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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
Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN2870697
Sakanyan, Hulin, Alves de Sousa, Silva, Hambardzumyan, Nedellec, Tomasoni, Logé, Pineau, Roussakis, Fleury, Artaud: Activation of EGFR by small compounds through coupling the generation of hydrogen peroxide to stable dimerization of Cu/Zn SOD1. in Scientific reports 2016
The crystal structures of BmSod1 in both holo and Cu-deficient forms, are reported.
CCS-D2 forms a stable complex with zinc-bound SOD1 in human cells, that has a twofold stabilizing effect: it both prevents the accumulation of unstructured mutant SOD1 and promotes zinc binding. CCS-D2 interacts with apo-SOD1 in vitro, suggesting that in cells CCS stabilizes mutant apo-SOD1 prior to zinc binding.
Spy1 plays a protective role in ALS motor neurons
The mean serum superoxide oxide dismutase in asthma cases and controls was 62.53+/- 15.23 and 55.65+/- 15.87, respectively. The superoxide dismutase genetic variants studied for the intronic polymorphism in copper-zinc superoxide dismutase showed increased risk of asthma compared with non-asthmatic controls.
Two amino acid positions in SOD1 that are in critical structural locations in the protein, Glu40 and Glu133, are studied. THe mutations in SOD1 that disrupt van der Waals interactions or introduce steric strain are poorly tolerated and are associated with a higher propensity to aggregate.
No sequence variations from wild type SOD1 were identified in any of 17 idiopathic Parkinson's disease cases in which was observed SOD1 dysfunction and aggregation. The absence of mutations in SOD1 in this Parkinson's disease cohort indicates that aggregated SOD1 in these cases is wild type protein.
MIF inhibits mutant SOD1 nuclear clearance when overexpressed in motor neuron-like NSC-34 cells.
The absence of SOD1 mutations in Parkinson disease highlights mounting evidence that SOD1 mutations are not the sole cause of SOD1 protein misfolding occasioning oligomerization and toxicity, reinforcing the importance of non-genetic factors, including protein metallation and post-translational modification in determining SOD1 stability and function.
SOD1 is a potential prognostic biomarker and a promising target for NPC therapy
MnSOD is a promising prognostic marker in ccRCC and implies that oxidative stress might be involved in the tumorigenesis and progression of ccRCC
Larvae injected with mutant SOD1 mRNA had significantly shorter and more aberrantly branched motor axons (p < 0.002) and traveled a significantly shorter distance during behavioral testing (p < 0.001) when compared with wild-type SOD1 and noninjected zebrafish larvae.
Study mutated four different Lys residues (K30, K36, K75, K91) in SOD1 that are not particularly well conserved. While some mutations to cause enhanced C4F6 binding, study did not observe that mutations that reduce charge at these positions caused the protein to form intracellular inclusions.
that SOD1 overexpression preserves normal baroreflex function but may differentially alter the functions of the aortic depressor nerve, vagal efferents, and central components.
The ligand, positioned in a region important for SOD1 fibrillation, offers the possibility that it, or a similar compound, could prevent the abnormal self-association that drives SOD1 toxicity in amyotrophic lateral sclerosis.
SOD1 Aggregation Is Highly Variable and Includes Two Distinct Structural Change Steps. SOD1 Forms a Mixture of Amorphous and Fibrillar Assemblies.
SOD1 polypeptides undergo hydrogelation accompanied by the formation of thioflavin T-positive fibrils at pH 3.0 and 4.0, but not at pH 5.0 where precipitates are formed. The results of viscoelastic analyses indicate that the properties of SOD1 hydrogels (2%) were similar to and slightly more fragile than a 0.25% agarose gel.
The observed loss of SOD1 function in pLG72-expressing cells may explain the elevated ROS levels and inhibition of U87 cell proliferation and has implications for understanding the onset of neurodegenerative diseases in humans.
Structural studies of the SOD1 variant segment of residues 28-38 suggest that oligomers of amyloid proteins are composed of single twisted sheets whereas fibrillar species are composed of mated b-sheets.
the outcomes from secondary structural propensities and free energy landscapes, together assertively suggested that L126S, N139H and G141A tend to increase the formation of aggregates in SOD1 relative to other mutants.
we also found that CTGF/CCN2 is expressed in astrocytes and neurons, predominantly in dorsal areas of spinal cord from symptomatic hSOD1G93A mice. Together, these results reveal that CTGF/CCN2 might be a novel therapeutic target to ameliorate symptoms and improve the quality of life of ALS patients.
the inhibition of mutant SOD1 aggregation by kaempferol was explored, thereby suggesting kaempferol could act as a drug candidate for the design of the natural therapeutics against familial amyotrophic lateral sclerosis S
the cytosolic SOD-null syndrome is largely consistent across sex and genetic background, but also significantly influenced by both.
