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Pastori, Carnevale, Menichelli, Nocella, Bartimoccia, Novo, Leo, Violi, Pignatelli: Is There an Interplay Between Adherence to Mediterranean Diet, Antioxidant Status, and Vascular Disease in Atrial Fibrillation Patients? in Antioxidants & redox signaling 2016
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Human SOD1 ELISA Kit for Sandwich ELISA - ABIN572327
Neyestani, Ghandchi, Eshraghian, Kalayi, Shariatzadeh, Houshiarrad: Evidence for augmented oxidative stress in the subjects with type 1 diabetes and their siblings: a possible preventive role for antioxidants. in European journal of clinical nutrition 2012
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Rat (Rattus) SOD1 ELISA Kit for Sandwich ELISA - ABIN416137
Moor, Tummel, Prather, Jung, Lopez, Connors, Gould: Consequences of age on ischemic wound healing in rats: altered antioxidant activity and delayed wound closure. in Age (Dordrecht, Netherlands) 2014
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Mouse (Murine) SOD1 ELISA Kit for Sandwich ELISA - ABIN367881
Lv, Deng, Yu, Wang, Gong, Jia, Wang: Nrf2-ARE signals mediated the anti-oxidative action of electroacupuncture in an MPTP mouse model of Parkinson's disease. in Free radical research 2015
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Mouse (Murine) SOD1 ELISA Kit for Sandwich ELISA - ABIN424085
Chu, Ci, He, Jiang, Wei, Cao, Guan, Xie, Deng, He: Effects of a natural prolyl oligopeptidase inhibitor, rosmarinic Acid, on lipopolysaccharide-induced acute lung injury in mice. in Molecules (Basel, Switzerland) 2012
Human SOD1 ELISA Kit for Competition ELISA - ABIN1117272
Zhao, Xu, Song, Nian, Zhou, Wang et al.: 2,3,5,4'-tetrahydroxystilbene-2-O-?-d-glucoside protects human umbilical vein endothelial cells against lysophosphatidylcholine-induced apoptosis by upregulating superoxide dismutase and glutathione ... in IUBMB life 2014
Our study provides the first direct evidence that Abeta, an AD-linked factor, is associated to the pathogenesis of ALS and provides molecular clues to understand common aggregation mechanisms in the pathogenesis of neurodegenerative diseases.
deletion-rescue experiments show that a respiration-defective mutant of SOD1 is also impaired in its ability to rescue cells from toxicity caused by SOD1 deletion
These findings indicate that a loss of Sig1R function is causative for juvenile amyotrophic lateral sclerosis (ALS16), and collapse of the mitochondria-associated membrane is a common pathomechanism in both Sig1R- and SOD1-linked ALS.
the aberrant mutant SOD1-G3BP1 (show G3BP1 ELISA Kits) interaction affects stress granule dynamics
the absence of IP3R2 led to increased innate immunity, which may contribute to the decreased survival of the SOD1(G93A) mice.our data indicate that IP3R2 protects against the negative effects of inflammation, suggesting that the increase in IP3R2 expression in ALS patients is a protective response.
the redox regulation of Jmjd3 (show Kdm6b ELISA Kits) is a unique regulatory mechanism for Cu,Zn-superoxide dismutase-mediated profibrotic macrophage polarization.
two ALS-linked factors, SQSTM1 (show SQSTM1 ELISA Kits) and ALS2 (show ALS2 ELISA Kits), have distinct but additive protective roles against mutant SOD1-mediated toxicity by modulating neuronal proteostasis possibly through the autophagy-endolysosomal system.
we showed that, in the absence of ERalpha (show ESR1 ELISA Kits), G93A-SOD1 failed to activate OMI (show HTRA2 ELISA Kits) and the proteasome, confirming the ERalpha (show ESR1 ELISA Kits) dependence of the response. Taken together, these results demonstrate the IMS-UPRmt activation in SOD1 familial Amyotrophic lateral sclerosis , and suggest that sex differences in the disease phenotype could be linked to differential activation of the ERa axis of the IMS-UPRmt
The cross-sectional area of the pial arteriolar wall was increased in SOD1 deficiency, and a hyperhomocysteinemic diet sensitized SOD1-deficient mice to this hypertrophic effect. Analysis of of the vascular wall demonstrated a increase in the content of smooth muscle and elastin (show ELN ELISA Kits). We conclude that superoxide is a driver of both cerebral vascular hypertrophy and vasomotor dysfunction in a model of hyperhomocysteinemia.
