copper-zinc superoxide
, copper-zinc superoxide dismutase
, cytoplasmic Cu/ZnSOD
, super oxide dismutase
, superoxidase dismutase
, superoxide dismutase
, superoxide dismutase 1
, superoxide dismutatase
, superoxido dismutase
, tetrazolium oxidase
, tetrazolium oxidase-1
, superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))
, superoxide dismutase 1 soluble
, Cu(2+)-Zn2+ superoxide dismutase
, Cu-Zn-superoxide dismutase
, Cu,Zn-superoxide dismutase
, Cu,Zn superoxide dismutase
, superoxide dismutase [Cu-Zn] B