The functional SOD1 and SOD2 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 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 in transgenic Drosophila.
survey of DNA sequence polymorphisms
Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity.
SOD1 and SOD2 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
Instability of superoxide dismutase 1 of Drosophila in mutants deficient for its cognate copper chaperone
switching SOD1-deficient flies from normoxia into hypoxia fails to alter their mortality
Mutant SOD1 overexpression led to an increase in TDP-43 modification in the detergent-insoluble fraction in the spinal cord of SOD1 mice and fALS patient. Additionally, we showed cellular apoptosis in response to the interaction of mutant SOD1 and fragment forms of TDP-43.
CNS-derived extracellular vesicles from superoxide dismutase 1 (SOD1)(G93A) ALS mice originate from astrocytes and neurons and carry misfolded SOD1
Molecular mechanism that triggers functional denervation associated with the toxic activity of muscle SOD1(G93A) expression.
Sod1 mRNA levels were reduced when Oct4, Sox2 and Nanog were down-regulated by a shRNA approach in mESCs.
Deletion of caspase 6 exacerbates symptom onset and disease progression in SOD1 (G93A) mice.
Mice overexpressing a mutated form of the SOD1 gene (SOD1(G93A)) develop a syndrome that closely resembles the human disease amyotrophic lateral sclerosis
These findings suggest unexpected specificity, mediated by both the primary protein pathology and cellular context, in the induced "secondary aggregation" of a mutant form of SOD1 that could be viewed as a reporter of proteostatic function
Presence of mutated SOD1 protein affects the MHC class I molecules expression and is associated with facial injured motoneurons.
DKO mice spontaneously develop severe liver failure at a relatively young stage, they have the potential for use as a model for hepatic disorders and for testing other potential treatments.
These results suggest that overexpression of SQSTM1 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, we wondered whether internalisation of SOD1 aggregates stimulated TDP-43 cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 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 expression increased in the spinal cord of SOD1G93A mice as the disease progressed. However, AQP4 polarization decreased as the disease progressed, and AQP4 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 reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of amyotrophic lateral sclerosis.
This study indicates that axonal and neuromuscular junction degeneration in the SOD1 model of amyotrophic lateral sclerosis is a complex and evolving sequence of events
The results showed that 60-min ischemia of the porcine uterus conducted at the mid-secretory estrous phase caused decreased HIF-1alpha and increased SOD-2 gene expression.
Sequence comparison between sows with high and low estimated breeding value (EBV) for litter size, revealed a total of eight single nucleotide polymorphisms (SNPs) in the noncoding sequence and no SNPs in the coding region.
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
the present study aims to evaluate the peritoneal fluid impact from infertile women with minimal and mild endometriosis and from fertile control women without endometriosis on SOD1, CAT, GSR gene's expression in experimental bovine oocytes matured in vitro.
Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle.
The three-dimensional structure of bSOD1 reveals the imidazole ring of His19 localized within 5A from the alpha-carbon of Gly31 providing a structural basis that copper ion, most likely coordinated by His19, catalyzes the specific cleavage reaction
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, 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, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1 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 by PGF 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.
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-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. 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)
Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions.
Raman spectrum analysis strongly suggests that the His41-mediated hydrogen bond bridge of Cu-Zn superoxide dismutase plays a crucial role in keeping the protein structure suitable for highly efficient catalytic reactions.
HCO(3)(-)-derived oxidant does not alter significantly the Cu(II) active site geometry and histidine coordination to Cu(II) in SOD1 as does H(2)O(2) alone
copper- and carbonate radical anion-mediated oxidations have roles in hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation
SOD1 mutants gain fatty acid binding abilities based on their structural instability and form cytotoxic granular aggregates
The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing 10(-4) M EDTA.
Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH).
communication between the two monomers of SOD1 such that the binding of one zinc ion per homodimer has a more profound effect on the homodimeric protein structure than the binding of subsequent metal ions
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 as a defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus.
a post-translational modification to the inactive enzyme during hypoxia
the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS 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 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, sp1 and sod1 in zebrafish.
depresses cathepsin L activity stimulated by free radicals and prevents otic complications associated with bone erosion
This isoform, when expressed in PC-12 cells affects t-butylhydroperoxide-induced apoptosis differentially from its isoenzyme.
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