SOD1 has a role in amyotrophic lateral sclerosis disease phenotype
the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS (show CCS ELISA Kits) 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.
The functional SOD1 and SOD2 (show SOD2 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) 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
The results show that the docking of the electrostatic loop to the rest of SOD1 plays a role in amyotrophic lateral sclerosis (ALS (show IGFALS ELISA Kits)) pathogenesis, in support of that structure acting as a solvent barrier for the metal site. The results provide a unified pathogenic mechanism for five different ALS (show IGFALS ELISA Kits)-linked mutations of SOD1.
SOD1 is the seeding particle responsible for the spread of SOD1-familial amyotrophic lateral sclerosis neurodegeneration from its initial onset site
The results suggest that SFH prevents the degeneration of pancreatic islets via increasing SOD while hyperglycemia is alleviated by maintaining beta cell mass in type 2 diabetes model mice.
study thus implies that the WT and mutant SOD1 indeed converge on a common mechanism for gain of cytotoxicity by abnormally interacting with membranes. Moreover, any genetic/environmental factors which can delay or impair its maturation might act to transform SOD1 into cytotoxic forms with the acquired capacity to abnormally interact with membranes.
Data suggest that multiple non-native species of misfolded SOD1 may exist in the SOD1(G93A) rat model, some of which are associated with mitochondrial damage, highlighting that variable potency/toxicity of different SOD1 species is possible even when only one SOD1 mutation is present.
SOD1 is one of the most commonly mutated genes in ALS.
superoxide dismutase function of SOD1 might not be required to preserve DNA integrity in motor neurons, at least when the function of TDP-43 (show TARDBP ELISA Kits) is unaltered
The results suggest that the 50 bp deletion has a moderate reducing effect on SOD1 synthesis.
Factors released in vitro from astrocytes derived from SOD-1 transgenic mice cause spinal motoneuron death and consequent neuromuscular dysfunction in vivo.
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
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 ELISA Kits), 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 ELISA Kits), CPNE3 (show CPNE3 ELISA Kits), IL1R2 (show IL1R2 ELISA Kits), IL6 (show IL6 ELISA Kits), TLR2 (show TLR2 ELISA Kits), TLR4 (show TLR4 ELISA Kits), and THY1 (show THY1 ELISA Kits) 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 ELISA Kits) by PGF (show PGF ELISA Kits) 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 ELISA Kits).
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 ELISA Kits)-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 ELISA Kits). The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution.
expression profile in follicles: oocytes (SOD1 throughout ooplasm (show NLRP5 ELISA Kits) & 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.
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.
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 ELISA Kits) 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 ELISA Kits), sp1 (show SP1 ELISA Kits) 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 (show GMFG ELISA Kits)-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.
superoxide dismutase [Cu-Zn]
, Cu/Zn superoxide dismutase
, superoxide dismutase 1 soluble
, superoxide dismutase
, Cu/Zn SOD
, insulin-like growth factor-binding protein complex acid labile subunit
, insulin-like growth factor binding protein complex acid-labile subunit
, insulin-like growth factor-binding protein complex acid labile chain
, 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 1
, superoxide dismutatase
, superoxido dismutase
, tetrazolium oxidase
, tetrazolium oxidase-1
, SOD, soluble
, indophenoloxidase A
, superoxide dismutase, cystolic
, Cu(2+)-Zn2+ superoxide dismutase
, superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))
, Cu-Zn-superoxide dismutase
, Cu,Zn-superoxide dismutase
, Cu,Zn superoxide dismutase
, superoxide dismutase [Cu-Zn] B